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rdf:type |
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lifeskim:mentions |
umls-concept:C0017243,
umls-concept:C0022680,
umls-concept:C0026882,
umls-concept:C0029974,
umls-concept:C0086418,
umls-concept:C0256073,
umls-concept:C0453543,
umls-concept:C0596311,
umls-concept:C0597357,
umls-concept:C1330957,
umls-concept:C1514562,
umls-concept:C1546857,
umls-concept:C1880389,
umls-concept:C1881293,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
26
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pubmed:dateCreated |
2002-12-24
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pubmed:abstractText |
Polycystin-1 plays an essential role in renal tubular morphogenesis, and disruption of its function causes cystogenesis in human autosomal-dominant polycystic kidney disease (ADPKD). We demonstrated that polycystin-1 undergoes cleavage at G protein coupled receptor proteolytic site in a process that requires the receptor for egg jelly domain. Most of the N-terminal fragment remains tethered at the cell surface, although a small amount is secreted. PKD1-associated mutations in the receptor for egg jelly domain disrupt cleavage, abolish the ability of polycystin-1 to activate signal transducer and activator of transcription-1, and induce tubulogenesis in vitro. We conclude that the cleavage of polycystin-1 is likely essential for its biologic activity.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-10469603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-10677526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-10838568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-10861291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-10923040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-11106764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-11115377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-11140688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-11593033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-11696547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-11728985,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-11786542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-12007403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-1633713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-2187866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-3283938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-7663510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-8321262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-8666666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-8755489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-8955192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-9171830,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-9208860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-9285784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-9734362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-9792824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12482949-9920906
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16981-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12482949-Amino Acid Sequence,
pubmed-meshheading:12482949-Humans,
pubmed-meshheading:12482949-Molecular Sequence Data,
pubmed-meshheading:12482949-Mutagenesis, Site-Directed,
pubmed-meshheading:12482949-Mutation,
pubmed-meshheading:12482949-Polycystic Kidney, Autosomal Dominant,
pubmed-meshheading:12482949-Proteins,
pubmed-meshheading:12482949-Receptors, Cell Surface,
pubmed-meshheading:12482949-Signal Transduction,
pubmed-meshheading:12482949-TRPP Cation Channels
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pubmed:year |
2002
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pubmed:articleTitle |
Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations.
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pubmed:affiliation |
Department of Medicine, Division of Nephrology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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