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Title: Formation and actions of calcium-mobilizing messenger, inositol 1,4,5-trisphosphate

Journal Article · · Am. J. Physiol.; (United States)
OSTI ID:6285084

A variety of surface membrane receptors can activate a phospholipase C, which degrades phosphatidylinositol 4,5-bisphosphate liberating a calcium mobilizing second messenger, inositol 1,4,5-trisphosphate ((1,4,5)IP3). The coupling of surface receptors to the phospholipase C involves one or more quanine nucleotide-dependent regulatory proteins that are similar but not identical to those that regulate adenylate cyclase. (1,4,5)IP3 has been shown to release CaS from a portion of the endoplasmic reticulum and is believed responsible for the initial phase of CaS mobilization ascribed to internal CaS release. (1,4,5)IP3 acts by binding to a specific receptor that either is a component of, or regulates, a CaS ion channel. The release of CaS from the (1,4,5)IP3-sensitive component of the endoplasmic reticulum may secondarily activate the second phase of CaS mobilization, which involves CaS entry. (1,4,5)IP3 is metabolized by two pathways. One involves the action of a 5-phosphatase that degrades (1,4,5)IP3 to inositol 1,4-bisphosphate, whereas the other involves a 3-kinase that phosphorylates (1,4,5)IP3 to produce inositol 1,3,4,5-tetrakisphosphate. The significance of this dual metabolism is not known, but it may be important in rapidly extinguishing the CaS -releasing activity (1,4,5)IP3.

OSTI ID:
6285084
Journal Information:
Am. J. Physiol.; (United States), Vol. 252:2
Country of Publication:
United States
Language:
English