Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 46 (2), 131-4

Inactivation of C3a and C5a Octapeptides by Carboxypeptidase R and Carboxypeptidase N

Affiliations

Inactivation of C3a and C5a Octapeptides by Carboxypeptidase R and Carboxypeptidase N

William D Campbell et al. Microbiol Immunol.

Abstract

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.

Similar articles

See all similar articles

Cited by 41 articles

See all "Cited by" articles

Publication types

MeSH terms

LinkOut - more resources

Feedback