Abstract
In the present study, we demonstrate that NLT (novel liver-specific transport protein) is a multispecific organic anion transporter of the liver. The amino acid sequence of NLT shows 42% identity to that of the renal multispecific organic anion transporter, OAT1. When expressed in Xenopus laevis oocytes, NLT mediated uptake of organic anions, such as salicylate, acetylsalicylate, PGE2, dicarboxylates and p-aminohippurate. [14C]Salicylate uptake via NLT was saturable (Km = 88.8 +/- 23.4 microM) and sodium-independent. Expression of the mRNA of NLT was detected in the liver and kidney (liver >> kidney). We propose that NLT be renamed OAT2.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Blotting, Northern
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Carrier Proteins / chemistry
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Carrier Proteins / genetics*
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Carrier Proteins / isolation & purification
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Carrier Proteins / metabolism
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Ion Transport
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Liver / metabolism*
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Membrane Proteins / chemistry
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Membrane Proteins / genetics*
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Membrane Proteins / isolation & purification
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Membrane Proteins / metabolism
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Organic Anion Transporters, Sodium-Independent*
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Rats
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Salicylates / metabolism
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Salicylic Acid
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Substrate Specificity
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Xenopus laevis
Substances
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Carrier Proteins
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Membrane Proteins
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Organic Anion Transporters, Sodium-Independent
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Salicylates
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Slc22a7 protein, rat
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Salicylic Acid