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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 |
1992-10-15
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pubmed:abstractText |
Since glycoprotein IV (GPIV) has been shown to play an important role in the interaction of platelets with collagen and thrombospondin, the aggregation and secretion of GPIV-deficient platelets were examined. Using a binding assay with monoclonal 125I-OKM5 antibody against CD36 antigen and crossed immunoelectrophoresis of the solubilized platelets against anti-GPIV antibody, the platelets from seven (4.1%) out of 170 healthy Japanese donors were found to be deficient in GPIV. The GPIV-deficient platelets showed normal aggregations in response to collagen as well as ADP, epinephrine, arachidonic acid and thrombin in comparison with GPIV-positive platelets. Polyclonal anti-GPIV antibody aggregated GPIV-positive platelets but not the GPIV-negative ones. The F(ab')2 fragments of the anti-GPIV antibody competitively inhibited the anti-GPIV-induced aggregation, but did not affect the collagen-induced aggregation of GPIV-positive platelets. These results suggest that the deficiency of GPIV does not affect platelet aggregability.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD36,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Epinephrine,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fab Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0007-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
81
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
86-92
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1381610-Adenosine Diphosphate,
pubmed-meshheading:1381610-Adolescent,
pubmed-meshheading:1381610-Adult,
pubmed-meshheading:1381610-Amino Acid Sequence,
pubmed-meshheading:1381610-Antigens, CD,
pubmed-meshheading:1381610-Antigens, CD36,
pubmed-meshheading:1381610-Arachidonic Acid,
pubmed-meshheading:1381610-Blood Platelets,
pubmed-meshheading:1381610-Collagen,
pubmed-meshheading:1381610-Epinephrine,
pubmed-meshheading:1381610-Female,
pubmed-meshheading:1381610-Flow Cytometry,
pubmed-meshheading:1381610-Humans,
pubmed-meshheading:1381610-Immunoelectrophoresis,
pubmed-meshheading:1381610-Immunoglobulin Fab Fragments,
pubmed-meshheading:1381610-Iodine Radioisotopes,
pubmed-meshheading:1381610-Japan,
pubmed-meshheading:1381610-Male,
pubmed-meshheading:1381610-Middle Aged,
pubmed-meshheading:1381610-Molecular Sequence Data,
pubmed-meshheading:1381610-Platelet Aggregation,
pubmed-meshheading:1381610-Protein Deficiency,
pubmed-meshheading:1381610-Thrombin
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pubmed:year |
1992
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pubmed:articleTitle |
Normal aggregations of glycoprotein IV (CD36)-deficient platelets from seven healthy Japanese donors.
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pubmed:affiliation |
Department of Cardiovascular Research, Tokyo Metropolitan Institute of Medical Science, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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