Phospholipase C-148: Chromosomal Location and Deletion Mapping of Functional Domains

Andrew Bristol, S.M. Hall, Ron Kriz, Mark Stahl, Yao‐Yun Fan, M.G. Byers, R.L. Eddy, T.B. Shows, John L. Knopf

Cold Spring Harbor Symposia on Quantitative Biology · 1988 · 81 citations · 0 references

Concepts

Abstract

The binding of various agonists to their specific cell-surface receptors rapidly induces the formation of two second-messenger molecules derived from phosphatidylinositol 4,5-bisphosphate: diacylglycerol and inositol 1,4,5-trisphosphate (Berridge 1984). The production of these second-messenger molecules is mediated by activated phosphatidylinositol-specific phospholipase C (PLC) enzymes (Berridge 1987). Evidence has accumulated that would suggest the existence of a number of immunologically distinct enzymes with phosphatidylinositol-specific PLC activities (Hoffman and Majerus 1982; Bennett and Crooke 1987; Katan and Parker 1987; Rebecchi and Rosen 1987; Ryu et al. 1987a,b). We have recently purified, cloned, and expressed one of these PLC subtypes, which we refer to as PLC-148 (Stahl et al. 1988). PLC-148 mRNA is expressed in most cell types and is present as a single-copy gene. A comparison of the PLC-148 amino acid sequence with those present in the National Biomedical Research Foundation (NBRF) data base revealed significant homology between PLC-148 and the nonreceptor protein...