| Autor: |
Stephen J. Taylor, John H. Exton, Stephen B. Bocckino, Jonathan S. Blank |
| Rok vydání: |
2007 |
| Předmět: |
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| Zdroj: |
Ciba Foundation Symposium 164-Interactions Among Cell Signalling Systems |
| DOI: |
10.1002/9780470514207.ch4 |
| Popis: |
Two G proteins that regulate phosphoinositide phospholipase C in liver plasma membranes have been purified to homogeneity in both the heterotrimeric and dissociated forms. The heterotrimers contain a 42 kDa or 43 kDa alpha subunit and a 35 kDa beta subunit. The alpha subunits are not ADP-ribosylated by pertussis toxin and are closely related immunologically to members of the recently identified Gq class of G proteins. The specific phosphoinositide phospholipase C isozyme that responds to the G proteins has been determined to the beta 1 isozyme. GTP analogues stimulate phosphatidylcholine hydrolysis in rat liver plasma membranes. The nucleotide specificity and Mg2+ dependency of the response indicate that it is mediated by a G protein. Phosphatidic acid, diacylglycerol, choline and phosphorylcholine are the products, indicating that both phospholipase D and C activities are involved. Activation of phospholipase D is also indicated by the enhanced production of phosphatidyl-ethanol in the presence of ethanol. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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