Inhibition of rat tissue kallikrein gene family members by rat kallikrein‐binding protein and α1‐proteinase inhibitor

FEBS Letters

Chao, J.²  Serveau, C.¹  Zhou, G.X.²  Moreau, T.¹  Gauthier, F.¹ 

[1] Laboratoire d'Enzymologie et Chimie des Protèines, URA CNRS1334, Université François Rabelais, 2bis Boulevard Tonnellè F-37032 Tours Cedex, France;Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425 USA

关键词: Kallikrein;    Serpin;    Proteinase inhibitor;    Kallikrein-binding protein;    Z;    benzyloxycarbonyl;    -MCA;    7-amido-4-methylcoumarin;    pNPGB;    p-nitrophenyl-p′guanidinobenzoate;    Abz;    α-aminobenzoyl;    EDDnp;    ethylenediamine 2-4-dinitrophenyl;    Tos-Arg-OMc;    p-tosyl-arginyl-methylester;    α1-PI;    α1-proteinase inhibitor;    rKBP;    rat kallikrein-binding protein;   

DOI  :  10.1016/0014-5793(92)80817-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The regulation of tissue kallikrein activity by plasma serine proteinase inhibitors (serpins) was investigated by measuring the association rate constants of six tissue-kallikrein family members isolated from the rat submandibular gland, with rat kallikrein-binding protein (rKBP) and α1-proteinase inhibitor (α1-PI). Both these serpins inhibited kallikreins rK2, rK7, rK8, rK9 and rK10¹ with association rate constants in the 10³–10⁴ M⁻¹·s⁻¹ range, whereas only ‘true’ tissue kallikrein rK1 was not suceptible to α1-PI. This results in slow inhibition of rK1 by plasma serpins, which could explain why this kallikrein is the ony member of the gene family identified so far that induces a transient decrease in blood pressure when injected in minute amounts into the circulation.

【 授权许可】

Unknown