Document Detail

Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis.
MedLine Citation:
PMID:  9323209     Owner:  NLM     Status:  MEDLINE    
The caspase-3 (CPP32, apopain, YAMA) family of cysteinyl proteases has been implicated as key mediators of apoptosis in mammalian cells. Gelsolin was identified as a substrate for caspase-3 by screening the translation products of small complementary DNA pools for sensitivity to cleavage by caspase-3. Gelsolin was cleaved in vivo in a caspase-dependent manner in cells stimulated by Fas. Caspase-cleaved gelsolin severed actin filaments in vitro in a Ca2+-independent manner. Expression of the gelsolin cleavage product in multiple cell types caused the cells to round up, detach from the plate, and undergo nuclear fragmentation. Neutrophils isolated from mice lacking gelsolin had delayed onset of both blebbing and DNA fragmentation, following apoptosis induction, compared with wild-type neutrophils. Thus, cleaved gelsolin may be one physiological effector of morphologic change during apoptosis.
S Kothakota; T Azuma; C Reinhard; A Klippel; J Tang; K Chu; T J McGarry; M W Kirschner; K Koths; D J Kwiatkowski; L T Williams
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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:  Science (New York, N.Y.)     Volume:  278     ISSN:  0036-8075     ISO Abbreviation:  Science     Publication Date:  1997 Oct 
Date Detail:
Created Date:  1997-10-23     Completed Date:  1997-10-23     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0404511     Medline TA:  Science     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  294-8     Citation Subset:  IM    
Chiron Corporation, Emeryville, CA 94608, USA.
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MeSH Terms
Actins / metabolism
Amino Acid Chloromethyl Ketones / pharmacology
Antigens, CD95 / physiology
Caspase 3
Cell Line
Cell Size*
Cycloheximide / pharmacology
Cysteine Endopeptidases / metabolism*
Cysteine Proteinase Inhibitors / pharmacology
Cytoskeleton / metabolism
DNA Fragmentation
Gelsolin / metabolism*
Neutrophils / cytology,  metabolism
Recombinant Proteins / metabolism
Tumor Cells, Cultured
Tumor Necrosis Factor-alpha / pharmacology
Grant Support
Reg. No./Substance:
0/Actins; 0/Amino Acid Chloromethyl Ketones; 0/Antigens, CD95; 0/Cysteine Proteinase Inhibitors; 0/Gelsolin; 0/Recombinant Proteins; 0/Tumor Necrosis Factor-alpha; 0/benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone; 66-81-9/Cycloheximide; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/Casp3 protein, mouse; 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

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