Factor XIII (plasma transglutaminase, fibrin stabilizing factor) is a plasma protein that plays an important role in the final stages of blood coagulation and fibrinolysis. It circulates in blood as a tetramer consisting of two “A” and two “B” subunits (1, 2). The amino acid sequence of the enzymatically active subunit, Factor XIII A, is unique and does not exhibit internal homology, but its active center is similar to that of the thiol proteases. Factor XIII A is activated by thrombin and calcium ion to a transglutaminase that catalyzes the cross linking of fibrin molecules, forming intermolecular isopeptide bonds, thus stabilizing blood clots (3, 4). In two diseases that share some histological resemblance (Lymphocyte-poor graft-versus-host-reaction and toxic epidermal necrolysis), Factor-XIII A-positive dendrocytes show some morphological changes, probably as a response to altered cytokine environment. Factor-XIII A-positive dendrocytes thus are reported to possibly play a role in the regulation of the connective tissue remodeling that may accompany epidermal destruction (5).
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