[Abstract] [Full Text PDF] (in Japanese / 2563KB) [Members Only And Two Factor Auth.]

J.Jpn. Surg. Soc.. 85(9): 882-886, 1984


Report on the annual meeting

FIBRONECTIN-ITS FUNCTIONS AND ROLES IN THE TISSUE REPAIR

Division of Hemostasis and Thrombosis Research, Institute of Hematology and Department of Surgery, Jichi Medical School, Tochigi, Japan

Michio Matsuda

Fibronectin is a recently charactrized 4.4×105 dalton glycoprotein consisting of two probably identical 2.2×105 dalton subunits held together by disulfide linkages.
It is present as a soluble fraction in plasma at about 30mg/dl and is widely distributed as an insoluble component to various tissues, in close association with fibrillar structures of connectiv tissue matrices, basement membranes and certain mesenchymal cells including fibroblasts and smooth muscle cells. Fibronectin binds to fibrin and collagen reversibly and crosslinks to these filamentous proteins catalyzed by the activated blood coagulation factor XIII (plasma transglutaminase).
Plasma fibronectin appears to be utilized at the healing wounds, thus its concentration decreases during early postoperative days. Immunofluorescence study shows that fibronectin is closely associated with newly generated fibroblasts and fibrillar structures in the early stage of wound healing, and that it diminishes in accordance with the maturation of collagen fibers.
Plasma fibronectin is shown to function to remove the colloidal debris from blood via the reticuloendothelial system and to play important roles in organizing the cytoskeleton and in the migration and spreading of interstitial cells.
Thus fibronectin seems to play a pivotal role in the tissue repair via a variety of biological functions.


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