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PMID: 10783895 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage.

Nature ·Vol. 404 ·No. 6779 ·2000-04-13 ·Pages 787-90

Nishikawa T, Edelstein D, Du XL, Yamagishi S, Matsumura T, Kaneda Y, Yorek MA, Beebe D, Oates PJ, Hammes HP, Giardino I, Brownlee M

Abstract

Diabetic hyperglycaemia causes a variety of pathological changes in small vessels, arteries and peripheral nerves. Vascular endothelial cells are an important target of hyperglycaemic damage, but the mechanisms underlying this damage are not fully understood. Three seemingly independent biochemical pathways are involved in the pathogenesis: glucose-induced activation of protein kinase C isoforms; increased formation of glucose-derived advanced glycation end-products; and increased glucose flux through the aldose reductase pathway. The relevance of each of these pathways is supported by animal studies in which pathway-specific inhibitors prevent various hyperglycaemia-induced abnormalities. Hyperglycaemia increases the production of reactive oxygen species inside cultured bovine aortic endothelial cells. Here we show that this increase in reactive oxygen species is prevented by an inhibitor of electron transport chain complex II, by an uncoupler of oxidative phosphorylation, by uncoupling protein-1 and by manganese superoxide dismutase. Normalizing levels of mitochondrial reactive oxygen species with each of these agents prevents glucose-induced activation of protein kinase C, formation of advanced glycation end-products, sorbitol accumulation and NFkappaB activation.

MeSH Terms
Animals Aspartic Acid/metabolism Blood Glucose/metabolism Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology Carrier Proteins/pharmacology Cattle Electron Transport Electron Transport Complex II Endothelium, Vascular/drug effects,metabolism,pathology Enzyme Activation Glycation End Products, Advanced/metabolism Hyperglycemia/etiology,metabolism,pathology Ion Channels Malates/metabolism Membrane Proteins/pharmacology Mitochondria/metabolism Mitochondrial Proteins Multienzyme Complexes/metabolism NF-kappa B/metabolism Oxidoreductases/metabolism Protein Kinase C/metabolism Reactive Oxygen Species/metabolism Rotenone/pharmacology Sorbitol/metabolism Succinate Dehydrogenase/metabolism Superoxide Dismutase/metabolism,pharmacology Thenoyltrifluoroacetone/analogs & derivatives,pharmacology Uncoupling Agents/pharmacology Uncoupling Protein 1
Chemicals
Blood Glucose Carrier Proteins Glycation End Products, Advanced Ion Channels Malates Membrane Proteins Mitochondrial Proteins Multienzyme Complexes NF-kappa B Reactive Oxygen Species Uncoupling Agents Uncoupling Protein 1 Rotenone thiothenoyltrifluoroacetone Aspartic Acid Thenoyltrifluoroacetone Sorbitol Carbonyl Cyanide m-Chlorophenyl Hydrazone malic acid Oxidoreductases Superoxide Dismutase Electron Transport Complex II Succinate Dehydrogenase Protein Kinase C
Authors & Affiliations
12 authors, click to expand affiliations / ORCID
Nishikawa T
Albert Einstein College of Medicine, Diabetes Research Centre, Bronx, New York 10461, USA.
Edelstein D
Du X L
Yamagishi S
Matsumura T
Kaneda Y
Yorek M A
Beebe D
Oates P J
Hammes H P
Giardino I
Brownlee M
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
2000-04-13
Pages
787-90
Language
English
Region
England
NLM ID
0410462
Subset
IM
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