Publication Date:
1993-11-26
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Asch, A S -- Liu, I -- Briccetti, F M -- Barnwell, J W -- Kwakye-Berko, F -- Dokun, A -- Goldberger, J -- Pernambuco, M -- HL02541/HL/NHLBI NIH HHS/ -- HL18828/HL/NHLBI NIH HHS/ -- HL44389/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1436-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology-Oncology, Cornell University Medical College, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7504322" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Antigens, CD/chemistry/genetics/*metabolism
;
Antigens, CD36
;
Base Sequence
;
Blood Platelets/*metabolism
;
Cell Adhesion
;
Cell Line
;
Collagen/*metabolism
;
Erythrocytes/cytology/parasitology
;
Humans
;
Megakaryocytes/metabolism
;
Membrane Glycoproteins/*metabolism
;
Molecular Sequence Data
;
Mutagenesis, Site-Directed
;
Phosphorylation
;
Plasmodium falciparum/physiology
;
Platelet Adhesiveness
;
Platelet Aggregation
;
Platelet Membrane Glycoproteins/chemistry/genetics/*metabolism
;
Protein Kinase C/metabolism
;
Receptors, Cytoadhesin/metabolism
;
Thrombospondins
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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