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Mol Cell Biochem. 2005 Jan;268(1-2):59-66.

Cardiac syntrophin isoforms: species-dependent expression, association with dystrophin complex and subcellular localization.

Author information

1
Department of Molecular Physiology, National Cardiovascular Center Research Institute, Fujishiro-dai, Suita, Osaka, Japan. yukoiwat@ri.ncvc.go.jp

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.

PMID:
15724438
DOI:
10.1007/s11010-005-2998-z
[Indexed for MEDLINE]

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