Abstract
Since the discovery in 1983 that Ins(1,4,5)P3 can cause the mobilization of intracellular stores of ca2+(Streb, et al., 1983), the factors that regulate the intracellular accumulation of this inositol polyphosphate have been important subjects for study in any attempt to understand ca2+ -dependent cellular activation. As is the case for any other transient compound, accumulation of Ins(1,4,5)P3 is controlled directly by its generation and metabolism. The generation of Ins(1,4,5)P3 occurs following the activation of cellular phosphoinositidase C (PIC), a receptor-dependent and, in most cell systems studied thus far, GTPbinding protein-dependent membrane event. Obviously, factors that perturb any of these stages will modulate the rate at which the substrate, PtdIns(4, 5)P2, is hydrolyzed by PIC. In addition, the availability of PtdIns(4,5)P2 is also an important consideration. Once formed, Ins(1,4,5)P3 can be acted upon by at least two enzymes, the most active and best characterized of which are 5-phosphomonoesterase (5-PME), yielding Ins(l,4)P2 (Downes, et al., 1982; Storey, et al., 1984), and 3-kinase, yielding Ins(1,3,4,5)P4 (Irvine, et al., 1986). Ins(1,3,4,5)P4 is also a substrate for 5-PME, becoming Ins(1,3,4)P3 (Batty, et al., 1985). Of the isolated myoinositol bis, tris, and tetrakisphosphates, Ins(1,4,5)P3 has been shown to be by far the most potent facilitator of intracellular ca2+ release, with Ins(1,4)P2 and Ins(1,3,4)P3 displaying negligible activity.
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© 1990 Plenum Press, New York
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Rittehouse, S.E., King, W.G., Downes, C.P., Kucera, G.L. (1990). The Role of Endogenously Stimulated Protein Kinase C in Regulating. In: Vanderhoek, J.Y. (eds) Biology of Cellular Transducing Signals. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0559-0_23
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DOI: https://doi.org/10.1007/978-1-4613-0559-0_23
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