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May 1987

Altered Production of Fibronectin and Collagen in Hypercortisolism May Inhibit Tissue Repair

Author Affiliations

Department of Anatomy and Cellular Biology Tufts University School of Medicine 136 Harrison Ave Boston, MA 02111

Arch Dermatol. 1987;123(5):570-571. doi:10.1001/archderm.1987.01660290034011

To the Editor.—  Fibronectin, a large glycoprotein found in the circulation and in the extracellular matrix of adherent cells, is present during wound healing and, like collagen, is important for tissue repair.1 Fibronectin contributes significantly to the formation of granulation tissue during wound healing.1,2 Fibroblasts migrate into the wound area and rapidly produce a transient matrix of fibronectin,2 which is important for the subsequent assembly of granulation tissue components—in particular, collagens type I and type III, heparin sulfate proteoglycan, and chondroitin sulfate.1I and others have observed that fibronectin biosynthesis is stimulated as much as fourfold in human skin fibroblasts by physiologic concentrations of glucocorticoids.3 In contrast, biosynthesis of collagens type I and III decreases as a result of glucocorticoid treatment, both in vivo and in cultured fibroblasts.4 The temporary increase in fibronectin production during the development of granulation tissue is probably a normal

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