RGD Reference Report - Molecular cloning and functional expression of different molecular forms of rat amiloride-binding proteins. - Rat Genome Database

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Molecular cloning and functional expression of different molecular forms of rat amiloride-binding proteins.

Authors: Lingueglia, E  Renard, S  Voilley, N  Waldmann, R  Chassande, O  Lazdunski, M  Barbry, P 
Citation: Lingueglia E, etal., Eur J Biochem 1993 Sep 1;216(2):679-87.
RGD ID: 724757
Pubmed: PMID:8375402   (View Abstract at PubMed)

The colon and lung amiloride-binding proteins were cloned from rat tissues. Two sizes of transcripts were identified. The 2.7-kb transcript codes for an 85-kDa protein, whereas the 1.2-kb transcript codes for a 25-kDa polypeptide. The 2.7-kb transcript was detected in the proximal and distal colon and in duodenum, liver, placenta and thymus. The 1.2-kb transcript was the only form present in lung and spleen, and it was also detected in placenta and colon. The short form corresponds to the 3' terminus of the longer one. It is formed by alternative transcription under the control of an internal promoter. Cells stably transfected with cDNAs encoding these two proteins were used for binding studies using [3H]phenamil, a potent blocker of the epithelial Na+ channel, derived from amiloride. Both the long and short forms of the protein bind amiloride and some of its derivatives, but they have distinct pharmacologies. The order of potency of the different amiloride derivatives to inhibit [3H]phenamil binding was phenamil (K0.5 = 10 nM) > benzamil (K0.5 = 43 nM) > amiloride (K0.5 = 1.4 microM) approximately ethylisopropylamiloride (K0.5 = 1.6 microM) for the long form, whereas it was phenamil (K0.5 = 68 nM) > amiloride (K0.5 = 3.2 microM) approximately ethylisopropylamiloride (K0.5 = 4 microM) approximately benzamil (K0.5 = 6.3 microM) for the short form. Although the binding proteins described here are distinct from the pore-forming protein of the epithelial Na+ channel, the pharmacological profile of the long form of the ABP is identical to that described previously in pig and human kidney, and similar to that expected for an epithelial Na+ channel. The pharmacological profile of the short form resembles that previously described for an amiloride-binding protein in pneumocytes. Results presented in this paper suggest that previously purified preparations showing Na+ channel activity contain different forms of the amiloride-binding protein, possibly associated with other proteins. The similarity between amiloride-binding proteins and a protein identified in seminal vesicles suggests that amiloride-binding proteins are the first members of a new family of epithelia-specific proteins.



Gene-Chemical Interaction Annotations    Click to see Annotation Detail View

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
AOC1Humanamiloride multiple interactionsISOAoc1 (Rattus norvegicus)Amiloride inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
AOC1Humanamiloride affects bindingISOAoc1 (Rattus norvegicus)Amiloride binds to Aoc1 proteinRGD 
Aoc1Ratamiloride affects bindingEXP Amiloride binds to Aoc1 proteinRGD 
Aoc1Ratamiloride multiple interactionsEXP Amiloride inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
Aoc1Mouseamiloride affects bindingISOAoc1 (Rattus norvegicus)Amiloride binds to Aoc1 proteinRGD 
Aoc1Mouseamiloride multiple interactionsISOAoc1 (Rattus norvegicus)Amiloride inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
AOC1HumanBenzamil multiple interactionsISOAoc1 (Rattus norvegicus)Benzamil inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
AOC1HumanBenzamil affects bindingISOAoc1 (Rattus norvegicus)Benzamil binds to Aoc1 proteinRGD 
Aoc1RatBenzamil affects bindingEXP Benzamil binds to Aoc1 proteinRGD 
Aoc1RatBenzamil multiple interactionsEXP Benzamil inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
Aoc1MouseBenzamil affects bindingISOAoc1 (Rattus norvegicus)Benzamil binds to Aoc1 proteinRGD 
Aoc1MouseBenzamil multiple interactionsISOAoc1 (Rattus norvegicus)Benzamil inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
AOC1Humanethylisopropylamiloride affects bindingISOAoc1 (Rattus norvegicus)Ethylisopropylamiloride binds to Aoc1 proteinRGD 
AOC1Humanethylisopropylamiloride multiple interactionsISOAoc1 (Rattus norvegicus)Ethylisopropylamiloride inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
Aoc1Ratethylisopropylamiloride affects bindingEXP Ethylisopropylamiloride binds to Aoc1 proteinRGD 
Aoc1Ratethylisopropylamiloride multiple interactionsEXP Ethylisopropylamiloride inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
Aoc1Mouseethylisopropylamiloride affects bindingISOAoc1 (Rattus norvegicus)Ethylisopropylamiloride binds to Aoc1 proteinRGD 
Aoc1Mouseethylisopropylamiloride multiple interactionsISOAoc1 (Rattus norvegicus)Ethylisopropylamiloride inhibits the reaction [Phenylamil binds to Aoc1 protein]RGD 
AOC1HumanPhenylamil affects bindingISOAoc1 (Rattus norvegicus)Phenylamil binds to Aoc1 proteinRGD 
Aoc1RatPhenylamil affects bindingEXP Phenylamil binds to Aoc1 proteinRGD 
Aoc1MousePhenylamil affects bindingISOAoc1 (Rattus norvegicus)Phenylamil binds to Aoc1 proteinRGD 

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Aoc1Ratorganic cyclic compound binding  IPIPhenylamil more ... RGD 

Objects Annotated

Genes (Rattus norvegicus)
Aoc1  (amine oxidase, copper containing 1)

Genes (Mus musculus)
Aoc1  (amine oxidase, copper-containing 1)

Genes (Homo sapiens)
AOC1  (amine oxidase copper containing 1)


Additional Information