Abstract
Hormone-receptor coupling often results in the activation of phospholipase C which in turn hydrolyzes phosphatidylinositol 4,5-bisphosphate into two second messengers, 1,2-diacylglycerol (DAG) and inositol 1,4,5-trisphosphate [Ins(1,4,5)]P3. It is well known that DAG remains in the membrane domain and activates protein kinase C while Ins(1,4,5)P3 is soluble and is known to increase the intracellular level of Ca2+. 1,2 Ins(l,4,5)P3 may subsequently be converted to Ins(1,3,4,5)P4 by a soluble inositol trisphosphate 3-Phosphokinase.3 Both Ins(1,4,5)P3 and Ins(1,3,4,5)P4 are substrates of a membrane-bound 5-Phosphomonoesterase being degraded to Ins(1,4)P2 and Ins(1,3,4)P3 respectively.4,5 Ins(1,4,5)P3 and Ins(1,3,4)P3 both mobilize Ca2+,2,6 while the physiological function of Ins(1,3,4,5)P4 is unknown although indirect evidence suggests that it may affect plasma membrane Ca2+ channels.7,8
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References
Nishizuka, Y., 1984, The role of protein kinase C in cell surface signal transduction and tumor promotion. Nature, 308:693.
Streb, H., Irvine, R.F., Berridge, M.J. and Schulz, I., 1983, Release of Ca2+ from a nonmitochrondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Biochem. J. 232:211.
Batty, I.R., Nahorski, S.R. and Irvine, R.F., 1985, Rapid formation of inositol 1,3,4,5-tetrakisphosphate following muscarinic receptor stimulation of rat cerebral cortical slices. Biochem. J., 233:211.
Downes, C.P., Mussat, M.C. and Micheli, R.H., 1982, The inositol trisphosphate phosphomonesterase of the human erythrocyte membrane. Biochem. J., 203:169.
Majerus, P.W., Connolly, T.M., Deckim, H., Ross, T.S., Boss, T.E., Ishii, H., Bansal, V.S. and Wilson, D.B., 1986, The metabolism of phosphoinositide-derived messenger molecules. Science, 234:1519.
Irvine, R.F., Letcher, A.J., Lander, D.J. and Berridge, M.J., 1986, Specificity of inositol phosphate-stimulated Ca2+ mobilization from Swiss-mouse 3T3 cells. Biochem. J., 240:301.
Irvine, R.F. and Moor, R.N., 1986, Micro-injection of inositol 1,3,4,5-tetrakisphosphate activates sea urchin eggs by a mechanism dependent on external Ca2+. Biochem. J., 240:917.
Morris, A.P., Gallacher, D.V., Irvine, R.F. and Petersen, O.H. 1987, Synergism of inositol trisphosphate and tetrakisphosphate in activating Ca2+-dependent K+ channels. 330:653.
Brandt, H., Killilea, S.D. and Lee, E.Y.C., 1974, Activation of Phosphorylase phosphatase by a novel procedure: Evidence for a regulatory mechanism involving the release of a catalytic subunit from enzyme-inhibitor complex(es) of higher molecular weight. Biochem. Biophys. Res. Commun., 61:598.
Meisler, M.H. and Langan, T.A., 1969, Characterization of a phosphatase specific for phosphorylated histones and protamine. J. Biol. Chem., 244:4961.
Killilea, S.D., Aylward, J.H., Mellgren, R.L. and Lee, E.Y.C., 1978, Purification and properties of bovine myocardial Phosphorylase phosphatase (protein phosphatase C). Arch. Biochem. Biophys., 191:638.
Gergely, P., Erdodi, F. and Bot, G., 1984, Heparin inhibits the activity of protein phosphatase-1. FEBS Lett. 169:45.
Mumby, M.C., Green, D.D. and Russell, K.L., 1985, Structural characterization of cardiac protein phosphatase with a monoclonal antibody. J. Biol. Chem., 260:13763.
Ingebritsen, T.S. and Cohen, P., 1983, The protein, phosphatases involved in cellular regulation. 1. Classification and substrate specificity. Eur. J, Biochem., 132:255.
Ingebritsen, T.S., Stewart, A.A. and Cohen, P., 1983, The protein phosphatases involved in cellular regulation. 6. Measurement of type-1 and type-2 protein phosphatases in extracts of mammalian tissue: An assessment of their physiological roles. Eur. J. Biochem., 132:297.
Brautigan, D.L., Gruppuso, P.A. and Mumby, M., 1986, Protein phosphatase type-1 and type-2 catalytic subunits both bind inhibitor-2 and monoclonal immunoglobulins. J. Biol. Chem., 261:14924.
Irvine, R.F., Brown, K.D. and Berridge, M.J., 1984, Specificity of inositol trisphosphate-induced calcium release from permeabilized Swiss-mouse 3T3 cells. Biochem. J., 222:269.
Hill, T.H., Berggren, P.O. and Boynton, A.L., 1987, Heparin inhibits inositol trisphosphate-induced calcium release from permeabilized rat liver cells. Biochem. Biophys. Res. Commun., 149:897.
Nilsson, T., Zwiller, J., Boynton, A.L. and Berggren, P.O., 1988, Heparin inhibits IP3-induced Ca2+ release in permeabilized pancreatic ß Cells. FEBS Letts, 229:221–214.
Zwiller, J., Ogasawara, E.M., Nakamoto, S.S. and Boynton, A.L. 1988, Stimulation by inositol trisphosphate and tetrakisphosphate of a protein phosphatase. Biochem. Biophys. Res. Commun., 155:767.
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© 1989 Plenum Press, New York
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Zwiller, J., Nakamoto, S.S., Boynton, A.L. (1989). Stimulation by Inositol Trisphosphate and Tetrakisphosphate of a Protein Phosphatase. In: Hidaka, H., Carafoli, E., Means, A.R., Tanaka, T. (eds) Calcium Protein Signaling. Advances in Experimental Medicine and Biology, vol 255. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5679-0_41
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DOI: https://doi.org/10.1007/978-1-4684-5679-0_41
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