Fibrinogen lysine residue A alpha 157 plays a crucial role in the fibrin-induced acceleration of plasminogen activation, catalyzed by tissue-type plasminogen activator.
In previous studies, we have shown that the stretch 148-197 of the fibrinogen A alpha chain plays a crucial role in the acceleration of the tissue-type plasminogen activator (t-PA)-catalyzed plasminogen activation. In this study we have synthesized parts of A alpha 148-197 and analogues thereof. We found that the peptides with sequences identical with A alpha 148-161 and A alpha 149-161 of human fibrinogen accelerate the plasminogen activation by t-PA, whereas the corresponding peptides in which lysine residues A alpha 157 had been replaced by valine or arginine had no accelerating capacity. Furthermore, succinylation of the lysine residue(s) in the synthesized peptides A alpha 148-161 and A alpha 149-161 leads to loss of accelerating action. These findings show that lysine residue A alpha 157 is crucial for the accelerating action of fibrin on the t-PA-catalyzed plasminogen activation.
D000596:Amino Acids / Q000032:analysis; D005337:Fibrin / Q000494:pharmacology*; D005340:Fibrinogen / Q000032:analysis*; D006801:Humans; D008239:Lysine / Q000032:analysis*; D010959:Tissue Plasminogen Activator / Q000494:pharmacology*
D000596:Amino Acids; D005337:Fibrin; D005340:Fibrinogen; D010959:Tissue Plasminogen Activator; D008239:Lysine