Abstract
The response of renal cells to extracellular signals has recently attracted increasing experimental evaluation. The cellular response to a variety of peptide hormones, neurotransmitters and growth factors are fundamental to understanding how the signals mediated by circulatory substances, which interact with cell surface receptors, produce their effects intracellularly. The cellular responses to a wide variety of signal molecules are somewhat limited. Occupancy of receptors initiates the production of intracellular messengers including cAMP, cGMP and the second messenger molecules derived from phosphoinositides (1–3). The phosphoinositides constitute 5–8% of lipids in the cell membranes of eukaryotic cells and are essential for cell viability (4). These phosphoinositides are storage forms for the messenger molecules that transmit signals across the cell membrane and evoke responses to extracellular signals.
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
Y. Nishizuka, Studies and perspectives of protein kinase C, Science 233:305–312 (1986).
M.J. Berridge and R.F. Irvine, Inositol trisphosphate, a novel second messenger in signal transduction, Nature (London) 312:315–321 (1984).
P.N. Majerus, T.M. Connolly, H. Deckmyer, T.S. Ross, T.E. Bross, H. Ishii, V.S. Bansal, D.B. Wilson, The metabolism of phosphoinositide-derived messenger molecule, Science 234:1519–1526 (1986).
J. Esko and C.R.H. Raetz, Mutants of Chinese hamster ovary cells with altered membrane phospholipid composition, J. Biol. Chem. 255:4474–4480 (1980).
S. Shin, Y. Fujiwara, A. Wada, T. Takama, Y. Orita, T. Kamada, K. Tagawa, Angiotensin II-induced increase in inositol 1, 4, 5-trisphosphate in cultured rat mesangial cells: evidence by refined High Performance Liquid Chromatography, BBRC 142:70–77 (1987).
J.E. Benabe, L.A. Spry, A.R. Morrison, Effects of angiotensin II on phosphatidylinositol and polyphosphatidylinositol turnover in rat kidney, J. Mol. Chem. 257:7430–7434 (1982).
J.A. Shayman and A.R. Morrison, Bradykinin-induced changes in phosphatidylinositol turnover in cultured rabbit papillary collecting tubule cells, J. Clin. Invest. 76:978–984 (1985).
D. Portilla and A.R. Morrison, Bradykinin-induced changes in inositol trisphosphate mass in MDCK cells, BBRC 140:644–649 (1986).
D.A. Troyer, J.I. Kreisberg, D.W. Schwertz, M. Venkatachalam, Effects of vasopressin on phosphoinositide and prostaglandin production in cultured mesangial cells.
K.A. Hruska, M. Goligorsky, J. Schoble, M. Tsutsumi, S. Westbrook, D. Moskowitz, Effects of parathyroid hormone on cytosolic calcium in renal proximal tubule primary cultures, Am. J. Physiol. 251:F188–F198 (1986).
M.S. Goligorsky, D.J. Loftus, K.A. Hruska, Cytoplasmic calcium in individual proximal tubular cells in culture, Am. J. Physiol. 251:F938–F944 (1986).
S.L. Hofmann and P.W. Majerus, Purification and properties of phosphatidylinositol specific phospholipase C from sheep seminal vesicular glands, J. Biol. Chem. 257:6461–6467 (1982).
M.G. Low, R.C. Carroll, W.B. Weglicki, Multiple forms of phosphoinositide-specific phospholipase C of different relative molecular masses in animal tissue, Biochem. J. 221:813–820 (1984).
M.G. Low, R.C. Carroll, A.C. Cox, Characterization of multiple forms of phosphoinositide-specific phospholipase C purified from human platelets, Biochem. J. 237:139–145 (1986).
S. Cockcroft, The dependence on Ca2+ of the guanine-nucleo tide-activated polyphosphoinositide phosphodiesterase in neutrophil plasma membrane, Biochem. J. 240:503–507 (1986).
S. Cockcroft, J.A. Taylor, Fluoroaluminates mimic guanosine 5′[γ-thio]-triphosphate in activating the polyphosphoinositide phosphodiesterase of hepatocyte membranes, Biochem. J. 241:409–414 (1987).
D.B. Wilson, T.E. Bross, S.L. Hoffmann, P.W. Majerus, Hydrolysis of polyphosphoinositides by purified sheep seminal vesicle phospholipase C enzymes, J. Biol. Chem. 259:11718–11724 (1984).
R.M. Dawson, N. Freinkel, F.B. Jungalwala, N. Clarke, The enzymatic formation of myoinositol 1,2 cyclic phosphate from phosphatidylinositol, Biochem. J. 122:605–607 (1971).
P.W. Majerus, T.M. Connolly, H. Deckmyn, T.S. Ross, T. E. Bross, H. Ishii, V.S. Bansal, D.B. Wilson, The metabolism of phosphoinositide devoid messenger molecules, Science 234:1519–1526 (1986).
