Linked Life Data

15499185

Source:http://linkedlifedata.com/resource/pubmed/id/15499185

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-10-22
pubmed:abstractText
The organic cation/carnitine transporter OCTN2 transports carnitine in a sodium-dependent manner, whereas it transports organic cations sodium-independently. To elucidate the functional domain in OCTN2, we constructed chimeric proteins of human OCTN2 (hOCTN2) and mouse OCTN3 (mOCTN3) and introduced mutations at several amino acids conserved among human, rat and mouse OCTN2. We found that transmembrane domains (TMD) 1-7 are responsible for organic cation transport and for sodium dependence in carnitine transport. Within TMD1-7, Q180 and Q207 of hOCTN2 are the critical amino acids for the sodium dependence, and double mutation of Q180 and Q207 resulted in minimal change in transport activity when sodium was removed from the uptake medium. We propose that sodium-dependent affinity for carnitine is dependent on sodium recognition by these critical amino acids in hOCTN2, whereas carnitine transport by OCTN2 requires functional linkage between TMD1-7 and TMD11.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1347-4367
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
180-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Functional regions of organic cation/carnitine transporter OCTN2 (SLC22A5): roles in carnitine recognition.
pubmed:affiliation
Faculty of Pharmaceutical Sciences, Kanazawa University, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't