Abstract
Less than two decades ago Sutherland and Rall (1958; Rall et al., 1957) discovered a heat stable factor now known as adenosine 3′,5′-monophosphate, which accumulated in particulate fractions of liver homogenates exposed to epinephrine. This factor activated the breakdown of glycogen by soluble cytoplasmic enzymes. Although epinephrine activates glycogenolysis in intact hepatocytes, the hormone has no such effect on the soluble enzymes. Sutherland and Rall (1960; Rall and Sutherland, 1958, 1961, 1962) proposed that epinephrine might trigger the glycogenolytic response of hepatocytes by activating the synthesis of this nucleotide (cyclic AMP) whose structure (Fig. 1) by then had been shown to contain a unique cyclic phosphate bond (Lipkin et al., 1959). The polypeptide hormone glucagon also triggers the glycogenolytic response of liver, and activates the synthesis of cyclic AMP. From these and related observations on the actions of other hormones, the concept arose that cyclic AMP functioned as an intracellular “second messenger”, synthesized in response to certain hormones and which, by activating the appropriate sequence of enzymes, produced the specific biologic response of the target cell to the hormone (Sutherland et al., 1965).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abdulla, Y.H., Hamadah, K.: 3′,5′-Cyclic adenosine monophosphate in depression and mania. Lancet 1970I, 378–381.
Adinolfi, A.M., Schmidt, S.Y.: Cytochemical localization of cyclic nucleotide phosphodiesterase activity at developing synapses. Brain Res. 76, 21–31 (1974).
Aghajanian, G.K., Haigler, H.J., Bloom, F.E.: Lysergic acid diethylamide and serotonin: direct actions on serotonin-containing neurons in rat brain. Life Sci. 11, 615–622 (1972).
Amer, M.S., Kreighbaum, E.: Cyclic nucleotide phosphodiesterase: properties, activators, inhibitors, structure-activity relationships and possible role in drug development. J. pharm. Sci. 64, 1–37 (1975).
Anagnoste, B., Shirron, C., Friedman, E., Goldstein, M.: Effect of dibutyryl cyclic adenosine monophosphate on C14 dopamine synthesis in rat brain striatal slices. J. Pharmacol. exp. Ther. 191, 370–376 (1974).
Anderson, E.G., Haas, H., Hosli, L.: Comparison of effects of noradrenaline and histamine with cyclic AMP on brain stem neurones. Brain Res. 49, 471–475 (1973a).
Anderson, W.B., Russell, T.R., Carchman, R.A., Pastan, I.: Interrelationship between adenylate cyclase activity, adenosine 3′,5′-cyclic monophosphate levels, and growth of cells in culture. Proc. nat. Acad. Sci. (Wash.) 70, 3802–3805 (1973b).
Appleman, M.M., Terasaki, W.L.: The regulation of cyclic nucleotide phosphodiesterase. In: Advances in Cyclic Nucleotide Research, vol. 5. New York: Raven Press (in press).
Appleman, M.M., Thompson, W.J., Russell, T.R.: Cyclic nucleotide phosphodiesterases. In: Advances in Cyclic Nucleotide Research, vol. 3. New York: Raven Press 1973.
Arbuthnott, G.W., Attree, T.J., Eccleston, D., Loose, R.W., Martin, M.J.: Is adenylate cyclase the dopamine receptor. Med. biol. III. 52, 350–353 (1974).
Ascher, P.: Excitatory effects of dopamine on molluscan neurons. In: Frontiers in Catecholamine Research. New York: Pergamon Press 1973.
Ashby, C.D., Walsh, D.A.: Characterization of the interaction of a protein inhibitor with adenosine 3′,5′-monophosphate-dependent protein kinases. J. biol. Chem. 247, 6637–6642 (1972).
Ashman, D.F., Lipton, R., Melicow, M.M., Price, T.D.: Isolation of adenosine 3′,5′-monophosphate and guanosine 3′,5′-monophosphate from rat urine. Biochem. biophys. Res. Commun. 11, 330–334 (1963).
Atkinson, D.E.: Citrate in the regulation of energy metabolism. In: Metabolic Roles of Citrate. New York: Academic Press 1968.
Aurbach, G.D., Fedak, S.A., Woodard, C.J., Palmer, J.S., Hauser, D., Troxler, F.: β-adrenergic receptor: stereospecific interaction of iodinated β-blocking agent with high affinity site. Science 186, 1223–1224 (1974).
Axelrod, J.: Noradrenaline: fate and control of its biosynthesis. Science 173, 598–606 (1971).
Barker, J.L., Crayton, J., Nicoll, R.: Noradrenaline and acetylcholine responses of supraoptic neurosecretory cells. J. Physiol. (Lond.) 218, 19–32 (1971).
Batzri, S., Selinger, Z., Schramm, M.: Potassium ion release and enzyme secretion: adrenergic regulation by α and β receptors. Science 174, 1029–1031 (1971).
Baudry, M., Martres, M-P., Schwartz, J-C.: H1 and H2 receptors in the histamine-induced accumulation of cyclic AMP in guinea pig slices. Nature (Lond.) 253, 362–363 (1975).
Baylor, D.A., Fuortes, M.G.F.: Electrical responses of single cones in the retina of the turtle. J. Physiol. (Lond.) 207, 77–92 (1970).
Beavo, J.A., Hardman, J.G., Sutherland, E.W.: Hydrolysis of cyclic guanosine and adenosine 3′,5′-monophosphate by rat and bovine tissues. J. biol. Chem. 245, 5649–5655 (1970).
Beer, B., Chasin, M., Clody, D.E., Vogel, J.R., Horovitz, Z.P.: Cyclic adenosine monophosphate phosphodiesterase in brain: Effect on anxiety. Science 176, 428–430 (1972).
Bensinger, R.E., Fletcher, R.T., Chader, G.J.: Guanylate cyclase: inhibition by light in retinal photoreceptors. Science 183, 86–87 (1974).
Berg, J.S.V.: Inhibitory effects of dibutyryl and cyclic AMP on the compound action potential in the frog (Rana Pipiens) sciatic nerve. Experientia (Basel) 30, 1025–1026 (1974).
Berger, B., Tassin, J.P., Blanc, O., Moyne, M.A., Thierry, A.M.: Histochemical confirmation for dopaminergic innervation of rat cerebral cortex after destruction of the noradrenergic ascending pathways. Brain Res. 81, 332–337 (1974).
Berkowitz, B.A., Tarver, J.H., Spector, S.: Release of norepinephrine in the central nervous system by theophylline and caffeine. Europ. J. Pharmacol. 10, 64–71 (1970).
Berne, R.M., Rubio, R., Curnish, R.R.: Release of adenosine from ischemic brain. Circulat. Res. 35, 262–271 (1974).
Berridge, M.J., Prince, W.T.: The electrical response of isolated salivary glands during stimulation with 5-hydroxytryptamine and cyclic AMP. Phil. Trans. B 262, 111–120 (1971).
Berridge, M.J., Prince, W.T.: Transepithelial potential changes during stimulation of isolated salivary glands with 5-hydroxytryptamine and cyclic AMP. J. exp. Biol. 56, 139–153 (1972).
Berti, F., Trabucchi, M., Bernareggi, V., Fumagalli, R.: The effect of prostaglandins on cyclic AMP formation in cerebral cortex of different mammalian species. Pharmacol. Res. Commun. 4, 253–259 (1972).
Bianchi, C.P.: Cell Calcium. New York: Appleton-Century-Crofts 1964.
Bilzekian, J.P., Aurbach, G.D.: The effects of nucleotides on the expression of β-adrenergic adenylate cyclase activity in membranes from turkey erythrocytes. J. biol. Chem. 249, 157–161 (1974).
Birnbaumer, L., Yang, P.C.: Studies on receptor-mediated activation of adenylyl cyclases. I. Preparation and description of general properties of an adenylyl cyclase system in beef renal medullary membranes sensitive to neurohypophyseal hormones. J. biol. Chem. 249, 7848–7856 (1974a).
Birnbaumer, L., Yang, P.C.: Studies on receptor-mediated activation of adenylyl cyclases. III. Regulation by purine nucleotides of the activation of adenylyl cyclases from target organs for prostaglandins, luteinizing hormone, neurohypophyseal hormones and catecholamines. Tissue and hormone-dependent variations. J. biol. Chem. 249, 7867–7873 (1974b).
Birnbaumer, L., Nakahara, T., Yang, P.C.: Studies on receptor-mediated activation of adenylyl cyclases. II. Nucleotide and nucleoside regulation of the activities of the beef renal medullary adenylyl cyclase and their stimulation by neurohypophyseal hormones. J. biol. Chem. 249 7857–7866 (1974).
Bitensky, M.W., Gorman, R.E., Miller, W.H.: Adenyl cyclase as a link between photon capture and changes in membrane permeability of frog photoreceptors. Proc. nat. Acad. Sci. (Wash) 68, 561–562 (1971).
Bitensky, M.W., Miki, N., Marcus, F.R., Keirns, J.J.: The role of cyclic nucleotides in visual excitation. Life Sci. 13, 1451–1472 (1973).
Björklund, A., Cegrell, L., Falck, B., Ritzen, M., Rosengren, E.: Dopamine-containing cells in sympathetic ganglia. Acta physiol. scand. 78, 334–338 (1970).
Björklund, A., Katzman, R., Stenevi, U., West, K.: Development and growth of axonal sprouts from NA and 5-hydroxytryptamine neurons in rat spinal cord. Brain Res. 31, 21–33 (1971).
Black, A.C., Bhalla, R.C., Williams, T.H.: Species differences in the adenyl cyclase responsiveness to neurotransmitters in the superior cervical ganglion. Abstr. 4th Annu. Meeting Soc. Neurosci St. Louis, p. 144 (1974).
Blecher, M., Hunt, N.H.: Enzymatic deacylation of mono- and dibutyryl derivatives of cyclic adenosine 3′,5′-monophosphate by extracts of rat tissues. J. biol. Chem. 247, 7479–7484 (1972).
Bloom, F.E.: Electrophysiological pharmacology of single nerve cells. In: Psychopharmacology — A Ten Year Progress Report. Washington, D.C.: U.S. Govt. Printing Office 1968.
Bloom, F.E.: Fine structural changes in rat brain after intracisternal injection of 6-hydroxydopamine. In: 6-Hydroxydopamine and Catecholamine Neurons. Amsterdam: North Holland Publishing Co. 1971.
Bloom, F.E.: Amino acids and polypeptides in neuronal function. Neurosci. Res. Program Bull 10, 122–251 (1972).
Bloom, F.E.: Ultrastructural identification of catecholamine-containing central synaptic terminals. J. Histochem. Cytochem. 21, 333–348 (1973a).
Bloom, F.E.: Dynamic synaptic communication: finding the vocabulary. Brain Res. 62, 299–305 (1973b).
Bloom, F.E.: To spritz or not to spritz: the doubtful value of aimless iontophoresis. Life Sci. 14, 1819–1834 (1974).
Bloom, F.E., Costa, E., Salmoiraghi, G.C.: Anesthesia and the responsiveness of individual neurons of the cat’s caudate nucleus to acetylcholine, norepinephrine, and dopamine administered by microelectrophoresis. J. Pharmacol. 150, 244–255 (1965).
Bloom, F.E., Hoffer, B.J.: Norepinephrine as a central synaptic transmitter. In: Frontiers in Catecholamine Research. New York: Pergamon Press 1973.
Bloom, F.E., Hoffer, B.J., Battenberg, E.F., Siggins, G.R., Steiner, A.L., Parker, C.W., Wedner, H.J.: Adenosine 3′,5′-monophosphate is localized in cerebellar neurons: Immunofluorescence evidence. Science 177, 436–438 (1972).
Bloom, F.E., Hoffer, B.J., Siggins, G.R.: Studies on norepinephrine containing afferents to Purkinje cells of rat cerebellum. I. Localization of the fibers and their synapses. Brain Res. 25, 501–521 (1971).
Bloom, F.E., Hoffer, B.J., Siggins, G.R.: Norepinephrine mediated synapses. A model system for neuropsychopharmacology. Biol. Psychiat. 4, 157–177 (1972).
Bloom, F.E., Krebs, H., Nicholson, J., Pickel, V.: The noradrenergic innervation of cerebellar Purkinje cells: Localization, function, synaptogenesis, and axonal sprouting of locus coeruleus. In: Dynamics of Degeneration and Growth in Neurons. England: Pergamon Press 1974b.
Bloom, F.E., Siggins, G.R., Hoffer, B.J.: Interpreting the failures to confirm the depression of cerebellar Purkinje cells by cyclic AMP. Science 185, 627–629 (1974a).
Bloom, F.E., Siggins, G.R., Hoffer, B.J., Segal, M., Oliver, A.P.: The role of cyclic nucleotides in the central synaptic actions of catecholamines. In: Advances in Cyclic Nucleotide Research, vol. 5. New York: Raven Press 1975.
Bloom, S., Sweat, F.W.: Covariance of myocardial cyclic AMP and calcium during β-adrenergic stimulation in vivo. Res. Commun. Chem. Pathol. Pharmacol. 8, 505–514 (1974).
Blumberg, J.B., Sulser, F.: The effect of antipsychotic drugs on the cyclic 3′,5′ adenosine monophosphate system on rat forebrain. Fed. Proc. 33, 286 (1974).
Booth, D.A.: Unlearned and learned effects of intrahypothalamic cyclic AMP injection on feeding. Nature (Lond.) New Biol. 237, 222–224 (1972).
Borasio, P.G., Vassalle, M.: Dibutyryl cyclic AMP and potassium transport in cardiac Purkinje fibers. Amer. J. Physiol. 226, 1232–1237 (1974).
Borgeat, P., Chavancy, G., Dupont, A., Labrie, F., Arimura, A., Schally, A.V.: Stimulation of adenosine 3′,5′-cyclic monophosphate accumulation in anterior pituitary gland in vitro by synthetic luteinizing hormone-releasing hormone. Proc. nat. Acad. Sci. (Wash.) 69, 2677–2681 (1972).
Bradshaw, C.M., Szabadi, E., Roberts, M.H.T.: The reflection of ejecting and retaining currents in the time course of neuronal responses to microelectrophoretically applied drugs. J. Pharm. Pharmacol. 25, 513–520 (1973).
Bray, J.J., Kon, C.M., Breckenridge, B.M.: Adenyl cyclase cyclic nucleotide phosphodiesterase and axoplasmic flow. Brain Res. 26, 385–394 (1971).
Brazeau, P., Vale, W., Burgus, R., Ling, N., Butcher, M., Riuier, J., Guillemin, R.: Hypothalamic polypeptide that inhibits the secretion of immuno-reactive pituitary growth hormone. Science 179, 77–79 (1973).
Breckenridge, B.M.: The measurement of cyclic adenylate in tissues. Proc. nat. Acad. Sci. (Wash.) 57, 1580–1586 (1964).