J.A. Shayman, R.J. Auchus, A.R. Morrison, Bradykinin-induced changes in myo-inositol 1,2 (cyclic) phosphate in rabbit papillary collecting tubule cells, Biochem. Biophys. Acta. 888:171–175 (1986).
D.B. Wilson, T.E. Bross, W.R. Sherman, R.A. Berger, P.W. Majerus, Inositol cyclic phosphates are produced by cleavage of phosphatidylphos-phoinositols (polyphosphoinositide) with purified sheep seminal vesicle phospholipase C enzymes, Proc. Natl. Acad. Sci. 82:4013–4017 (1985).
D.B. Wilson, T. Connolly, T.E. Bross, P.W. Majerus, W.R. Sherman, A. Tyler, L.J. Rubin, J.E. Brown, Isolation and characterization of the inositol cyclic phosphate products of polyphosphoinositide cleavage by phospholipase C, J. Biol. Chem. 260:13496–13581 (1985).
R.F. Irvine, A.J. Letcher, D.J. Lander, M.S. Berridge, Specificity of inositol phosphate-stimulated Ca2+ mobilization from Swiss mouse 3T3 cells, Biochem. J. 240:301–304 (1986).
F.A. O’Rourke, S.P. Halenda, G.B. Zavoico, M.B. Feinstein, Inositol 1, 4, 5 trisphosphate releases Ca2+ from a Ca2+ -transporting membrane vesicle fraction derived from human platelets, J. Biol. Chem. 260:956–962 (1985).
I.R. Batty, S.R. Nahorski, R.F. Irvine, Rapid formation of inositol 1, 3, 4, 5 tetrakis phosphate following muscarinic receptor stimulation of rat cerebral cortical slices, Biochem. J. 232:211–215 (1985).
R.F. Irvine, A.J. Letcher, J.P. Heslop, M.J. Berridge, The inositol tris/tetrakisphosphate pathway — demonstration of Ins(1, 4, 5)P33-kinase activity in animal tissues, Nature (London) 320:631–634 (1986).
C.A. Hansener, S. Mah, J.R. Williamson, Formation and metabolism of inositol 1, 3, 4, 5 tetrakisphosphate in liver, J. Biol. Chem. 261: 8100–8103 (1986).
R.F. Irvine, A.J. Letcher, D.J. Lander, J.P. Heslop, M.J. Berridge, Inositol(3, 4) bisphosphate and inositol(l,3) bisphosphate in GH4 cells — evidence for complex breakdown of inositol(1, 3, 4) bisphosphate, BBRC 143:353–359 (1987).
R.C. Inborn, V.S. Bansal, P.W. Majerus, Pathway for inositol 1, 3, 4 trisphosphate and 1,4 bisphosphate metabolism, Proc. Natl. Acad. Sci. 84: 2170–2174 (1987).
C.D. Downes, M.C. Mussat, R.H. Michell, The inositol trisphosphate Phosphomonoesterase of the human erythrocyte membrane, Biochem. J. 203: 169–177 (1982).
G.J. Tertoolen, B.C. Tilly, R.F. Irvine, W.H. Moolenaar, Electrophysiological responses to bradykinin and microinjected polyphosphates in neuroblastoma cells. Possible role of inositol 1,3,A trisphosphate in altering membrane potential, FEBS Lett. 214:365–369 (1987).
R.F. Irvine and R.M. Moor, Microinjection of inositol 1, 3, 4, 5 tetrakisphosphate activates sea urchin eggs by a mechanism dependent in external Ca2+, Biochem. J. 240:917–920 (1986).
M.D. Honsay, Egg activation unscrambles a potential role for IP4, TIBS 12:133–134 (1987).
Y. Takai, U. Kikkawa, Y. Kaibuchi, Y. Nishizuka, Membrane phospholipid metabolism and signal transduction for protein phosphorylation, Adv. Cyclic Nucl. Protein Phos. Res. 18:119–158 (1984).
A.M. Speigel, Signal transduction by guanine nucleotide binding proteins, Molecular and Cellular Endocrinology 49:1–16 (1987).
M. Oinuma, T. Katuda, M. Ui, A new GTP-binding protein in differentiated Human Leukenic (HL-60) cells serving as the specific substrate of islet activating protein pertussis toxin, J. Biol. Chem. 262:8347–8353 (1987).
I. Magnaldo, H. Talwar, W.D. Anderson, J. Pouyssegur, Evidence for a GTP-binding protein coupling thrombin receptor to PIP2-phospho-lipase C in membranes of hamster fibroblasts, FEBS Lett. 210:6–10 (1987).
S. Cockcroft, The dependence on Ca2+ of the guanine nucleotide-activated polyphosphoinositide phosphodiesterase in neutrophil plasma membranes, Biochem. J. 240:503–507 (1986).
