Document Detail


Scurvy leads to endoplasmic reticulum stress and apoptosis in the liver of Guinea pigs.
MedLine Citation:
PMID:  16251606     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Insufficient ascorbate intake causes scurvy in certain species. Beyond its known functions, it has been suggested that ascorbate participates in oxidative protein folding in the endoplasmic reticulum (ER). Because redox imbalance in this organelle might cause ER stress and apoptosis, we hypothesized that this might contribute to the pathology of scurvy. Guinea pigs were divided into 7 groups: the control group was fed a commercial guinea pig food containing 0.1 g/100 g ascorbate for 4 wk, 5 groups consumed an ascorbate-free food for 0, 1, 2, 3, or 4 wk and 1 group was fed this scorbutic diet for 2 wk and then the commercial food plus 1 g/L ascorbate in drinking water for 2 wk. TBARS generation and the expression of some ER chaperones and foldases were determined in hepatic microsomes. The apoptotic index was assessed in histological sections. Although ascorbate, measured by HPLC, was undetectable in the livers of the guinea pigs after they had consumed the scorbutic diet for 2 wk, the microsomal TBARS level was elevated relative to the initial value only at wk 4. Western blot revealed the induction of GRP78, GRP94, and protein disulfide isomerase at wk 3 and 4. Apoptosis was greater than in the control, beginning at wk 3. None of the alterations occurred in the groups fed the commercial guinea pig food or ascorbate-free food followed by ascorbate supplementation. Therefore, persistent ascorbate deficiency leads to ER stress, unfolded protein response, and apoptosis in the liver, suggesting that insufficient protein processing participates in the pathology of scurvy.
Authors:
Eva Margittai; Gábor Bánhegyi; András Kiss; Gábor Nagy; József Mandl; Zsuzsa Schaff; Miklós Csala
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of nutrition     Volume:  135     ISSN:  0022-3166     ISO Abbreviation:  J. Nutr.     Publication Date:  2005 Nov 
Date Detail:
Created Date:  2005-10-27     Completed Date:  2006-02-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0404243     Medline TA:  J Nutr     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2530-4     Citation Subset:  IM    
Affiliation:
Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Endoplasmic Reticulum Research Group of The Hungarian Academy of Science, Budapest, Hungary.
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MeSH Terms
Descriptor/Qualifier:
Animals
Apoptosis*
Ascorbic Acid / analysis
Blotting, Western
Body Weight
Endoplasmic Reticulum / pathology*,  physiology
Guinea Pigs
Heat-Shock Proteins / analysis
Liver / chemistry,  pathology*
Male
Membrane Glycoproteins / analysis
Microsomes, Liver / chemistry
Molecular Chaperones / analysis
Organ Size
Proteins / analysis
Scurvy / pathology*
Thiobarbituric Acid Reactive Substances / analysis
Chemical
Reg. No./Substance:
0/Heat-Shock Proteins; 0/Membrane Glycoproteins; 0/Molecular Chaperones; 0/Proteins; 0/Thiobarbituric Acid Reactive Substances; 0/endoplasmin; 0/molecular chaperone GRP78; 50-81-7/Ascorbic Acid

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


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