Effect of H-ras proteins on the activity of polyphosphoinositide phospholipase C in HL60 membranes

Cockcroft, S., Bar-Sagi, D. (1990) Effect of H-ras proteins on the activity of polyphosphoinositide phospholipase C in HL60 membranes. Cell Signal, 2 (3). pp. 227-34. ISSN 0898-6568 (Print)0898-6568 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/2169290
DOI: 10.1016/0898-6568(90)90050-K

Abstract

The present study was undertaken to investigate whether purified ras proteins can affect the activity of polyphosphoinositide specific phospholipase C in a cell-free membrane system. For this purpose we used homogenous preparations of the proto-oncogenic (H-ras(gly 12)) and the oncogenic (H-ras(val 12)) forms of the human H-ras proteins and membranes prepared from the human leukemic HL60 cells. We demonstrate that both the proto-oncogenic and the oncogenic form of H-ras proteins stimulate phospholipase C activity only when coupled to non-hydrolysable analogues of GTP.

Item Type: Paper
Uncontrolled Keywords: Cell Line Cell Membrane/*enzymology Cell-Free System GTP-Binding Proteins/metabolism Genes, ras Guanosine 5'-O-(3-Thiotriphosphate) Guanosine Diphosphate/metabolism Guanosine Triphosphate/analogs & derivatives/metabolism Humans Phosphoinositide Phospholipase C Phosphoric Diester Hydrolases/*metabolism Proto-Oncogene Proteins/*metabolism/pharmacology Proto-Oncogene Proteins p21(ras) Thionucleotides/metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > oncogene
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > phospholipase C
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein > Ras
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: 1990
Date Deposited: 30 Mar 2016 20:05
Last Modified: 30 Mar 2016 20:05
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32279

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