Abstract
Carrier-mediated prostaglandin transport has been postulated to occur in many tissues. On the basis of sequence homology, the protein of unknown function encoded by the rat matrin F/G complementary DNA was predicted to be an organic anion transporter. Expression of the matrin F/G complementary DNA in HeLa cells or Xenopus oocytes conferred the property of specific transport of prostaglandins. The tissue distribution of matrin F/G messenger RNA and the sensitivity of matrin F/G-induced prostaglandin transport to inhibitors were similar to those of endogenous prostaglandin transport. The protein encoded by the matrin F/G complementary DNA is thus preferably called PGT because it is likely to function as a prostaglandin transporter.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Antiporters*
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Base Sequence
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Biological Transport / drug effects
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Codon
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Colon / metabolism
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DNA, Complementary / genetics
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Epithelium / metabolism
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HeLa Cells
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Humans
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Kidney Medulla / metabolism
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Molecular Sequence Data
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Organic Anion Transporters
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Prostaglandins / metabolism*
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RNA, Messenger / analysis
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Rats
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Xenopus
Substances
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Antiporters
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Carrier Proteins
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Codon
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DNA, Complementary
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DNA-Binding Proteins
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Organic Anion Transporters
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Prostaglandins
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RNA, Messenger
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SLCO2A1 protein, human
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Slco2a1 protein, rat