Linked Life Data

8375402

Source:http://linkedlifedata.com/resource/pubmed/id/8375402

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-15
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
216
pubmed:geneSymbol
ABP
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
679-87
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8375402-Amine Oxidase (Copper-Containing), pubmed-meshheading:8375402-Amino Acid Sequence, pubmed-meshheading:8375402-Animals, pubmed-meshheading:8375402-Base Sequence, pubmed-meshheading:8375402-Carrier Proteins, pubmed-meshheading:8375402-Cloning, Molecular, pubmed-meshheading:8375402-Colon, pubmed-meshheading:8375402-DNA, pubmed-meshheading:8375402-Humans, pubmed-meshheading:8375402-Lung, pubmed-meshheading:8375402-Molecular Sequence Data, pubmed-meshheading:8375402-Promoter Regions, Genetic, pubmed-meshheading:8375402-RNA, Messenger, pubmed-meshheading:8375402-Rats, pubmed-meshheading:8375402-Sequence Homology, Amino Acid, pubmed-meshheading:8375402-Sequence Homology, Nucleic Acid, pubmed-meshheading:8375402-Species Specificity, pubmed-meshheading:8375402-Transcription, Genetic
pubmed:year
1993
pubmed:articleTitle
Molecular cloning and functional expression of different molecular forms of rat amiloride-binding proteins.
pubmed:affiliation
Institut de Pharmacologie Moléculaire et Cellulaire, CNRS, Valbonne, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't