G.M. Bokoch and A.G. Gilman, Inhibition of receptor-mediated release of arachidonic acid by pertussis toxin, Cell 39:301–308 (1984).
P.C. Grenier, T.E. Rollins, W.L. Smith, Kinin induced prostaglandin synthesis by renal papillary collecting tubule cells in culture, Am. J. Physiol. F94–F104 (1981).
J.A. Shayman, K. Hruska, A.R. Morrison, Bradykinin stimulates increased intracellular calcium in papillary collecting tubules of the rabbit, Biochem. Biophys. Res. Comm. 134:299–306 (1986).
P.C. Isakson, A. Raz, S.E. Denny, A. Wyche, P. Needleman, Hormonal stimulation of arachidonate release from isolated perfused organs: relationship to prostaglandin biosynthesis, Prostaglandins 14:853–871 (1977).
J.A. Shayman, R.J. Auchas, A.R. Morrison, Bradykinin-induced changes in myoinositol 1,2(cyclic) phosphate in rabbit papillary collecting tubule cells, Biochem. Biophys. Acta. 888:171–175 (1986).
R.M. Zusman, J.R. Keiser, J.E. Handler, Vasopressin-stimulated prostaglandin E biosynthesis in the toad urinary bladder, J. Clin. Invest. 60:1339–1347 (1977).
J.E. Bisordi, D. Schlondorff, R.M. Hayes, Interaction of vasopressin and prostaglandins in the toad urinary bladder, J. Clin. Invest. 66: 1200–1210 (1980).
J.M. Forrest, C.J. Schneider, D.B. Goodman, Role of prostaglandin E2 in mediating the effects of pH on the hydrosomotic response to vasopressin in the toad urinary bladder, J. Clin. Invest. 69:499–506 (1982).
R.M. Burch and P.V. Halushka, Vasopressin stimulates prostaglandin and thromboxane synthesis in toad bladder epithelial cells, Am. J. Physiol. 243:F593–F597 (1982);
M. Sato and M. Dunn, Interactions of vasopressin, prostaglandins, and cAMP in rat renal papillary collecting tubule cells in culture, Am. J. Physiol. 247:F423–F433 (1984).
A. Garcia-Perez and W.L. Smith, Use of monoclonal antibodies to isolate cortical collecting tubule cells: AVP induces PGE release, Am. J. Physiol. 244:C211–C220 (1983).
M. Kirschenbaum, A.G. Lower, W. Trizma, L.G. Fine, Regulation of vasopressin action by prostaglandins, J. Clin. Invest. 70:1193–1204 (1982).
B.M. Altura, Selective microvascular constrictor actions of some neurohypophyseal peptides, Eur. J. Pharmacol. 24:43–60 (1973).
B.M. Altura and B.T. Altura, Actions of vasopressin, oxytocin, and synthetic analogs on vascular smooth muscle, Fed. Proc. 43:80–86 (1984).
J. Grantham and J. Orloff, Effect of prostaglandin E1 on the permeability response of the isolated collecting tubule to vasopressin, adenosine 3′-5′-monophosphate, and theophylline, J. Clin. Invest. 47:1154–1161 (1968).
S.Z. Katasic, J.T. Shepherd, P.M. Van Loutte, Vasopressin causes endothelium -dependent relaxations of the canine basilar artery, Circ. Res. 55:575–579 (1984).
T. Nabika, P.A. Velletri, W. Lovenberg, M. Beaven, Increase in cytosolic calcium and phosphoinositide metabolism induced by angiotensin II and [Arg]vasopressin in vascular smooth muscle cells, J. Biol. Chem. 260:4661–4670 (1985).
D. Rhodes, V. Prpic, J.H. Exton, P.F. Blackmore, Stimulation of phosphatidylinositol 4,5-bisphosphate hydrolysis in hepatocytes by vasopressin, J. Biol. Chem. 258:2770–2773 (1983).
J.R. Williamson, R.H. Cooper, K.J. Suresh, A.L. Thomas, Inositol trisphosphate and diacylglycerol as intracellular second messengers in liver, Am. J. Physiol. 248:C203–C216 (1985).
S.N. Prescott and P.W. Majerus, Characterization of 1, 2-diacylglycerol hydrolysis in human platelets, J. Biol. Chem. 258:764–769 (1983).
L.M. Hallacher and W.R. Sherman, The effects of lithium ion and other agents on the activity of myoinositol-1-phosphatase from bovine brain, J. Biol. Chem. 255:10896–10901 (1980).
L.R. Chase and G.D. Aurbach, Parathyroid function and renal excretion of 3′5′ adenylic acid, Proc. Natl. Acad. Sci. USA 58:518–525 (1967).
