Source:http://linkedlifedata.com/resource/pubmed/id/11168980
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
3-deoxyglucosone (3-DG) is accumulated not only in uremic serum but also in uremic erythrocytes. 3-DG rapidly reacts with protein amino groups to form advanced glycation end products (AGEs) such as imidazolone, pyrraline, and N(epsilon)-(carboxymethyl)lysine, among which imidazolone is the AGE that is most specific for 3-DG. In diabetes, hyperglycemia enhances the synthesis of 3-DG via the Maillard reaction and the polyol pathway and thereby leads to its high plasma and erythrocyte levels. In uremia, however, the decreased catabolism of 3-DG that may be due to the loss of 3-DG reductase activity in the end-stage kidneys may lead to a high plasma 3-DG level. The elevated 3-DG levels in uremic patients may promote the formation of AGEs such as imidazolone in erythrocytes, aortas, and dialysis-related amyloid deposits. Treatment with an aldose reductase inhibitor reduced the erythrocyte levels of 3-DG and AGEs such as imidazolone in diabetic uremic patients. This finding demonstrates an important role of the polyol pathway in the formation of erythrocyte 3-DG and AGEs. The erythrocyte levels of 3-DG are elevated in not only diabetic uremic but also nondiabetic uremic patients. 3-DG showed some cytotoxicities by inducing intracellular oxidative stress. In contrast, oxidative stress was demonstrated to cause accumulation of intracellular 3-DG. Recently, we have demonstrated that 3-DG inactivates intracellular enzymes such as glutathione peroxidase, a key enzyme in the detoxification of hydrogen peroxide. Thus, intracellular accumulation of 3-DG may enhance oxidative stress by inactivating the antioxidant enzymes. In conclusion, 3-DG may play a principal role in the development of uremic complications, such as dialysis-related amyloidosis, atherosclerosis, and enhanced oxidative stress.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-deoxyglucosone,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyglucose,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylation End Products, Advanced,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/heparin-binding EGF-like growth...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0098-6577
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
S37-41
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11168980-Amyloidosis,
pubmed-meshheading:11168980-Animals,
pubmed-meshheading:11168980-Apoptosis,
pubmed-meshheading:11168980-Arteriosclerosis,
pubmed-meshheading:11168980-Cell Division,
pubmed-meshheading:11168980-Deoxyglucose,
pubmed-meshheading:11168980-Epidermal Growth Factor,
pubmed-meshheading:11168980-Erythrocytes,
pubmed-meshheading:11168980-Glucose,
pubmed-meshheading:11168980-Glutathione Peroxidase,
pubmed-meshheading:11168980-Glutathione Reductase,
pubmed-meshheading:11168980-Glycosylation End Products, Advanced,
pubmed-meshheading:11168980-Humans,
pubmed-meshheading:11168980-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:11168980-Oxidative Stress,
pubmed-meshheading:11168980-Uremia
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pubmed:year |
2001
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pubmed:articleTitle |
3-deoxyglucosone and AGEs in uremic complications: inactivation of glutathione peroxidase by 3-deoxyglucosone.
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pubmed:affiliation |
Nagoya University Daiko Medical Center, Nagoya, Japan. tniwa@med.nagoya-u.ac.jp
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pubmed:publicationType |
Journal Article,
Review
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