Breckenridge, B.M., Burn, J.H., Matschinsky, F.M.: Theophylline, epinephrine, and neostigmine facilitation of neuromuscular transmission. Proc. nat. Acad. Sci. (Wash.) 57, 1893–1897 (1967).
Breckenridge, B.M., Johnston, R.E.: Cyclic 3′,5′-nucleotide phosphodiesterase in brain. J. Histochem. Cytochem. 17, 505–511 (1969).
Breckenridge, B.M., Lisk, R.D.: Cyclic adenylate and hypothalamic regulatory functions. Proc. Soc. exp. Biol. (N.Y.) 131, 934–935 (1969).
Brooker, G.: Oscillation of cyclic adenosine monophosphate concentration during the myocardial contraction cycle. Science 182, 933–934 (1973).
Broström, C.O., Huang, Y-C., Breckenridge, B. McL., Wolff, D.J.: Identification of a calciumbinding protein as a calcium-dependent regulation of brain adenylate cyclase. Proc. nat. Acad. Sci. (Wash.) 72, 64–68 (1975).
Brown, J.H., Makman, M.H.: Stimulation by dopamine of adenylate cyclase in retinal homogenates and of adenosine-3′,5′-cyclic monophosphate formation in intact retina. Proc. nat. Acad. Sci. (Wash.) 69, 539–543 (1972).
Brown, J.H., Makman, M.H.: Influence of neuroleptic drugs and apomorphine on dopamine sensitive adenylate cyclase of retina. J. Neurochem. 21, 477–479 (1973).
Brunton, W.J.: Beta-adrenergic stimulation of transmembrane potential and short circuit current of isolated rabbit oviduct. Nature (Lond.) New Biol. 236, 12–14 (1972).
Bülbring, E., Tomita, T.: Increase of membrane conductance by adrenaline in the smooth muscle of guinea-pig taenia coli. Proc. roy. Soc. B 172, 89–102 (1969).
Bunney, B.S., Aghajanian, G.K.: Electrophysiological effects of amphetamine in dopaminergic neurons. In: Frontiers in Catecholamine Research. New York: Pergamon Press 1973.
Burgus, R., Guillemin, R.: Hypothalamic releasing factors. Ann. Rev. Biochem. 39, 490–526 (1970).
Burnstock, G.: Purinergic nerves. Pharmacol. Rev. 24, 509–581 (1972).
Carlsoo, B., Danielsson, A., Marklund, S., Stigbrand, T.: Effects of 3′,5′-cyclic adenosine monophosphate, 5-hydroxytryptamine, noradrenaline and theophylline on the simultaneous release of peroxidase and amylase from the guinea pig submandibular gland. Acta physiol. scand. 91 203–210 (1974).
Carnegie, P.R., Kemp, B.E., Dunkley, P.R., Murray, A.W.: Phosphorylation of myelin basic protein by an adenosine 3′,5′-cyclic monophosphate-dependent protein kinase. Biochem. J. 135, 569–572 (1973).
Carpenter, D.O., Gaubatz, G.L.: Octopamine receptors on Aplysia neurones mediate hyperpolarization by increasing membrane conductance. Nature (Lond.) 252, 483–485 (1974).
Casnellie, J.E., Greengard, P.: Guanosine 3′:5′-cyclic monophosphate-dependent phosphorylation of endogenous substrate proteins in membranes of mammalian smooth muscle. Proc. nat Acad Sci. (Wash.) 71, 1891–1895 (1974).
Cedar, H., Kandel, E.R., Schwartz, J.H.: Cyclic adenosine monophosphate in the nervous system of aplysia californica. I. Increased synthesis in response to synaptic stimulation. J. gen. Physiol 60, 558–569 (1972).
Cedar, H., Schwartz, J.H.: Cyclic adenosine monophosphate in the nervous system of aplysia californica: II. Effect of serotonin and dopamine. J. gen. Physiol. 60, 570–587 (1972).
Chalazonitis, A., Greene, L.A.: Enhancement in excitability properties of mouse neuroblastoma cells cultured in the presence of dibutyryl cyclic AMP. Brain Res. 72, 340–345 (1974).
Chasin, M., Mamrak, F., Samaniego, S.G.: Preparation and properties of a cell-free, hormonally responsive adenylate cyclase from guinea pig brain. J. Neurochem. 22, 1031–1038 (1974).
Chasin, M., Mamrak, F., Samaniego, S.G., Hess, S.M.: Characteristics of the catecholamine and histamine receptor sites mediating accumulation of cyclic adenosine 3′,5′-monophosphate in guinea pig brain. J. Neurochem. 21, 1415–1427 (1973).
Chasin, M., Rivkin, I., Mamrak, F., Samaniego, G., Hess, S.M.: α- and β-adrenergic receptors as mediators of accumulation of cyclic adenosine 3′,5′-monophosphate in specific areas of guinea pig brain. J. biol. Chem. 246, 3037–3041 (1971).
Chatzkel, S., Zimmerman, I., Berg, A.: Modulation of cyclic AMP synthesis in the cat superior cervical ganglion by short term presynaptic stimulation. Brain Res. 80, 523–526 (1974).
Cheung, W.Y.: Properties of cyclic 3′,5′-nucleotide phosphodiesterase from rat brain Biochemistry (Wash.) 6, 1079–1087 (1970).
Chiarandini, D.J., Bentley, P.J.: The effects of verapamil on metabolism and contractility of the toad skeletal muscle. J. Pharmacol. exp. Ther. 186, 52–59 (1973).
Chou, W.S., Ho, A.K.S., Loh, H.H.: Neurohormones on brain adenyl cyclase activity in vivo. Nature (Lond.) New Biol. 233, 280–281 (1971).
Chu, N-S., Bloom, F.E.: Norepinephrine-containing neurons: changes in spontaneous discharge patterns during unrestrained sleeping and waking. Science 179, 908–910 (1973).
Chu, N-S., Bloom, F.E.: The catecholamine-containing neurons in the cat dorso-lateral pontine tegmentum: distribution of the cell bodies and some axonal projections. Brain Res 66 1–21 (1974a).
Chu, N-S., Bloom, F.E.: Activity patterns of catecholamine-containing pontine neurons in the dorsolateral tegmentum of unrestrained cats. J. Neurobiol. 5, 527–544 (1974b).
Huang, D-M., Costa, E.: Biosynthesis of tyrosine hydroxylase in rat adrenal medulla after exposure to cold. Proc. nat. Acad. Sci. (Wash.) 71, 4570–4574 (1974).
Clark, R.B., Gross, R., Su, Y-F., Perkins, J.P.: Regulation of adenosine 3′,5′-monophosphate content in human astrocytoma cells by adenosine and adenine nucleotides. J. biol. Chem. 249, 5296–5303 (1974).
Clark, R.B., Perkins, J.P.: Regulation of adenosine 3′,5′-monophosphate concentration in cultured human astrocytoma cells by catecholamines and histamine. Proc. nat. Acad. Sci. (Wash.) 68, 2757–2760 (1971).
Clark, W.G., Cumby, H.R., Davis, H.E.: The hyperthermic effect of intracerebroventricular cholera enterotoxin in the unanesthetized cat. J. Physiol. (Lond.) 240, 493–504 (1974).
Clarke, G., Hill, R.G., Simmonds, M.A.: Microiontophoretic release of drugs from micropipettes: use of 24Na as a model. Brit. J. Pharmacol. 48, 156–161 (1973).
Clement-Cormier, Y.C., Kebabian, J.W., Petzold, G.I., Greengard, P.: Dopamine-sensitive adenylate cyclase in mammalian brain: a possible site of action of antipsychotic drugs. Proc. nat. Acad. Sci. (Wash.) 71, 1113–1171 (1974).
Cohn, M.L., Cohn, M., Taylor, F.H.: Norepinephrine — an antagonist of dibutyryl cyclic AMP in the regulation of narcosis in the rat. Res. Commun. Chem. Pathol. Pharmacol. 7, 687–699 (1974).
Connor, J.D.: Caudate nucleus neurones: correlation of the effects of substantia nigra stimulation with iontophoretic dopamine. J. Physiol. (Lond.) 208, 691–703 (1970).
Contreras, E., Castillo, S., Quijada, L.: Effect of drugs that modify 3′,5′-AMP concentrations on morphine analgesia. J. Pharm. Pharmacol. 24, 65–66 (1972).
Corrodi, H., Fuxe, K., Jonsson, G.: Effects of caffeine on central monoamine neurons. J. Pharm. Pharmacol. 24, 155–158 (1972).
Costa, E., Guidotti, A., Hanbauer, I.: Do cyclic nucleotides promote the trans-synaptic induction of tyrosine hydroxylase. Life Sci. 14, 1169–1188 (1974).
Couteaux, R.: Localization of cholinesterases at neuromuscular junctions. Int. Rev. Cytol. 4, 335–375 (1955).
Crain, S.M., Pollack, E.D.: Restorative effects of cyclic AMP on complex bioelectric activities of cultured fetal rodent CNS tissues after acute Ca++ deprivation. J. Neurobiol. 4, 321–342 (1973).
Cramer, H., Johnson, D.G., Hanbauer, L, Silberstein, S.D., Kopin, I.J.: Accumulation of adenosine 3′,5′-monophosphate induced by catecholamines in the rat superior cervical ganglion In Vitro. Brain Res. 53, 97–104 (1973).
Cramer, H., Ng, L.K.Y., Chase, T.N.: Effect of probenecid on levels of cyclic AMP in human cerebro-spinal fluid. J. Neurochem. 19, 1601–1602 (1972).
Cuatrecasas, P.: Interaction of vibrio cholerae enterotoxin with cell membranes. Biochemistry 12, 3547–3581 (1973).
Cuatrecasas, P.: Membrane receptors. Ann. Rev. Biochem. 45, 169–214 (1974).
Cuatrecasas, P.: Hormone receptors — their function in cell membranes and some problems related to methodology. In: Advances in Cyclic Nucleotide Research, vol. 5. New York: Raven Press 1975.
Curtis, D.R.: Microelectrophoresis. In: Physical Techniques in Biological Research, vol. 5. New York: Academic Press 1964.
Curtis, D.R., Johnston, G.A.R.: Amino acid transmitters in the mammalian central nervous system. Ergebn. Physiol. 69, 97–188 (1974).
Dale, H.H., Feldberg, W., Vogt, M.: Release of acetylcholine at voluntary motor nerve endings. J. Physiol. (Lond.) 86, 353–380 (1936).
Dalton, C., Crowley, H.J., Sheppard, H., Schallek, W.: Regional cyclic nucleotide phosphodiesterase activity in cat central nervous system: effects of benzodiazepines. Proc. Soc. exp. Biol. (N.Y.) 145, 407–410 (1974).
Daly, J.: The role of cyclic nucleotides in the nervous system. In: Handbook of Psychopharmacology. New York: Plenum Press 1975.
Daly, J.W., Huang, M., Shimizu, H.: Regulation of cyclic AMP levels in brain tissue. In: Advances in Cyclic Nucleotide Research, vol. 1. New York: Raven Press 1972.
Dambach, G., Friedmann, N.: Substrate-induced membrane potential changes in the perfused rat liver. Biochim. biophys. Acta (Amst.) 367, 366–370 (1974).
Davidoff, R.A.: Gamma amino butyric acid antagonism and presynaptic inhibition in the frog spinal cord. Science 175, 331–333 (1972).
Deguchi, T., Axelrod, J.: Superinduction of serotonin N-acetyl-transferase and supersensitivity of adenyl cyclase to catecholamines in denervated pineal gland. Molec. Pharmacol. 9, 612–618 (1973).
Delcastillo, J., Katz, B.: A comparison of acetylcholine and stable depolarizing agents. Proc. roy. Soc. B 146, 362–368 (1957).
Dhalla, N.S., Sulakhe, P.V., McNamara, D.B.: Studies on the relationship between adenylate cyclase activity and calcium transport by cardiac sarcotubular membranes. Biochim. biophys. Acta (Amst.) 323, 276–284 (1973).
Diamond, J.: Phosphorylase, calcium, and cyclic AMP in smooth-muscle contraction. Amer. J. Physiol. 225, 930–737 (1973).
Dousa, T., Hechter, O.: Lithium and brain adenyl cyclase. Lancet 1970I, 834–835.
Drummond, G.I., Powell, C.A.: Analogues of adenosine 3′,5′-cyclic phosphate as activators of Phosphorylase b kinase and as substrates for cyclic 3′,5′-nucleotide phosphodiesterase. Molec. Pharmacol. 6, 24–30 (1970).
Dun, N., Nishi, S.: Effects of dopamine on the superior cervical ganglion on the rabbit. J. Physiol. (Lond.) 239, 155–164 (1974).
Ebstein, B., Roberge, C., Tabachnik, J., Goldstein, M.: The effect of dopamine and of apomorphine and dB-cAMP-induced stimulation of synaptosomal tyrosine hydroxylase. J. Pharm. Pharmacol 26, 975–977 (1974).
Eccles, J.C.: The Physiology of Synapses. New York: Academic Press 1964.
Eccles, R., Libet, B.: Origin and blockade of the synaptic responses of curarized sympathetic ganglia. J. Physiol. (Lond.) 157, 484 (1961).
Edström, A., Kanje, M., Walum, E.: Effects of dibutyryl cyclic AMP and prostaglandin E1 on cultured human glioma cells. Exp. Cell Res. 85, 217–223 (1974).
Eipper, B.A.: Rat brain tubulin and protein kinase activity. J. biol. Chem. 249, 1398–1406 (1974).
Engberg, I., Flatman, J.A., Kadzlelawa, K.: The hyperpolarisation of motoneurones by electrophoretically applied amines and other agents. Acta physiol. scand. 91, 3A–4A (1974).
Engberg, I., Marshall, K.C.: Mechanism of Noradrenaline hyperpolarization in spinal cord motoneurones of the cat. Acta physiol. scand. 83, 142–144 (1971).
Erankö, O., Harkonen, M.: Monoamine-containing small cells in the superior cervical ganglion of the rat and one organ composed of them. Acta physiol. scand. 63, 511–512 (1965).
Fallon, E.F., Agrawal, R., Furth, E., Steiner, A.L., Cowden, R.: Cyclic guanosine and adenosine 3′,5′-monophosphates in canine thyroid: localization by immunofluorescence. Science 184 1089–1091 (1974).
Fatt, P., Katz, B.: An analysis of the endplate potential recorded with an intracellular electrode J. Physiol. (Lond.) 115, 320–370 (1951).
Ferrendelli, J.A., Chang, M.M., Kinscherf, D.A.: Elevation of cyclic GMP levels in central nervous system by excitatory and inhibitory amino acids. J. Neurochem. 22, 535–540 (1974).
Ferrendelli, J.A., Kinscherf, D.A., Chang, M.M.: Regulation of levels of guanosine cyclic 3′,5′-monophosphate in the central nervous system: effects of depolarizing agents. Molec. Pharmacol 9, 445–454 (1973).
