ArticleMolecular and cellular biochemistry2005
Cardiac syntrophin isoforms: species-dependent expression, association with dystrophin complex and subcellular localization.
Article in Molecular and cellular biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed, 8 citations in OpenAlex.
- A Distinct Pool of NaFrontiers in physiology · 2019Article
- Distinct pathophysiological mechanisms of cardiomyopathy in hearts lacking dystrophin or the sarcoglycan complex.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
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3 authors at 2 institutions in 1 country.
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Abstract
Syntrophin is known to be a component of the dystrophin-glycoprotein complex (DGC), a membrane/cytoskeleton-anchoring structure that is essential for the maintenance of viability of sarcolemma. We purified DGC from hearts of human and several animal species, and compared their protein composition. While almost all components of DGC were present in various species, proteins with the apparent molecular mass of 50-65 kDa corresponding to syntrophin isoforms were very different among them. Three isoforms of syntrophin (alpha1, beta1, beta2) were expressed in hamster, rat and canine ventricles, whereas only alpha1-isoform was mainly expressed in human and rabbit ventricles. Immunohistochemical analysis revealed that alpha1-and beta2-syntrophins were co-localized in sarcolemma and in T-tubules of canine ventricles. However, despite membrane localization of most syntrophins, subcellular fractionation revealed that part of syntrophins were recovered in the cytosolic fraction devoid of other components of DGC, raising the possibility that syntrophins may play multiple roles in various intracellular sites of cardiac muscle cells. Species-dependent expression and unique subcellular localization of syntrophins in cardiac muscle may contribute to the variable severity of muscle dysgenesis caused by the same primary defect in components of DGC of human and other animal species.
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