Linked Life Data

18977311

Source:http://linkedlifedata.com/resource/pubmed/id/18977311

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-12-23
pubmed:abstractText
All-trans-retinoic acid (atRA), an activated metabolite of vitamin A, is incorporated covalently into proteins both invivo and invitro. AtRA reduced the transport activity of the oxoglutarate carrier (OGC) isolated from testes mitochondria to 58% of control via retinoylation reaction. Labeling of testes mitochondrial proteins with (3)HatRA demonstrated the binding of atRA to a 31.5 KDa protein. This protein was identified as OGC due to the competition for the labeling reaction with 2-oxoglutarate, the specific OGC substrate. The role of retinoylated proteins is currently being explored and here we have the first evidence that retinoic acids bind directly to OGC and inhibit its activity in rat testes mitochondria via retinoylation reaction. This study indicates the evidence of a specific interaction between atRA and OGC and establishes a novel mechanism for atRA action, which could influence the physiological biosynthesis of testosterone in situations such as retinoic acid treatment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1791
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3-7
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Influence of all-trans-retinoic acid on oxoglutarate carrier via retinoylation reaction.
pubmed:affiliation
Department of Pharmaco-Biology, University of Calabria, Edificio Polifunzionale, 87036 Rende (CS), Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't