Human kidney amiloride-binding protein: cDNA structure and functional expression
| Autor: | Guy Champigny, M Champe, André Tartar, P Maes, Christian Frelin, S Munemitsu, A Ullrich, Pascal Barbry, Olivier Chassande, Eric Lingueglia |
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| Rok vydání: | 1990 |
| Předmět: |
Signal peptide
Epithelial sodium channel Swine Molecular Sequence Data Biology Transfection Peptide Mapping Cell Line Amiloride Sequence Homology Nucleic Acid Complementary DNA medicine Animals Humans Amino Acid Sequence RNA Messenger Cloning Molecular Peptide sequence Gene Library Multidisciplinary Base Sequence cDNA library Binding protein Cell Membrane Protein primary structure DNA Molecular biology Recombinant Proteins Kinetics Biochemistry Amine Oxidase (Copper-Containing) Carrier Proteins Oligonucleotide Probes Research Article medicine.drug |
| Zdroj: | Europe PubMed Central |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | 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: | OpenAIRE |
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