Ferrendelli, J.A., Kinscherf, D.A., Kipnis, D.M.: Effects of amphetamine, chlorpromazine and reserpine on cyclic GMP and cyclic AMP levels in mouse cerebellum. Biochem. biophys Res Commun. 46, 2114–2120 (1972).
Ferrendelli, J.A., Steiner, A.L., McDougal, D.B., Kipnis, D.M.: The effect of oxotremorine and atropine on cGMP and cAMP levels in mouse cerebral cortex and cerebellum. Biochem biophys. Res. Commun. 41, 1061–1067 (1970).
Field, M.: Mode of action of cholera toxin: stabilization of catecholamine-sensitive adenylate cyclase in turkey erythrocytes. Proc. nat. Acad. Sci. (Wash.) 71, 3299–3303 (1974).
Fikus, M., Kwast-Welfeld, J., Kazi-Mierczuk, Z., Shugar, D.: Biochemical studies on some new analogues of adenosine-3′,5′-cyclic phosphate including isoguanosine-3′,5′-cyclic phosphate Acta biochim. pol. 21, 465–474 (1974).
Filler, R., Litwack, G.: Differences in macromolecular binding between cyclic AMP and its dibutyryl derivative in vitro. Biochem. biophys. Res. Commun. 52, 159–167 (1973).
Florendo, N.T., Barrnett, R.J., Greengard, P.: Cyclic 3′,5′-nucleotide phosphodiesterase: cytochemical localization in cerebral cortex. Science 173, 745–747 (1971).
Folbergrova, J.: Energy metabolism of mouse cerebral cortex during homocysteine convulsions. Brain Res. 81, 443–454 (1974).
Forn, J., Krishna, G.: Effects of biogenic amines on the rate of adenosine 3′,5′ monophosphate formation in brain slices of different animal species. Fed. Proc. 29, 480 (1970).
Forn, J., Krishna, G.: Effect of norepinephrine, histamine, and other drugs on cyclic 3′,5′-AMP formation in brain slices of various animal species. Pharmacology (Basel) 5, 193–204 (1971).
Forn, J., Krueger, B.K., Greengard, P.: Adenosine 3′,5′-monophosphate content in rat caudate nucleus. Demonstration of dopaminergic and adrenergic receptors. Science 186, 1118–1119 (1974).
Forn, J., Valdecasas, F.G.: Effects of lithium on brain adenyl cyclase activity. Biochem. Pharmacol. 20, 2773–2779 (1971).
Frederickson, R.C.A., Jordan, L.M., Phillis, J.W.: The action of noradrenaline on cortical neurons: effects of pH. Brain Res. 35, 556–560 (1971).
Frederickson, R.C.A., Jordan, L.M., Phillis, J.W.: A reappraisal of the actions of noradrenaline and 5-hydroxytryptamine on cerebral cortical neurons. Comp. Gen. Pharmacol. 3, 443–456 (1972).
Freedman, R., Hoffer, B.J.: Phenothiazine antagonism of the noradrenergic inhibition of cerebellar Purkinje neurons. J. Neurobiol. 6, 277–288 (1975).
Friedman, N., Somlyo, A.V., Somlyo, A.P.: Cyclic adenosine and guanosine monophosphate and glucagon: effect on liver membrane potentials. Science 171, 400–402 (1971).
Froehlich, J.E., Rachmeler, M.: Effect of adenosine 3′,5′-cyclic monophosphate on cell proliferation. J. Cell. Biol. 55, 19–31 (1972).
Fumagalli, R., Bernareggi, V., Berti, F., Trabucchi, M.: Cyclic AMP formation in human brain: an in vitro stimulation by neurotransmitters. Life Sci. 10, 1111–1115 (1971).
Fuxe, K., Hökfelt, T., Johansson, O., Jonsson, O., Lidbrink, P., Ljungdahl, A.: The origin of dopamine nerve terminals in limbic and frontal cortex. Evidence for meso-cortical dopamine neurons. Brain Res. 82, 349–355 (1974).
Fuxe, K., Jonsson, G.: The histochemical fluorescence method for the demonstration of catecholamines: Theory, practice and application. J. Histochem. Cytochem. 21, 293–311 (1973).
Fuxe, K., Olson, L., Zotterman, Y.: Dynamics of Degeneration and Growth in Neurons. Oxford and New York: Pergamon 1974b.
Fuxe, K., Ungerstedt, U.: Action of caffeine and theophylline on supersensitive dopamine receptors: considerable enhancement of receptor response to treatment with dopa and dopamine agonists. Med. biol. Ill. 52, 48–54 (1974).
Gabballah, S., Popoff, C.: Cyclic 3′,5′-nucleotide phosphodiesterase in nerve endings of developing rat brain. Brain Res. 25, 220–222 (1971).
Galindo, A., Krnjevic, K., Schwartz, S.: Microiontophoretic studies on neurones in the cuneate nucleus. J. Physiol. (Lond.) 158, 296–323 (1967).
Garbarg, M., Barbin, G., Feger, J., Schwartz, J-C.: Histaminergic pathway in rat brain evidenced by lesions of the medial forebrain bundle. Science 186, 833–834 (1974).
Gardner, D., Kandel, E.R.: Diphasic postsynaptic potential: a chemical synapse capable of mediating conjoint excitation and inhibition. Science 176, 675–677 (1972).
George, W.J., Polson, J.B., O’Toole, A.G., Goldberg, N.D.: Elevation of guanosine 3′,5′-cyclic phosphate in rat heart after perfusion with acetylcholine. Proc. nat. Acad. Sci. (Wash.) 66, 398–403 (1970).
Gergely, J.: Some aspects of the role of the sarcoplasmic reticulum and the tropomyosin-troponin system in the control of muscle contraction by calcium ions. Circulat. Res. 34 and 35 (Suppl. III) 74–82 (1974).
Gibson, D.A., Reichlin, S., Vernadakis, A.: 3H Uridine uptake and incorporation into RNA in the C-6 glial cells following dibutyryl cyclic AMP treatment. Brain Res. 81, 354–360 (1974).
Gilman, A.G.: The regulation of cyclic AMP metabolism in cultured cells of the nervous system. In: Advances in Cyclic Nucleotide Research, vol. 1. New York: Raven Press 1972x.
Gilman, A.G., Nirenberg, M.: Effect of catecholamines on the adenosine 3′,5′-cyclic concentrations of clonal satellite cells of neurons. Proc. nat. Acad. Sci. (Wash.) 68, 2165–2168 (1971a).
Gilman, A.G., Nirenberg, M.: Regulation of adenosine 3′,5′-monophosphate metabolism in cultured neuroblastoma cells. Nature (Lond.) 234, 356–358 (1971 b).
Gilman, A.G., Schrier, B.K.: Adenosine cyclic 3′,5′-monophosphate in fetal rat brain cell cultures. Molec. Pharmacol. 8, 410–416 (1972).
Ginsborg, B.L.: Ion movements in junctional transmission. Pharmacol. Rev. 19, 289–316 (1967).
Godfraind, J.M., Pumain, R.: Cyclic adenosine monophosphate and norepinephrine: effect on Purkinje cells in rat cerebellar cortex. Science 174, 1257 (1971).
Goldberg, A.L., Singer, J.J.: Evidence for a role of cyclic AMP in neuromuscular transmission. Proc. nat. Acad. Sci. (Wash.) 64, 134–141 (1969).
Goldberg, N.D.: The Yin Yang hypothesis of biological control: opposing influences of cyclic GMP and cyclic AMP in bidirectionally regulated systems. In: Advances in Cyclic Nucleotide Research, vol. 5. New York: Raven Press (in press).
Goldberg, N.D., Dietz, S.B., O’Toole, A.G.: Cyclic guanosine 3′,5′-monophosphate in mammalian tissues and urine. J. biol. Chem. 244, 4458–4466 (1969).
Goldberg, N.D., Haddox, M.K., Hartle, D.K., Hadden, J.W.: The biological role of cyclic 3′,5′-guanosine monophosphate. In: Cellular Mechanisms. Basel: S. Karger 1973 a.
Goldberg, N.D., Lust, W.D., O’Dea, R.F., Wei, S., O’Toole, A.G.: A role of cyclic nucleotides in brain metabolism. Advanc. Biochem. Psychopharmacol. 3, 67–87 (1970).
Goldberg, N.D., O’Dea, R.F., Haddox, M.K.: Cyclic GMP. In: Advances in Cyclic Nucleotide Research, vol. 3. New York: Raven Press 1973b.
Goldberg, N.D., O’Toole, A.G.: The properties of glycogen synthetase and regulation of glycogen biosynthesis in rat brain. J. biol. Chem. 244, 3053–3061 (1969).
Goldstein, M., Anagnoste, B., Shirron, C.: The effect of trivastal, haloperidol, and dibutyryl cyclic AMP on (14C) dopamine synthesis in rat striatum. J. Pharm. Pharmacol. 25, 348–351 (1973).
Goodman, D.B.P., Rasmussen, H., Dibella, F., Gothrow, C.E.: Cyclic adenosine 3′:5′-monophosphate-stimulated phosphorylation of isolated neurotubule subunits. Proc. nat. Acad. Sci. (Wash.) 67, 652–659 (1970).
Goodman, F.R., Weiss, G.B.: Dissociation by lanthanum of smooth muscle responses to potassium and acetylcholine. Amer. J. Physiol. 220, 759–766 (1971).
Greengard, P., Kebabian, J.W.: Role of cyclic AMP in synaptic transmission in the mammalian peripheral nervous system. Fed. Proc. 33, 1059–1068 (1974).
Greengard, P., Kebabian, J.W., McAfee, D.A.: Studies on the role of cyclic AMP in neural function. In: Cellular Mechanisms. Basel: S. Karger 1973.
Guidotti, A., Cheney, D.L., Trabucchi, M., Doteuchi, M., Wang, C.: Focussed microwave radiation: a technique to minimize post-mortem changes of cyclic nucleotides, DOPA and choline and to preserve brain morphology. Neuropharmacology 13, 1115–1122 (1974).
Guidotti, A., Costa, E.: Involvement of adenosine 3′,5′-monophosphate in the activation of tyrosine hydroxylase elicited by drugs. Science 179, 902–904 (1973).
Guidotti, A., Costa, E.: A role for nicotinic receptors in the regulation of the adenylate cyclase of adrenal medulla. J. Pharmacol. exp. Ther. 189, 665–675 (1974).
Guidotti, A., Kurosawa, A., Chuang, D.M., Costa, E.: Protein kinase activation as an early event in the trans-synaptic induction of tyrosine-3-mono-oxygenase in adrenal medulla. Proc. nat. Acad. Sci. (Wash.) (in press).
Guidotti, A., Zivkovic, B., Pfeiffer, R., Costa, E.: Involvement of 3′,5′-cyclic adenosine monophos phate in the increase of tyrosine hydroxylase activity elicited by cold exposure. Naunyn-Schmiedeberg’s Arch. Pharmacol. 278, 195–206 (1973).
Gunaga, K.P., Menon, K.M.J.: Effect of catecholamines and ovarian hormones on cyclic AMP accumulation in rat hypothalamus. Biochem. biophys. Res. Commun. 54, 440–448 (1973).
Hamprecht, B., Schultz, J.: Stimulation by prostaglandin E1 of adenosine 3′,5′-cyclic monophosphate formation in neuroblastoma cells in the presence of phosphodiesterase inhibitors. FEBS Letters 34, 85–89 (1973).
Hanna, P.E., O’Dea, R.F., Goldberg, N.D.: Phosphodiesterase inhibition by papaverine and structurally related compounds. Biochem. Pharmacol. 21, 2266–2268 (1972).
Hardman, J.G., Sutherland, E.W.: Guanyl cyclase, an enzyme catalyzing the formation of guanosine 3′,5′-monophosphate from guanosine triphosphate. J. biol. Chem. 244, 6363–6370 (1969).
Harris, J.E., Morgenroth, V.H., Roth, R.H., Baldessarini, R.J.: Regulation of catecholamine synthesis in the rat brain in vitro by cyclic AMP. Nature (Lond.) 252, 156–158 (1974).
Hax, W.M.A., Van Venrooij, G.E.P.M., Vossenberg, J.B.J.: Cell communication: a cyclic AMP mediated phenomenon. J. Membrane Biol. 19, 253–266 (1974).
Hayaishi, O., Greengard, P., Colowick, S.B.: On the equilibrium of the adenylate cyclase reaction. J. biol. Chem. 246, 5840–5843 (1971).
Haylett, D.G., Jenkinson, D.H.: Effects of noradrenaline on the membrane potential and ionic permeability of parenchymal cells in the liver of the guinea-pig. Nature (Lond.) 224, 80–81 (1969).
Heisler, S., Fast, D., Tenenhouse, A.: Role of Ca2+ and cyclic AMP in protein secretion from rat exocrine pancreas. Biochim. biophys. Acta (Amst.) 279, 561–572 (1972).
Herman, Z.S.: Behavioral effects of dibutyryl cyclic 3′,5′ AMP, noradrenaline and cyclic 3′,5′ AMP in rats. Neuropharmacology 12, 705–709 (1973).
Hidaka, T., Kuriyama, H.: Effects of catecholamines on the cholinergic neuromuscular transmission in fish red muscle. J. Physiol. (Lond.) 201, 61–71 (1969).
Hill, R.G., Simmonds, M.A.: A method for comparing the potencies of γ-aminobutyric acid antagonists on single cortical neurones using microiontophoretic techniques. Brit. J. Pharmacol. 48, 1–11 (1973).
Ho, I.K., Loh, H.H., Way, E.L.: Cyclic adenosine monophosphate antagonism of morphine analgesia. J. Pharmacol. exp. Ther. 185, 336–346 (1973 a).
Ho, I.K., Loh, H.H., Way, E.L.: Effects of cyclic 3′,5′-adenosine monophosphate on morphine tolerance and physical dependence. J. Pharmacol. exp. Ther. 185, 347–357 (1973 b).
Hökfelt, T., Ungerstedt, U.: Specificity of 6-hydroxydopamine induced degeneration of central monoamine neurons: electron and fluorescence microscopic study with special reference to intracerebral injection of the nigro striatal dopamine system. Brain Res. 60, 269–298 (1973).
Hoffer, B.J., Siggins, G.R., Bloom, F.E.: Prostaglandins E1 and E2 antagonize norepinephrine effects on cerebellar Purkinje cells: Microelectrophoretic study. Science 166, 1418–1420 (1969).
Hoffer, B.J., Siggins, G.R., Bloom, F.E.: Studies on norepinephrine-containing afferents to Purkinje cells of rat cerebellum. II. Sensitivity of Purkinje cells to norepinephrine and related substances administered by microiontophoresis. Brain Res. 25, 523–534 (1971 a).
