Asch A S, Silbiger S, Heimer E, Nachman R L
Specialized Center for Research in Thrombosis, Cornell University Medical College, New York, NY 10021.
Biochem Biophys Res Commun. 1992 Feb 14;182(3):1208-17. doi: 10.1016/0006-291x(92)91860-s.
To clarify the role of CD36 as a TSP receptor and to investigate the mechanisms of the TSP-CD36 interaction, transfection studies were performed using CD36-cDNA in a CDM8 plasmid. Jurkat cells transfected with CD36 cDNA express an 88kD membrane surface protein and acquire the ability to bind thrombospondin. The TSP amino acid sequence, CSVTCG, mediates the interaction of thrombospondin with CD36. CD36 transfectants but not control transfectants bind radiolabeled tyrosinated peptide (YCSVTCG). The hexapeptide inhibits thrombospondin expression on activated human platelets and results in diminished platelet aggregation. CSVTCG-albumin conjugates support CD36-dependent adhesion of tumor cells. We conclude that the CSVTCG repeat sequence is a crucial determinant of CD36 thrombospondin binding.
为阐明CD36作为血小板反应蛋白（TSP）受体的作用，并研究TSP与CD36相互作用的机制，使用CDM8质粒中的CD36 - cDNA进行了转染研究。用CD36 cDNA转染的Jurkat细胞表达一种88kD的膜表面蛋白，并获得结合血小板反应蛋白的能力。TSP的氨基酸序列CSVTCG介导血小板反应蛋白与CD36的相互作用。CD36转染细胞而非对照转染细胞能结合放射性标记的酪氨酸化肽（YCSVTCG）。该六肽抑制活化的人血小板上血小板反应蛋白的表达，并导致血小板聚集减少。CSVTCG - 白蛋白缀合物支持肿瘤细胞的CD36依赖性黏附。我们得出结论，CSVTCG重复序列是CD36与血小板反应蛋白结合的关键决定因素。
