Phosphatidylinositide-specific phospholipase C enzymes (PLCs) catalyze the conversion of the phosphoinositides to biologically important signal transducing molecules. These enzymes may be grouped into "families" which share similar structures and modes of regulation. The existence of a structurally distinct family of PLC termed "α" has been recently called into question. In the current paper we show by immunoblotting experiments that PLC "α" from sheep seminal vesicles is recognized by monoclonal antibodies raised against the σ1 isoform of bovine brain PLC, and appears to be derived from a higher molecular weight band at 85 kDa. We also show that antibodies raised against PLC α efficiently immunoprecipitate the 85-kDa PLC σ1 isoform from bovine brain and Chinese hamster lung fibroblasts. These data provide strong evidence that the PLC a from sheep seminal vesicles is a proteolytic fragment of PLC σ1. Thus, there is still no conclusive evidence for a separate "α" class of PLC.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Nov 16 1992|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology