Literature DB >> 9573526

A novel frameshift mutation induced by an adenosine insertion in the polycystic kidney disease 2 (PKD2) gene.

Y Pei1, K Wang, M Kasenda, A D Paterson, Y Liang, E Huang, J Lian, E Rogovea, S Somlo, P St George-Hyslop.   

Abstract

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.

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Year:  1998        PMID: 9573526     DOI: 10.1046/j.1523-1755.1998.00890.x

Source DB:  PubMed          Journal:  Kidney Int        ISSN: 0085-2538            Impact factor:   10.612


  2 in total

1.  Coordinate expression of the autosomal dominant polycystic kidney disease proteins, polycystin-2 and polycystin-1, in normal and cystic tissue.

Authors:  A C Ong; C J Ward; R J Butler; S Biddolph; C Bowker; R Torra; Y Pei; P C Harris
Journal:  Am J Pathol       Date:  1999-06       Impact factor: 4.307

2.  Domain mapping of the polycystin-2 C-terminal tail using de novo molecular modeling and biophysical analysis.

Authors:  Andjelka Celić; Edward T Petri; Borries Demeler; Barbara E Ehrlich; Titus J Boggon
Journal:  J Biol Chem       Date:  2008-08-11       Impact factor: 5.157

  2 in total

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