Source:http://linkedlifedata.com/resource/pubmed/id/20599757
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2010-8-3
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pubmed:abstractText |
The presence of high and low sodium affinity states for the Na(+)-dependent [(14)C]-l-alanine uptake in immortalized renal proximal tubular epithelial (PTE) cells was previously reported (Am. J. Physiol. 293 (2007) R538-R547). This study evaluated the role of H(2)O(2) on the Na(+)-dependent [(14)C]-l-alanine uptake of ASCT2 in immortalized renal PTE cells from Wistar Kyoto rat (WKY) and spontaneously hypertensive rat (SHR). Na(+) dependence of [(14)C]-l-alanine uptake was investigated replacing NaCl with an equimolar concentration of choline chloride in vehicle- and apocynin-treated cells. Na(+) removal from the uptake solution abolished transport activity in both WKY and SHR PTE cells. Decreases in H(2)O(2) levels in the extracellular medium significantly reduced Na(+)-K(m) and V(max) values of the low-affinity high-capacity component in SHR PTE cells, with no effect on the high-affinity low-capacity state of the Na(+)-dependent [(14)C]-l-alanine uptake. After removal of apocynin from the culture medium, H(2)O(2) levels returned to basal values within 1 to 3h in both WKY and SHR PTE cells and these were found stable for the next 24h. Under these experimental conditions, the Na(+)-K(m) and V(max) of the high-affinity low-capacity state were unaffected and the low-affinity high-capacity component remained significantly decreased 1day but not 4days after apocynin removal. In conclusion, H(2)O(2) in excess is required for the presence of a low-affinity high-capacity component for the Na(+)-dependent [(14)C]-l-alanine uptake in SHR PTE cells only. It is suggested that Na(+) binding in renal ASCT2 may be regulated by ROS in SHR PTE cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport System ASC,
http://linkedlifedata.com/resource/pubmed/chemical/Asct2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1090-2104
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
30
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pubmed:volume |
398
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
553-8
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pubmed:meshHeading |
pubmed-meshheading:20599757-Alanine,
pubmed-meshheading:20599757-Amino Acid Transport System ASC,
pubmed-meshheading:20599757-Animals,
pubmed-meshheading:20599757-Cells, Cultured,
pubmed-meshheading:20599757-Epithelial Cells,
pubmed-meshheading:20599757-Hydrogen Peroxide,
pubmed-meshheading:20599757-Kidney Tubules, Proximal,
pubmed-meshheading:20599757-Rats,
pubmed-meshheading:20599757-Rats, Inbred SHR,
pubmed-meshheading:20599757-Rats, Inbred WKY,
pubmed-meshheading:20599757-Sodium
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pubmed:year |
2010
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pubmed:articleTitle |
Role of H(2)O(2) on the kinetics of low-affinity high-capacity Na(+)-dependent alanine transport in SHR proximal tubular epithelial cells.
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pubmed:affiliation |
Institute of Pharmacology and Therapeutics, Faculty of Medicine, University of Porto, 4200-319 Porto, Portugal.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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