Document Detail


Sustained versus transient ERK1/2 signaling underlies the anti- and proapoptotic effects of oxidative stress in human RPE cells.
MedLine Citation:
PMID:  17003459     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
PURPOSE: Oxidative stress is thought to contribute to the pathogenesis of age-related macular degeneration (AMD), which involves retinal pigmented epithelial (RPE) cell death. However, signaling pathways involved in the oxidative-stress-induced RPE cell death are poorly understood. This study was conducted to investigate the involvement of the MAP kinase pathways during the induction of RPE cell death by oxidative stress. METHODS: ARPE-19 cells were exposed to the oxidant tert-butyl hydroperoxide (t-BHP). Cell viability was assessed by cell counting and MTT-staining, and apoptosis was quantified by TUNEL and flow cytometry. Activation of JNK1/3, p38 alphabeta MAPKs and ERK1/2 and their potential targets was detected by Western blot analysis and immunochemistry with specific anti-phospho protein antibodies. Specific pharmacologic inhibitors directed against the MAPKs were used to analyze the signaling involved in cell death of RPE cells exposed to t-BHP. RESULTS: Exposure of RPE cells to t-BHP, associated with increase in reactive oxygen species and intracellular glutathione depletion, induced time- and concentration-dependent apoptosis, which was associated with the accumulation of inactive ERK1/2 in cell nuclei and a transient and weak ERK1/2 activation. This activation was accompanied by a deactivation of P90(RSK), the major target of ERK1/2 and consequently by the delayed activation of its transcription factor CREB. MEK1/2 inhibition completely suppressed the transient activation of ERK1/2 and completely blocked apoptosis, demonstrating the role of the MEK-ERK module in mediating oxidative-stress-induced RPE cell death. In contrast, neither JNKs nor p38 alphabeta MAPKs were involved in mediating t-BHP-induced apoptotic signaling in RPE cells. CONCLUSIONS: The results suggest that inhibiting the MEK-ERK module may allow the development of selective methods for treating oxidative-stress-induced RPE degeneration, such as AMD.
Authors:
Anne-Lise Glotin; Armelle Calipel; Jean-Yves Brossas; Anne-Marie Faussat; Jacques Tréton; Frédéric Mascarelli
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Investigative ophthalmology & visual science     Volume:  47     ISSN:  0146-0404     ISO Abbreviation:  Invest. Ophthalmol. Vis. Sci.     Publication Date:  2006 Oct 
Date Detail:
Created Date:  2006-09-27     Completed Date:  2006-10-24     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  7703701     Medline TA:  Invest Ophthalmol Vis Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4614-23     Citation Subset:  IM    
Affiliation:
Institut Biomédical des Cordeliers, INSERM (Institut National de la Santé et de la Recherche Médicale) Unité 598, Paris, France.
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MeSH Terms
Descriptor/Qualifier:
Apoptosis*
Blotting, Western
Cell Count
Cell Survival / drug effects
Cells, Cultured
Dose-Response Relationship, Drug
Flow Cytometry
Glutathione / metabolism
Humans
In Situ Nick-End Labeling
MAP Kinase Signaling System / physiology*
Mitogen-Activated Protein Kinase 1 / metabolism*
Mitogen-Activated Protein Kinase 10 / metabolism
Mitogen-Activated Protein Kinase 3 / metabolism*
Mitogen-Activated Protein Kinase 8 / metabolism
Oxidative Stress / drug effects*
Phosphorylation
Pigment Epithelium of Eye / drug effects,  metabolism,  pathology*
Reactive Oxygen Species / metabolism
p38 Mitogen-Activated Protein Kinases / metabolism
tert-Butylhydroperoxide / toxicity*
Chemical
Reg. No./Substance:
0/Reactive Oxygen Species; 70-18-8/Glutathione; 75-91-2/tert-Butylhydroperoxide; EC 2.7.1.-/Mitogen-Activated Protein Kinase 10; EC 2.7.11.24/Mitogen-Activated Protein Kinase 1; EC 2.7.11.24/Mitogen-Activated Protein Kinase 3; EC 2.7.11.24/Mitogen-Activated Protein Kinase 8; EC 2.7.11.24/p38 Mitogen-Activated Protein Kinases

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


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