Abstract
Three types of catecholamine-storing vesicles have been characterized: (1) the chromaffin granules from adrenal medulla (2) the large dense core vesicles of sympathetic nerves and (3) the small dense core vesicles, which are also found in these nerves. The composition and molecular organization of chromaffin granules have been analyzed in great detail (see Winkler and Westhead 1980, Winkler and Carmichael 1982). The large dense core vesicles of sympathetic nerve closely resemble chromaffin granules in their biochemical composition and in their functional properties (Klein 1982). In addition it has become obvious that several features of these catecholamine-storing vesicles are of more general significance. As we will discuss below, the peptides present in the content of chromaffin granules, the chromagranins and neuropeptides, have a widespread distribution in endocrine and nervous tissues. Thus studies on their biosynthesis and their function have relevance not only for the adrenal medulla, but, e.g., also for large dense core vesicles in brain containing nonadrenergic transmitters.
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References
Aberer W, Stitzel R, Winkler H, Huber E (1979) Accumulation of 3H-ATP in small dense core vesicles of superfused vasa deferentia. J Neurochem 33:797–801
Anderson DC, King SC, Parsons SM (1982) Proton gradient linkage to active uptake of 3H acetylcholine by Torpedo electric organ synaptic vesicles. Biochemistry 21:3037–3043
Apps DK, Pryde JG, Phillips JH (1980) Cytochrome b-561 is identical with chromomembrin B, a major polypeptide of chromaffin granule membranes. Neuroscience 5:2279–2287
Apps DK, Phillips JH, Purves FC (1985) Glycoproteins of the chromaffin-granule matrix. Neuroscience 16:477–487
Blaschko H, Comline RS, Schneider FH, Silver M, Smith AD (1967) Secretion of a chromaffin granule protein, chromogranin from the adrenal gland after splanchnic stimulation. Nature (London) 215:58–59
Cohn DV, Zangerle R, Fischer-Colbrie R, Chu LLH, Elting JJ, Hamilton JW, Winkler H (1982) Similarity of secretory protein I from parathyroid gland to chromogranin A from adrenal medulla. Proc Natl Acad Sci USA 79:6056–6059
Cohn DV, Elting JJ, Frick M, Elde R (1984) Selective localization of the parathyroid secretory protein-I/adrenal medulla chromogranin A protein family in a wide variety of endocrine cells of the rat. Endocrinology 114:1963–1974
Comb M, Seeburg PH, Adelman J, Eiden L, Herbert E (1982) Primary structure of the human Met- and Leu-enkephalin precursor and its mRNA. Nature (London) 295:663–666
Douglas WW (1986) Stimulus-secretion coupling: the concept and clues from chromaffin and other cells. Br J Pharmacol Chemother 34:451–474
Dowd DJ, Edwards C, Englert D, Mazurkiewicz JE, Ye HZ (1983) Immunofluorescent evidence for exocytosis and internalization of secretory granule membrane in isolated chromaffin cells. Neuroscience 10:1025–1033
Falkensammer G, Fischer-Colbrie R, Richter K, Winkler H (1985a) Cell-free and cellular synthesis of chromogranin A and B of bovine adrenal medulla. Neuroscience 14:735–746
Falkensammer G, Fischer-Colbrie R, Winkler H (1985b) Biogenesis of chromaffin granules: Incorporation of sulphate into chromogranin B and into a proteoglycan. J Neurochem 45:1475–1480
Fischer-Colbrie R, Diez-Guerra J, Emson PC, Winkler H (1986) Bovine chromaffin granules: Immunological studies with antisera against neuropeptide y, met-enkephalin and bombesin. Neuroscience, in press
Fischer-Colbrie R, Frischenlager I (1985) Immunological characterization of secretory proteins of chromaffin granules: Chromogranins A, chromogranins B and enkephalin-containing peptides. J Neurochem 44:1854–1861
Fischer-Colbrie R, Lassmann H, Hagn C, Winkler H (1985) Immunological studies on the distribution of chromogranin A and B in endocrine and nervous tissues. Neuroscience, in press
Fischer-Colbrie R, Schachinger M, Zangerle R, Winkler H (1982) Dopamine β-hydroxylase and other glycoproteins from the soluble content and the membranes of adrenal chromaffin granules: Isolation and carbohydrate analysis. J Neurochem 38:725–732
Fischer-Colbrie R, Zangerle R, Frischenschlager I, Weber A, Winkler H (1984) Isolation and immunological characterization of a glycoprotein from adrenal chromaffin granules. J Neurochem 42:1008–1016