Hoffer, B.J., Siggins, G.R., Oliver, A.P., Bloom, F.E.: Cyclic AMP mediation of norepinephrine inhibition in rat cerebellar cortex: A unique class of synaptic responses. Ann. N.Y. Acad. Sci. 185, 531–549 (1971b).
Hoffer, B.J., Siggins, G.R., Oliver, A.P., Bloom, F.E.: Cyclic adenosine monophosphate mediated adrenergic synapses to cerebellar Purkinje cells. In: Advances in Cyclic Nucleotide Research, vol. 1, 411–423 (1972).
Hoffer, B.J., Siggins, G.R., Oliver, A.P., Bloom, F.E.: Activation of the pathway from locus coeruleus to rat cerebellar Purkinje neurons: pharmacological evidence of noradrenergic central inhibition. J. Pharmacol. exp. Ther. 184, 553–569 (1973).
Hoffer, B.J., Siggins, G.R., Woodward, D.J., Bloom, F.E.: Spontaneous discharge of Purkinje neurons after destruction of catecholamine-containing afferents by 6-hydroxydopamine. Brain Res. 30, 425–430(1971).
Hofmann, F., Sold, G.: A protein kinase activity from rat cerebellum stimulated by guanosine 3′,5′-monophosphate. Biochem. biophys. Res. Commun. 49, 1100–1107(1972).
Honda, F., Imamura, H.: Inhibition of cyclic 3′,5′-nucleotide phosphodiesterase by phenothiazine and reserpine derivatives. Biochim. biophys. Acta (Amst.) 161, 267–269 (1968).
Horowitz, J.M., Horwitz, B.A., Smith, R.E.: Effect in vivo of norepinephrine on the membrane resistance of brown fat cells. Experientia (Basel) 27, 1419 (1971).
Horwitz, B.A., Horowitz, J.M., Smith, R.E.: Norepinephrine-induced depolarization of brown fat cells. Proc. nat. Acad. Sci. (Wash.) 64, 113–120 (1969).
Howell, S.L., Whitfield, M.: Localization of adenyl cyclase in islet cells. J. Histochem. Cytochem. 20, 873 (1972).
Huang, M., Gruenstein, E., Daly, J.W.: Depolarizing-evoked accumulation of cyclic AMP in brain slices: inhibition by exogenous adenosine deaminase. Biochim. biophys. Acta (Amst.) 329, 147–151 (1973a).
Huang, M., Ho, A.K.S., Daly, J.W.: Accumulation of adenosine cyclic 3′,5′-monophosphate in rat cerebral cortical slices. Stimulatory effects of alpha and beta adrenergic agents after treatment with 6-hydroxydopamine, 2,3,5-trihydroxyphenethylamine and dehydroxytryptamines. Molec. Pharmacol. 9, 711–717 (1973 b).
Huang, M., Shimizu, H., Daly, J.: Regulation of adenosine cyclic 3′,5′-phosphate formation in cerebral cortical slices. Interaction among norepinephrine, histamine, serotonin. Molec. Pharmacol. 7, 155–162 (1971).
Huxley, A.F.: Muscular contraction. J. Physiol. (Lond.) 243, 1–44 (1974).
Huxley, J.S.: Chemical regulation and the hormone concept. Biol. Rev. 10, 427–441 (1935).
Ito, Y., Kuriyama, H., Tashiro, N.: Effects of catecholamines on the neuromuscular junction of the somatic muscle of the earthworm pheretima communissima. J. exp. Biol. 54, 167–186 (1971).
Jacobowitz, D.: Catecholamine fluorescence studies of adrenergic neurons and chromaffin cells in sympathetic ganglia. Fed. Proc. 29, 1929–1944 (1970).
Janiec, W., Trzeciak, H., Herman, Z.: The influence of adrenaline and optical isomers of INPEA on the adenyl cyclase activity in main hemispheres of rats in vitro. Arch. int. Pharmacodyn 185, 254–258 (1970).
Jenkinson, D.H., Stamenovic, B.A., Whitaker, B.D.L.: The effect of noreadrenaline on the end-plate potential in twitch fibres of the frog. J. Physiol. (Lond.) 195, 743–754 (1968).
Johnson, E.M., Maeno, H., Greengard, P.: Phosphorylation of endogenous protein of rat brainby a cyclic adenosine 3′,5′-monophosphate dependent protein kinase. J. biol. Chem. 246, 7731–7739 (1971).
Johnson, E.M., Ueda, T., Maeno, H., Greengard, P.: Adenosine 3′,5′-monophosphate-dependent phosphorylation of a specific protein in synaptic membrane fractions from rat cerebrum. J. biol. Chem. 247, 5650–5652 (1972).
Jordan, L.M., Lake, N., Phillis, J.W.: Mechanism of noradrenaline depression of cortical neurones: a species comparison. Europ. J. Pharmacol. 20, 381–384 (1972).
Jouvet, M.: The role of monoamines and acetylcholine containing neurons in the regulation of the sleep-waking cycle. Ergebn. Physiol. 64, 168–307 (1972).
Kadlec, O., Masek, K., Seferna, I.: The effect of papaverine on 45Ca2+ uptake in partly depolarized taeni coli of the guinea-pig. J. Pharm. Pharmacol. 25, 914–916 (1973).
Kakiuchi, K.S., Marks, B.H.: Adrenergic effects on pineal cell membrane potential. Life Sci. 11, 285–291 (1972).
Kakiuchi, S.: Cyclic 3′,5′-nucleotide phosphodiesterase of rat brain and other tissues: regulation of activity by Ca2+ and the modulator protein. In: Cellular Mechanisms. Basel: S. Karger 1973.
Kakiuchi, S.: Ca2+ plus Mg2+-dependent phosphodiesterase and its modulator from various rat tissues. In: Advances in Cyclic Nucleotide Research, vol.5. New York: Raven Press (in press).
Kakiuchi, S., Rall, T.W.: Studies on adenosine 3′,5′-phosphate in rabbit cerebral cortex. Molec. Pharmacol. 4, 379–388 (1968a).
Kakiuchi, S., Rall, T.W.: The influence of chemical agents on the accumulation of adenosine 3′,5′-phosphate in slices of rabbit cerebellum. Molec. Pharmacol. 4, 367–378 (1968 b).
Kakiuchi, S., Rall, T.W., McIlwain, H.: The effect of electrical stimulation upon the accumulation of adenosine 3′,5′-phosphate in isolated cerebral tissue. J. Neurochem. 16, 485–491 (1969).
Kakiuchi, S., Yamazaki, R.: Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain. Studies on cyclic 3′,5′-nucleotide phosphodiesterase. Biochem. biophys. Res. Commun. 41, 1104–1110 (1970).
Kakiuchi, S., Yamazaki, R., Teshima, Y.: Cyclic 3′,5′-nucleotide phosphodiesterase. IV. Two enzymes with different properties from brain. Biochem. biophys. Res. Commun. 42, 968–974 (1971).
Kakiuchi, S., Yamazaki, R., Teshima, Y., Uenishi, K.: Regulation of nucleoside cyclic 3′,5′-monophosphate phosphodiesterase activity from rat brain by a modulator and Ca2+. Proc. nat. Acad. Sci. (Wash.) 70, 3526–3535 (1973).
Kakiuchi, S., Yamazaki, R., Teshima, Y., Uenishi, K., Miyamoto, E.: Multiple cyclic nucleotide phosphodiesterase activities from rat tissues and occurrence of a calcium-plus-magnesium-ion-dependent phosphodiesterase and its protein activator. Biochem. J. 146, 109–120 (1975).
Kalix, P., McAfee, D.A., Chorderet, M., Greengard, P.: Pharmacological analysis of synaptically mediated increase in cyclic AMP in rabbit superior cervical ganglion. J. Pharmacol. exp. Ther. 188, 676–687 (1974).
Kandel, E.R.: Dale’s principle and the functional specificity of neurons. In: Psychopharmacology — A Ten Year Progress Report. Washington, D.C.: U.S. Govt. Printing Office 1968.
Karobath, M., Leitich, H.: Antipsychotic drugs and dopamine-stimulated adenylate cyclase prepared from corpus striatum of rat brain. Proc. nat. Acad. Sci. (Wash.) 71, 2915–2918 (1974).
Katz, A.M., Tada, M., Repke, D.J., Iorio, J.M., Krichberger, M.A.: Adenylate cyclase: Its probable localization in sarcoplasmic reticulum as well as sarcolemma of the canine heart. J. Mol. Cell. Cardiol. 6, 73–78 (1974).
Katz, B.: Nerve, Muscle, and Synapse. New York: McGraw-Hill 1966.
Katz, S., Tenenhouse, A.: The relationship of adenyl cyclase to the activity of other ATP utilizing enzymes and phosphodiesterase in preparations of rat brain. Mechanism of stimulation of cyclic AMP accumulation by adrenaline, ouabain, and Mg++. Brit. J. Pharmacol. 48, 516–526 (1973).
Katzman, R., Björklund, A., Owman, C., Stenevi, U., West, K.: Evidence for regenerative axon sprouting of central catecholamine neurons in rat mesencephalon following electrolytic lesions. Brain Res. 25, 579–596 (1971).
Kauffman, F.E., Harkonen, M.H.A., Johnson, E.E.: Adenyl cyclase and phosphodiesterase activity in cerebral cortex of normal and undernourished neonatal rats. Life Sci. 11, 613–621 (1972).
Kaukel, E., Hilz, H.: Permeation of dibutyryl cAMP into hela cells and its conversion to monobutyryl cAMP. Biochem. biophys. Res. Commun. 46, 1011–1018 (1972).
Kebabian, J.W., Greengard, P.: Dopamine-sensitive adenyl cyclase: possible role in synaptic transmission. Science 174, 1346–1349 (1971).
Kebabian, J.W., Petzold, G.L., Greengard, P.: Dopamine-sensitive adenylate cyclase in caudate nucleus of rat brain and its similarities to the dopamine receptor. Proc. nat. Acad. Sci. (Wash.) 69, 2145–2150 (1972).
Keen, P., McLean, W.G.: Effect of dibutyryl-cyclic AMP and dexamethasone on noradrenaline synthesis in isolated superior cervical ganglia. J. Neurochem. 22, 5–10 (1974).
Kimura, H., Thomas, E., Murad, F.: Effects of decapitation, ether and pentobarbital on guanosine 3′-5′ phosphate and adenosine 3′,5′ phosphate levels in rat tissues. Biochim. biophys. Acta (Amst.) 343, 519–528 (1974).
Kirchberger, M.A., Tada, M., Katz, A.M.: Adenosine 3′,5′-monophosphate-dependent protein kinase-catalyzed phosphorylation reaction and its relationship to calcium transport in cardiac sarcoplasmic reticulum. J. biol. Chem. 249, 6166–6173 (1974).
Klainer, L.M., Chi, Y-M., Friedberg, S.L., Rall, T.W., Sutherland, E.: Adenyl cyclase. IV. The effects of neurohormones on the formation of adenosine 3′,5′ phosphate by preparations from brain and other tissues. J. biol. Chem. 237, 1239–1243 (1962).
Klawans, H.L., Moses, H., Beaulieu, D.M.: The influence of caffeine on d-amphetamine- and pomorphine-induced stereotyped behavior. Life Sci. 14, 1493–1500 (1974).
Klein, D.C., Yuwiler, A., Weller, J.L., Plotkin, S.: Postsynaptic adrenergic-cyclic AMP control f the serotonin content of cultured rat pineal glands. J. Neurochem. 21, 1261–1271 (1973).
Knull, H.R., Taylor, W.F., Wells, W.W.: Insulin effects on brain energy metabolism and the elated hexokinase distribution. J. biol. Chem. 249, 6930–6935 (1974).
Kodama, T., Matsuko, Y., Shimizu, H.: The cyclic AMP system of human brain. Brain Res. 50, 135–146 (1973).
Koelle, G.B., Friedenwald, J.S.: A histochemical method for localizing Cholinesterase activity. Proc. Soc. exp. Biol. (N.Y.) 70, 617–622 (1949).
Krishna, G., Ditzion, B.R., Gessa, G.L.: Intense ergotrophic stimulation induced by intracerebral injection of dibutyryl cyclic 3′-5′ AMP. Proc. Int. Union Physiol. Sci., Washington, D.C. 1, 247 (1968).
Krishna, G., Moskowitz, J., Dempsey, P., Brodie, B.B.: The effect of norepinephrine and insulin on brown fat cell membrane potentials. Life Sci. 9, 1353–1361 (1970).
Krnjevic, K., Dumain, R., Renaud, L.: The mechanism of excitation by acetylcholine in the cerebral cortex. J. Physiol. (Lond.) 215, 247–268 (1971).
Kroeger, E.A., Marshall, J.M.: Beta-adrenergic effects on rat myometrium: mechanisms of membrane hyperpolarization. Amer. J. Physiol. 225, 1339–1345 (1973).
Kuba, K.: Effects of catecholamines on the neuromuscular junction in the rat diaphragm. J. Physiol. (Lond.) 211, 551–570 (1970).
Kuba, K., Koketsu, K.: Ionic mechanism of the slow excitatory postsynaptic potential in bullfrog sympathetic ganglion cells. Brain Res. 81, 338–342 (1974).
Kuba, K., Tomita, T.: Noradrenaline action on nerve terminal in the rat diaphragm. J. Physiol. (Lond.) 217, 19–31 (1971).
Kuffler, S.W.: Transmitter mechanism at the nerve-muscle junction. Arch. Sci. physiol. 3, 585–601 (1949).
Kuo, J.F.: Guanosine 3′:5′-monophosphate-dependent protein kinases in mammalian tissues. Proc. nat. Acad. Sci. (Wash.) 71, 4037–4041 (1974).
Kuo, J.F., Greengard, P.: Cyclic nucleotide-dependent protein kinases. IV. Widespread occurrence of adenosine 3′,5′-monophosphate dependent protein kinase in various tissues and phyla of the animal kingdom. Proc. nat. Acad. Sci. (Wash.) 64, 1349–1355 (1969 a).
Kuo, J.F., Greengard, P.: Adenosine 3′,5′-monophosphate dependent protein kinase from brain. Science 165, 63–65 (1969b).
Kuo, J.F., Greengard, P.: Stimulation of adenosine 3′,5′-monophosphate-dependent protein kinases by some analogs of adenosine 3′,5′-monophosphate. Biochem. biophys. Res. Commun. 40, 1032–1038 (1970a).
Kuo, J.F., Greengard, P.: Cyclic nucleotide-dependent protein kinases. VII. Comparison of various histones as substrates for adenosine 3′,5′-monophosphate-dependent and guanosine 3′,5′-monophosphate-dependent protein kinases. Biochim. biophys. Acta (Amst.) 212, 434 440 (1970 b).
Kuo, J.F., Greengard, P.: Stimulation of cyclic GMP dependent protein kinase by a protein fraction which inhibits cyclic AMP-dependent protein kinases. Fed. Proc. 30, 1089 (1973).
