Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
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DOI：
10.1111/j.1348-0421.2002.tb02669.x
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发表时间：
2002-01-01
影响因子：
2.6
通讯作者：
Okada, H
中科院分区：
文献类型：
--
作者：
Campbell, WD;Lazoura, E;Okada, H
羧肽酶原 R (proCPR)，也称为凝血酶激活的纤溶抑制剂 (TAFI)，是羧肽酶 U 和血浆羧肽酶 B 的前体，存在于血浆中，被凝血酶/血栓调节蛋白和/或纤溶酶激活后，可以从 C3a 和 C5a 的羧基末端去除精氨酸。我们已经证明，这种酶可以比经典的过敏毒素灭活剂羧肽酶 N (CPN) 更有效地从 C5a 八肽中去除末端精氨酸。由于我们之前已经证明 proCPR 在炎症状态下显着上调，因此这种酶似乎对 C5a 的失活有显着贡献，C5a 是补体衍生的过敏毒素中最有效的。
Pro-carboxypeptidase R (proCPR), also known as thrombin-activatable fibrinolysis inhibitor (TAFI), precursor of carboxypeptidase U and plasma carboxypeptidase B is present in plasma and following activation by thrombin/thrombomodulin and/or plasmin can remove arginine from the carboxyterminal of C3a and C5a. We have shown that this enzyme can remove terminal arginine from the C5a octapeptide much more efficiently than the classical anaphylatoxin inactivator, carboxypeptidase N (CPN). Since we have previously demonstrated that proCPR is significantly upregulated in the inflammatory state, this enzyme would appear to significantly contribute to the inactivation of C5a, the most potent of the complement derived anaphylatoxins.