Fleminger G, Ezra E, Kilpatrick DL, Udenfriend S (1983) Processing of enkephalin-containing peptides in isolated bovine adrenal chromaffin granules. Proc Natl Acad Sci USA 80:6418–6421
Fricker LD, Snyder SH (1983) Purification and characterization of enkephalin convertase, an enkephalin-synthesizing carboxypeptidase. J Biol Chem 258:10950–10955
Fried G (1978) Cytochrome b-561 in sympathetic nerve terminal vesicles from rat vas deferens. Biochim Biophys Acta 507:175–177
Fried G (1980) Small noradrenergic storage vesicles isolated from rat vas deferens-biochemical and morphological characterization. Acta Physiol Scand Suppl 493:1–28
Fried G (1981) Noradrenaline release and uptake in isolated small dense cored vesicles from rat seminal ducts. Acta Physiol Scand 112:41–46
Geissler D, Martinek A, Margolis RU, Margolis RK, Skrivanek JA, Ledeen R, König P, Winkler H (1977) Composition and biogenesis of complex carbohydrates of ox adrenal chromaffin granules. Neuroscience 2:685–693
Gubler U, Seeburg P, Hoffman BJ, Gage LP, Udenfriend S (1982) Molecular cloning establishes proenkephalin as precursor of enkephalin-containing peptides. Nature (London) 295:206–208
Hamill OP, Marty A, Neher E, Sakmann B, Sigworth FJ (1981) Improved patch clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pfluegers Arch 391:85–100
Helle KB (1971) Biochemical studies of the chromaffin granule-II. Properties of membrane-bound and water-soluble forms of chromogranin A and dopamine 3-hydroxylase activity. Biochim Biophys Acta 245:94–104
Herzog V (1981) Endocytosis in secretory cells. Philos Trans R Soc London Ser B 296:67–72
Hille A, Rosa P, Huttner WB (1984) Tyrosine sulfation: a post-translational modification of proteins destined for secretion? FEBS Lett 177:129–134
Hörtnagl H, Lochs H, Winkler H (1974) Immunological studies on the acidic chromogranins and on dopamine β-hydroxylase (E.C.1.14.2.1) of bovine chromaffin granules. J Neurochem 22:197–199
Holtzman E, Dominitz R (1968) Cytochemical studies of lysosomes, golgi apparatus and endoplasmatic reticulum in secretion and protein uptake by adrenal medulla cells of the rat. J Histochem Cytochem 16:320–336
Hook VYH (1984) Carboxypeptidase B-like activity for the processing of enkephalin precursors in the membrane component of bovine and adrenomedullary chromaffin granules. Neuropeptides 4:117–126
Johnson RG, Scarpa A (1981) The electron transport chain of serotonin-dense granules of platelets. J Biol Chem 256:11966–11969
Kemper B, Habener JF, Rich A, Potts Jr JT (1974) Parathyroid secretion: discovery of a major calcium-dependent protein. Science 184:167–169
Kiang W-L, Krusius T, Finne J, Margolis RU, Margolis RK (1982) Glycoproteins and proteoglycans of the chromaffin granule matrix. J Biol Chem 257:1651–1659
Kilpatrick L, Gavine F, Apps D, Phillips J (1983) Biosynthetic relationship between the major matrix proteins of adrenal chromaffin granules. FEBS Lett 164:383–388
Kirshner AG, Kirshner N (1969) A specific soluble protein from the catecholamine storage vesicles of bovine adrenal medulla. Biochim Biophys Acta 181:219–225
Klein RH (1982) Chemical composition of the large noradrenergic vesicles. In: Klein RL, Lagercrantz H, Zimmermann H (eds) Neurotransmitter vesicles. Academic Press, London New York, pp 133–173
Lee RWH, Huttner WB (1983) Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase. J Biol Chem 258:11326–11334
Lindberg I, Yang H-YT, Costa E (1984) Further characterization of an enkephalin-generating enzyme from adrenal medullary chromaffin granules. J Neurochem 42:1411–1419
Lingg G, Fischer-Colbrie R, Schmidt W, Winkler H (1983) Exposure of an antigen of chromaffin granules on cell surface during exocytosis. Nature (London) 301:610–611
Majzoub JA, Dee PC, Habener JF (1982) Cellular and cell-free processing of parathyroid secretory proteins. J Biol Chem 257:3581–3588
Neher E, Marty A (1982) Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells. Proc Natl Acad Sci USA 79:6712–6716
Neuman B, Wiedermann CJ, Fischer-Colbrie R, Schober M, Sperk G, Winkler H (1984) Biochemical and functional properties of large and small-dense core vesicles in sympathetic nerves of rat and ox vas deferens. Neuroscience 13:921–931
Njus D (1983) The chromaffin vesicle and the energetics of storage organelles. J Auton Nerv Syst 7:35–40