D. Charbardes, M. Imbert, A. Clique, M. Montegut, F. Morel, PTH-sensitive adenylate cyclase activity of the rabbit nephron, Pflugers Arch. 354:229 (1975).
Z.S. Agus, L.B. Gardner, L.H. Beck, M. Goldberg, Effects of parathyroid hormone on renal tubular reabsorption of calcium, sodium and phosphate, Am. J. Physiol. 224:1143–1148 (1973).
K. Kurokawa, T. Ohno, H. Rasmussen, Ionic control of renal gluconeogenesis II. Effects of Ca2+ and H+ upon response to parathyroid hormone and cyclic AMP, Biochim. Biophys. Acta. 313:32–41 (1973).
Z.S. Agus, J.B. Puschett, D. Senesky, M. Goldberg, Mode of action of parathyroid hormone and cyclic adenosine 3′5′-monophosphate on renal tubular phosphate reabsorption in the dog, J. Clin. Invest. 50:617–626 (1971).
M.R. Hammerman and K.A. Hruska, Cyclic AMP-dependent protein phosphorylation in canine renal brush-border membrane vesicles is associated with decreased phosphate transport, J. Biol. Chem. 257:992–999 (1982).
M.R. Hammerman, V.A. Hansen, J.J. Morrissey, Cyclic AMP-dependent protein phosphorylation and dephosphorylation alter phosphate transport in canine renal brush border vesicles, Biochim. Biophys. Acta. 755: 10–16 (1983).
N. Yanagawa and O.D. Jo, Possible role of calcium mediators in parathyroid hormone action on phosphate transport in rabbit renal brush border membrane, BBRC 128:278–284 (1985).
N. Yanagawa and O.D. Jo, Possible role of calcium in parathyroid hormone actions in rabbit renal proximal tubules, Am. J. Physiol. 250: F942–F948 (1986).
T.D. McKinney and P. Myers, PTH inhibition of bicarbonate transport by proximal convoluted tubules, Am. J. Physiol. 239:F127–F134 (1980).
S. Sabatini, Parathyroid hormone inhibits water flow in isolated toad bladder, Am. J. Physiol. 250:F532–F538 (1986).
P.A. Mennes, J. Yates, S. Klahr, Effects of ionophore A23187 and external calcium concentrations on renal gluconeogenesis, Proc. Soc. Exp. Med. 157:168–174 (1978).
N. Yanagawa, Cytosolic free calcium in isolated perfused rabbit proximal tubules: effect of parathyroid hormone (Abstract), Kidney Int. 31:361(A) (1987).
G.M. Dolson, M.K. Hise, E.J. Weinman, Relationship among parathyroid hormone, cAHP, and calcium on proximal tubule sodium transport, Am. J. Physiol. 249:F409–F416 (1985).
C. Kleeman, D. Yamaguchi, S. Muallem, Regulation of parathyroid hormone-activated calcium channel by phorbol ester, Kidney Int. 31:351(A) (1987).
A. Besarab and J.W. Swanson, Tachyphylaxis to PTH in the isolated perfused rat kidney: resistance of anticalciuria, Am. J. Physiol. 247: F240–F245 (1984).
P. Bidot-Lopez, R.V. Farese, M.A. Sabiro, Parathyroid hormone and adenosine 3′,5′ monophosphate acutely increases phospholipids of the phosphatidate-polyphosphoinositide pathway in rabbit kidney cortex tubules in vitro by a cycloheximide-sensitive process, Endocrinology 108:2078–2081 (1981).
V. Metzler, S. Weinreb, E. Bellorin-Font, K.A. Hruska, Parathyroid hormone stimulation of renal phosphoinositide metabolism is a cyclic nucleotide-independent effect, Biochim. Biophys. Acta. 712:258–267 (1982).
H. Lo,. D.C. Lehotay, D. Katz, G.S. Levey, Parathyroid hormone-mediated incorporation of 32P-orthophosphate into phosphatidic acid and phosphatidylinositol in renal cortical slices, Endocrin. Res. Commun. 3(Suppl. 6):377–385 (1976).
K.A. Hruska, D. Moskowitz, P. Esbrit, R. Civitelli, S. Westbrook, M. Huskey, Stimulation of inositol triphosphate and diacylglycerol production in renal tubular cells by parathyroid hormone, J. Clin. Invest. 79:230–239 (1987).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1989 Plenum Press, New York
About this chapter
Cite this chapter
Morrison, A.R., Portilla, D., Coyne, D. (1989). Peptide Hormones, Cytosolic Calcium and Renal Epithelial Response. In: Dunn, M.J., Patrono, C., Cinotti, G.A. (eds) Renal Eicosanoids. Advances in Experimental Medicine and Biology, vol 259. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5700-1_7
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5700-1_7
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5702-5
Online ISBN: 978-1-4684-5700-1
eBook Packages: Springer Book Archive