Kuo, J.F., Lee, T.P., Reyes, P.L., Walton, K.G., Donnelly, T.E., Greengard, P.: Cyclic nucleotide-dependent protein kinases. X. An assay method for the measurement of guanosine 3′,5′-monophosphate in various biological materials and a study of agents regulating its levels on heart and brain. J. biol. Chem. 247, 16–22 (1972).
Kuo, J.F., Miyamoto, E., Reyes, P.L.: Activation and dissociation of adenosine 3′,5′-monophosphate-dependent protein kinase by various cyclic nucleotide analogs. Biochem. Pharmacol. 23, 2011–2021 (1974).
Kuriyama, K., Isreal, M.A.: Effect of ethanol administration on cyclic 3′,5′-adenosine-monophosphate metabolism in brain. Biochem. Pharmacol. 22, 2919–2922 (1973).
Lake, N., Jordan, L.M.: Failure to confirm cyclic AMP as second messenger for norepinephrine in rat cerebellum. Science 183, 663–664 (1974).
Lake, N., Jordan, L.M., Phillis, J.W.: Mechanism of noradrenaline actions in cat cerebral cortex. Nature (Lond.) 240, 249–250 (1972).
Lake, N., Jordan, L.M., Phillis, J.W.: Evidence against cyclic adenosine 3′,5′-monophosphate (AMP) mediation of noradrenaline depression of cerebral cortical neurones. Brain Res. 60, 411–421 (1973).
Landis, S.C., Bloom, F.E.: Fluorescence and electron microscopic analysis of catecholamine containing fibers in mutant mouse cerebellum. 4th Annu. Meeting Soc. Neurosci. 297, 1974.
Langan, T.: Protein kinases and protein kinase substrates. In: Advances in Cyclic Nucleotide Research, vol. 1. New York: Raven Press 1972.
Lee, T-P., Kuo, J.F., Greengard, P.: Role of muscarinic cholinergic receptors in regulation of guanosine 3′,5′-cyclic monophosphate content in mammalian brain, heart muscle, and intestinal smooth muscle. Proc. nat. Acad. Sci. (Wash.) 69, 3287–3289 (1972).
Lefkowitz, R.J.: Stimulation of catecholamine-sensitive adenylate by 5’-guanylyl imido-diphosphate J. biol. Chem. 249, 6119–6124 (1974).
Lefkowitz, R.J., Mukherjee, C., Coverstone, M., Caron, M.G.: Stereospecific (3H) (-) — alprenolol binding sites, β-adrenergic receptors and adenylate cyclase. Biochem. biophys. Res. Commun. 60, 703–709 (1974).
Lentz, T.L.: A role of cyclic AMP in a neurotrophic process. Nature (Lond.) 238, 154–155 (1972).
Levitan, I.B., Barondes, S.H.: Octopamine- and serotonin-stimulated phosphorylation of specific protein in the abdominal ganglion of Aplysia californica. Proc. nat. Acad. Sci (Wash) 72 1145–1148 (1974).
Levitan, I.B., Madsen, C.J., Barondes, S.H.: Cyclic AMP and amine effects on phosphorylation of specific protein in abdominal ganglion of aplysia californica: localization and kinetic analysis. J. Neurobiol. 5, 475–588 (1974).
Libet, B.: Generation of slow inhibitory and excitatory postsynaptic potentials. Fed. Proc 29 1945–1949 (1970).
Libet, B., Kobayashi, H.: Generation of adrenergic and cholinergic potentials in sympathetic ganglion cells. Science 164, 1530–1532 (1969).
Lin, Y.M., Liu, Y.P., Cheung, W.Y.: Cyclic 3′:5′-nucleotide phosphodiesterase. Purification, characterization, and active form of the protein activator from bovine brain. J. biol. Chem. 249, 4943–4954 (1974).
Lindl, T., Cramer, H.: Formation, accumulation and release of adenosine 3′,5′-monophosphate induced by histamine in the superior cervical ganglion of the rat in vivo. Biochim. biophys.Acta (Amst.) 343, 182–191 (1974).
Lindvall, O., Björklund, A.: The organization of the ascending catecholamine neuron systems in the rat brain. Acta physiol. scand. 412, 1–48 (1974).
Lindvall, O., Björklund, A., Moore, R.Y., Stenevi, U.: Mesencephalic dopamine neurons projecting to neocortex. Brain Res. 81, 325–331 (1974).
Ling, G., Gerard, R.W.: Normal membrane potential of frog sartorius fibers. J. cell. comp. Physiol. 34, 383–394 (1949).
Lipkin, D., Cook, W.H., Markham, R.: Adenosine-3′:5′-phosphoric acid: A proof of structure. J. Amer. chem. Soc. 81, 6198–6203 (1959).
Loewi, O.: Über humorale Übertragbarkeit der Herznervenwirkung. Pflügers Arch. ges. Physiol. 189, 239–242 (1921).
Londos, C., Solomon, Y., Lin, M.C., Harwood, J.P., Schramm, M., Wolff, J., Rodbell, M.: 5-Guanylyl-imidodiphosphate, a potent activator of adenylate cyclase systems in eukaryotic cells. Proc. nat. Acad. Sci. (Wash.) 71, 3087–3090 (1974).
Lorenzo, R. de, Greengard, P.: Activation by adenosine 3′:5′-monophosphate of a membrane bound phosphoprotein phosphatase from toad bladder. Proc. nat. Acad. Sci. (Wash.) 70, 1831–1835 (1973).
Lorenzo, R. de, Walton, K.G., Curran, P.F., Greengard, P.: Regulation of phosphorylation of a specific protein in toad bladder membrane by antidiuretic hormone and cyclic AMP, and its possible relationship to membrane permeability changes. Proc. nat. Acad. Sci. (Wash.) 70, 880–884 (1973).
Lowry, O.H., Passonneau, J.V., Hasselberger, F.X., Schultz, D.W.: Effect of ischemia on known substrates and cofactors of the glycolytic pathway in brain. J. biol. Chem. 239, 18–30 (1964).
Lust, W.D., Passonneau, J.V., Veech, R.L.: Cyclic adenosine monophosphate metabolites and Phosphorylase in neuronal tissue. A comparison of methods of fixation. Science 181, 280–282 (1973).
Mackay, A.V.P., Iversen, L.L.: Increased tyrosine hydroxylase activity of sympathetic ganglia cultured in the presence of dibutyryl cyclic AMP. Brain Res. 48, 424–426 (1972).
Maeda, T., Tohyama, M., Shimizu, N.: Modification of postnatal development of neocortex in rat brain with experimental deprivation of locus coeruleus. Brain Res. 70, 515–520 (1974).
Maeno, H., Greengard, P.: Phosphoprotein phosphatases from rat cerebral cortex. J. biol. Chem. 247, 3269–3277 (1972).
Maeno, H., Johnson, E.M., Greengard, P.: Subcellular distribution of adenosine 3′,5′-monophosphate-dependent protein kinase in rat brain. J. biol. Chem. 246, 134–142 (1971).
Maeno, H., Ueda, T., Greengard, P.: Adenosine 3′:5′-monophosphate dependent protein phosphatase activity in synaptic membrane fractions. J. Cyclic Nucleotide Res. 1, 37–38 (1975).
Magaribuchi, M., Kuriyama, H.: Effects of noradrenaline and isoprenaline on the electrical and mechanical activities of guinea pig depolarized taenia coli. Jap. J. Physiol. 22, 253–270 (1972).
Magun, B.: Two actions of cyclic AMP on melanosome movement in frog skin. J. Cell Biol. 57, 845–858 (1973).
Mao, C.C., Guidotti, A., Costa, E.: Inhibition by diazepam of the tremor and the increase of cerebellar cGMP content elicited by harmaline. Brain Res. 83, 526–529 (1974a).
Mao, C.C., Guidotti, A., Costa, E.: Interactions between γ-amino-bytyric acid and guanosine cyclic 3′-5′ monophosphate in rat cerebellum. Molec. Pharmacol. 10, 736–745 (1974b).
Mao, C.C., Guidotti, A., Costa, E.: The regulation of cyclic guanosine monophosphate in rat cerebellum: possible involvement of putative amino acid neurotransmitters. Brain Res. 79, 510–514 (1974c).
Matthews, E.K., Saffran, M.: Ionic dependence of adrenal steroidogenesis and ACTH-induced changes in the membrane potential of adreno-cortical cells. J. Physiol. (Lond.) 234, 43–64 (1973).
Mayer, S.E.: Effect of catecholamines on cardiac metabolism. Circulat. Res. Suppl. III 34–35, 129–137 (1974).
McAfee, D.A., Greengard, P.: Adenosine 3′:5′-monophosphate: electrophysiological evidence for a role in synaptic transmission. Science 178, 310–312 (1972).
McAfee, D.A., Schorderet, M., Greengard, P.: Adenosine 3′:5′-monophosphate in nervous tissue: increase associated with synaptic transmission. Science 171, 1156–1158 (1971).
McCune, R.W., Gill, T.H., von Hungen, K., Roberts, S.: Catecholamine sensitive adenyl cyclase in cell-free preparations from rat cerebral cortex. Life Sci. 10, 443–450 (1971).
McManus, J.P., Whitfield, J.F.: Cyclic AMP, prostaglandins and the control of cell proliferation. Prostaglandins 6, 475–487 (1974).
Meinertz, T., Nawrath, H., Scholz, H., Winter, K.: Effect of DB-c-AMP on mechanical characteristics of ventricular and atrial preparations of several mammalian species. Naunyn-Schmiedeberg’s Arch. Pharmacol. 282, 143–153 (1974).
Meyer, R.B. Jr., Miller, J.P.: Analogs of cyclic AMP and cyclic GMP: general methods of synthesis and the relationship of structure to enzymic activity. Life Sci. 14, 1019–1040 (1974).
Miki, N., Keirns, J.J., Markus, F.R., Freeman, J., Bitensky, M.W.: Regulation of cyclic nucleotide concentrations in photoreceptors: An ATP-dependent stimulation of cyclic nucleotide phosphodiesterase by light. Proc. nat. Acad. Sci. (Wash.) 70, 3820–3824 (1973).
Miller, C.A., Levine, E.M.: Neuroblastoma: synchronization of neurite growth in cultures grown in collagen. Science 177, 799–801 (1972).
Miller, J.P., Boswell, K.H., Muneyana, K., Simon, L.N., Robins, R.K., Shuman, D.A.: Synthesis and biochemical studies of various 8-substituted derivatives of guanosine 3′:5′-cyclic phosphate, inosine 3′:5′-cyclic phosphate and xanthosine 3′:5′-cyclic phosphate. Biochemistry (Wash.) 12, 5310–5319 (1973).
Miller, R.J., Horn, A.S., Iversen, L.L.: The action of neuroleptic drugs on dopamine-stimulated adenosine cyclic 3,5′-monophosphate production in rat neostriatum and limbic forebrain. Molec. Pharmacol. 10, 759–766 (1974).
Miller, W.H.: Cyclic nucleotides and photoreception. Exp. Eye Res. 16, 357–363 (1973).
Minor, A.V., Sakina, N.L.: Role of cyclic adenosine 3′-5′ monophosphate in olfactory reception. Neurofizilogia 2, 415–422 (1973).
Mishra, R.K., Gardner, E.L., Katzman, R., Makman, M.H.: Enhancement of dopamine-stimulated adenylate cyclase activity in rat caudate after lesions in substantia nigra: evidence for denervation supersensitivity. Proc. nat. Acad. Sci. (Wash.) 71, 3883–3887 (1974).
Mitznegg, P., Schubert, E., Heim, F.: The influence of low and high doses of theophylline on spontaneous motility and cyclic 3′,5′ AMP content in isolated rat uterus. Life Sci. 14, 711–717 (1974).
Miyamoto, E., Kakiuchi, S.: In Vitro and In Vivo phosphorylation of myelin basic protein by exogenous and endogenous adenosine 3′5′-monophosphate-dependent protein kinases in brain. J. biol. Chem. 249, 2569–2777 (1974).
Miyamoto, E., Kuo, J.F., Greengard, P.: Adenosine 3′5′-monophosphate-dependent protein kinase from brain. Science 165, 63–65 (1969a).
Miyamoto, E., Kuo, J.F., Greengard, P.: Cyclicnucleotide-dependent protein kinases. I. Purification and properties of adenosine 3′,5′-monophosphate-dependent protein kinase from bovine brain. J. biol. Chem. 244, 6395–6402 (1969b).
Miyamoto, E., Petzold, G.L., Harris, J.S., Greengard, P.: Dissociation and concomitant activation of adenosine 3′,5′-monophosphate-dependent protein kinase by histone. Biochem. biophys. Res. Commun. 44, 305–312 (1971).
Molinoff, P.B., Axelrod, J.: Biochemistry of catecholamines. Ann. Rev. Biochem. 40, 465–500 (1971).
Monn, E., Christiansen, R.O.: Adenosine 3′,5′-monophosphate phosphodiesterase: multiple molecular forms. Science 173, 540–541 (1971).
Moore, R.Y., Björklund, A., Stenevi, U.: Plastic changes in the adrenergic innervation of the rat septal area in response to denervation. Brain Res. 33, 13–35 (1971).
Morgenroth, V.H. III., Boadle-Biber, M., Roth, R.H.: Tyrosine hydrolase: Activation by nerve stimulation. Proc. nat. Acad. Sci. (Wash.) 71, 4283–4287 (1974).
Moses, H.L., Rosenthal, A.S.: Pitfalls in the use of lead ion for histochemical localization of nucleoside phosphatases. J. Histochem. Cytochem. 16, 530–539 (1968).
Mueller, R.A., Otten, U., Thoenen, H.: The role of adenosine cyclic 3′,5′-monophosphate in reserpine-initiated adrenal medullary tyrosine hydroxylase induction. Molec. Pharmacol. 10, 855–860 (1974).
Mueller, R.A., Thoenen, H., Axelrod, J.: Increase in tyrosine hydroxylase activity after reserpine administration. J. Pharmacol. exp. Ther. 169, 74–79 (1969).
Mulleroe, B., Schwabe, B.: Role of cyclic AMP for function of peripheral and central nervous system. Fortsch. Neurol. Psychiat. 41, 509–526 (1973).
Murad, F., Manganiello, V., Vaughan, M.: A simple sensitive protein binding assay for guanosine 3′-5′ monophosphate. Proc. nat. Acad. Sci. (Wash.) 68, 736–739 (1971).
Murphy, D.L., Donnelly, C., Moskowitz, J.: Inhibition by lithium of prostaglandin E1 and norepinephrine effects on cyclic adenosine monophosphate production in human platelets. Clin. Pharmacol. Ther. 14, 810–814 (1973).
