The mechanism of phospholipase C-gamma1 regulation.
- Author:
Myung Jong KIM
1
;
Eui Kyung KIM
;
Sung Ho RYU
;
Pann Ghill SUH
Author Information
1. Department of Life Science, Pohang University of Science and Technology, Kyungbuk, Korea.
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't ; Review
- Keywords:
phospholipase C;
protein kinase C
- MeSH:
Cell Division;
Enzyme Activation;
Isoenzymes/metabolism*;
Phospholipase C/metabolism*;
Second Messenger Systems;
T-Lymphocytes
- From:Experimental & Molecular Medicine
2000;32(3):101-109
- CountryRepublic of Korea
- Language:English
-
Abstract:
Phospholipase C (PLC)1 hydrolyzes phosphatidylinositol 4,5-bisphosphate to generate the second messengers, inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 induces a transient increase in intracellular free Ca2+, while DAG directly activates protein kinase C. Upon stimulation of cells with growth factors, PLC-gamma1 is activated upon their association with and phosphorylation by receptor and non-receptor tyrosine kinases. In this review, we will focus on the activation mechanism and regulatory function of PLC-gamma1.
