Document Detail

Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32.
MedLine Citation:
PMID:  8670109     Owner:  NLM     Status:  MEDLINE    
Interleukin-1 beta converting enzyme (ICE)-like proteases, which are synthesized as inactive precursors, play a key role in the induction of apoptosis. We now demonstrate that benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK), an ICE-like protease inhibitor, inhibits apoptosis by preventing the processing of CPP32 to its active form. These results suggest that novel inhibitors of apoptosis can be developed which prevent processing of proforms of ICE-like proteases.
E A Slee; H Zhu; S C Chow; M MacFarlane; D W Nicholson; G M Cohen
Related Documents :
9190289 - A combinatorial approach for determining protease specificities: application to interle...
16413409 - Specific protein interaction of human pag with omi/htra2 and the activation of the prot...
12910449 - Investigation of the induced-fit mechanism and catalytic activity of the human cytomega...
20070259 - Taking the plunge: integrating structural, enzymatic and computational insights into a ...
11701129 - Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate bin...
2536819 - Proteolytic cleavage of encephalomyocarditis virus capsid region substrates by precurso...
8515459 - Stability and folding kinetics of ribonuclease t1 are strongly altered by the replaceme...
17224199 - Serine scanning: a tool to prove the consequences of n-glycosylation of proteins.
19368529 - Structure-activity analysis of aging and reactivation of human butyrylcholinesterase in...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  315 ( Pt 1)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1996 Apr 
Date Detail:
Created Date:  1996-08-05     Completed Date:  1996-08-05     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  21-4     Citation Subset:  IM    
MRC Toxicology Unit, University of Leicester, Lancaster Road, Leicester, U.K.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Chloromethyl Ketones / pharmacology*
Amino Acid Sequence
Apoptosis / drug effects*
Caspase 3
Cysteine Endopeptidases / drug effects*,  metabolism*
Cysteine Proteinase Inhibitors / pharmacology
Enzyme Activation / drug effects
Leukemia, Monocytic, Acute / enzymology,  pathology
Leukemia, T-Cell / enzymology,  pathology
Molecular Sequence Data
Oligopeptides / pharmacology
Poly(ADP-ribose) Polymerases / antagonists & inhibitors,  metabolism
Protease Inhibitors / pharmacology*
Tumor Cells, Cultured
Reg. No./Substance:
0/Amino Acid Chloromethyl Ketones; 0/Cysteine Proteinase Inhibitors; 0/Oligopeptides; 0/Protease Inhibitors; 0/acetyl-aspartyl-glutamyl-valyl-aspartal; 0/benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone; EC Polymerases; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspases; EC 3.4.22.-/Cysteine Endopeptidases

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

Previous Document:  Alpha and beta isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mam...
Next Document:  Characterization, cell-surface expression and ligand-binding properties of different truncated N-ter...