| Literature DB >> 12571597 |
Peter J Mohler1, Jean-Jacques Schott, Anthony O Gramolini, Keith W Dilly, Silvia Guatimosim, William H duBell, Long-Sheng Song, Karine Haurogné, Florence Kyndt, Mervat E Ali, Terry B Rogers, W J Lederer, Denis Escande, Herve Le Marec, Vann Bennett.
Abstract
Mutations in ion channels involved in the generation and termination of action potentials constitute a family of molecular defects that underlie fatal cardiac arrhythmias in inherited long-QT syndrome. We report here that a loss-of-function (E1425G) mutation in ankyrin-B (also known as ankyrin 2), a member of a family of versatile membrane adapters, causes dominantly inherited type 4 long-QT cardiac arrhythmia in humans. Mice heterozygous for a null mutation in ankyrin-B are haploinsufficient and display arrhythmia similar to humans. Mutation of ankyrin-B results in disruption in the cellular organization of the sodium pump, the sodium/calcium exchanger, and inositol-1,4,5-trisphosphate receptors (all ankyrin-B-binding proteins), which reduces the targeting of these proteins to the transverse tubules as well as reducing overall protein level. Ankyrin-B mutation also leads to altered Ca2+ signalling in adult cardiomyocytes that results in extrasystoles, and provides a rationale for the arrhythmia. Thus, we identify a new mechanism for cardiac arrhythmia due to abnormal coordination of multiple functionally related ion channels and transporters.Entities:
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Year: 2003 PMID: 12571597 DOI: 10.1038/nature01335
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962