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- W2077460064 endingPage "951" @default.
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- W2077460064 abstract "Summary. Background: Various types of laminin (LN) are ubiquitous components of basement membrane and exposed to blood upon localized damage of vascular endothelial cells. Fibronectin is a plasma protein that is insolubilized into fibrils in a regulated fashion by, for example, lysophosphatidic acid (LPA)-stimulated fibroblasts or platelets spread on supportive adhesive ligands. Objective: To study assembly of plasma fibronectin by LPA-activated platelets adherent to LN-111 via α6β1 integrin. Results: Platelets adherent to LN-111-bound plasma fibronectin or its N-terminal 70 kD fragment in fibrillar arrays at the periphery of spread platelets under static but not shear conditions. Formation of fibronectin arrays under static conditions was inhibited by co-incubation with the N-terminal 70 kD fragment or with a 49-amino acid peptide that binds to the N-terminal region of fibronectin. Approximately 7000 fibronectin dimers bound per adherent platelet with a Kd of 50 nm. Bound 70 kD fragment was readily solubilized with deoxycholate (DOC), whereas bound fibronectin became progressively insoluble. Bound 70 kD fragment became resistant to DOC extraction after treatment with a cell-impermeable, reducible crosslinker. Crosslinked 70 kD fragment was found in a high molecular weight complex. As with fibroblasts, signaling molecules modulating actin cytoskeletal organization controlled expression of binding sites for the N-terminal 70 kD region of fibronectin on adherent platelets. Conclusions: These results indicate that platelets adherent to LN-111 via α6β1 support subsequent assembly of fibronectin, but possibly only under conditions of intermittent or stagnant blood flow." @default.
- W2077460064 created "2016-06-24" @default.
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- W2077460064 date "2006-05-01" @default.
- W2077460064 modified "2023-09-30" @default.
- W2077460064 title "Characterization of fibronectin assembly by platelets adherent to adsorbed laminin‐111" @default.
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- W2077460064 doi "https://doi.org/10.1111/j.1538-7836.2006.01862.x" @default.
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