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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1998-6-30
|
| pubmed:abstractText |
Autosomal dominant polycystic kidney disease (ADPKD) is one of the most common Mendelian disorders and is genetically heterogeneous. Linkage studies have shown that the majority (approximately 85%) of ADPKD cases are due to mutations in PKD1 on chromosome 16p13.3, while mutations in PKD2 on chromosome 4q21-q23 are thought to account for most of the remaining cases. In this report, we describe the mutation in a large four-generation ADPKD family (TOR-PKD77) which we had mapped to the PKD2 locus by linkage analysis. In this family, we screened for mutations by directly sequencing two nested RT-PCR fragments (PKD2N1 and PKD2N2) that cover approximately 90% of the PKD2 open reading frame. In the affected members, we identified a novel single adenosine insertion (2160InsA) in the PKD2N2 fragment. This mutation occurred in the polyadenosine tract (nt2152-2159) of exon 11 and is predicted to result in a frameshift with premature translation termination of the PKD2 product, polycystin 22, immediately after codon 723. The truncated polycystin 2 is predicted to lack the calcium-binding EF-hand domain and two cytoplasmic domains required for the homodimerization of polycystin 2 with itself and for the heterodimerization of polycystin 2 with polycystin 1.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TRPP Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/polycystic kidney disease 2 protein
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0085-2538
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
53
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1127-32
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:9573526-Adenosine,
pubmed-meshheading:9573526-Alleles,
pubmed-meshheading:9573526-Amino Acid Sequence,
pubmed-meshheading:9573526-Base Sequence,
pubmed-meshheading:9573526-Chromosomes, Human, Pair 4,
pubmed-meshheading:9573526-DNA Primers,
pubmed-meshheading:9573526-Exons,
pubmed-meshheading:9573526-Female,
pubmed-meshheading:9573526-Frameshift Mutation,
pubmed-meshheading:9573526-Genetic Linkage,
pubmed-meshheading:9573526-Genotype,
pubmed-meshheading:9573526-Humans,
pubmed-meshheading:9573526-Male,
pubmed-meshheading:9573526-Membrane Proteins,
pubmed-meshheading:9573526-Middle Aged,
pubmed-meshheading:9573526-Models, Molecular,
pubmed-meshheading:9573526-Nucleic Acid Hybridization,
pubmed-meshheading:9573526-Pedigree,
pubmed-meshheading:9573526-Polycystic Kidney, Autosomal Dominant,
pubmed-meshheading:9573526-Polymerase Chain Reaction,
pubmed-meshheading:9573526-Protein Conformation,
pubmed-meshheading:9573526-TRPP Cation Channels
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
A novel frameshift mutation induced by an adenosine insertion in the polycystic kidney disease 2 (PKD2) gene.
|
| pubmed:affiliation |
Department of Medicine, Toronto Hospital, Ontario, Canada. ypei@torhosp.toronto.on.ca
|
| pubmed:publicationType |
Journal Article,
Case Reports,
Research Support, Non-U.S. Gov't
|