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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1984-3-6
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pubmed:abstractText |
Neutrophil homogenates contained a high affinity guanosine triphosphatase (GTPase) that was stimulatable (+27%) by the addition of 100 nM N-formyl chemotactic peptide (CHO-pep), but not by 1 microgram X ml-1 phorbolmyristate acetate (PMA). Kinetic analysis of the stimulation demonstrated an apparent lagtime of 14.3 +/- 6.9 s between the addition of CHO-pep and the optimal GTPase stimulation. The GTPase activity (but not CHO-pep-stimulated GTPase activity) was preserved in a highly purified plasma membrane fraction of the homogenate. From these observations we suggest that both a high affinity guanine nucleotide binding protein and GTPase are closely associated with the plasma membrane CHO-pep receptor. The possibility that GTPase activity may influence guanine nucleotide regulation of adenylate cyclase during CHO-pep stimulation of neutrophils is discussed.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
165-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6141069-Adenylate Cyclase,
pubmed-meshheading:6141069-Cell-Free System,
pubmed-meshheading:6141069-GTP Phosphohydrolases,
pubmed-meshheading:6141069-GTP-Binding Proteins,
pubmed-meshheading:6141069-Humans,
pubmed-meshheading:6141069-Kinetics,
pubmed-meshheading:6141069-Neutrophils,
pubmed-meshheading:6141069-Phosphoric Monoester Hydrolases,
pubmed-meshheading:6141069-Receptors, Cell Surface,
pubmed-meshheading:6141069-Receptors, Formyl Peptide
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pubmed:year |
1984
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pubmed:articleTitle |
Evidence for N-formyl chemotactic peptide-stimulated GTPase activity in human neutrophil homogenates.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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