Source:http://linkedlifedata.com/resource/pubmed/id/16520240
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
2006-3-7
|
pubmed:abstractText |
Several lines of research suggest that mitochondria play a role in the etiopathogenesis of diabetic cardiomyopathy, although the mechanisms involved are still debated. In the present study, we report that State 3 oxygen consumption decreases by approximately 35% with glutamate and by approximately 30% with succinate in mitochondria from diabetic rat hearts compared to controls. In these mitochondria the enzymatic activities of complex I and complex II are also decreased to a comparable extent. Western blot analysis of mitochondrial protein pattern using antibodies recognizing proteins modified by the lipid peroxidation product 4-hydroxynonenal indicates the FAD-containing subunit of succinate dehydrogenase as one of the targets of this highly reactive aldehyde. In rats diabetic for 6 or 12 weeks, insulin supplementation for 2 weeks decreases the level of protein modified by 4-hydroxynonenal and restores mitochondrial respiration and enzyme activity to control level. Taken together, these results: (1) indicate that 4-hydroxynonenal is endogenously produced within diabetic mitochondria and forms an adduct with selective mitochondrial proteins, (2) identify one of these proteins as a subunit of succinate dehydrogenase, and (3) provide strong evidence that insulin treatment can reverse and ameliorate free radical damage and mitochondrial function under diabetic conditions.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-hydroxy-2-nonenal,
http://linkedlifedata.com/resource/pubmed/chemical/Aldehydes,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex II,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Succinate Dehydrogenase
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0891-5849
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
40
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
886-96
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:16520240-Aldehydes,
pubmed-meshheading:16520240-Animals,
pubmed-meshheading:16520240-Cardiomyopathies,
pubmed-meshheading:16520240-Cell Respiration,
pubmed-meshheading:16520240-Diabetes Mellitus, Experimental,
pubmed-meshheading:16520240-Electron Transport Complex II,
pubmed-meshheading:16520240-Free Radicals,
pubmed-meshheading:16520240-Insulin,
pubmed-meshheading:16520240-Lipid Peroxidation,
pubmed-meshheading:16520240-Male,
pubmed-meshheading:16520240-Mitochondria, Heart,
pubmed-meshheading:16520240-Mitochondrial Proteins,
pubmed-meshheading:16520240-Oxygen Consumption,
pubmed-meshheading:16520240-Rats,
pubmed-meshheading:16520240-Rats, Sprague-Dawley,
pubmed-meshheading:16520240-Succinate Dehydrogenase
|
pubmed:year |
2006
|
pubmed:articleTitle |
Decreased complex II respiration and HNE-modified SDH subunit in diabetic heart.
|
pubmed:affiliation |
Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106-4970, USA. amr5@po.cwru.edu
|
pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|