Document Detail


Roles of cathepsins in reperfusion-induced apoptosis in cultured astrocytes.
MedLine Citation:
PMID:  12421595     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Astrocytic apoptosis may play a role in the central nervous system injury. We previously showed that reperfusion of cultured astrocytes with normal medium after exposure to hydrogen peroxide (H(2)O(2))-containing medium causes apoptosis. This study examines the involvement of the lysosomal enzymes cathepsins B and D in the astrocytic apoptosis. Reperfusion after exposure to H(2)O(2) caused a marked increase in caspase-3 and cathepsin D activities and a marked decrease in cathepsin B activity. Pepstatin A, an inhibitor of cathepsin D, and acetyl-L-aspartyl-L-methionyl-L-glutaminyl-L-aspart-1-aldehyde (Ac-DMQD-CHO), a specific inhibitor of caspase-3, blocked the H(2)O(2)-induced decrease in cell viability and DNA ladder formation in cultured rat astrocytes. The (L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester (CA074 Me), a specific inhibitor of cathepsin B, did not affect the H(2)O(2)-induced cell injury. On the other hand, CA074 Me decreased cell viability with DNA ladder formation when cultured in the presence of Ac-DMQD-CHO. This caspase-independent apoptosis was attenuated by the addition of the cathepsin D inhibitor pepstatin A. Caspase-3 like activity was markedly inhibited by Ac-DMQD-CHO and partially by pepstatin A. Pepstatin A and CA074 Me inhibited cathepsin B and cathepsin D activities, respectively, in the presence and absence of Ac-DMQD-CHO. These results suggest that cathepsins B and D are involved in astrocytic apoptosis: cathepsin D acts as a death-inducing factor upstream of caspase-3 and the caspase-independent apoptosis is regulated antagonistically by cathepsins B and D.
Authors:
Kazuhiro Takuma; Makiko Kiriu; Koichi Mori; Eibai Lee; Riyo Enomoto; Akemichi Baba; Toshio Matsuda
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Neurochemistry international     Volume:  42     ISSN:  0197-0186     ISO Abbreviation:  Neurochem. Int.     Publication Date:  2003 Jan 
Date Detail:
Created Date:  2002-11-07     Completed Date:  2003-01-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8006959     Medline TA:  Neurochem Int     Country:  England    
Other Details:
Languages:  eng     Pagination:  153-9     Citation Subset:  IM    
Affiliation:
Department of Analytical Chemistry, Faculty of Pharmaceutical Sciences, High Technology Research Center, Kobe Gakuin University, Kobe 651-2180, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Apoptosis / physiology
Astrocytes / pathology*
Caspase 3
Caspases / antagonists & inhibitors,  metabolism
Cathepsin B / antagonists & inhibitors,  physiology
Cathepsin D / antagonists & inhibitors,  physiology
Cathepsins / antagonists & inhibitors,  physiology*
Cell Survival / drug effects
Cells, Cultured
DNA / biosynthesis,  genetics
Enzyme Inhibitors / pharmacology
Hydrogen Peroxide / toxicity
Peptide Hydrolases / metabolism
Rats
Rats, Wistar
Reperfusion Injury / pathology*
Chemical
Reg. No./Substance:
0/Enzyme Inhibitors; 7722-84-1/Hydrogen Peroxide; 9007-49-2/DNA; EC 3.4.-/Cathepsins; EC 3.4.-/Peptide Hydrolases; EC 3.4.22.-/Casp3 protein, rat; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspases; EC 3.4.22.1/Cathepsin B; EC 3.4.23.5/Cathepsin D

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


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