Nahorski, S.R., Rogers, K.J., Pinns, J.: Cerebral phosphodiesterase and dopamine receptor. J. Pharm. Pharmacol. 25, 912–913 (1973).
Naito, K., Kuriyama, K.: Effect of morphine administration on adenyl cyclase and 3′,5′-cyclic nucleotide phosphodiesterase activities in the brain. Jap. J. Pharmacol. 23, 274–276 (1973).
Nakazawa, K., Sano, M.: Studies on guanylate cyclase. A new assay method for guanylate cyclase and properties of the cyclase from rat brain. J. biol. Chem. 249, 4207–4211 (1974).
Nathanson, J.A., Greengard, P.: Octopamine-sensitive adenylate cyclase: evidence for a biological role of octopamine in nervous tissue. Science 180, 308–310 (1973).
Nathanson, J.A., Greengard, P.: Serotonin-sensitive adenylate cyclase in neural tissue and its similarity to the serotonin receptor: a possible site of lysergic acid diethylamide. Proc. nat. Acad. Sci. (Wash.) 71, 797–801 (1974).
Neelon, F.A., Birch, B.M.: Cyclic adenosine 3′:5′-monophosphate-dependent protein kinase. J. biol. Chem. 248, 8361–8365 (1973).
Nelson, C.N., Hoffer, B.J., Chu, N-S., Bloom, F.E.: Cytochemical and pharmacological studies on polysensory neurons in the primate frontal cortex. Brain Res. 62, 115–133 (1973).
Norberg, K.A., Ritzen, M., Ungerstedt, U.: Histochemical studies on a special catecholamine- containing cell type in sympathetic ganglia. Acta physiol. scand. 67, 260–270 (1966).
Obata, K., Takeda, K., Shinozaki, H.: Electrophoretic release of γ-aminobutyric acid and glutamic acid from micropipettes. Neuropharmacol. 9, 191–194 (1970).
Obata, K., Yoshida, M.: Caudate-evoked inhibition and actions of GABA and other substances on cat pallidal neurons. Brain Res. 64, 455–459 (1973).
Oliver, A.P., Segal, M.: Transmembrane changes in hippocampal neurons: hyperpolarizing actions of norepinephrine, cyclic AMP, and locus coeruleus. Proc. Soc. Neurosci. 361 (1974).
Olson, L., Fuxe, K.: On the projections from the locus coeruleus noradrenaline neurons. Brain Res. 28, 165–171 (1971).
Olson, L., Fuxe, K.: Further mapping out of central noradrenaline nervous systems: Projections of the subcoeruleus area. Brain Res. 43, 289–295 (1972).
Otten, U., Mueller, R.A., Oesch, F., Thoenen, H.: Location of an isoproterenol-responsive cyclic AMP pool in adrenergic nerve cell bodies and its relationship to tyrosine 3-monooxygenase induction. Proc. nat. Acad. Sci. (Wash.) 71, 2217–2221 (1974).
Otten, U., Oesch, F., Thoenen, H.: Dissociation between changes in cyclic AMP and subsequent induction of tyrosine hydroxylase in rat superior cervical ganglion and adrenal medulla. Naunyn-Schmiedeberg’s Arch. Pharmacol. 280, 129–140 (1973).
Palay, S.L., Chan-Palay, V.: Cerebellar Cortex. Cytology and Organization. Berlin-Heidelberg-New York: Springer 1974.
Palmer, G.C.: Increased cyclic AMP response to norepinephrine in the rat brain following 6-hydroxy-dopamine. Neuropharmacol. 11, 145–149 (1972).
Almer, G.C.: Adenyl cyclase in neuronal and glial-enriched fractions from rat and rabbit brain. Res. Commun. Chem. Path. Pharmacol. 5, 603–613 (1973a).
Palmer, G.C.: Influence of amphetamines, protriptyline and pargyline on the time course of the norepinephrine-induced accumulation of cyclic AMP in rat brain. Life Sci. 12, 345–355 (1973b).
Palmer, G.C., Burks, T.F.: Central and peripheral adrenergic blocking actions of LSD and BOL. Europ. J. Pharmacol. 16, 113–116 (1971).
Palmer, G.C., Robison, G.A., Manian, A.A., Sulser, F.: Modification by psychotropic drugs of the cyclic AMP response to norepinephrine in the rat brain in vitro. Psychopharmacologia (Berl.) 23, 201–211 (1972a).
Palmer, G.C., Schmidt, M.J., Robison, G.A.: Development and characteristics of the histamine-induced accumulation of cyclic AMP in the rabbit cerebral cortex. J. Neurochem. 19, 2251–2256 (1972b).
Palmer, G.C., Sulser, F., Robison, G.A.: Effects of neurohumoral and adrenergic agents on cyclic AMP levels in various areas of the rat brain in vitro. Neuropharmacol. 12, 327–337 (1973).
Pannbacker, R.G.: Control of guanylate cyclase activity in the rod outer segment. Science 182, 1138–1139 (1973).
Pannbacker, R.G., Fleischman, D.E., Reed, D.W.: Cyclic nucleotide phosphodiesterase: high activity in a mammalian photoreceptor. Science 175, 757–758 (1972).
Papahadjopoulos, D., Poste, G., Mayhew, E.: Cellular uptake of cyclic AMP captured within phospholipid vesicles and effect on cell growth behavior. Biochim. biophys. Acta (Amst.) 363, 404–418 (1974).
Paton, W.D.M.: Central and synaptic transmission in the nervous system (pharmacological aspects). Ann. Rev. Pharmacol. 20, 431–462 (1958).
Paul, M.I., Cramer, H., Bunney, W.E. Jr.: Urinary adenosine 3′5′-monophosphate in the switch process from depression to mania. Science 171, 300–303 (1971a).
Paul, M.I., Cramer, H., Goodwin, F.K.: Urinary cyclic AMP excretion in depression and mania. Arch. gen. Psychiat. 24, 327–333 (1971b).
Perkins, J.P.: Adenyl cyclase. In: Advances in Cyclic Nucleotide Research, vol. 3. New York: Raven Press 1973.
Perkins, J.P., Moore, M.M.: Adenyl cyclase of rat cerebral cortex. J. biol. Chem. 246, 62–68 (1971).
Perkins, J.P., Moore, M.M.: Regulation of the adenosine cyclic 3′,5′-monophosphate content of rat cerebral cortex: ontogenetic development of the responsiveness to catecholamines and adenosine. Molec. Pharmacol. 9, 774–782 (1973 a).
Perkins, J.P., Moore, M.M.: Characterization of the adrenergic receptors mediating a rise in cyclic 3′,5′-adenosine monophosphate in rat cerebral cortex. J. Pharmacol. exp. Ther. 185, 371–378 (1973b).
Petersen, O.H.: The effect of glucagon on the liver cell membrane potential. J. Physiol. (Lond.) 239, 647–656 (1974).
Phillis, J.W.: Evidence for cholinergic transmission in the cerebral cortex. Advan. Behav. Biol. 10, 57–80 (1974a).
Phillis, J.W.: The role of calcium in the central effects of biogenic amines. Life Sci. 14, 1189–1201 (1974b).
Phillis, J.W., Kostopoulos, G.K., Limacher, J.J.: A potent depressant action of adenine derivatives on cerebral cortical neurons. Europ. J. Pharmacol. 30, 125–129 (1975).
Phillis, J.W., Lake, N., Yarborough, G.: Calcium mediation of the inhibitory effects of biogenic amines on cerebral cortical neurones. Brain Res. 53, 465–469 (1973).
Pickel, V.M., Segal, M., Bloom, F.E.: A radioautographic study of the efferent pathways of the nucleus locus coeruleus. J. comp. Neurol. 155, 15–42 (1974a).
Pickel, V.M., Segal, M., Bloom, F.E.: Axonal proliferation following lesions of cerebellar peduncles. A combined fluorescence microscopic and radioautographic study. J. comp. Neurol. 155, 43–60 (1974b).
Posternak, T., Sutherland, E.W., Henion, W.F.: Derivatives of cyclic 3′5′-adenosine monophosphate. Biochim. biophys. Acta (Amst.) 65, 558–560 (1962).
Prasad, K.N., Gilmer, K., Kumar, S.: Morphologically “differentiated” mouse neuroblastoma cells induced by noncyclic AMP agents: levels of cyclic AMP, nucleic acid and protein. Proc. Soc. exp. Biol. (N.Y.) 143, 1168–1171 (1973a).
Prasad, K.N., Hsie, A.W.: Morphologic differentiation of mouse neuroblastoma cells induced in vitro by dibutyryl adenosine 3′,5′-cyclic monophosphate. Nature (Lond.) 233, 141–142 (1971).
Prasad, K.N., Mandal, B., Waymire, J.C., Lees, G.J., Vernadakis, A., Weiner, N.: Basal level of neurotransmitter synthesizing enzymes and effect of cyclic AMP agents on the morphological differentiation of isolated neuroblastoma clones. Nature (Lond.) 241, 117–119 (1973b).
Purpura, D.P., Shofer, R.J.: Excitatory action of dibutyryl cyclic adenosine monophosphate on immature cerebral cortex. Brain Res. 38, 179–181 (1972).
Rall, T.W.: Role of adenosine 3′,5′-monophosphate (cyclic AMP) in actions of catecholamines. Pharmacol. Rev. 24, 399–409 (1972).
Rall, T.W., Gilman, A.G.: The role of cyclic AMP in the nervous system. Neurosci. Res. Program Bull. 8, (3) 221–317 (1970).
Rall, T.W., Sattin, A.: Factors influencing the accumulation of cyclic AMP in brain tissue. Advanc. Biochem. Psychopharmacol. 3, 113–133 (1970).
Rall, T.W., Sutherland, E.W., Berthet, J.: The relationship of epinephrine and glucagon to liver Phosphorylase. IV. Effect of epinephrine and glucagon on the reactivation of Phosphorylase in liver homogenates. J. biol. Chem. 224, 463–475 (1957).
Rall, T.W., Sutherland, E.: Formation of a cyclic adenine ribonucleotide by tissue particles. J. biol. Chem. 232, 1065–1076 (1958).
Rall, T.W., Sutherland, E.W.: The regulatory role of adenosine 3′,5′-phosphate. Cold Spr. Harb. Symp. quant. Biol. 26, 347–354 (1961).
Rall, T.W., Sutherland, E.W.: Adenyl cyclase. II. The enzymatically catalyzed formation of adenosine 3′-5′ phosphate and inorganic pyrophosphate from adenosine triphosphate. J. biol. Chem. 237, 1228–1232(1962).
Rasmussen, H.: Cell communication, calcium ion, and cyclic adenosine monophosphate. Science 170, 404–412 (1970).
Reik, L., Petzold, G.L., Higgins, J.A., Greengard, P., Barrnett, R.J.: Hormone-sensitive adenyl cyclase: cytochemical localization in rat liver. Science 168, 382–384 (1970).
Richelson, E.: Stimulation of tyrosine hydroxylase activity in an adrenergic clone of mouse neuroblastoma by dibutyryl cyclic AMP. Nature (Lond.) 242, 175–177 (1973).
Robertis, E. de, Rodriguez de Lores Arnaiz, G., Alberici, M., Butcher, R.W., Sutherland, E.W.: Subcellular distribution of adenyl cyclase and cyclic phosphodiesterase in rat brain cortex. J. biol. Chem. 242, 3487–3493 (1967).
Robison, G.A., Butcher, R.W., Sutherland, E.W.: Cyclic AMP. New York: Academic Press 1971.
Rodbell, M.: The role of nucleotides in the activity and response of adenylate cyclase to hormones. In: Advance in Cyclic Nucleotide Research, vol. 5. New York: Raven Press (in press).
Rodbell, M., Birnbaumer, L., Pohl, S.L.: Hormones, receptors and adenyl cyclase activity in mammalian cells. In: The Role of Adenyl Cyclase and Cyclic 3′,5′-AMP in Biological Systems, Fogarty International Center Proceedings. Washington, D.C.: U.S. Government Printing Office 1971.
Roisen, F.J., Murphy, R.A.: Neurite development in vitro. II. The role of microfilaments and microtubules in dibutyryl adenosine 3′,5′-cyclic monophosphate and nerve-growth factor stimulated maturation. J. Neurobiol. 4, 397–417 (1973).
Roisen, F.J., Murphy, R.A., Braden, W.G.: Dibutyryl cyclic adenosine monophate stimulation of colcemid-inhibited axonal elongation. Science 177, 809–811 (1972a).
Roisen, F.J., Murphy, R.A., Braden, W.G.: Neurite development in vitro. I. The effects of adenosine 3′,5′-cyclic monophosphate (cyclic AMP). J. Neurobiol. 4, 347–368 (1972b).
Roisen, F.J., Murphy, R.A., Pichichero, M.E., Braden, W.G.: Cyclic adenosine monophosphate stimulation of axonal elongation. Science 175, 73–74 (1972c).
Rozear, M., DeGroof, R., Somjen, G.: Effects of microiontophoretic administration of divalent metal ions on neurons of the central nervous system of cats. J. Pharmacol. exp. Ther. 176, 109–118 (1971).
Rubin, R.P., Jaanus, S.D., Carchman, R.A.: Role of calcium and adenosine cyclic 3′-5′ phosphate in action of adreno corticotropin. Nature (Lond.) 240, 150–152 (1972).
Rudland, P.S., Gospodarowicz, D., Siefert, W.E.: Cyclic GMP and growth control in cultured fibroblasts: activation of guanyl cyclase and intracellular cGMP by a purified growth factor. Nature (Lond.) 250, 741–742 (1974).
Rudolph, S.A., Johnson, E.M., Greengard, P.: The entholpy of hydrolysis of various 3′,5′- and 2′,2′-cyclic nucleotides. J. biol. Chem. 246, 1271–1273 (1971).
Russell, J.R., Thompson, W.J., Schneider, F.W., Appleman, M.M.: 3′,5′-Cyclic adenosine monophosphate phosphodiesterase: negative cooperativity. Proc. nat. Acad. Sci. (Wash.) 69, 1791–1795 (1972).
Russell, T.R., Pastan, LH.: Cyclic adenosine 3′:5′-monophosphate and cyclic guanosine 3′:5′-monophosphate phosphodiesterase activities are under separate genetic control. J. biol. Chem. 249, 7764–7769 (1974).
Sakai, K., Marks, B.: Adrenergic effects on pineal cell membrane potential. Life Sci. 11, 285–291 (1972).
Salmoiraghi, G.C., Bloom, F.E.: The pharmacology of individual neurons. Science 144, 493–497 (1964).
Sasa, M., Munekiyo, K., Ikeda, H., Takaori, S.: Noradrenaline-mediated inhibition by locus coeruleus of spinal trigeminal neurons. Brain Res. 80, 443–460 (1974).
Sattin, A., Rall, T.W.: The effect of adenosine and adenine nucleotides on the cyclic adenosine 3′,5′-phosphate content of guinea pig cerebral cortex slices. Molec. Pharmacol. 6, 13–23 (1970).
