| Autor: |
Barbry, P, Champe, M, Chassande, O, Munemitsu, S, Champigny, G, Lingueglia, E, Maes, P, Frelin, C, Tartar, A, Ullrich, A |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; October 1990, Vol. 87 Issue: 19 p7347-7351, 5p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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