Abstract
The glycosaminoglycan, hyaluronan (HA), previously known as hyaluronic acid, is a major component in pericellular coats of proliferating and migrating cells that are active in developing, regenerating and repairing tissues. Although the concentration of HA is very low in plasma it does become elevated in the extracellular space of tissues shortly after fibrin clot formation. It is known that HA binds to several extracellular, cell surface and plasma proteins including fibrinogen/fibrin. HA was observed to bind specifically to fibrinogen (Kd10 -7 M -1 ) [1] and to increase the rate of fibrin monomer polymerization causing an associated increase in the turbidity of the clots [2]. The structure of HA consists of a repeat disaccharide unit comprised of glucuronic acid and N-acetylated glucosamine-the degree of polymerization ranging from 500 to several thousand of such units [3]. In investigating the properties of HA and derivatives prepared by esterification of the free carboxyl of glucuronic acid, we have observed both inhibition of clot lysis and a stimulation of clot formation by HA which is lost upon esterification
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