Linked Life Data

2642908

Source:http://linkedlifedata.com/resource/pubmed/id/2642908

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pubmed-article:2642908pubmed:abstractTextThe influence of nucleotides and pyrophosphate on phospholipase C from rabbit thymocytes was investigated by using two different methods for the determination of phospholipase C activity. In a first approach the release of radiolabeled inositol phosphates from [3H]inositol-labeled membranes was examined. By a second type of experiment the cleavage of exogenously added radiolabeled phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) was measured. Using internally labeled membranes only guanosine 5'-O-(thiotriphosphate) exhibited a stimulatory effect on the phospholipase C suggesting the involvement of a G-protein. When exogenous [3H]PtdIns-4,5-P2 was used as substrate, cleavage of PtdIns-4,5-P2 was stimulated by all nucleotides investigated; in addition pyrophosphate showed a stimulatory effect. From these data we conclude that the increased cleavage of exogenous PtdIns-4,5-P2 induced by GTP analogues is not conclusive in terms of the involvement of a G-protein. Rather than induced by a G-protein this activation may be caused by an increased substrate accessibility. Our experiments with endogenous substrate clearly established the regulatory role of G-proteins for membrane-bound phospholipase C.lld:pubmed
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pubmed-article:2642908pubmed:pagination906-9lld:pubmed
pubmed-article:2642908pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:2642908pubmed:articleTitleEffects of nucleotides on the activity of phospholipase C in rabbit thymus lymphocytes. Differences in assays using endogenous [3H]inositol-prelabeled membranes or exogenous [3H]phosphatidylinositol 4,5-bisphosphate as substrate.lld:pubmed
pubmed-article:2642908pubmed:affiliationDepartment of Pharmacology and Toxicology, Medical School Hannover, Federal Republic of Germany.lld:pubmed
pubmed-article:2642908pubmed:publicationTypeJournal Articlelld:pubmed
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