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PubMed · 2217167

Human kidney amiloride-binding protein: cDNA structure and functional expression.

P Barbry·M Champe·O Chassande·S Munemitsu·G Champigny·E Lingueglia·P Maes·C Frelin·A Tartar·A Ullrich
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Abstract

Phenamil, an analog of amiloride, is a potent blocker of the epithelial Na+ channel. It has been used to purify the porcine kidney amiloride-binding protein. Synthetic oligonucleotides derived from partial sequences have been used to screen a human kidney cDNA library and to isolate the cDNA encoding the human amiloride-binding protein. The primary structure was deduced from the DNA sequence analysis. The protein is 713 residues long, with a 19-amino acid signal peptide. The mRNA was expressed in 293-S and NIH 3T3 cells, yielding a glycoprotein (i) that binds amiloride and amiloride analogs with affinities similar to the amiloride receptor associated with the apical Na+ channel in pig kidney membranes and (ii) that is immunoprecipitated with monoclonal antibodies raised against pig kidney amiloride-binding protein.

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AmilorideAmine Oxidase (Copper-Containing)Amino Acid SequenceAnimalsBase SequenceCarrier ProteinsCell LineCell MembraneCloning, MolecularDNAGene LibraryHumansKineticsMolecular Sequence DataOligonucleotide ProbesPeptide MappingRNA, MessengerRecombinant ProteinsSequence Homology, Nucleic AcidSwineTransfectionComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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P Barbry, M Champe, O Chassande, S Munemitsu, G Champigny, E Lingueglia, P Maes, C Frelin, A Tartar, A Ullrich. 1990. Human kidney amiloride-binding protein: cDNA structure and functional expression.. https://doi.org/10.1073/pnas.87.19.7347

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