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凝血酶对纤维蛋白(原)-内皮细胞相互作用无影响。

Lack of effect of thrombin on fibrin(ogen)-endothelial cell interaction.

机构信息

Research Center, University Hospital La Fe, Valencia, Spain.

出版信息

Cytotechnology. 1995 Jun;19(2):143-51. doi: 10.1007/BF00749769.

DOI:10.1007/BF00749769
PMID:22359014
Abstract

In the present study we investigate the fibrin(ogen)-endothelial cell binding and the effect of thrombin on the endothelial cells in relation to fibrin(ogen) binding capacity. Endothelial cell fibrinogen binding was concentration and time-dependent, reaching saturation at 1.4 μM of added ligand. At equilibrium, the number of fibrinogen molecules bound per endothelial cell in the monolayer was 5.8±0.7×10(6). When endothelial cells were activated by different concentrations of thrombin (0-0.1 NIH units ml(-1)), no increase in fibrinogen binding capacity was observed at all the thrombin concentration tested. Whereas disruption of endothelial cell monolayers was observed at thrombin concentrations higher than 0.05 NIH units ml(-1), no increase in the amount of fibrinogen bound was observed. Therefore, resting and thrombin-activated endothelial cells show the same fibrinogen binding capacity.The adhesion of endothelial cells in suspension on immobilized fibrinogen or fibrin was studied to ascertain whether the behavior of fibrin is similar to that of fibrinogen. The extent of endothelial cell attachment to immobilized fibrinogen and fibrin was similar (4275±130 cells cm(-2) for fibrinogen and 4350±235 cells cm(-2) for fibrin) and represent approximately 40% of the added endothelial cells. However, endothelial cell adhesion to immobilized fibrin was significantly faster than endothelial cell adhesion to immobilized fibrinogen. The maximum binding rate was 66±9 and 46±8 cells cm(-2) min(-1) for fibrin and fibrinogen, respectively. Therefore, the fibrinopeptides released by thrombin from fibrinogen induce qualitative changes which enhance the fibrin interaction with the endothelial cells.

摘要

在本研究中,我们研究了纤维蛋白(原)-内皮细胞结合以及凝血酶对与纤维蛋白(原)结合能力相关的内皮细胞的影响。内皮细胞纤维蛋白原结合具有浓度和时间依赖性,在加入配体 1.4 μM 时达到饱和。在平衡时,单层内皮细胞结合的纤维蛋白原分子数为 5.8±0.7×10(6)。当内皮细胞被不同浓度的凝血酶(0-0.1 NIH 单位 ml(-1))激活时,在所有测试的凝血酶浓度下,纤维蛋白原结合能力都没有增加。然而,在凝血酶浓度高于 0.05 NIH 单位 ml(-1)时观察到内皮细胞单层的破坏,但没有观察到结合的纤维蛋白原数量增加。因此,静止和凝血酶激活的内皮细胞显示出相同的纤维蛋白原结合能力。研究了悬浮内皮细胞在固定化纤维蛋白原或纤维蛋白上的黏附,以确定纤维蛋白的行为是否与纤维蛋白原相似。内皮细胞固定化纤维蛋白原和纤维蛋白上的附着程度相似(纤维蛋白原上为 4275±130 个细胞 cm(-2),纤维蛋白上为 4350±235 个细胞 cm(-2)),分别代表加入的内皮细胞的约 40%。然而,内皮细胞对固定化纤维蛋白的黏附速度明显快于对固定化纤维蛋白原的黏附。最大结合速率分别为 66±9 和 46±8 个细胞 cm(-2) min(-1),用于纤维蛋白和纤维蛋白原。因此,凝血酶从纤维蛋白原释放的纤维肽引起定性变化,增强了纤维蛋白与内皮细胞的相互作用。

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