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)
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: | https://repository.cshl.edu/id/eprint/32279 |
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