Document Detail

Oxidative stress induces S-thiolation of specific proteins in cultured gastric mucosal cells.
MedLine Citation:
PMID:  8141298     Owner:  NLM     Status:  MEDLINE    
Oxidative stress induces the formation of protein-mixed disulfides with low-molecular-weight thiols, especially glutathione. We analyzed this process, termed S-thiolation, in cultured gastric mucosal cells from guinea pigs by gel electrophoresis and autoradiography after radiolabeling of the intracellular glutathione pool with 35S. Hydrogen peroxide (H2O2) or diamide initiated rapid and reversible S-thiolation of specific proteins with molecular masses of 42, 30, 29, 28, and 22 kDa. Diamide caused particularly prominent S-thiolation of the 42 kDa protein. This protein was identified as actin by immunoblot analysis and actin-myosin precipitation. Fluorescence microscopy revealed that diamide caused a disappearance of normal stress fibers and a concomitant increase in actin polymerization in association with contraction of the cells. These morphological changes were completely reversible within minutes. With cells depleted of glutathione by incubation with DL-buthionine-[S,R]-sulfoximine, diamide caused severe contraction and rounding, and the cells detached from the culture plates. S-thiolation of actin could help protect gastric mucosal cells against irreversible organization of microfilaments by preserving microfilament dynamics under oxidative stress.
K Rokutan; R B Johnston; K Kawai
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The American journal of physiology     Volume:  266     ISSN:  0002-9513     ISO Abbreviation:  Am. J. Physiol.     Publication Date:  1994 Feb 
Date Detail:
Created Date:  1994-04-28     Completed Date:  1994-04-28     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370511     Medline TA:  Am J Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  G247-54     Citation Subset:  IM    
Department of Nutrition, School of Medicine, University of Tokushima, Japan.
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MeSH Terms
Actins / metabolism
Cells, Cultured
Cystine / pharmacokinetics
Diamide / pharmacology*
Gastric Mucosa / cytology,  metabolism*,  ultrastructure
Glutathione / metabolism
Guinea Pigs
Hydrogen Peroxide / pharmacology*
Intracellular Membranes / metabolism
Microfilaments / ultrastructure
Microscopy, Fluorescence
Proteins / metabolism*
Sulfhydryl Compounds / metabolism*
Grant Support
Reg. No./Substance:
0/Actins; 0/Proteins; 0/Sulfhydryl Compounds; 10465-78-8/Diamide; 56-89-3/Cystine; 70-18-8/Glutathione; 7722-84-1/Hydrogen Peroxide

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