| pubmed-article:10375455 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10375455 | lifeskim:mentions | umls-concept:C0007258 | lld:lifeskim |
| pubmed-article:10375455 | lifeskim:mentions | umls-concept:C0010422 | lld:lifeskim |
| pubmed-article:10375455 | lifeskim:mentions | umls-concept:C0598528 | lld:lifeskim |
| pubmed-article:10375455 | lifeskim:mentions | umls-concept:C0681828 | lld:lifeskim |
| pubmed-article:10375455 | lifeskim:mentions | umls-concept:C0547047 | lld:lifeskim |
| pubmed-article:10375455 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10375455 | pubmed:dateCreated | 1999-7-30 | lld:pubmed |
| pubmed-article:10375455 | 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. | lld:pubmed |
| pubmed-article:10375455 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375455 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10375455 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375455 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10375455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375455 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10375455 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10375455 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10375455 | pubmed:issn | 0014-4835 | lld:pubmed |
| pubmed-article:10375455 | pubmed:author | pubmed-author:CarterA LAL | lld:pubmed |
| pubmed-article:10375455 | pubmed:author | pubmed-author:Swamy-Mruthin... | lld:pubmed |
| pubmed-article:10375455 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10375455 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10375455 | pubmed:volume | 69 | lld:pubmed |
| pubmed-article:10375455 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10375455 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10375455 | pubmed:pagination | 109-15 | lld:pubmed |
| pubmed-article:10375455 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:meshHeading | pubmed-meshheading:10375455... | lld:pubmed |
| pubmed-article:10375455 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10375455 | pubmed:articleTitle | Acetyl- L -carnitine decreases glycation of lens proteins: in vitro studies. | lld:pubmed |
| pubmed-article:10375455 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta, GA, 30912-2100, USA. | lld:pubmed |
| pubmed-article:10375455 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10375455 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10375455 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10375455 | lld:pubmed |
