Different inhibition characteristics of intracellular transglutaminase activity by cystamine and cysteamine.
- Author:
Ju Hong JEON
1
;
Hye Jin LEE
;
Gi Yong JANG
;
Chai Wan KIM
;
Dong Myung SHIN
;
Sung Yup CHO
;
Eui Ju YEO
;
Sang Chul PARK
;
In Gyu KIM
Author Information
1. Department of Biochemistry and Molecular Biology/Aging Apoptosis Research Center (AARC) Seoul National University College of Medicine Seoul 110-799, Korea. igkim@plaza.snu.ac.kr
- Publication Type:Original Article ; Comparative Study ; Research Support, Non-U.S. Gov't
- Keywords:
cystamine;
cysteamine;
inhibitor;
polyamine;
transglutaminase
- MeSH:
Cell Line, Tumor;
Comparative Study;
Cystamine/*pharmacology;
Cysteamine/*pharmacology;
Enzyme Inhibitors/*pharmacology;
Humans;
Research Support, Non-U.S. Gov't;
Transglutaminases/*antagonists & inhibitors
- From:Experimental & Molecular Medicine
2004;36(6):576-581
- CountryRepublic of Korea
- Language:English
-
Abstract:
The treatment of cystamine, a transglutaminase (TGase) inhibitor, has beneficial effects in several diseases including CAG-expansion disorders and cataract. We compared the inhibition characteristics of cystamine with those of cysteamine, a reduced form of cystamine expected to be present inside cells. Cystamine is a more potent inhibitor for TGase than cysteamine with different kinetics pattern in a non- reducing condition. By contrast, under reducing conditions, the inhibitory effect of cystamine was comparable with that of cysteamine. However, cystamine inhibited intracellular TGase activity more strongly than cysteamine despite of cytoplasmic reducing environment, suggesting that cystamine itself inhibits in situ TGase activity by forming mixed disulfides.
