van de Stolpe A, Jacobs N, Hage W J, Tertoolen L, van Kooyk Y, Nováková I R, de Witte T
Department of Hematology, University Hospital Nijmegen, Netherlands.
Thromb Haemost. 1996 Jan;75(1):182-9.
Fibrinogen is a ligand for Intercellular Adhesion Molecule-1 (ICAM-1), and enhances monocyte-endothelial cell interaction by coupling Mac-1 on monocytes to ICAM-1 on endothelial cells. We investigated the role of the cytoskeleton in fibrinogen binding to the human endothelial cell line EA.hy 926 using immunofluorescence techniques. In this cell line TNF alpha induced the simultaneous appearance of stress fibers and of ICAM-1, which was clustered predominantly on endothelial cell projections. Incubation of TNF alpha-stimulated endothelial cells with fibrinogen resulted in binding of fibrinogen to ICAM-1 on these cell projections. Disruption of the cytoskeleton by cytocholasin B abolished fibrinogen binding. Activation of protein kinase C with 12-O-tetradecanoyl phorbol-13-acetate resulted in simultaneous loss of both stress fibers and fibrinogen binding. These results suggest that a connection between ICAM-1 and the cytoskeleton results in clustering of ICAM-1 on cell projections, which is required for fibrinogen binding.
纤维蛋白原是细胞间黏附分子-1（ICAM-1）的配体，它通过将单核细胞上的Mac-1与内皮细胞上的ICAM-1偶联，增强单核细胞与内皮细胞的相互作用。我们使用免疫荧光技术研究了细胞骨架在纤维蛋白原与人内皮细胞系EA.hy 926结合中的作用。在该细胞系中，肿瘤坏死因子α（TNFα）诱导应激纤维和ICAM-1同时出现，ICAM-1主要聚集在内皮细胞突起上。用纤维蛋白原孵育TNFα刺激的内皮细胞，导致纤维蛋白原与这些细胞突起上的ICAM-1结合。细胞松弛素B破坏细胞骨架可消除纤维蛋白原结合。用12-O-十四酰佛波醇-13-乙酸酯激活蛋白激酶C会导致应激纤维和纤维蛋白原结合同时丧失。这些结果表明，ICAM-1与细胞骨架之间的联系导致ICAM-1在细胞突起上聚集，这是纤维蛋白原结合所必需的。
