Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator.
Article Details
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Skidgel RA, Erdos EG
Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator.
Int Immunopharmacol. 2007 Dec 20;7(14):1888-99. doi: 10.1016/j.intimp.2007.07.014. Epub 2007 Aug 15.
- PubMed ID
- 18039526 [ View in PubMed]
- Abstract
Human carboxypeptidase N (CPN) was discovered in the early 1960s as a plasma enzyme that inactivates bradykinin and was identified 8 years later as the major "anaphylatoxin inactivator" of blood. CPN plays an important role in protecting the body from excessive buildup of potentially deleterious peptides that normally act as local autocrine or paracrine hormones. This review summarizes the structure, enzymatic properties and function of this important human enzyme, including insights gained by the recent elucidation of the crystal structure of the CPN catalytic subunit and structural modeling of the non-catalytic regulatory 83 kDa subunit. We also discuss its physiological role in cleaving substrates such as kinins, anaphylatoxins, creatine kinase, plasminogen receptors, hemoglobin and stromal cell-derived factor-1alpha (SDF-1alpha).
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Zinc chloride Carboxypeptidase N catalytic chain Protein Humans UnknownCofactorDetails Zinc chloride Carboxypeptidase N subunit 2 Protein Humans UnknownCofactorDetails Zinc sulfate, unspecified form Carboxypeptidase N catalytic chain Protein Humans UnknownCofactorDetails Zinc sulfate, unspecified form Carboxypeptidase N subunit 2 Protein Humans UnknownCofactorDetails