Inositol 1,4,5-trisphosphate (Ins(1,4,5)P 3) was first shown to stimulate mobilization of intracellular Ca2+ from permeabilized pancreatic acinar cells (Streb et al., 1983) and has since become recognized as an intracellular messenger formed after receptor activation and then responsible for mobilizing Ca2+ from the intracellular stores of many different cell types. The interactions between most receptors and the phosphoinositidase C (PIC) that catalyzes formation of Ins(1,4,5)P 3 and 1,2-diacylglycerol (DG) have much in common with the more completely understood interactions between receptors and adenylyl cyclase (Gilman, 1987; Taylor, 1990b; Fig. 1). In both cases, agonist-occupied receptors catalyze activation of a specific guanine nucleotide dependent regulatory protein(s) (G protein) by allowing it to lose its tightly bound GDP and replace it with GTP. The active GTP-bound G protein, which has yet to be identified for the phosphoinositide pathway, then regulates the activity of an intracellular effector, for example, adenylyl cyclase or PIC. Stimulation of the latter causes increased hydrolysis of the membrane phospholipid, phosphatidylinositol 4,5-bisphosphate (PtdInsP 2), and the formation of Ins(1,4,5)P 3 and DG.
- Sarcoplasmic Reticulum
- Ryanodine Receptor
- Intracellular Store
- Inositol Phosphate
- Pancreatic Acinar Cell
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© 1992 The Humana Press Inc.
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Taylor, C.W., Bond, J.M., Nunn, D.L., Oldershaw, K.A. (1992). Inositol Triphosphate Receptors and Intracellular Calcium. In: Boulton, A.A., Baker, G.B., Taylor, C.W. (eds) Intracellular Messengers. Neuromethods, vol 20. Humana Press. https://doi.org/10.1385/0-89603-207-8:79
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Online ISBN: 978-1-59259-625-6
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