PI-specific phospholipase c "α" from sheep seminal vesicles is a proteolytic fragment of pi-plc σ

Gregory D. Taylor; Judy A. Feet; David F. Silbertt; Sandra L. Hofmann

doi:10.1016/0006-291X(92)91355-T

PI-specific phospholipase c "α" from sheep seminal vesicles is a proteolytic fragment of pi-plc σ

Gregory D. Taylor, Judy A. Feet, David F. Silbertt, Sandra L. Hofmann

Research output: Contribution to journal › Article › peer-review

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Abstract

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)
Pages (from-to)	1176-1183
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	188
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(92)91355-T
State	Published - Nov 16 1992

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "PI-specific phospholipase c {"}α{"} from sheep seminal vesicles is a proteolytic fragment of pi-plc σ",

abstract = "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.",

author = "Taylor, {Gregory D.} and Feet, {Judy A.} and Silbertt, {David F.} and Hofmann, {Sandra L.}",

note = "Funding Information: We wish to thank Drs. Phil Majerus, Sue Coo Rhee, Paul Stemweis and Alan Smyrcka for antibodies and helpful discussions. This work was supported by grants from the Robert A. Welch Foundation (#I-1187), National Institutes of Health @GM38540), and the American Cancer Society (#BE153).",

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doi = "10.1016/0006-291X(92)91355-T",

language = "English (US)",

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AU - Taylor, Gregory D.

AU - Feet, Judy A.

AU - Silbertt, David F.

AU - Hofmann, Sandra L.

N1 - Funding Information: We wish to thank Drs. Phil Majerus, Sue Coo Rhee, Paul Stemweis and Alan Smyrcka for antibodies and helpful discussions. This work was supported by grants from the Robert A. Welch Foundation (#I-1187), National Institutes of Health @GM38540), and the American Cancer Society (#BE153).

PY - 1992/11/16

Y1 - 1992/11/16

N2 - 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.

AB - 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.

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PI-specific phospholipase c "α" from sheep seminal vesicles is a proteolytic fragment of pi-plc σ

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