title: Fibronectin remodelling: cell-mediated regulation of the microenvironment.
abstract: The biophysical, mechanical and chemical characteristics of extracellular matrixes influence many cellular functions to control tissue homoeostasis and drive progression of cancer and inflammatory diseases. To maintain normal tissue function, fibronectin-rich matrixes are subject to dynamic cell-mediated structural and chemical modification. In this article, we discuss how localized application of mechanical force, heterodimer-specific integrin engagement and matrix proteolysis regulate fibronectin assembly and turnover. We also speculate that recently identified integrin trafficking, syndecan signalling and adhesion receptor-growth factor receptor cross-talk mechanisms might dynamically control the function, assembly and mechanical properties of a viable, and mechanoresponsive, fibronectin network.
authors.affiliation: *Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Nuffield Building, Crown Street, Liverpool L69 3BX, U.K.
authors.forename: Katarzyna I
authors.initials: KI
authors.lastname: Wolanska
authors.affiliation: *Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Nuffield Building, Crown Street, Liverpool L69 3BX, U.K.
authors.forename: Mark R
authors.initials: MR
authors.lastname: Morgan
mesh_terms: D000818:Animals; D002448:Cell Adhesion; D005109:Extracellular Matrix / Q000378:metabolism* / Q000648:ultrastructure; D005353:Fibronectins / Q000502:physiology* / Q000648:ultrastructure; D022001:Focal Adhesions / Q000378:metabolism / Q000648:ultrastructure; D006706:Homeostasis; D006801:Humans; D020782:Matrix Metalloproteinases / Q000378:metabolism; D021381:Protein Transport; D059748:Proteolysis
chemical_list: D005353:Fibronectins; D020782:Matrix Metalloproteinases