Effects of Various N-Terminal Peptides of Glu-Plasminogen on Keeping Its Tight Conformation of Glu-Plasminogen
Glu-plasminogen (Glu-plg) is a single chain plasma glycoprotein, which is the zymogen form of a serine protease, plasmin. The conversion from the precursor to the enzyme occurs as a result of cleavage of the Arg560-Val561 peptide bond in plasminogen splitting to the heavy chain and the light chain, by several activators, which include tissue type plasminogen activator (tPA), urokinase type plasminogen activator (uPA) and streptokinase . In heavy chain of plasmin which coincides with the sequence of Glu1-Arg450 of Glu-plg, there are five conformationaly similar loop domains called kringle domain which binds to many regulatory molecules like fibrin and lysine analogues. Glu-plg possesses a tight conformation in the presence of chloride ion and absence of lysine analogues, and is hardly activated by activators, whereas Lys-plasminogen (Lys-plg), which is generated by the cleavage of Lys76-Lys77 peptide bond of Glu-plg by plasmin, has a looser conformation and is readily activatable [2~9]. The tight conformation of Glu-plg is considered to be caused by the intramolecular binding of N-terminal portion to the kringle 1 [10, 11] or the kringle 4 domain  through lysine binding site (LBS) or kringle 5 domain through amino-hexyl (AH) site  on the same molecule. Lysine analogues, therefore, could alter the conformation of Glu-plg to the looser form [3, 6, 8, 14] by dissociating the N-terminal peptides from LBS or AH site.
KeywordsLysine Residue Peptide Bond Tranexamic Acid Urokinase Type Plasminogen Activator Type Plasminogen Activator
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