在纤维蛋白原和α2-巨球蛋白存在的情况下凝血酶与内皮细胞的相互作用。
Interaction of thrombin with endothelial cells in the presence of fibrinogen and alpha 2-macroglobulin.
作者信息
Léránt I, Kovács T, Papp B, Mandl J, Lambin P, Machovich R
机构信息
2nd Institute of Biochemistry, Semmelweis University Medical School, Budapest, Hungary.
出版信息
Haematologia (Budap). 1990;23(3):161-9.
Binding of thrombin to cultured endothelial cells has been studied in the presence of fibrinogen and alpha 2-macroglobulin. Both fibrinogen and alpha 2-macroglobulin inhibit the interaction of thrombin with endothelial cells. Whereas fibrinogen decreases the rate of activation by the thrombin-thrombomodulin complex of protein C, thrombomodulin inhibits the rate of inactivation by alpha 2-macroglobulin thrombin. alpha 2-macroglobulin also binds to endothelial cells; (Kd = 3 x 10(-7) M with 3 x 10(5) binding sites/cell), and the rate of binding of the alpha 2-macroglobulin to endothelial cells is faster than its complex formation with the thrombin. The data suggest that essentially the cell-bound form of fibrinogen and alpha 2-macroglobulin influences thrombin binding and functions.
已在纤维蛋白原和α2-巨球蛋白存在的情况下研究了凝血酶与培养的内皮细胞的结合。纤维蛋白原和α2-巨球蛋白均抑制凝血酶与内皮细胞的相互作用。纤维蛋白原降低了凝血酶-血栓调节蛋白复合物对蛋白C的激活速率，而血栓调节蛋白则抑制了α2-巨球蛋白对凝血酶的灭活速率。α2-巨球蛋白也与内皮细胞结合；（解离常数Kd = 3×10^(-7) M，每个细胞有3×10^5个结合位点），且α2-巨球蛋白与内皮细胞的结合速率比其与凝血酶形成复合物的速率更快。数据表明，本质上细胞结合形式的纤维蛋白原和α2-巨球蛋白会影响凝血酶的结合及功能。
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