Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
30
|
| pubmed:dateCreated |
1996-9-3
|
| pubmed:abstractText |
Apx, the amphibian protein associated with renal amiloride-sensitive Na+ channel activity and with properties consistent with the pore-forming 150-kDa subunit of an epithelial Na+ channel complex initially purified by Benos et al. (Benos, D. J., Saccomani, G., and Sariban-Sohraby, S.(1987) J. Biol. Chem. 262, 10613-10618), has previously failed to generate amiloride-sensitive Na+ currents (Staub, O., Verrey, F., Kleyman, T. R., Benos, D. J., Rossier, B. C., and Kraehenbuhl, J.-P.(1992) J. Cell Biol. 119, 1497-1506). Renal epithelial Na+ channel activity is tonically inhibited by endogenous actin filaments (Cantiello, H. F., Stow, J., Prat, A. G., and Ausiello, D. A.(1991) Am. J. Physiol. 261, C882-C888). Thus, Apx was expressed and its function examined in human melanoma cells with a defective actin-based cytoskeleton. Apx-transfection was associated with a 60-900% increase in amiloride-sensitive (Ki = 3 microM) Na+ currents. Single channel Na+ currents had a similar functional fingerprint to the vasopressin-sensitive, and actin-regulated epithelial Na+ channel of A6 cells, including a 6-7 pS single channel conductance and a perm-selectivity of Na+:K+ of 4:1. Na+ channel activity was either spontaneous, or induced by addition of actin or protein kinase A plus ATP to the bathing solution of excised inside-out patches. Therefore, Apx may be responsible for the ionic conductance involved in the vasopressin-activated Na+ reabsorption in the amphibian kidney.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Amiloride,
http://linkedlifedata.com/resource/pubmed/chemical/Apx protein, Xenopus,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
26
|
| pubmed:volume |
271
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
18045-53
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8663566-Actins,
pubmed-meshheading:8663566-Amiloride,
pubmed-meshheading:8663566-Amino Acid Sequence,
pubmed-meshheading:8663566-Animals,
pubmed-meshheading:8663566-Binding Sites,
pubmed-meshheading:8663566-Biological Transport,
pubmed-meshheading:8663566-Cytoskeleton,
pubmed-meshheading:8663566-Dose-Response Relationship, Drug,
pubmed-meshheading:8663566-Electric Conductivity,
pubmed-meshheading:8663566-Epithelium,
pubmed-meshheading:8663566-Humans,
pubmed-meshheading:8663566-Kidney,
pubmed-meshheading:8663566-Melanoma,
pubmed-meshheading:8663566-Molecular Sequence Data,
pubmed-meshheading:8663566-Protein Binding,
pubmed-meshheading:8663566-Recombinant Proteins,
pubmed-meshheading:8663566-Sodium Channels,
pubmed-meshheading:8663566-Tumor Cells, Cultured,
pubmed-meshheading:8663566-Xenopus Proteins,
pubmed-meshheading:8663566-Xenopus laevis
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Renal epithelial protein (Apx) is an actin cytoskeleton-regulated Na+ channel.
|
| pubmed:affiliation |
Renal Unit, Massachusetts General Hospital East, Charlestown, Massachusetts 02129, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|