rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
4
|
pubmed:dateCreated |
2003-11-19
|
pubmed:abstractText |
Aspartic acid (Asp) undergoes l-isomer-selective efflux transport across the blood-brain barrier (BBB). This transport system appears to play an important role in regulating l- and d-Asp levels in the brain. The purpose of this study was to identify the responsible transporters and elucidate the mechanism for l-isomer-selective Asp transport at the BBB. The l-isomer-selective uptake of Asp by conditionally immortalized mouse brain capillary endothelial cells used as an in vitro model of the BBB took place in an Na+- and pH-dependent manner. This process was inhibited by system ASC substrates such as l-alanine and l-serine, suggesting that system ASC transporters, ASCT1 and ASCT2, are involved in the l-isomer selective transport. Indeed, l-Asp uptake by oocytes injected with either ASCT1 or ASCT2 cRNA took place in a similar manner to that in cultured BBB cells, whereas no significant d-Asp uptake occurred. Although both ASCT1 and ASCT2 mRNA were expressed in the cultured BBB cells, the expression of ASCT2 mRNA was 6.7-fold greater than that of ASCT1. Moreover, immunohistochemical analysis suggests that ASCT2 is localized at the abluminal side of the mouse BBB. These results suggest that ASCT2 plays a key role in l-isomer-selective Asp efflux transport at the BBB.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport System ASC,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Asct2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Slc1a4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Slc1a4 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Slc1a5 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0022-3042
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
87
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
891-901
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:14622120-Amino Acid Transport System ASC,
pubmed-meshheading:14622120-Amino Acids,
pubmed-meshheading:14622120-Animals,
pubmed-meshheading:14622120-Aspartic Acid,
pubmed-meshheading:14622120-Biological Transport,
pubmed-meshheading:14622120-Blood-Brain Barrier,
pubmed-meshheading:14622120-Brain,
pubmed-meshheading:14622120-Capillaries,
pubmed-meshheading:14622120-Cell Membrane,
pubmed-meshheading:14622120-Cells, Cultured,
pubmed-meshheading:14622120-Dose-Response Relationship, Drug,
pubmed-meshheading:14622120-Endothelium, Vascular,
pubmed-meshheading:14622120-Hydrogen-Ion Concentration,
pubmed-meshheading:14622120-Immunohistochemistry,
pubmed-meshheading:14622120-Isomerism,
pubmed-meshheading:14622120-Mice,
pubmed-meshheading:14622120-Oocytes,
pubmed-meshheading:14622120-RNA, Messenger,
pubmed-meshheading:14622120-Rabbits,
pubmed-meshheading:14622120-Rats,
pubmed-meshheading:14622120-Rats, Wistar,
pubmed-meshheading:14622120-Sodium,
pubmed-meshheading:14622120-Substrate Specificity,
pubmed-meshheading:14622120-Xenopus
|
pubmed:year |
2003
|
pubmed:articleTitle |
The l-isomer-selective transport of aspartic acid is mediated by ASCT2 at the blood-brain barrier.
|
pubmed:affiliation |
Department of Molecular Biopharmacy and Genetics, Graduate School of Pharmaceutical Sciences New Industry Creation Hatchery Center, Tohoku University, Sendai, Japan. terasaki@mail.pharm.tohoku.ac.jp
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|