2000
DOI: 10.1161/01.res.87.6.489
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Dissociation of Sarcoglycans and the Dystrophin Carboxyl Terminus From the Sarcolemma in Enteroviral Cardiomyopathy

Abstract: Enteroviral infection can cause an acquired form of dilated cardiomyopathy. We recently reported that dystrophin is cleaved, functionally impaired, and morphologically disrupted in vitro as well as in vivo during infection with coxsackievirus B3. Genetic dystrophin truncations lead to a marked decrease in dystrophin-associated glycoproteins, whereas expression of only the naturally occurring dystrophin carboxyl terminus, Dp-71, restores the sarcolemmal association of the dystrophin-associated glycoproteins. We… Show more

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Cited by 44 publications
(25 citation statements)
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“…This is consistent with our previous data demonstrating that the absence of dystrophin increased susceptibility to viral infection (5). Apart from the loss of dystrophin at the sarcolemma, which has been shown to increase susceptibility to viral infection, there are other genetic and secondary alterations in the dystrophin-glycoprotein complex (DGC) that affect sarcolemmal stability and could affect susceptibility to viral infection (12)(13)(14)(15)(16)(17). Therefore, it is possible that genetic variability in the core components of the DGC or alterations that affect the level of dystrophin expression (such as occurs in Becker muscular dystrophy or X-linked dilated cardiomyopathy) (18) could have a profound permissive or inhibitory effect on susceptibility to enteroviral infection.…”
Section: Figuresupporting
confidence: 92%
“…This is consistent with our previous data demonstrating that the absence of dystrophin increased susceptibility to viral infection (5). Apart from the loss of dystrophin at the sarcolemma, which has been shown to increase susceptibility to viral infection, there are other genetic and secondary alterations in the dystrophin-glycoprotein complex (DGC) that affect sarcolemmal stability and could affect susceptibility to viral infection (12)(13)(14)(15)(16)(17). Therefore, it is possible that genetic variability in the core components of the DGC or alterations that affect the level of dystrophin expression (such as occurs in Becker muscular dystrophy or X-linked dilated cardiomyopathy) (18) could have a profound permissive or inhibitory effect on susceptibility to enteroviral infection.…”
Section: Figuresupporting
confidence: 92%
“…1 Membrane fractions were prepared by layering ventricular extracts onto a linear 5% to 20% sucrose density gradient and subjecting them to ultracentrifugation, fractionation, and concentration as described previously. 27 Immunodetection of ␣-catenin (Sigma-Aldrich, Inc, St Louis, Mo), ␣-T catenin (kind gift from Dr Frans van Roy, Ghent University, Ghent, Belgium), ␤-catenin (Affiniti Research Products Ltd, Plymouth Meeting, Pa), vinculin (Sigma-Aldrich), dystrophin, 27 pan-cadherin (SigmaAldrich), desmoplakin (Serotec, Raleigh, NC), plakoglobin (Transduction Laboratories, BD Biosciences, San Jose, Calif), connexin 43 (Chemicon, Temecula, Calif), and all actin (Sigma-Aldrich), was performed as described previously. 1,28 …”
Section: Protein Analysismentioning
confidence: 99%
“…After overnight incubation at 4°C with primary anti-Ca V ␣2␦1 antibody (1:50) (Santa Cruz Biotechnology) in 1% donkey serum with 0.05% Triton X-100, cells were incubated with the secondary Alexa 488 antibody (Life Technologies, Inc.) (1:800) for 90 min at room temperature. Cells were stained with DAPI (1:1000) (Life Technologies, Inc.) for 10 min to identify the nucleus and with the wheat germ agglutinin-647 (WGA-647) (1:200) (Life Technologies, Inc.) to visualize cell membrane glycoproteins (51,52). WGA is a carbohydrate-binding protein of approximately 36 kDa that selectively recognizes sialic acid and N-acetylglucosaminyl sugar residues.…”
Section: Methodsmentioning
confidence: 99%