A G-protein-coupled 130 kDa phospholipase C isozyme, PLC-beta 4, from the particulate fraction of bovine cerebellum

FEBS Lett. 1993 Sep 27;331(1-2):38-42. doi: 10.1016/0014-5793(93)80293-4.

Abstract

A 130 kDa PLC isozyme was purified from the particulate fraction of bovine cerebellum. This PLC was recognized by a polyclonal antiserum generated against the purified 97 kDa PLC-beta 4. Reconstitution of the purified 130 kDa PLC with the membranes of C6 Bu-1 cells in the presence of GTP gamma S or AlF4- resulted in PLC activation as well as the association of PLC with the membranes. Both the association and activation were revoked when the membrane was washed with 2 M KCl. The 97 kDa PLC-beta 4 did not associate with membranes. These data suggest that the 130 kDa PLC is the intact form of PLC-beta 4 the activity of which is likely to be regulated by a G-protein on the membrane.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Cerebellum / enzymology*
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Activation
  • GTP-Binding Proteins / metabolism*
  • Isoenzymes / metabolism*
  • Rats
  • Tumor Cells, Cultured
  • Type C Phospholipases / metabolism*

Substances

  • Isoenzymes
  • Type C Phospholipases
  • GTP-Binding Proteins