Sattin, A., Rall, T.W., Zanella, J.: Regulation of cyclic adenosine 3′,5′-monophosphate levels in guinea pig cerebral cortex by interaction of alpha adrenergic and adenosine receptor activity. J. Pharmacol. exp. Ther. 192, 22–32 (1975).
Sayers, G., Beall, R.J., Seelig, S.: Isolated adrenal cells: adreno-corticotropic hormone, calcium, steroidogenesis and cyclic adenosine monophosphate. Science 175, 1131–1133 (1972).
Schimmer, B.P.: Effects of catecholamines and monovalent cations on adenylate cyclase activity in cultured glial tumor cells. Biochim. biophys. Acta (Amst.) 252, 567–573 (1971).
Schimmer, B.P.: Influence of Li+ on epinephrine-stimulated adenylate cyclase activity in cultured glial tumor cells. Biochim. biophys. Acta (Amst.) 326, 186–192 (1973).
Schmidt, M.J., Hopkins, J.T., Schmidt, D.E., Robison, G.A.: Cyclic AMP in brain areas: effects of amphetamine and norepinephrine assessed through the use of microwave radiation as a means of tissue fixation. Brain Res. 42, 465–477 (1972).
Schmidt, M.J., Palmer, E.C., Dettborn, W.-D., Robison, G.A.: Cyclic AMP and adenyl cyclase in the developing rat brain. Develop. Psychobiol. 3, 53–67 (1970).
Schmidt, M.J., Robison, G.A.: The effect of norepinephrine on cyclic AMP levels in discrete regions of the developing rabbit brain. Life Sci. 10, 459–464 (1971).
Schmidt, M.J., Schmidt, D.E., Robison, G.A.: Cyclic adenosine monophosphate in brain areas: microwave irradiation as a means of tissue fixation. Science 173, 1142–1143 (1971).
Schmidt, M.J., Sokoloff, L.: Activity of cyclic AMP-dependent microsomal protein kinase and phosphorylation of ribosomal protein in rat brain during postnatal development. J. Neurochem. 21, 1193–1205 (1973).
Schroeder, J.: Analogs of α-tocopherol as inhibitors of cyclic AMP and cyclic GMP phosphodiesterases and effects of a-tocopherol deficiency on cyclic AMP-controlled metabolism. Biochim. biophys. Acta (Amst.) 343, 173–181 (1974).
Schultz, G., Böhme, E., Munske, K.: Guanyl cyclase: Determination of enzyme activity. Life Sci. 8, 1323–1332 (1969).
Schultz, G., Hardman, J.G., Schultz, K., Baird, C.E., Sutherland, E.W.: The importance of calciums ions for the regulation of guanosine 3′,5′-cyclic monophosphate levels. Proc. nat. Acad. Sci. (Wash.) 70, 3889–3893 (1973).
Schultz, J.: Inhibition of phosphodiesterase activity in brain cortical slices from guinea pig and rat. Pharmacol. Res. Commun. 6, 335–341 (1974).
Schultz, J., Daly, J.W.: Cyclic adenosine 3′,5′-monophosphate in guinea pig cerebral cortical slices. II. The role of phosphodiesterase activity in the regulation of levels of cyclic adenosine 3′,5′-monophosphate. J. biol. Chem. 248, 853–859 (1973a).
Schultz, J., Daly, J.W.: Cyclic adenosine 3′,5′-monophosphate in guinea pig cerebral cortical slices. III. Formation, degradation, and reformation of cyclic adenosine 3′,5′-monophosphate during sequential stimulations by biogenic amines and adenosine. J. biol. Chem. 248, 860–866 (1973b).
Schultz, J., Daly, J.W.: Adenosine 3′,5′-monophosphate in guinea pig cerebral cortical slices: effects of α- and β-adrenergic agents, histamine, serotonin, and adenosine. J. Neurochem. 21, 573–579 (1973c).
Schultz, J., Daly, J.W.: Accumulation of cyclic adenosine 3′,5′-monophosphate in cerebral cortical slices from rat and mouse stimulatory effect of α- and β-adrenergic agents and adenosine. J. Neurochem. 21, 1319–1326 (1973d).
Schultz, J., Hamprecht, B., Daly, J.W.: Accumulation of adenosine 3′,5′-cyclic monophosphate in clonal glial cells: labeling of intracellular adenine nucleotides with radioactive adenine. Proc. nat. Acad. Sci. (Wash.) 69, 1266–1270 (1972).
Schwartz, J.P., Morris, N.R., Breckenridge, B.M.: Adenosine 3′,5′-monophosphate in glial tumor cells. J. biol. Chem. 248, 2699–2704 (1973).
Seeds, N.W., Gilman, A.G.: Norepinephrine stimulated increase of cyclic AMP levels in developing mouse brain cell cultures. Science 174, 292 (1971).
Seeman, P., Lee, T.: Tranquilizer-blockade of dopamine release from stimulated striatal slices. 4th Annu. Meeting Soc. for Neurosci., St. Louis, 620, 1974.
Segal, M., Bloom, F.E.: The action of norepinephrine in the rat hippocampus. I. Iontophoretic studies. Brain Res. 72, 79–97 (1974a).
Segal, M., Bloom, F.E.: The action of norepinephrine in the rat hippocampus. II. Activation of the input pathway. Brain Res. 72, 99–114 (1974b).
Shashoua, V.E.: Dibutyryl adenosine cyclic 3′,5′-monophosphate effects on goldfish behavior and brain RNA metabolism. Proc. nat. Acad. Sci. (Wash.) 68, 2835–2838 (1971).
Shein, H.M., Wurtman, R.J.: Cyclic adenosine monophosphate: stimulation of melatonin and serotonin synthesis in cultured rat pineals. Science 166, 519–520 (1969).
Sheppard, H., Burghardt, C.R.: The dopamine-sensitive adenylate cyclase of rat caudate nucleus. I. Comparison with the isoproterenol-sensitive adenylate cyclase (beta receptor system) of rat erythrocytes in responses to dopamine derivatives. Molec. Pharmacol. 10, 721–726 (1974).
Sheppard, J.R., Hudson, T.H., Larson, J.R.: Adenosine 3′,5′-monophosphate analogus promote a circular morphology of cultured schwannoma cells. Science 187, 179–181 (1975).
Sheppard, J.R., Prasad, K.N.: Cyclic AMP levels and the morphological differentiation of mouse neuroblastoma cells. Life Sci. 12, 431–439 (1973).
Sherrington, C.S.: Remarks on some aspects of reflex inhibition. Proc. roy. Soc. B 97, 519–544 (1925).
Shimizu, H., Daly, J.: Formation of cyclic adenosine 3′,5′ monophosphate from adenosine in brain slices. Biochim. biophys. Acta (Amst.) 222, 465–473 (1970).
Shimizu, H., Daly, J.W.: Effect of depolarizing agents on accumulation of cyclic adenosine 3′,5′-monophosphate in cerebral cortical slices. Europ. J. Pharmacol. 17, 240–252 (1972).
Shimizu, H., Creveling, C.R., Daly, J.: Stimulated formation of adenosine 3′,5′-cyclic phosphate in cerebral cortex: synergism between electrical activity and biogenic amines. Proc. nat. Acad. Sci. (Wash.) 65, 1033–1040 (1970a).
Shimizu, H., Creveling, C.R., Daly, J.W.: Cyclic adenosine 3′,5′-monophosphate formation in brain slices: stimulation by batrachotoxin, ouabain, veratridine and potassium ions. Molec. Pharmacol. 6, 184–188 (1970b).
Shimizu, H., Creveling, C.R., Daly, J.W.: The effect of histamines and other compounds on the formation of adenosine 3′,5′-monophosphate in slices from cerebral cortex. J. Neurochem. 17, 441–444 (1970c).
himizu, H., Ichisita, H., Odagiri, H.: Stimulated formation of cyclic adenosine 3′,5′-monophosphate by aspartate and glutamate in cerebral cortical slices of guinea pig. J. biol. Chem. 249, 5955–5962 (1974).
Shimizu, H., Tanaka, S., Suzuki, T., Matsukado, Y.: The response of human cerebrum adenyl cyclase to biogenic amines. J. Neurochem. 18, 1157–1161 (1971).
Shoemaker, W.J., Balentine, L.T., Siggins, G.R., Hoffer, B.J., Henriksen, S.J., Bloom, F.E.: Characteristics of the release of cyclic adenosine 3′,5′-monophosphate from micropipets by micro-iontophoresis. J. Cyclic Nucleotide Res. 1, 97–106 (1975).
Siggins, G.R., Battenberg, E.F., Hoffer, B.J., Bloom, F.E., Steiner, A.L.: Noradrenergic stimulation of cyclic adenosine monophosphate in rat Purkinje neurons: an immunocytochemical study. Science 179, 585–588 (1973).
Siggins, G.R., Henriksen, S.J.: Inhibition of rat Purkinje neurons by analogues of cyclic adenosine monophosphate: correlation with protein kinase activation. Science 189, 557–560 (1975).
Siggins, G.R., Hoffer, B.J., Bloom, F.E.: Cyclic 3′,5′-adenosine monophosphate: possible mediator for the response of cerebellar Purkinje cells to microelectrophoresis of norepinephrine. Science 165, 1018–1020 (1969).
Siggins, G.R., Hoffer, B.J., Bloom, F.E.: Studies on norepinephrine-containing afferents to Purkinje cells of rat cerebellum. III. Evidence for mediation of norepinephrine effects by cyclic 3′,5′-adenosine monophosphate. Brain Res. 25, 535–553 (1971a).
Siggins, G.R., Hoffer, B.J., Oliver, A.P., Bloom, F.E.: Activation of a central noradrenergic projection to cerebellum. Nature (Lond.) 233, 481–483 (1971b).
Siggins, G.R., Hoffer, B.J., Bloom, F.E.: Prostaglandin-norepinephrine interactions in brain: microelectrophoretic and histochemical correlates. Ann. N.Y. Acad. Sci. 180, 302–323 (1971c).
Siggins, G.R., Hoffer, B.J., Ungerstedt, U.: Electrophysiological evidence for involvement of cyclic adenosine monophosphate in dopamine responses of caudate neurons. Life Sci. 15, 779–792 (1974).
Siggins, G.R., Oliver, A.P., Hoffer, B.J., Bloom, F.E.: Cyclic adenosine monophosphate and norepinephrine: effects on transmembrane properties of cerebellar Purkinje cells. Science 171, 192–194 (1971d).
Simon, L.N., Shuman, D.A., Robins, R.K.: The synthesis and biological activity of analogs of cyclic nucleotides. In: Cellular Mechanisms. Basel: S. Karger 1973.
Skolnick, P., Daly, J.W.: The accumulation of adenosine 3′,5′-monophosphate in cerebral cortical slices of the awaking mouse, a neurologic mutant. Brain Res. 73, 513–525 (1974).
Skolnick, P., Huang, M., Daly, J., Hoffer, B.J.: Accumulation of adenosine 3′,5′-monophosphate in incubated slices from discrete regions of squirrel monkey cerebral cortex: effect of norepinephrine, serotonin, and adenosine. J. Neurochem. 21, 237–240 (1973).
Sloboda, R.D., Rudolph, S.A., Rosenbaum, J.L., Greengard, P.: Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein. Proc. nat. Acad. Sci. (Wash.) 72, 177–181 (1975).
Soifer, D.: Enzymatic activity in tubulin preparations: Cyclic AMP dependent protein kinase activity of brain microtubule protein. J. Neurochem. 24, 21–33 (1975).
Somlyo, A.V., Haeusler, G., Somlyo, A.P.: Cyclic adenosine monophosphate: potassium-dependent action on vascular smooth muscle membrane potential. Science 169, 490–491 (1970).
Spiegel, A.M., Aurbach, G.D.: Binding of 5′-guanylyl-imidodiphosphate to turkey erythrocyte membranes and effects on β-adrenergic activated adenylate cyclase. J. biol. Chem. 249, 7630–7636 (1974).
Stavinoha, W.B., Pepelko, B., Smith, P.: Microwave radiation to inactivate Cholinesterase in the rat brain prior to analysis for acetylcholine. Pharmacologist 12, 257 (1970).
Steiner, A.L., Parker, C.W., Kipnis, D.M.: The measurement of cyclic nucleotides by radioimmunoassay. Advanc. Biochem. Psychopharmacol. 3, 89–112 (1970).
Steiner, A.L., Parker, C.W., Kipnis, D.M.: Radioimmuno-assay for cyclic nucleotides. I. Preparation of antibodies and iodinated cyclic nucleotides. J. biol. Chem. 247, 1106–1113 (1972a).
Steiner, A.L., Paghara, A.W., Chase, L.R., Kipnis, D.M.: Radioimmunoassay for cyclic nucleodies. II. Adenosine 3′,5′-monophosphate and guanosine 3′,5′-monophosphate in mammalian tissues and body fluids. J. biol. Chem. 247, 1114–1120 (1972b).
Steiner, A.L., Ferrendelli, J.A., Kipnis, D.M.: Radioimmunoassay for cyclic nucleotides. III. Effect of ischemia, changes during development and regional distribution of adenosine 3′,5′-monophosphate and guanosine 3′,5′ monophosphate in mouse brain. J. biol. Chem. 247, 1121–1124 (1972c).
Stone, T.W., Taylor, D.A., Bloom, F.E.: Cyclic AMP and cyclic GMP may mediate opposite neuronal responses in the rat cerebral cortex. Science 187, 845–847 (1975).
Strada, S.J., Uzunov, P., and Weiss, B.: Ontogenetic development of a phosphodiesterase activator and the multiple forms of cyclic AMP phosphodiesterase of rat brain. J. Neurochem. 23, 1097–1103 (1974).
Sutherland, E.W., Oye, I., Butcher, R.W.: The action of epinephrine and the role of the adenyl cyclase system in hormone action. Recent Progr. Hormone Res. 21, 623–642 (1965).
Sutherland, E.W., Rall, T.W.: Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles. J. biol. Chem. 232, 1077–1091 (1958).
Sutherland, E.W., Rall, T.W., Menon, T.: Adenyl cyclase. I. Distribution, preparation and properties. J. biol. Chem. 237, 1220–1227 (1962).
Swillens, S., Cauter, E. von, Dumont, J.E.: Protein kinase and cyclic 3′,5′-AMP: significance of binding and activation constants. Biochim. biophys. Acta (Amst.) 364, 250–259 (1974).
Tada, M., Kirchberger, M.A., Repke, D.I., Katz, A.M.: The stimulation of calcium transport in cardiac sarcoplasmic reticulum by adenosine 3′,5′-monophosphate dependent protein kinase J. biol. Chem. 249, 6174–6180 (1974).
