Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4 Pt 2
|
| pubmed:dateCreated |
1994-11-18
|
| pubmed:abstractText |
Vasopressin-regulated water permeability of the kidney collecting duct is a key component of the urine concentration machinery. Recently, a cDNA for AQP-CD, the vasopressin-regulated water channel, initially reported as WCH-CD, has been isolated (K. Fushimi, S. Uchida, Y. Hara, Y. Hirata, F. Marumo, and S. Sasaki. Nature Lond. 361: 549-552, 1993). AQP-CD was expressed in oocyte membrane using a Xenopus expression vector, and functional characteristics of AQP-CD were examined. Osmotic water permeability (Pf) of oocytes expressing AQP-CD was 138 +/- 19 microns/s (mean +/- SE), 12 times greater than the control (11 +/- 3 microns/s), 90% inhibited by 0.3 mM HgCl2, and weakly temperature dependent (energy of activation for Pf was 4.0 kcal/mol). Urea influx measured from 15-min [14C]urea uptake by oocytes injected with AQP-CD/expression vector 1 cRNA was 86 +/- 17% of the control. Two-electrode voltage-clamp experiments revealed insignificant ion conductance of AQP-CD. Immunoblots of membranes from rat kidney medulla and oocytes expressing AQP-CD using anti-AQP-CD COOH-terminal antibody showed a 29-kDa protein and 35- to 50-kDa high-molecular-mass forms. Immunohistochemistry showed apical and subapical localization of AQP-CD in the collecting duct principal cells. Our results indicated that AQP-CD is a 29-kDa protein, a selective water channel, distinct from a urea channel, and localized to the membranes of vasopressin-sensitive components in kidney collecting duct principal cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aqp1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporins,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Complementary
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0002-9513
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
267
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
N
|
| pubmed:pagination |
F573-82
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7524358-Amino Acid Sequence,
pubmed-meshheading:7524358-Animals,
pubmed-meshheading:7524358-Aquaporin 1,
pubmed-meshheading:7524358-Aquaporins,
pubmed-meshheading:7524358-Cell Membrane Permeability,
pubmed-meshheading:7524358-Electric Conductivity,
pubmed-meshheading:7524358-Female,
pubmed-meshheading:7524358-Fluorescent Antibody Technique,
pubmed-meshheading:7524358-Immunohistochemistry,
pubmed-meshheading:7524358-Ion Channels,
pubmed-meshheading:7524358-Kidney Cortex,
pubmed-meshheading:7524358-Kidney Medulla,
pubmed-meshheading:7524358-Kidney Tubules, Collecting,
pubmed-meshheading:7524358-Membrane Potentials,
pubmed-meshheading:7524358-Microscopy, Immunoelectron,
pubmed-meshheading:7524358-Models, Structural,
pubmed-meshheading:7524358-Molecular Sequence Data,
pubmed-meshheading:7524358-Molecular Weight,
pubmed-meshheading:7524358-Oocytes,
pubmed-meshheading:7524358-Protein Structure, Secondary,
pubmed-meshheading:7524358-Proton-Translocating ATPases,
pubmed-meshheading:7524358-RNA, Complementary,
pubmed-meshheading:7524358-Rats,
pubmed-meshheading:7524358-Rats, Sprague-Dawley,
pubmed-meshheading:7524358-Xenopus laevis
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Functional characterization and cell immunolocalization of AQP-CD water channel in kidney collecting duct.
|
| pubmed:affiliation |
Second Department of Internal Medicine, Tokyo Medical and Dental University, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|