Pro-Carboxypeptidase R Cleaves Bradykinin following Activation

Tsurayuki Shinohara(Fukuoka University), Chikai Sakurada(Nagoya City University), Takashi Suzuki(Nagoya City University), Oki Takeuchi(Nagoya City University), William Campbell(Nagoya City University), Seiyo Ikeda(Fukuoka University), Noriko Okada, Hidechika Okada(Nagoya City University)
International Archives of Allergy and Immunology
September 3, 2009
Cited by 81

Abstract

Arginine carboxypeptidase (CPR) is a labile enzyme present in human serum which is unrelated to carboxypeptidase N. In this study we demonstrate that CPR exists in a precursor form in plasma and can be converted to the active form by trypsin and presumable trypsin-like enzymes. The trypsin-generated active form can not only cleave a small synthetic substrate, hippuryl-L-arginine, but can remove terminal arginine from bradykinin.


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