Alpha-lipoic acid does not alter stress protein response to acute exercise in diabetic brain

Heat shock proteins (HSPs) are molecular chaperones which may act protective in cerebrovascular insults and peripheral diabetic neuropathy. We hypothesized that alpha‐lipoic acid (LA), a natural thiol antioxidant, may enhance brain HSP response in diabetes. Rats with or without streptozotocin‐induce...

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Published inCell biochemistry and function Vol. 28; no. 8; pp. 644 - 650
Main Authors Lappalainen, Jani, Lappalainen, Zekine, Oksala, Niku K. J., Laaksonen, David E., Khanna, Savita, Sen, Chandan K., Atalay, Mustafa
Format Journal Article
LanguageEnglish
Published Chichester, UK John Wiley & Sons, Ltd 02.12.2010
Subjects
Animals
antioxidant
Antioxidants - pharmacology
brain
Brain - drug effects
Brain - metabolism
diabetes
Diabetes Mellitus, Experimental - chemically induced
Diabetes Mellitus, Experimental - metabolism
exercise
HSP70 Heat-Shock Proteins - biosynthesis
HSP90 Heat-Shock Proteins - biosynthesis
lipoic acid
Male
Membrane Proteins - biosynthesis
Physical Conditioning, Animal
Physical Exertion
Rats
Rats, Wistar
Thioctic Acid - pharmacology
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Abstract Heat shock proteins (HSPs) are molecular chaperones which may act protective in cerebrovascular insults and peripheral diabetic neuropathy. We hypothesized that alpha‐lipoic acid (LA), a natural thiol antioxidant, may enhance brain HSP response in diabetes. Rats with or without streptozotocin‐induced diabetes were treated with LA or saline for 8 weeks. Half of the rats were subjected to exhaustive exercise to investigate HSP induction, and the brain tissue was analyzed. Diabetes increased constitutive HSC70 mRNA, and decreased HSP90 and glucose‐regulated protein 75 (GRP75) mRNA without affecting protein levels. Exercise increased HSP90 protein and mRNA, and also GRP75 and heme oxygenase‐1 (HO‐1) mRNA only in non‐diabetic animals. LA had no significant effect on brain HSPs, although LA increased HSC70 and HO‐1 mRNA in diabetic animals and decreased HSC70 mRNA in non‐diabetic animals. Eukaryotic translation elongation factor‐2, essential for protein synthesis, was decreased by diabetes and suggesting a mechanism for the impaired HSP response related to translocation of the nascent chain during protein synthesis. LA supplementation does not offset the adverse effects of diabetes on brain HSP mRNA expression. Diabetes may impair HSP translation through elongation factors related to nascent chain translocation and subsequent responses to acute stress. Copyright © 2010 John Wiley & Sons, Ltd.
AbstractList Heat shock proteins (HSPs) are molecular chaperones which may act protective in cerebrovascular insults and peripheral diabetic neuropathy. We hypothesized that alpha-lipoic acid (LA), a natural thiol antioxidant, may enhance brain HSP response in diabetes. Rats with or without streptozotocin-induced diabetes were treated with LA or saline for 8 weeks. Half of the rats were subjected to exhaustive exercise to investigate HSP induction, and the brain tissue was analyzed. Diabetes increased constitutive HSC70 mRNA, and decreased HSP90 and glucose-regulated protein 75 (GRP75) mRNA without affecting protein levels. Exercise increased HSP90 protein and mRNA, and also GRP75 and heme oxygenase-1 (HO-1) mRNA only in non-diabetic animals. LA had no significant effect on brain HSPs, although LA increased HSC70 and HO-1 mRNA in diabetic animals and decreased HSC70 mRNA in non-diabetic animals. Eukaryotic translation elongation factor-2, essential for protein synthesis, was decreased by diabetes and suggesting a mechanism for the impaired HSP response related to translocation of the nascent chain during protein synthesis. LA supplementation does not offset the adverse effects of diabetes on brain HSP mRNA expression. Diabetes may impair HSP translation through elongation factors related to nascent chain translocation and subsequent responses to acute stress.
