Basic carboxypeptidases: regulators of peptide hormone activity

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Abstract

The importance of basic carboxypeptidases (i.e. enzymes that cleave C-terminal arginine or lysine from proteins or peptides) has recently become more evident, in part because of the dramatic growth of research on biologically active peptides. It has been known for many years that carboxypeptidase B acts in concert with other digestive enzymes to degrade proteins and peptides in the digestive tract and that plasma carboxypeptidase N (kininase I) can inactivate peptides such as kinins and anaphylatoxins in the circulation. Randal Skidgel reviews more recent findings that have expanded the possible roles for this type of carboxypeptidase to include participation in the processing of peptide hormone precursors and in the regulation of the receptor specificity of active peptides. Two recently described basic carboxypeptidases have these roles: carboxypeptidase H (enkephalin convertase), an enzyme in secretory granules involved in peptide hormone processing; and carboxypeptidase M, a plasma membrane-bound enzyme, which could regulate peptide hormone activity at the cell surface.

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