Document Detail


Catecholamine-induced oligodendrocyte cell death in culture is developmentally regulated and involves free radical generation and differential activation of caspase-3.
MedLine Citation:
PMID:  12420309     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Oligodendrocyte cultures were used to study the toxic effects of catecholamines. Our results showed that catecholamine-induced toxicity was dependent on the dose of dopamine or norepinephrine used and on the developmental stage of the cultures, with oligodendrocyte progenitors being more vulnerable. A role for oxidative stress and apoptosis on the mechanism of action of catecholamines on oligodendrocyte cell death was next assessed. Catecholamines caused a reduction in intracellular glutathione levels, an accumulation in reactive oxygen species and in heme oxygenase-1, the 32 kDa stress-induced protein. All these changes were prevented by N-acetyl-L-cysteine, a thiocompound with antioxidant activity and a precursor of glutathione, and were more pronounced in progenitors than mature cells, which could contribute to their higher susceptibility. Apoptotic cell death, as assessed by activation of caspase-9 and -3 and cleavage of poly(ADP-ribose) polymerase (a substrate of caspase-3), was only observed in oligodendrocyte progenitors. Pretreatment with zVAD, a general caspase inhibitor, prevented activation of caspase-9 and -3, DNA fragmentation, and decreased progenitors cell death. Furthermore, the expression levels of procaspase-3 and the ratio of the proapoptotic protein bax to antiapoptotic protein bcl-xl were several folds higher in immature than mature oligodendrocytes. Taken together, these results strongly suggest that the catecholamine-induced cytotoxicity in oligodendrocytes is developmentally regulated, mediated by oxidative stress, and have characteristics of apoptosis in progenitor cells.
Authors:
Amani Khorchid; Gabriela Fragoso; Gordon Shore; Guillermina Almazan
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Glia     Volume:  40     ISSN:  0894-1491     ISO Abbreviation:  Glia     Publication Date:  2002 Dec 
Date Detail:
Created Date:  2002-11-06     Completed Date:  2003-08-01     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8806785     Medline TA:  Glia     Country:  United States    
Other Details:
Languages:  eng     Pagination:  283-99     Citation Subset:  IM    
Copyright Information:
Copyright 2002 Wiley-Liss, Inc.
Affiliation:
Department of Pharmacology and Therapeutics, McGill University, Montreal, Quebec, Canada.
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MeSH Terms
Descriptor/Qualifier:
Acetylcysteine / metabolism,  pharmacology
Animals
Animals, Newborn
Apoptosis / drug effects,  physiology*
Asphyxia Neonatorum / enzymology,  physiopathology
Brain / enzymology,  growth & development*,  physiopathology
Caspase 3
Caspases / metabolism
Catecholamines / metabolism,  toxicity*
Cell Differentiation / drug effects,  physiology*
Cells, Cultured
Enzyme Inhibitors / pharmacology
Free Radicals / metabolism
Genes, bcl-2 / genetics
Glutathione / metabolism
Heme Oxygenase (Decyclizing) / metabolism
Heme Oxygenase-1
Humans
Infant, Newborn
Leukomalacia, Periventricular / enzymology,  etiology,  physiopathology
Membrane Proteins
Oligodendroglia / drug effects,  enzymology*
Oxidative Stress / drug effects,  physiology*
Poly(ADP-ribose) Polymerases / metabolism
Rats
Rats, Sprague-Dawley
Stem Cells / drug effects,  enzymology*
Chemical
Reg. No./Substance:
0/Catecholamines; 0/Enzyme Inhibitors; 0/Free Radicals; 0/Membrane Proteins; 616-91-1/Acetylcysteine; 70-18-8/Glutathione; EC 1.14.99.3/HMOX1 protein, human; EC 1.14.99.3/Heme Oxygenase (Decyclizing); EC 1.14.99.3/Heme Oxygenase-1; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/Casp3 protein, rat; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspases

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