Heat shock proteins (HSPs) are molecular chaperones which may act protective in cerebrovascular insults and peripheral diabetic neuropathy. We hypothesized that alpha‐lipoic acid (LA), a natural thiol antioxidant, may enhance brain HSP response in diabetes. Rats with or without streptozotocin‐induced diabetes were treated with LA or saline for 8 weeks. Half of the rats were subjected to exhaustive exercise to investigate HSP induction, and the brain tissue was analyzed. Diabetes increased constitutive HSC70 mRNA, and decreased HSP90 and glucose‐regulated protein 75 (GRP75) mRNA without affecting protein levels. Exercise increased HSP90 protein and mRNA, and also GRP75 and heme oxygenase‐1 (HO‐1) mRNA only in non‐diabetic animals. LA had no significant effect on brain HSPs, although LA increased HSC70 and HO‐1 mRNA in diabetic animals and decreased HSC70 mRNA in non‐diabetic animals. Eukaryotic translation elongation factor‐2, essential for protein synthesis, was decreased by diabetes and suggesting a mechanism for the impaired HSP response related to translocation of the nascent chain during protein synthesis. LA supplementation does not offset the adverse effects of diabetes on brain HSP mRNA expression. Diabetes may impair HSP translation through elongation factors related to nascent chain translocation and subsequent responses to acute stress. Copyright © 2010 John Wiley & Sons, Ltd.
Abstract Heat shock proteins (HSPs) are molecular chaperones which may act protective in cerebrovascular insults and peripheral diabetic neuropathy. We hypothesized that alpha‐lipoic acid (LA), a natural thiol antioxidant, may enhance brain HSP response in diabetes. Rats with or without streptozotocin‐induced diabetes were treated with LA or saline for 8 weeks. Half of the rats were subjected to exhaustive exercise to investigate HSP induction, and the brain tissue was analyzed. Diabetes increased constitutive HSC70 mRNA, and decreased HSP90 and glucose‐regulated protein 75 (GRP75) mRNA without affecting protein levels. Exercise increased HSP90 protein and mRNA, and also GRP75 and heme oxygenase‐1 (HO‐1) mRNA only in non‐diabetic animals. LA had no significant effect on brain HSPs, although LA increased HSC70 and HO‐1 mRNA in diabetic animals and decreased HSC70 mRNA in non‐diabetic animals. Eukaryotic translation elongation factor‐2, essential for protein synthesis, was decreased by diabetes and suggesting a mechanism for the impaired HSP response related to translocation of the nascent chain during protein synthesis. LA supplementation does not offset the adverse effects of diabetes on brain HSP mRNA expression. Diabetes may impair HSP translation through elongation factors related to nascent chain translocation and subsequent responses to acute stress. Copyright © 2010 John Wiley & Sons, Ltd.
Author Oksala, Niku K. J.
Sen, Chandan K.
Lappalainen, Zekine
Lappalainen, Jani
Laaksonen, David E.
Atalay, Mustafa
Khanna, Savita
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  surname: Atalay
  fullname: Atalay, Mustafa
  organization: Institute of Biomedicine, Physiology, University of Eastern Finland, Kuopio, Finland
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CitedBy_id crossref_primary_10_3892_etm_2017_4527
crossref_primary_10_1016_j_bbadis_2014_06_010
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Snippet Heat shock proteins (HSPs) are molecular chaperones which may act protective in cerebrovascular insults and peripheral diabetic neuropathy. We hypothesized...
Abstract Heat shock proteins (HSPs) are molecular chaperones which may act protective in cerebrovascular insults and peripheral diabetic neuropathy. We...
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crossref
pubmed
wiley
istex
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StartPage 644
SubjectTerms Animals
antioxidant
Antioxidants - pharmacology
brain
Brain - drug effects
Brain - metabolism
diabetes
Diabetes Mellitus, Experimental - chemically induced
Diabetes Mellitus, Experimental - metabolism
exercise
HSP70 Heat-Shock Proteins - biosynthesis
HSP90 Heat-Shock Proteins - biosynthesis
lipoic acid
Male
Membrane Proteins - biosynthesis
Physical Conditioning, Animal
Physical Exertion
Rats
Rats, Wistar
Thioctic Acid - pharmacology
Title Alpha-lipoic acid does not alter stress protein response to acute exercise in diabetic brain
URI https://api.istex.fr/ark:/67375/WNG-34MQL934-5/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fcbf.1702
https://www.ncbi.nlm.nih.gov/pubmed/21104931
https://search.proquest.com/docview/1367482603
https://search.proquest.com/docview/1758240378
https://search.proquest.com/docview/1758240975
https://search.proquest.com/docview/812130127
Volume 28
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