Source:http://linkedlifedata.com/resource/pubmed/id/11591158
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
41
|
| pubmed:dateCreated |
2001-10-9
|
| pubmed:abstractText |
At least five distinct carrier proteins form the family of mammalian cationic amino acid transporters (CATs). We have cloned a cDNA containing the complete coding region of human CAT-3. hCAT-3 is glycosylated and localized to the plasma membrane. Transport studies in Xenopus laevis oocytes revealed that hCAT-3 is selective for cationic L-amino acids and exhibits a maximal transport activity similar to other CAT proteins. The apparent substrate affinity and sensitivity to trans-stimulation of hCAT-3 resembles most closely hCAT-2B. This is in contrast to rat and murine CAT-3 proteins that have been reported to display a very low activity and to be inhibited by neutral and anionic L-amino acids as well as D-arginine (Hosokawa, H., et al. (1997) J. Biol. Chem. 272, 8717-8722; Ito, K., and Groudine, M. (1997) J. Biol. Chem. 272, 26780-26786). Also, in adult rat and mouse, CAT-3 has been found exclusively in central neurons. Human CAT-3 expression is not restricted to the brain, in fact, by far the highest expression was found in thymus. Also in other peripheral tissues, hCAT-3 expression was equal to or higher than in most brain regions, suggesting that hCAT-3 is not a neuron-specific transporter.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
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| pubmed:issn |
0006-2960
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
16
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| pubmed:volume |
40
|
| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
12387-94
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11591158-Amino Acid Sequence,
pubmed-meshheading:11591158-Amino Acid Transport Systems, Basic,
pubmed-meshheading:11591158-Animals,
pubmed-meshheading:11591158-Base Sequence,
pubmed-meshheading:11591158-Brain,
pubmed-meshheading:11591158-Carrier Proteins,
pubmed-meshheading:11591158-Cell Line,
pubmed-meshheading:11591158-DNA, Complementary,
pubmed-meshheading:11591158-Female,
pubmed-meshheading:11591158-Gene Expression,
pubmed-meshheading:11591158-Humans,
pubmed-meshheading:11591158-Male,
pubmed-meshheading:11591158-Membrane Proteins,
pubmed-meshheading:11591158-Mice,
pubmed-meshheading:11591158-Oocytes,
pubmed-meshheading:11591158-Rats,
pubmed-meshheading:11591158-Thymus Gland,
pubmed-meshheading:11591158-Tissue Distribution,
pubmed-meshheading:11591158-Xenopus laevis
|
| pubmed:year |
2001
|
| pubmed:articleTitle |
Human cationic amino acid transporter hCAT-3 is preferentially expressed in peripheral tissues.
|
| pubmed:affiliation |
Department of Pharmacology, Johannes Gutenberg University, Obere Zahlbacher Strasse 67, 55101 Mainz, Germany.
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|