Document Detail


Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins.
MedLine Citation:
PMID:  14581476     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Increasing evidence suggests that lysosomal proteases are actively involved in apoptosis. Using HeLa cells as the model system, we show that selective lysosome disruption with L-leucyl-L-leucine methyl ester results in apoptosis, characterized by translocation of lysosomal proteases into the cytosol and by the cleavage of a proapoptotic Bcl-2-family member Bid. Apoptosis and Bid cleavage, but not translocation of lysosomal proteases to the cytosol, could be prevented by 15 microM L-trans-epoxysuccinyl(OEt)-Leu-3-methylbutylamide, an inhibitor of papain-like cysteine proteases. Incubation of cells with 15 microM N-benzoyloxycarbonyl-VAD-fluoromethyl ketone prevented apoptosis but not Bid cleavage, suggesting that cathepsin-mediated apoptosis in this system is caspase-dependent. In vitro experiments performed at neutral pH showed that papain-like cathepsins B, H, L, S, and K cleave Bid predominantly at Arg(65) or Arg(71). No Bid cleavage was observed with cathepsins C and X or the aspartic protease cathepsin D. Incubation of full-length Bid treated with cathepsins B, H, L, and S resulted in rapid cytochrome c release from isolated mitochondria. Thus, Bid may be an important mediator of apoptosis induced by lysosomal disruption.
Authors:
Tina Cirman; Kristina Oresić; Gabriela Droga Mazovec; Vito Turk; John C Reed; Richard M Myers; Guy S Salvesen; Boris Turk
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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.     Date:  2003-10-27
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  279     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2004 Jan 
Date Detail:
Created Date:  2004-01-26     Completed Date:  2004-03-11     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3578-87     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia.
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MeSH Terms
Descriptor/Qualifier:
Animals
Apoptosis*
BH3 Interacting Domain Death Agonist Protein
Carrier Proteins / metabolism,  physiology*
Caspase 8
Caspases / metabolism
Cathepsins / metabolism*
Cell Line
Cell Line, Tumor
Cytochromes c / metabolism
Cytosol / metabolism
Flow Cytometry
Hela Cells
Humans
Hydrogen-Ion Concentration
Liver / metabolism
Lysosomes / metabolism*
Mice
Mitochondria / metabolism
Models, Biological
Models, Molecular
Myocardium / metabolism
Papain / chemistry*
Protein Structure, Secondary
Protein Transport
Recombinant Proteins / metabolism
Temperature
Transfection
Grant Support
ID/Acronym/Agency:
GM60554/GM/NIGMS NIH HHS; NS37878/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/BH3 Interacting Domain Death Agonist Protein; 0/BID protein, human; 0/Bid protein, mouse; 0/Carrier Proteins; 0/Recombinant Proteins; 9007-43-6/Cytochromes c; EC 3.4.-/Cathepsins; EC 3.4.22.-/CASP8 protein, human; EC 3.4.22.-/Casp8 protein, mouse; EC 3.4.22.-/Caspase 8; EC 3.4.22.-/Caspases; EC 3.4.22.2/Papain

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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