Journal article
Enteroviral protease 2A cleaves dystrophin: Evidence of cytoskeletal disruption in an acquired cardiomyopathy
Nature medicine, Vol.5(3), pp.320-326
03/1999
DOI: 10.1038/6543
PMID: 10086389
Abstract
Enteroviruses such as Coxsackievirus B3 can cause dilated cardiomyopathy, but the mechanism of this pathology is unknown. Mutations in cytoskeletal proteins such as dystrophin cause hereditary dilated cardiomyopathy, but it is unclear if similar mechanisms underlie acquired forms of heart failure. We demonstrate here that purified Coxsackievirus protease 2A cleaves dystrophin in vitro as predicted by computer analysis. Dystrophin is also cleaved during Coxsackievirus infection of cultured myocytes and in infected mouse hearts, leading to impaired dystrophin function. In vivo, dystrophin and the dystrophin-associated glycoproteins α-sarcoglycan and β-dystroglycan are morphologically disrupted in infected myocytes. We suggest a molecular mechanism through which enteroviral infection contributes to the pathogenesis of acquired forms of dilated cardiomyopathy.
Details
- Title: Subtitle
- Enteroviral protease 2A cleaves dystrophin: Evidence of cytoskeletal disruption in an acquired cardiomyopathy
- Creators
- Kevin P Campbell - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of MedicineKirk U Knowlton - Department of Medicine, University of CaliforniaRobert E Rhoads - Department of Biochemistry and Molecular Biology, Louisiana State University Medical CenterCornel Badorff - Department of Medicine, University of CaliforniaMaryann E Martone - Department of Neurosciences, National Center for Microscopy and Imaging Research, University of CaliforniaBarry J Lamphear - Department of Biochemistry and Molecular Biology, Louisiana State University Medical CenterGil-Hwan Lee - Department of Medicine, University of California
- Resource Type
- Journal article
- Publication Details
- Nature medicine, Vol.5(3), pp.320-326
- DOI
- 10.1038/6543
- PMID
- 10086389
- ISSN
- 1078-8956
- eISSN
- 1546-170X
- Language
- English
- Date published
- 03/1999
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984020776302771
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