Carboxypeptidase N: a pleiotropic regulator of inflammation.
Carboxypeptidase N (CPN) is a plasma zinc metalloprotease, which consists of two enzymatically active small subunits (CPN1) and two large subunits (CPN2) that protect the protein from degradation. CPN cleaves carboxy-terminal arginines and lysines from peptides found in the bloodstream such as complement anaphylatoxins, kinins, and creatine kinase MM (CK-MM). By removing only one amino acid, CPN has the ability to change peptide activity and receptor binding. CPN is a member of a larger family of carboxypeptidases, many of which also cleave arginine and lysine. Because of the highly conserved active sites and the possible redundant functions of carboxypeptidases, it has been difficult to elucidate the role of CPN in disease processes. The future use of gene ablation technology may be the most appropriate way to understand the function of CPN in vivo.
Matthews
Kirstin W
KW
Institute of Molecular Medicine for the Prevention of Human Diseases, University of Texas-Houston, 2121 West Holcombe Blvd, Houston, TX 77030, USA.
Mueller-Ortiz
Stacey L
SL
Wetsel
Rick A
RA
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D007249:Inflammation / Q000378:metabolism*; D001121:Lysine Carboxypeptidase / Q000172:deficiency / Q000235:genetics* / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D009569:Nitric Oxide / Q000378:metabolism; D051381:Rats; D017422:Sequence Analysis, DNA; D020539:Sequence Analysis, Protein; D013379:Substrate Specificity
D009569:Nitric Oxide; D001121:Lysine Carboxypeptidase