Molecular cloning and partial characterization of rat procarboxypeptidase R and carboxypeptidase N.
Microbiol Immunol
; 44(8): 719-28, 2000.
Article
en En
| MEDLINE
| ID: mdl-11021404
ABSTRACT
Carboxypeptidase R (EC 3.4.17.20) (CPR) and carboxypeptidase N (EC 3.4.17.3) (CPN) cleave carboxy-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Although CPN is present in a stable active form in plasma, CPR is generated from proCPR, a plasma zymogen, by proteolytic enzymes such as thrombin, thrombin-thrombomodulin complex and plasmin. We have isolated rat proCPR and CPN cDNA clones which can induce enzymatic activities in culture supernatants of the transfected cells. mRNA of proCPR was detected only in rat liver by Northern hybridization and showed hepatocyte-specific expression. Expression of proCPR mRNA was enhanced following LPS injection, indicating that proCPR production is increased under inflammatory conditions.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Lisina Carboxipeptidasa
/
Carboxipeptidasas
Límite:
Animals
Idioma:
En
Revista:
Microbiol Immunol
Año:
2000
Tipo del documento:
Article
País de afiliación:
Japón