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Merck

Platelets drive fibronectin fibrillogenesis using integrin αIIbβ3.

Science advances (2022-03-12)
Sebastian Lickert, Martin Kenny, Kateryna Selcuk, Johanna L Mehl, Markus Bender, Susanna M Früh, Melanie A Burkhardt, Jan-Dirk Studt, Bernhard Nieswandt, Ingmar Schoen, Viola Vogel
摘要

Platelets interact with multiple adhesion proteins during thrombogenesis, yet little is known about their ability to assemble fibronectin matrix. In vitro three-dimensional superresolution microscopy complemented by biophysical and biochemical methods revealed fundamental insights into how platelet contractility drives fibronectin fibrillogenesis. Platelets adhering to thrombus proteins (fibronectin and fibrin) versus basement membrane components (laminin and collagen IV) pull fibronectin fibrils along their apical membrane versus underneath their basal membrane, respectively. In contrast to other cell types, platelets assemble fibronectin nanofibrils using αIIbβ3 rather than α5β1 integrins. Apical fibrillogenesis correlated with a stronger activation of integrin-linked kinase, higher platelet traction forces, and a larger tension in fibrillar-like adhesions compared to basal fibrillogenesis. Our findings have potential implications for how mechanical thrombus integrity might be maintained during remodeling and vascular repair.

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Sigma-Aldrich
黏着斑蛋白单克隆抗体 小鼠抗, clone hVIN-1, ascites fluid
Sigma-Aldrich
Anti-Tensin 1 antibody produced in rabbit, ~1.0 mg/mL, affinity isolated antibody
Sigma-Aldrich
抗磷酸化ILK (Ser246) 抗体, from rabbit, purified by affinity chromatography