Noda M, Furutani Y, Takahashi H, Toyosato M, Hirose T, Inayama S Nakanishi S, Numa S (1982) Cloning and sequence analysis of cDNA for bovine adrenal preproenkephalin. Nature (London) 295:202–206
O’Connor DT (1983) Chromogranin: widespread immunoreactivity in polypeptide hormone producing tissues and in serum. Regul Peptides 6:263–280
O’Connor DT, Frigon RP (1984) Chromogranin A, the major catecholamine storage vesicle soluble protein. J Biol Chem 259:3237–3247
Patey G, Liston D, Rossier J (1984) Characterization of new enkephalin-containing peptides in the adrenal medulla by immunoblotting. FEBS Lett 172:303–308
Patzak A, Böck G, Fischer-Corbie R, Schauenstein K, Schmidt W, Lingg G, Winkler H (1984) Exocytotic exposure and retrieval of membrane antigens of chromaffin granules: Quantitative evaluation of immunofluorescence on the surface of chromaffin cells. J Cell Biol 98:1817–1824
Patzak A, Winkler H (1986) Exocytotic exposure and recycling of membrane antigens of chromaffin granules: Ultrastructural evaluation after immunolabeling. J Cell Biol in press
Phillips JH, Burridge K, Wilson SP, Kirshner N (1983) Visualization of the exocytosis/endocytosis secretory cycle in cultured adrenal chromaffin cells. J Cell Biol 97:1906–1917
Schultzberg M, Lundberg JM, Hökfelt T, Terenius L, Brandt J, Elde RP, Goldstein M (1978) Enkephalin like immunoreactivity in gland cells and nerve terminals of the adrenal medulla. Neuroscience 3:1169–1186
Serck-Hanssen G, O’Connor DT (1984) Immunological identification and characterization of chromogranins coded by Poly(A) mRNA from bovine adrenal medulla and pituitary gland and human phaeochromocytoma. J Biol Chem 259:11597–11600
Settleman J, Fonseca R, Nolan J, Hogue-Angeletti R (1985) Relationship of multiple forms of chromogranin. J Biol Chem 260:1645–1651
Smith AD, Winkler H (1967) Purification and properties of an acidic protein from chromaffin granules of bovine adrenal medulla. Biochem J 103:483–492
Somogyi P, Hodgson AJ, De Potter RW, Fischer-Colbrie R, Schober M, Winkler H, Chubb IW (1984) Chromogranin immunoreactivity in the central nervous system. Immunochemical characterization, distribution and relationship to catecholamine and enkephalin pathways. Brain Res Rev 8:193–230
Steiner DF, Kemmler W, Tager HS, Peterson JD (1974) Proteolytic processing in the biosynthesis of insulin and other proteins. Fed Proc 33:2105–2115
Suchard SJ, Corcoran JJ, Pressman BC, Rubin RW (1981) Evidence for secretory granule membrane recycling in cultured adrenal chromaffin cells. Cell Biol Int Rep 5:953–962
Udenfriend S, Kilpatrick DL (1983) Biochemistry of the enkephalins and enkephalin-containing peptides. Arch Biochem Biophys 221:309–323
Wildman J, Dewair M, Matthaei H (1981) Immunochemical evidence for exocytosis in isolated chromaffin cells after stimulation with depolarizing agents. J Neuroimmunol 1:353–364
Wilson BS, Lloyd RV (1984) Detection of chromogranin in neuroendocrine cells with a monoclonal antibody. Am J Pathol 115:458–468
Winkler H, Apps DK, Fischer-Colbrie R (1986) The molecular function of adrenal chromaffin granules. Neuroscience, in press
Winkler H, Carmichael SW (1982) The chromaffin granule. In: Poisner AM, Trifaro JM (eds) The secretory granule. Elsevier Biomed Press, Amsterdam, pp 3–79
Winkler H, Westhead E (1980) The molecular organization of adrenal chromaffin granules. Neuroscience 5:1803–1823
Winkler H, Schöpf JAL, Hörtnagl H, Hörtnagl H (1972) Bovine adrenal medulla: subcellular distribution of newly synthesized catecholamines, nucleotides and chromogranins. Naunyn-Schmiedebergs Arch Exp Pathol Pharmakol 273:43–61
Winkler H, Falkensammer G, Patzak A, Fischer-Colbrie R, Schober M, Weber A (1984) Life cycle of the catecholaminergic vesicles: From biogenesis to secretion. In: Vizi ES, Magyar K (eds) Regulation of transmitter function: Basic and clinical aspects. Akadémiai Kiadó, Budapest, pp 65–73
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Winkler, H., Fischer-Colbrie, R. (1985). Catecholamine-Storing Vesicles: From Biosynthesis to Exo/Endocytosis. In: Hamprecht, B., Neuhoff, V. (eds) Neurobiochemistry. Colloquium der Gesellschaft für Biologische Chemie 18.–20. April 1985 in Mosbach/Baden, vol 36. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70940-1_9
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DOI: https://doi.org/10.1007/978-3-642-70940-1_9
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