Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4 Pt 2
|
| pubmed:dateCreated |
1997-5-28
|
| pubmed:abstractText |
PKD1, the gene that is mutated in approximately 85% of autosomal dominant polycystic kidney disease (ADPKD) cases in humans, has recently been identified (Eur. PKD Consortium. Cell 77: 881-894, 1994; also, erratum in Cell 78: 1994). The longest open-reading frame of PKD1 encodes polycystin, a novel approximately 460-kDa protein that contains a series of NH2-terminal adhesive domains (J. Hughes, C. J. Ward, B. Peral, R. Aspinwall, K. Clark, J. San Millan, V. Gamble, and P. C. Harris. Nat. Genet. 10: 151-160, 1995; and Int. PKD Consortium. Cell 81: 289-298, 1995) and several putative transmembrane segments. To extend studies of polycystin to an experimentally accessible animal, we have isolated a cDNA clone encoding the 3' end of Pkd1, the mouse homologue of PKD1, and raised a specific antibody to recombinant murine polycystin. This antibody was used to determine the subcellular localization and tissue distribution of the protein by Western analysis and immunocytochemistry. In the mouse, polycystin is an approximately 400-kDa molecule that is predominantly found in membrane fractions of tissue and cell extracts. It is expressed in many tissues including kidney, liver, pancreas, heart, intestine, lung, and brain. Renal expression, which is confined to tubular epithelia, is highest in late fetal and early neonatal life and drops 20-fold by the third postnatal week, maintaining this level into adulthood. Thus the temporal profile of polycystin expression coincides with kidney tubule differentiation and maturation.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TRPP Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/polycystic kidney disease 1 protein
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0002-9513
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
272
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
F451-9
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:9140045-Aging,
pubmed-meshheading:9140045-Amino Acid Sequence,
pubmed-meshheading:9140045-Animals,
pubmed-meshheading:9140045-Cloning, Molecular,
pubmed-meshheading:9140045-Embryonic and Fetal Development,
pubmed-meshheading:9140045-Female,
pubmed-meshheading:9140045-Gene Expression Regulation, Developmental,
pubmed-meshheading:9140045-Gestational Age,
pubmed-meshheading:9140045-Humans,
pubmed-meshheading:9140045-Immunohistochemistry,
pubmed-meshheading:9140045-Kidney,
pubmed-meshheading:9140045-Mice,
pubmed-meshheading:9140045-Molecular Sequence Data,
pubmed-meshheading:9140045-Open Reading Frames,
pubmed-meshheading:9140045-Polycystic Kidney, Autosomal Dominant,
pubmed-meshheading:9140045-Pregnancy,
pubmed-meshheading:9140045-Protein Biosynthesis,
pubmed-meshheading:9140045-Proteins,
pubmed-meshheading:9140045-Recombinant Fusion Proteins,
pubmed-meshheading:9140045-Sequence Homology, Amino Acid,
pubmed-meshheading:9140045-Subcellular Fractions,
pubmed-meshheading:9140045-TRPP Cation Channels
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Distribution and developmentally regulated expression of murine polycystin.
|
| pubmed:affiliation |
Renal Division, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|