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. 1990 Oct;87(19):7347–7351. doi: 10.1073/pnas.87.19.7347

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

P Barbry 1, M Champe 1, O Chassande 1, S Munemitsu 1, G Champigny 1, E Lingueglia 1, P Maes 1, C Frelin 1, A Tartar 1, A Ullrich 1, et al.
PMCID: PMC54743  PMID: 2217167

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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Selected References

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