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rdf:type |
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lifeskim:mentions |
umls-concept:C0023688,
umls-concept:C0037791,
umls-concept:C0332298,
umls-concept:C0936012,
umls-concept:C1158884,
umls-concept:C1167622,
umls-concept:C1366645,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
5138
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pubmed:dateCreated |
1993-12-23
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pubmed:abstractText |
The protein CD36 is a membrane receptor for thrombospondin (TSP), malaria-infected erythrocytes, and collagen. Three functional sequences were identified within a single disulfide loop of CD36: one that mediates TSP binding (amino acids 87 to 99) and two that support malarial cytoadhesion (amino acids 8 to 21 and 97 to 110). One of these peptides (p87-99) is a consensus protein kinase C (PKC) phosphorylation site. Dephosphorylation of constitutively phosphorylated CD36 in resting platelets and a megakaryocytic cell line led to the loss of collagen adhesion and platelet reactivity to collagen, with a reciprocal increase in TSP binding. PKC-mediated phosphorylation of this ectodomain resulted in a loss of TSP binding and the reciprocal acquisition of collagen binding. In site-directed mutagenesis studies, when the threonine phosphorylation site was changed to alanine, CD36 was expressed in a dephosphorylated state and bound to TSP constitutively.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD36,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoadhesin,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombospondins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1436-40
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7504322-Amino Acid Sequence,
pubmed-meshheading:7504322-Animals,
pubmed-meshheading:7504322-Antigens, CD,
pubmed-meshheading:7504322-Antigens, CD36,
pubmed-meshheading:7504322-Base Sequence,
pubmed-meshheading:7504322-Blood Platelets,
pubmed-meshheading:7504322-Cell Adhesion,
pubmed-meshheading:7504322-Cell Line,
pubmed-meshheading:7504322-Collagen,
pubmed-meshheading:7504322-Erythrocytes,
pubmed-meshheading:7504322-Humans,
pubmed-meshheading:7504322-Megakaryocytes,
pubmed-meshheading:7504322-Membrane Glycoproteins,
pubmed-meshheading:7504322-Molecular Sequence Data,
pubmed-meshheading:7504322-Mutagenesis, Site-Directed,
pubmed-meshheading:7504322-Phosphorylation,
pubmed-meshheading:7504322-Plasmodium falciparum,
pubmed-meshheading:7504322-Platelet Adhesiveness,
pubmed-meshheading:7504322-Platelet Aggregation,
pubmed-meshheading:7504322-Platelet Membrane Glycoproteins,
pubmed-meshheading:7504322-Protein Kinase C,
pubmed-meshheading:7504322-Receptors, Cytoadhesin,
pubmed-meshheading:7504322-Thrombospondins
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pubmed:year |
1993
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pubmed:articleTitle |
Analysis of CD36 binding domains: ligand specificity controlled by dephosphorylation of an ectodomain.
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pubmed:affiliation |
Division of Hematology-Oncology, Cornell University Medical College, New York, NY 10021.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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