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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0024264,
umls-concept:C0025255,
umls-concept:C0028630,
umls-concept:C0031669,
umls-concept:C0034493,
umls-concept:C0040113,
umls-concept:C0070798,
umls-concept:C0205227,
umls-concept:C0205228,
umls-concept:C0441655,
umls-concept:C1280500,
umls-concept:C1510438,
umls-concept:C1705241,
umls-concept:C1705242,
umls-concept:C1710236
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pubmed:issue |
2
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pubmed:dateCreated |
1989-2-17
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pubmed:abstractText |
The 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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/guanosine 5'-O-(2-thiodiphosphate)
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
906-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2642908-Adenosine Triphosphate,
pubmed-meshheading:2642908-Animals,
pubmed-meshheading:2642908-Cell Membrane,
pubmed-meshheading:2642908-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:2642908-Guanosine Diphosphate,
pubmed-meshheading:2642908-Guanosine Triphosphate,
pubmed-meshheading:2642908-Kinetics,
pubmed-meshheading:2642908-Rabbits,
pubmed-meshheading:2642908-T-Lymphocytes,
pubmed-meshheading:2642908-Thionucleotides,
pubmed-meshheading:2642908-Thymus Gland,
pubmed-meshheading:2642908-Type C Phospholipases
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pubmed:year |
1989
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pubmed:articleTitle |
Effects 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.
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pubmed:affiliation |
Department of Pharmacology and Toxicology, Medical School Hannover, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article
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