Tagliamonte, A., Tagliamonte, P., Forn, J., Perez-Cruet, J., Krishna, G., Gessa, G.L.: Stimulation of brain serotonin synthesis by dibutyryl cyclic AMP in rats. J. Neurochem. 18 1191–1196 (1971).
Takamori, M., Ishii, N., Mori, M.: The role of cyclic 3′,5′-adenosine monophosphate in neuromuscular transmission. Arch. Neurol. 29, 420–424 (1973).
Tamarind, D.C., Quilliam, J.P.: Synaptic organization and other ultrastructural features of the superior cervical ganglion of the rat, kitten and rabbit. Micron 2, 204–234 (1971).
Teshima, Y., Yamazaki, R., Kakiuchi, S.: Effects of ATP on the activity of nucleoside 3′,5′-cyclic monophosphate phosphodiesterase from brain. J. Neurochem. 22, 789–791 (1974).
Thierry, A.M., Blanc, G., Sobel, A., Stinus, L., Glowinski, J.: Dopaminergic terminals in the rat cortex. Science 182, 499–501 (1973).
Thoenen, H.: Induction of tyrosine hydroxylase in peripheral and central adrenergic neurones by cold exposure of rats. Nature (Lond.) 228, 861–862 (1970).
Thoenen, H., Mueller, R.A., Axelrod, J.: Trans-synaptic induction of adrenal tyrosine hydroxylase. J. Pharmacol. exp. Ther. 169, 249–254 (1969).
Thoenen, H., Otten, U., Oesch, F.: Trans-synaptic regulation of tyrosine hydroxylase. In: Frontiers in Catecholamine Research. New York: Pergamon Press 1974.
Thompson, W.J., Appleman, M.M.: Multiple cyclic nucleotide phosphodiesterases activities from rat brain. Biochemistry (Wash.) 10, 311–316 (1971).
Tomita, T., Sakamoto, Y., Ohba, M.: Conductance increase by adrenaline in guinea pig taenia coli studied with voltage clamp method. Nature (Lond.) 250, 432 (1974).
Triggle, D.J.: Neurotransmitter-receptor Interactions. New York: Academic Press 1971.
Tsien, R.W.: Adrenaline-like effects of intracellular iontophoresis of cyclic AMP in cardiac Purkinje fibres. Nature (Lond.) 245, 120–122 (1973).
Tsien, R.W., Giles, W., Greengard, P.: Cyclic AMP mediates the effects of adrenaline on cardiac Purkinje fibers. Nature (Lond.) 240, 181–183 (1972).
Tsien, R.W., Weingart, R.: Cyclic AMP: Cell-to-cell movement and inotropic effect in ventricular muscle, studied by a cut-end method. J. Physiol. (Lond.) 242, 95–96 (1974).
Tsou, K.C., Yip, K.F., Lo, K.W.: 1,N6 Etheno-2-aza-adenosine 3′,5′-monophosphate: a new fluorescent substrate for cycle nucleotide phosphodiesterase. Analyt. Biochem. 60, 163–169 (1974).
Ueda, T., Maeno, H., Greengard, P.: Regulation of endogenous phosphorylation of specific proteins in synaptic membrane fractions from rat brain by adenosine 3′,5′-monophosphate. J. biol. Chem. 248, 8295–8305 (1973).
Ungerstedt, U.: Stereotaxic mapping of the monoamine pathways in rat brain. Acta physiol. scand. 67, 1–48 (1971).
Uzunov, P., Revuelta, A., Costa, E.: A role for the endogenous activator of 3′,5′-nucleotide phosphodiesterase in rat adrenal medulla. Molec. Pharmacol. (in press, 1975).
Uzunov, P., Shein, H.M., Weiss, B.: Cyclic AMP phosphodiesterase in cloned astrocytoma cells: norepinephrine induces a specific enzyme form. Science 180, 304–306 (1973).
Uzunov, P., Shein, H.M., Weiss, B.: Multiple forms of cyclic 3′,5′-AMP phosphodiesterase of rat cerebrum and cloned astrocytoma and neuroblastoma cells. Neuropharmacol. 13, 377–391 (1974).
Uzunov, P., Weiss, B.: Effects of phenothiazine tranquillizers on the cyclic 3′,5′-adenosine monophosphate system of rat brain. Neuropharmacol. 10, 697–708 (1971).
Uzunov, P., Weiss, B.: Psychopharmacological Agents and the cyclic AMP system of rat brain. In: Advances in Cyclic Nucleotide Research, vol. 1. New York: Raven Press 1972.
Vassalle, M., Barnabel, O.: Norepinephrine and potassium fluxes in cardiac Purkinje fibers. Pflügers Arch. 322, 287–303 (1971).
Veech, R.L., Harris, R.L., Veloso, D., Veech, E.H.: Freezeblowing: a new technique for the study of brain in vivo. J. Neurochem. 20, 183–188 (1973).
Vellis, J. de, Brooker, G.: Reversal of catecholamine refractoriness by inhibitors of RNA and protein synthesis. Science 186, 1221–1222 (1974).
Verma, S.C., McNeill, J.H.: Action of imidazole on the cardiac inotropic, Phosphorylase activating and cyclic AMP producing effects of norepinephrine and histamine. Res. Commun. Chem. Pathol. Pharmacol. 7, 305–319 (1974).
Vesin, M.F., Harbon, S.: The effect of epinephrine, prostaglandins, and their antagonists on adenosine cyclic 3′,5′-monophosphate concentrations and motility of the rat uterus. Molec. Pharmacol. 10, 457–473 (1974).
Voaden, M.J.: The effects of superior cervical ganglionectomy and/or bilateral adrenalectomy on the mitotic acitivity of the adult rat cornea. Exp. Eye Res. 12, 337–341 (1971).
Vokaer, A., Iacobelli, S., Kram, R.: Phosphoprotein phosphatase activity associated with estrogen-induced protein in rat uterus. Proc. nat. Acad. Sci. (Wash.) 71, 4482–4486 (1974).
Volicer, L., Gold, B.I.: Effect of ethanol on cyclic AMP levels in the rat brain. Life Sci. 13, 269–280 (1973).
von Hungen, K., Roberts, S.: Catecholamine and Ca2+ activation of adenylate cyclase systems in synaptosomal fractions from rat cerebral cortex. Nature (Lond.) 242, 58–60 (1973).
von Hungen, K., Roberts, S.: Neurotransmitter-sensitive adenylate cyclase systems in the brain. In: Reviews of Neuroscience, vol. 1. New York: Raven Press 1974.
Wagner, R.C., Bitensky, M.W.: Adenylate Cyclase. In: Electron Microscopy of Enzymes. New York: Van Nostrand, Rienhold Co. 1974.
Wagner, R.C., Kriener, P., Barrnett, R.J., Bitensky, M.W.: Biochemical characterization and cytochemical localization of a catecholamine-sensitive adenylate cyclase in isolated capillary endothelium. Proc. nat. Acad. Sci. (Wash.) 69, 3175–3180 (1972).
Walker, J.B., Walker, J.P.: Neurohumoral regulation of adenylate cyclase activity in rat striatum. Brain Res. 54, 386–390 (1973a).
Walker, J.B., Walker, J.P.: Properties of adenylate cyclase from senescent rat brain. Brain Res. 54, 391–396 (1973b).
Walsh, D.A., Perkins, J.P., Krebs, E.G.: An adenosine 3′,5′ monophosphate dependent protein kinase from rabbit skeletal muscle. J. biol. Chem. 243, 3763–3765 (1968).
Watanabe, A.M., Besch, H.R. Jr.: Cyclic adenosine monophosphate modulation of slow calcium influx channels in guinea pig heart. Circulat. Res. 35, 316–324 (1974).
Waymire, J.C., Weiner, N., Prasad, K.N.: Regulation of tyrosine hydroxylase activity in cultured mouse neuroblastoma cells: elevation induced by analogs of adenosine 3′,5′ cyclic monophosphate. Proc. nat. Acad. Sci. (Wash.) 69, 2241–2245 (1972).
Weber, A., Murray, J.M.: Molecular control mechanisms in muscle contraction. Physiol. Rev. 53, 612–673 (1973).
Wedner, H.J., Hoffer, B.J., Battenberg, E., Steiner, A.L., Parker, C.W., Bloom, F.E.: A method for detecting intracellular cyclic adenosine monophosphate by immunofluorescence. J. Histochem. Cytochem. 20, 293–295 (1972).
Weight, F.F.: Mechanisms of synaptic transmission. Neurosci. Res. Program Bull. 4, 1–27 (1971).
Weight, F.F.: Physiological mechanisms of synaptic modulation. In: The Neurosciences: 3rd Study Program. Cambridge: MIT Press 1974.
Weight, F.F., Padjen, A.: Acetylcholine and slow synaptic inhibition in frog sympathetic ganglion cells. Brain Res. 55, 225–228 (1973a).
Weight, F.F., Padjen, A.: Slow synaptic inhibition: evidence for synaptic inactivation of sodium conductance in sympathetic ganglion cells. Brain Res. 55, 219–224 (1973b).
Weight, F.F., Petzold, G., Greencard, P.: Guanosine 3′,5′-monophosphate in sympathetic ganglia: increase associated with synaptic transmission. Science 186, 942–944 (1974).
Weight, F.F., Votava, J.: Slow synaptic excitation in sympathetic ganglion cells: evidence for synaptic activation of potassium conductance. Science 170, 755–758 (1970).
Weinrub, I., Chasin, M., Free, C.A., Harris, D.N., Goldenberg, H., Michel, I.M., Palk, U.S., Phillips, M., Samaniego, S., Hess, S.M.J.: Effects of therapeutic agents on cyclic AMP metabolism in vitro. J. pharm. Sci. 61, 1556–1657 (1972).
Weiss, B.: Psychopharmacological agents and the cyclic AMP system of rat brain. In: Advances in Cyclic Nucleotide Research, vol. 1. New York: Raven Press 1972.
Weiss, B., Costa, E.: Regional and subcellular distribution of adenyl cyclase and 3′,5′-cyclic nucleotide phosphodiesterase in brain and pineal gland. Biochem. Pharmacol. 17, 2107–2116 (1968).
Weiss, B., Kidman, A.D.: Neurobiological significance of cyclic 3′,5′-adenosine monophosphate. Advanc. Biochem. Psychopharmacol. 1, 132–164 (1969).
Weller, M., Rodnight, R.: Stimulation by cyclic AMP of intrinsic protein kinase activity in ox brain membrane preparations. Nature (Lond.) 225, 187–188 (1970).
Werman, R.: CNS cellular level: membranes. Ann. Rev. Physiol. 34, 337–374 (1972).
White, A.A., Aurbach, G.D.: Detection of guanyl cyclase in mammalian tissues. Biochim. biophys Acta (Amst.) 191, 686–697 (1969).
Whitfield, J.F., Rixon, R.H., McManus, J.P., Balk, S.D.: Calcium, cyclic adenosine 3′,5′-monophosphate, and the control of cell proliferation: a review. In Vitro. 8, 257–278 (1973).
Wicks, W.D.: Regulation of protein synthesis by cyclic AMP. In: Advances in Cyclic Nucleotide Research, vol. 4. New York: Raven Press 1974.
Wickson, R.D., Boudreau, R.J., Drummond, G.I.: Activation of 3′,5′-cyclic adenosine monophosphate phosphodiesterase by calcium ion and a protein activator. Biochemistry (Wash.) 14, 669–675 (1975).
Will, H., Schirpke, B., Wollenberger, A.: Binding of calcium to a cell membrane-enriched preparation from pig myocardium: increase in calcium affinity upon membrane protein phosphorylation enhanced by a membrane-bound cyclic AMP dependent protein kinase. Acta biol. med. germ. 31, 45–52 (1973).
Williams, B.J., Pirch, J.H.: Correlation between brain adenyl cyclase activity and spontaneous motor activity in rats after chronic reserpine treatment. Brain Res. 68, 227–234 (1974).
Williams, M., Rodnight, R.: Evidence for a role for protein phosphorylation in synaptic function in the cerebral cortex mediated through a β-noradrenergic receptor. Brain Res. 77, 502–506 (1974).
Williams, R.H., Thompson, W.J.: Effect of age upon guanyl cyclase, adenyl cyclase, and cyclic nucleotide phosphodiesterases in rats. Proc. Soc. exp. Biol. (N.Y.) 143, 382–387 (1973).
Williams, T.H., Palay, S.L.: Ultrastructure of the small neurons in the superior cervical ganglion. Brain Res. 15, 17–34 (1969).
Wilson, D.F.: The effects of dibutyryl cyclic adenosine 3′,5′-monophosphate, theophylline, and aminophylline on neuromuscular transmission in the rat. J. Pharmacol. exp. Ther. 188, 447–452 (1974).
Wilson, D.F., Stubbs, M., Veech, R.L., Erecinska, M., Krebs, H.A.: Equilibrium relations between the oxidation-reduction reactions and the adenosine triphosphate synthesis in suspensions of isolated liver cells. Biochem. J. 140, 57–64 (1974).
Woodward, D.J., Hoffer, B.J., Altman, J.: Physiological and pharmacological properties of Purkinje cells in rat cerebellum degranulated by postnatal X-irradiation. J. Neurobiol. 5, 283–304 (1974).
Yarbrough, G.G., Lake, N., Phillis, J.W.: The role of calcium in monoamine induced depression of cerebral cortical neurones. Life Sci. 13, 703–711 (1973).
Yokota, R.: The granule-containing cell somata in the superior cervical ganglion of the rat, as studied by a serial sampling method for electron microscopy. Z. Zellforsch. 141, 331–346 (1973).
York, D.H.: Dopamine receptor blockade: a central action of chlorpromazine on striatal neurones. Brain Res. 37, 91–99 (1972).
Yount, R.G., Bobcock, D., Ballentyne, W., Ohala, D.: Adenylyl-immidodiphosphate; an adenosine triphosphate analog containing a P-N-P linkage. Biochemistry (Wash.) 10, 2484 (1971).
Zanella, J. Jr., Rall, T.W.: Evaluation of electrical pulses and elevated levels of potassium ions as stimulants of adenosine 3′,5′-monophosphate (cyclic AMP) accumulation in guinea pig brain. J. Pharmacol. exp. Ther. 186, 241–252 (1973).
Zigmond, R.E., Schon, F., Iversen, L.L.: Increased tyrosine hydroxylase activity in the locus coeruleus of rat brain stem after reserpine treatment and cold stress. Brain Res. 70, 547–552 (1974).
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1975 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Bloom, F.E. (1975). The Role of Cyclic Nucleotides in Central Synaptic Function. In: The Role of Cyclic Nucleotides in Central Synaptic Function / Renal Transport of Amino Acids. Reviews of Physiology, Biochemistry and Pharmacology, vol 74 . Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-35091-1_1
Download citation
DOI: https://doi.org/10.1007/978-3-662-35091-1_1
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-34770-6
Online ISBN: 978-3-662-35091-1
eBook Packages: Springer Book Archive