Source:http://linkedlifedata.com/resource/pubmed/id/15562031
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-2-8
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pubmed:abstractText |
Oxidative stress plays a role in cardiovascular dysfunction. This is of interest in diabetes, a clinical condition characterized by oxidative stress and increased prevalence of cardiovascular disease. The role of p66(shc) in oxidative stress-related response has been demonstrated by resistance to and reduction of oxidative stress and prolonged lifespan in p66(shc-/-) mice. In this study we assess p66(shc) gene expression in peripheral blood mononuclear cells (PBM) from type 2 diabetic patients and healthy subjects. The p66(shc) mRNA level was assessed using RT-PCR with two sets of primers mapping for different p66(shc) regions. p66(shc) is expressed in both monocytes and lymphocytes. The level of p66(shc) mRNA was significantly higher in type 2 diabetic patients compared with controls (0.38 +/- 0.07 densitometric units vs. 0.13 +/- 0.08; P < 0.0001). In addition, total plasma 8-isoprostane levels, a marker of oxidative stress, were higher in type 2 diabetics (0.72 +/- 0.04 ng/ml) than in normal subjects (0.43 +/- 0.04, P < 0.001) and were significantly correlated to the p66(shc) mRNA level in PBM from type 2 diabetics (r(2) = 0.47; P = 0.0284). In conclusion, diabetes induces p66(shc) gene expression in circulating PBM; this up-regulation in expression is significantly associated with markers of oxidative stress. p66(shc) gene expression in PBM may represent a useful tool to investigate the oxidative stress involved in the pathogenesis of long-term diabetic complications.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/8-epi-prostaglandin F2alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprost,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/SHC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Shc1 protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-972X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1130-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15562031-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:15562031-Animals,
pubmed-meshheading:15562031-Diabetes Mellitus,
pubmed-meshheading:15562031-Diabetes Mellitus, Type 2,
pubmed-meshheading:15562031-Dinoprost,
pubmed-meshheading:15562031-Gene Expression Regulation,
pubmed-meshheading:15562031-Humans,
pubmed-meshheading:15562031-Leukocytes, Mononuclear,
pubmed-meshheading:15562031-Mice,
pubmed-meshheading:15562031-Mice, Knockout,
pubmed-meshheading:15562031-Middle Aged,
pubmed-meshheading:15562031-Oxidative Stress,
pubmed-meshheading:15562031-RNA, Messenger,
pubmed-meshheading:15562031-Reference Values,
pubmed-meshheading:15562031-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15562031-Shc Signaling Adaptor Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Diabetes induces p66shc gene expression in human peripheral blood mononuclear cells: relationship to oxidative stress.
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pubmed:affiliation |
Department of Clinical and Experimental Medicine, University of padova School of Medicine, 35128 Padova, Italy.
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pubmed:publicationType |
Journal Article
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