Source:http://linkedlifedata.com/resource/pubmed/id/10375455
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1999-7-30
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pubmed:abstractText |
Although the role of carnitine system in the ocular tissues is not clearly understood, earlier studies showed that lenticular levels of L -carnitine were the highest among ocular tissues and there was a dramatic depletion of lenticular L -carnitine and acetyl- L -carnitine in streptozotocin-diabetic rats. As protein glycation has been implicated in the development of several diabetic complications including cataracts, this study was initiated to show the possible effects of L -carnitine and acetyl- L -carnitine on the glycation and advanced glycation (AGEs) of lens proteins. Calf lens soluble fraction (crystallins) was incubated with 50 m m glucose (containing14C glucose) with or without 5-50 m ml -carnitine, 5-50 m m acetyl- L -carnitine and 5-50 m m acetyl salicylic acid, for 15 days. The results show that while L -carnitine did not have any effect on in vitro glycation of lens crystallins, acetyl- L -carnitine and acetyl salicylic acid decreased crystallin glycation by 42% and 63%, respectively-this decrease was concentration dependent. Glycated crystallins were separated on HPLC which showed that the rate of glycation is in the following order: alpha>beta>gamma. Interestingly, acetyl- L -carnitine inhibited glycation of alpha crystallin more than other crystallins. In vitro incubations with [3H-acetyl] acetyl- L -carnitine showed that acetyl- L -carnitine acetylates lens crystallins (non-enzymatically) and alpha crystallin is the major acetylated protein. Furthermore, there was a 70% reduction in anti-AGE antibody reactivity when 50 m m acetyl- L -carnitine was included in the incubation of lens crystallins and 10 m m erythrose, suggesting that inhibition of glycation by acetyl- L -carnitine also affected the generation of AGEs. This in vitro study shows, for the first time, that acetyl- L -carnitine could acetylate potential glycation sites of lens crystallins, and protect them from glycation-mediated protein damage.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-4835
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
69
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
109-15
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10375455-Acetylation,
pubmed-meshheading:10375455-Acetylcarnitine,
pubmed-meshheading:10375455-Animals,
pubmed-meshheading:10375455-Carnitine,
pubmed-meshheading:10375455-Cattle,
pubmed-meshheading:10375455-Chromatography, High Pressure Liquid,
pubmed-meshheading:10375455-Crystallins,
pubmed-meshheading:10375455-Dose-Response Relationship, Drug,
pubmed-meshheading:10375455-Glycosylation,
pubmed-meshheading:10375455-Glycosylation End Products, Advanced
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pubmed:year |
1999
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pubmed:articleTitle |
Acetyl- L -carnitine decreases glycation of lens proteins: in vitro studies.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta, GA, 30912-2100, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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