Document Detail


Inhibition of homodimerization of poly(ADP-ribose) polymerase by its C-terminal cleavage products produced during apoptosis.
MedLine Citation:
PMID:  10713134     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The biochemical role of the C-terminal fragment of poly(ADP-ribose) polymerase (PARP) was investigated in HeLa cells undergoing UV-mediated apoptosis. During the course of apoptosis, the C-terminal cleavage product of PARP interacted with intact PARP and down-regulated PARP activity by blocking the homodimerization of PARP. The basic leucine zipper motif in the auto-modification domain of the C-terminal fragment of PARP represented the site of association, and Leu(405) was critical to the ability of the basic leucine zipper motif to associate with intact PARP. The expression of the C-terminal fragment of PARP stimulated UV-mediated apoptosis. These results suggest that the C-terminal cleavage product of PARP produced during apoptosis blocks the homodimerization of PARP and inhibits the cellular PARP activity. The inhibition of the cellular PARP activity might prevent cellular NAD(+) depletion and stimulate apoptosis by maintaining the basal cellular energy level required for the completion of apoptosis.
Authors:
J W Kim; K Kim; K Kang; C O Joe
Related Documents :
16226814 - Non-lethal active caspase-3 expression in bergmann glia of postnatal rat cerebellum.
14686614 - Teratogen-induced activation of caspase-6 and caspase-7 in early postimplantation mouse...
10388534 - Caspase-8 mediates caspase-3 activation and cytochrome c release during singlet oxygen-...
12067274 - Inhibitor specificity of recombinant and endogenous caspase-9.
16034134 - Il-4 and il-13 induce protection of porcine endothelial cells from killing by human com...
9854424 - Immune response of electroeluted detergent soluble 29 kda antigen from setaria digitata...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  275     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2000 Mar 
Date Detail:
Created Date:  2000-04-12     Completed Date:  2000-04-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  8121-5     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejon, 305-701, South Korea.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adenosine Diphosphate Ribose / metabolism
Apoptosis / drug effects*
Dimerization
Hela Cells / radiation effects
Humans
Leucine Zippers
Peptide Fragments / pharmacology*
Poly(ADP-ribose) Polymerases / antagonists & inhibitors*
Ultraviolet Rays
Chemical
Reg. No./Substance:
0/Peptide Fragments; 20762-30-5/Adenosine Diphosphate Ribose; EC 2.4.2.30/Poly(ADP-ribose) Polymerases

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


Previous Document:  Yin-yang 1 and glucocorticoid receptor participate in the Stat5-mediated growth hormone response of ...
Next Document:  Cloning and function of rabbit peroxisome proliferator-activated receptor delta/beta in mature osteo...