Document Detail


Specific inhibition of hypoxia inducible factor 1 exaggerates cell injury induced by in vitro ischemia through deteriorating cellular redox environment.
MedLine Citation:
PMID:  19183269     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Hypoxia inducible factor 1 (HIF-1) has been suggested to play a critical role in the fate of cells exposed to hypoxic stress. However, the mechanism of HIF-1-regulated cell survival is still not fully understood in ischemic conditions. Redox status is critical for decisions of cell survival, death and differentiation. We investigated the effects of inhibiting HIF-1 on cellular redox status in SH-SY5Y cells exposed to hypoxia or oxygen and glucose deprivation (OGD), coupled with cell death analyses. Our results demonstrated that inhibiting HIF-1alpha expression by HIF-1alpha specific small interfering RNA (siRNA) transfection increased reactive oxygen species generation, and transformed the cells to more oxidizing environments (low GSH/GSSG ratio, low NADPH level) under either hypoxic or OGD exposure. Cell death increased dramatically in the siRNA transfected cells, compared to non-transfected cells after hypoxic/OGD exposures. In contrast, increasing HIF-1alpha expression by desferrioxamine, a metal chelator and hydroxylase inhibitor, induced a more reducing environment (high GSH/GSSG ratio, high NADPH level) and reduced cell death. Further studies showed that HIF-1 regulated not only glucose transporter-1 expression, but also the key enzymes of the pentose phosphate pathway such as glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. These enzymes are important in maintaining cellular redox homeostasis by generating NADPH, the primary reducing agent in cells. Moreover, catalase significantly decreased cell death in the siRNA-transfected cells induced by hypoxia and OGD. These results suggest that maintenance of cellular redox status by HIF-1 protects cells from hypoxia and ischemia mediated injuries.
Authors:
Shuhong Guo; Minoru Miyake; Ke Jian Liu; Honglian Shi
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2009-01-29
Journal Detail:
Title:  Journal of neurochemistry     Volume:  108     ISSN:  1471-4159     ISO Abbreviation:  J. Neurochem.     Publication Date:  2009 Mar 
Date Detail:
Created Date:  2009-03-23     Completed Date:  2009-04-22     Revised Date:  2011-09-26    
Medline Journal Info:
Nlm Unique ID:  2985190R     Medline TA:  J Neurochem     Country:  England    
Other Details:
Languages:  eng     Pagination:  1309-21     Citation Subset:  IM    
Affiliation:
University of New Mexico Health Sciences Center, Albuquerque, USA.
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MeSH Terms
Descriptor/Qualifier:
Analysis of Variance
Cell Death / drug effects
Cell Hypoxia / drug effects,  physiology*
Cell Line, Tumor
Deferoxamine / pharmacology
Enzyme-Linked Immunosorbent Assay
Gene Expression Regulation, Neoplastic / drug effects
Glucose / deficiency
Glucose Transporter Type 1 / metabolism
Glutathione / metabolism
Glutathione Disulfide / metabolism
Humans
Hypoxia-Inducible Factor 1 / antagonists & inhibitors,  genetics,  metabolism*
L-Lactate Dehydrogenase / metabolism
NADP / metabolism
Neuroblastoma
Oxidation-Reduction / drug effects
RNA, Small Interfering / genetics,  metabolism
Reactive Oxygen Species / metabolism
Siderophores / pharmacology
Transcriptional Activation
Transfection / methods
Grant Support
ID/Acronym/Agency:
P20 RR15636/RR/NCRR NIH HHS; R01 NS058807-01A1/NS/NINDS NIH HHS; R01NS058807/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Glucose Transporter Type 1; 0/Hypoxia-Inducible Factor 1; 0/RNA, Small Interfering; 0/Reactive Oxygen Species; 0/Siderophores; 27025-41-8/Glutathione Disulfide; 50-99-7/Glucose; 53-59-8/NADP; 70-18-8/Glutathione; 70-51-9/Deferoxamine; EC 1.1.1.27/L-Lactate Dehydrogenase
Comments/Corrections

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