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• W2005641346 abstract "We investigated whether activation of integrin receptors could modulate the expression of monocyte chemotactic protein‐1 (MCP‐1) in human hepatic stellate cells (HSC), mesenchymal cells responsible for extracellular matrix synthesis within the liver. When compared to non‐adherent cells, HSC plated on collagen types I or IV, or fibronectin, showed increased MCP‐1 gene expression and protein secretion in the conditioned medium. Increased MCP‐1 secretion was also observed when cells were plated on dishes coated with a monoclonal antibody directed against the β1‐integrin subunit, demonstrating that ligation of β1‐integrins is sufficient to stimulate MCP‐1 expression. Conversely, integrin‐independent cell adhesion on poly‐ l ‐lysine did not modify MCP‐1 secretion. Disruption of the actin cytoskeleton by cytochalasin D blocked the collagen‐dependent increase in MCP‐1 secretion. Chemotactic assay of HSC‐conditioned medium showed that HSC plated on collagen secrete higher amounts of chemotactic factors for lymphomonocytes, and that MCP‐1 accounts for the great majority of this effect. These findings indicate a novel mechanism of MCP‐1 regulation possibly relevant in those conditions where HSC interact with an altered extracellular matrix." @default.
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• W2005641346 date "1997-09-08" @default.
• W2005641346 modified "2023-10-18" @default.
• W2005641346 title "Integrin‐mediated stimulation of monocyte chemotactic protein‐1 expression" @default.
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• W2005641346 doi "https://doi.org/10.1016/s0014-5793(97)01004-1" @default.
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