IL-1β enhances cell adhesion to degraded fibronectin
Autor: | Gregory P. Downey, Christopher A. McCulloch, Dhaarmini Rajshankar |
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Jazyk: | angličtina |
Rok vydání: | 2012 |
Předmět: |
Talin
Integrin Interleukin-1beta Gingiva Biology Biochemistry Research Communications Extracellular matrix Focal adhesion Cell membrane Mice Genetics medicine Cell Adhesion Animals Humans RNA Small Interfering Cell adhesion Molecular Biology Cells Cultured Cell adhesion molecule Integrin beta1 Cell Membrane Membrane Proteins Adhesion Fibroblasts Cell biology Fibronectins Neoplasm Proteins Fibronectin medicine.anatomical_structure Gene Expression Regulation Gene Knockdown Techniques biology.protein Matrix Metalloproteinase 3 Biotechnology Protein Binding Signal Transduction |
Popis: | IL-1β is a prominent proinflammatory cytokine that mediates degradation of extracellular matrix proteins through increased expression of matrix metalloproteinases, which involves a signaling pathway in adherent cells that is restricted by focal adhesions. Currently, the mechanism by which IL-1β affects cell adhesion to matrix proteins is not defined, and it is not known whether degraded matrix proteins affect IL-1β signaling. We examined adhesion-related IL-1β signaling in fibroblasts attaching to native or MMP3-degraded fibronectin. IL-1β increased cell attachment, resistance to shear force and the numbers of focal adhesions containing activated β1 integrins. IL-1β-enhanced attachment required FAK, kindlins 1/2, and talin. MMP3-degraded fibronectin-inhibited IL-1β-enhanced cell adhesion and promoted spontaneous ERK activation that was independent of IL-1β treatment. We conclude that IL-1β enhances the adhesion of anchorage-dependent cells to MMP3-degraded fibronectin, which, in turn, is associated with deregulated cellular responses to IL-1β. These data point to a novel role of IL-1β as a proadhesive signaling molecule in inflammation that employs kindlins and talin to regulate adhesion.—Rajshankar, D., Downey, G. P., McCulloch, C. A. IL-1β enhances cell adhesion to degraded fibronectin. |
Databáze: | OpenAIRE |
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