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首页> 外文期刊>Thrombosis Research: An International Journal on Vascular Obstruction, Hemorrhage and Hemostasis >Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase.
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Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase.

机译：纤溶酶，白细胞组织蛋白酶G和弹性蛋白酶对内皮下粘附糖蛋白（纤连蛋白，血小板反应蛋白和von Willebrand因子）进行蛋白水解。

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摘要

The degradation of extracellular matrix (ECM) adhesive glycoproteins, fibronectin (FN), thrombospondin (TSP) and von Willebrand factor (vWF), by human leukocyte cathepsin G and elastase, and by plasmin or thrombin, was analysed by immunoblotting after incubation of physiologic doses of the proteases with confluent human umbilical vein endothelial cells. Elastase induced an almost complete disappearance of intact FN, TSP, and vWF from the ECM at 0.02 units/ml within 5 minutes of incubation at 37 degrees C. Plasmin (0.2 units/ml) was also active on all three substrates, whereas cathepsin G (0.2 units/ml) had a preferential effect on TSP. Most remarkably, these degradations occurred with no apparent change in endothelial cell morphology, as shown by phase-contrast microscopy. In contrast, thrombin (0.2 units/ml) had no apparent proteolytic action on ECM glycoproteins, where it induced cell retraction and rounding. The release of adhesive glycoproteins from the ECM was accompanied by the detection of proteolytic fragments in the conditioned medium. Kinetic studies indicated that proteolysis started within minutes and proceeded for at least 1 hour. TSP was extremely sensitive to degradation by all enzymes except thrombin, whereas vWF released from the ECM was more resistant to proteolysis than constitutively secreted vWF, and FN was poorly degraded by plasmin. Our results indicate that serine proteinases, locally produced during inflammation and/or thrombolysis, can release extracellular matrix components and generate proteolytic fragments with potential biological activities.
机译：孵育生理学后，通过免疫印迹分析了人白细胞组织蛋白酶G和弹性蛋白酶以及纤溶酶或凝血酶对细胞外基质（ECM）粘附糖蛋白，纤连蛋白（FN），血小板反应蛋白（TSP）和血管性血友病因子（vWF）的降解。剂量的蛋白酶与人脐静脉内皮细胞融合。弹性蛋白酶诱导完整的FN，TSP和vWF从ECM以0.02单位/毫升的浓度在37摄氏度下孵育的5分钟内几乎完全消失。血浆纤溶酶（0.2单位/毫升）在所有三种底物上均具有活性，而组织蛋白酶G （0.2单位/毫升）对TSP具有优先作用。最显着的是，这些降解的发生没有内皮细胞形态的明显改变，如相差显微镜所示。相反，凝血酶（0.2单位/毫升）对ECM糖蛋白没有明显的蛋白水解作用，可诱导细胞收缩和变圆。粘附糖蛋白从ECM的释放伴随着条件培养基中蛋白水解片段的检测。动力学研究表明，蛋白水解在几分钟内开始，并进行了至少1小时。 TSP对除凝血酶以外的所有酶的降解都极为敏感，而从ECM释放的vWF比组成型分泌的vWF对蛋白水解的抵抗力更强，而FN却很难被纤溶酶降解。我们的结果表明，在炎症和/或溶栓过程中局部产生的丝氨酸蛋白酶可以释放细胞外基质成分，并产生具有潜在生物学活性的蛋白水解片段。

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