Autoactivation of pancreatic trypsinogen is controlled by carbohydrate-specific interaction

被引：3

作者：

Ogawa, Haruko ^{[1
,2
]}

Kusumi, Izumi ^{[1
]}

Ogata, Aya ^{[1
]}

Wada, Arisa ^{[1
]}

Sakagami, Hiromi ^{[1
]}

Mitsuhashi, Kana ^{[1
]}

Date, Kimie ^{[1
]}

机构：

[1] Ochanomizu Univ, Grad Sch Humanities & Sci, Bunkyo Ku, Tokyo 1128610, Japan

[2] Ochanomizu Univ, Glycosci Inst, Bunkyo Ku, Tokyo 1128610, Japan

来源：

FEBS LETTERS | 2015年 / 589卷 / 05期

关键词：

Trypsinogen; Autoactivation-inhibition; Carbohydrate-recognition; Zymogen granule; Pancreatitis; Self-defense mechanism; BINDING-PROPERTIES; ALPHA-AMYLASE; GLYCOPROTEINS; LECTIN; OLIGOSACCHARIDES; GLYCOSYLATION; PURIFICATION; VITRONECTIN; MEMBRANE; PROTEINS;

D O I：

10.1016/j.febslet.2015.01.015

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Activation of bovine pancreatic trypsinogen (BPTG) by trypsin (BPT) was found to be inhibited by D GalN/GalNAc at pH 5.5, the pH of secretory granules in the pancreas. Binding studies with biotinylated sugar-polymers indicated that BPTG and BPT bind to alpha-GalNAc, alpha-Man, and alpha-Gal better at pH 5.5 than at pH 7.5. Ultraviolet-difference spectra indicated that BPTG binding to alpha-GalNAc differs substantially from BPTG binding to other sugars. The N-alpha-benzoyl-D,L-arginine-p-nitroanilide hydrochloride- hydrolyzing activity of BPT was only slightly affected by these sugars. The results indicate that the binding of GalNAc - containing glycoconjugates protects BPTG from autoactivation, and this may be a self-defense mechanism against intrapancreatic activation. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：569 / 575

页数：7

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