Tuszynski G P, Rothman V, Murphy A, Siegler K, Smith L, Smith S, Karczewski J, Knudsen K A
Science. 1987 Jun 19;236(4808):1570-3. doi: 10.1126/science.2438772.
The physiological role of the platelet-secreted protein thrombospondin (TSP) is poorly understood, although it has been postulated to be involved in platelet aggregation and cellular adhesion. In this report, TSP isolated from human platelets was found to promote, in vitro, the cell-substratum adhesion of a variety of cells, including platelets, melanoma cells, muscle cells, endothelial cells, fibroblasts, and epithelial cells. The adhesion-promoting activity of TSP was species independent, specific, and not due to contamination by fibronectin, vitronectin, laminin, or platelet factor 4. The cell surface receptor for TSP is protein in nature and appears distinct from that for fibronectin.
血小板分泌蛋白血小板反应蛋白(TSP)的生理作用尚未完全明确,尽管有人推测它与血小板聚集和细胞黏附有关。在本报告中,从人血小板中分离出的TSP在体外可促进多种细胞与底物的黏附,这些细胞包括血小板、黑色素瘤细胞、肌肉细胞、内皮细胞、成纤维细胞和上皮细胞。TSP的黏附促进活性不具有物种依赖性,具有特异性,且并非由纤连蛋白、玻连蛋白、层粘连蛋白或血小板因子4污染所致。TSP的细胞表面受体本质上是蛋白质,且似乎与纤连蛋白的受体不同。