A secreted caspase-3-substrate-cleaving activity at low pH belongs to cathepsin B: a study on primary brain cell cultures

被引：11

作者：

Onufriev, M. V. ^{[1
]}

Yakovlev, A. A. ^{[1
,2
]}

Lyzhin, A. A.

Stepanichev, M. Yu. ^{[1
]}

Khaspekov, L. G. ^{[3
]}

Gulyaeva, N. V. ^{[1
]}

机构：

[1] Russian Acad Sci, Inst Higher Nervous Activ & Neurophysiol, Moscow 117485, Russia

[2] Russian Acad Sci, Inst Theoret & Expt Biophys, Pushchino 142290, Moscow Region, Russia

[3] Russian Acad Med Sci, Neurol Res Ctr, Moscow 125367, Russia

来源：

BIOCHEMISTRY-MOSCOW | 2009年 / 74卷 / 03期

基金：

俄罗斯基础研究基金会;

关键词：

cathepsin B; caspase-3; ischemia/reoxygenation; neurons; glia; FOCAL CEREBRAL-ISCHEMIA; POLY(ADP-RIBOSE) POLYMERASE; CATALYZED HYDROLYZES; CYSTEINE PROTEASES; INDUCED APOPTOSIS; NEURONAL DEATH; CLEAVAGE; CASPASE; DEGRADATION; INHIBITION;

D O I：

10.1134/S0006297909030067

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：

The cysteine proteases caspase-3 and cathepsins are involved in both neuronal plasticity and neuropathology. Using primary neuroglial and glial cerebellar cultures, the pH dependence of cleavage of a synthetic caspase-3 substrate, Ac-DEVD-AMC, was studied. At acidic pH, cathepsin B cleaved Ac-DEVD, this activity being significantly higher than that of caspase-3 at pH 7.4. This activity is blocked by peptide inhibitors of both caspase-3 and cathepsin B. Substitution of culture medium for balanced salt solution stimulated cathepsin B secretion in both types of cultures. Ischemia (oxygen-glucose deprivation) significantly decreased secretion of cathepsin B activities into the culture medium.

引用

页码：281 / 287

页数：7

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