Retinoid — Regulated Expression of Tissue Transglutaminase in Normal and Leukemic Myeloid Cells
Transglutaminases are a group of enzymes that catalyze the covalent cross-Unking of proteins by facilitating the formation of ε-(γ-glutaminyl)-lysyl isopeptide bonds between protein-bound glutamine and lysine residues (1). Since the isopeptie bond is an unusually stable form of protein cross-link one may reasonably ask what is the purpose for inducing such stable bonds between polypeptide chains. In the case of the extracellular transglutaminases the answer to this question seems to be linked to the formation of mechanically stable protein clots. For instance, the seminal plasma of certain rodents contains a specific transglutaminase that cross-links seminal plasma proteins leading to the formation of a dense copulatory plug that forms in the cervical canal (2). The extensive cross-Unking of these proteins is linked to the formation of a clot that is stable for weeks. Blood plasma also contains a specific transglutaminase, plasma factor XIIIa, that is involved in the stabilization of fibrin clots. This enzyme is activated during the clotting reaction and covalently cross-links fibrin chains (3). Factor XIII also cross-links fibrin to fibronectin and possibly to collagen, a reaction that may stabilize the association of the clot with the vessel wall and platelets (4). Factor XIII also covalently incorporates A2-antiplasmin into the nascent fibrin clot (5).
KeywordsRetinoic Acid Factor Xiii Leukemic Myeloid Cell Mouse Peritoneal Macrophage Tissue Transglutaminase
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