Abstract
Fibronectins are modular cell-adhesive and matrix-organizing glycoproteins that aid wound healing by stimulating cell attachment and migration and by forming part of the initial connective tissue matrix at wound sites (Hynes, 1986; Hynes and Yamada, 1982; Yamada et al., 1985; Mosher, 1984; Grinnell, 1984; D’Ardenne and McGee, 1984; J. McDonagh, 1985). In vivo, fibronectins occur in soluble form in plasma as well as in basal lamina and loose connective tissue matrices. In culture, so-called cellular fibronectin is produced by many cells, where it is secreted and assembled into an insoluble matrix under and around professional matrix-secreting cells such as fibroblasts, under epithelial cells or largely secreted into the culture medium as is the case for macrophages (Villiger et al., 1981; Alitalo et al., 1980). At wound-healing sites, fibronectin may arise from local synthesis by cells involved in wound healing (macrophages, endothelial cells, fibroblasts, certain epithelial cells) as well as from deposition from plasma (Oh et al., 1981). This chapter reviews recent developments in the fibronectin gene and polypeptide structure, its binding activities, and potential role in extracellular matrix organization and wound healing.
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Mcdonald, J.A. (1988). Fibronectin. In: Clark, R.A.F., Henson, P.M. (eds) The Molecular and Cellular Biology of Wound Repair. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1795-5_18
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