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IL‐1β enhances cell adhesion to degraded fibronectin
Author(s) -
Rajshankar Dhaarmini,
Downey Gregory P.,
McCulloch Christopher A.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.12-207381
Subject(s) - library science , medicine , gerontology , computer science
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 β 1 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. FASEB J. 26, 4429–4444 (2012). www.fasebj.org