The fourth component of the sarcoglycan complex

Yoshida, Motoaki; Noguchi, S.; Wakabayashi, Eriko; Piluso, Giulio; Belsito, Angela; Nigro, Vincenzo; Ozawa, Eijiro

doi:10.1016/s0014-5793(97)00040-9

Cited by 25 publications

(17 citation statements)

References 20 publications

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“…In collaboration with him, we 55) showed that δ-SG (glycoprotein) is also contained in the purified SG complex preparation. Therefore, the SG complex is composed of four subunits.…”

Section: Dystrophin and The Dystrophin-associated Protein (Dap) Complmentioning

confidence: 89%

“…54) They 72) showed that the 5q33 mapping patients had mutations on the δ -SG gene. We, in collaboration with Nigro, 55) showed that its protein product is actually present in a purified SG complex. After a while, Zatz and Kunkel 73) reported that in all the cases originating from mutations in any of four SG genes, the patient muscles lack the entire SG complex by immunohistochemistry, although low levels of some subunits are sometimes observed.…”

Section: The Second Stage Of the Dystrophin Eramentioning

confidence: 92%

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Our trails and trials in the subsarcolemmal cytoskeleton network and muscular dystrophy researches in the dystrophin era

Ozawa

2010

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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In 1987, about 150 years after the discovery of Duchenne muscular dystrophy (DMD), its responsible gene, the dystrophin gene, was cloned by Kunkel. This was a new substance. During these 20 odd years after the cloning, our understanding on dystrophin as a component of the subsarcolemmal cytoskeleton networks and on the pathomechanisms of and experimental therapeutics for DMD has been greatly enhanced. During this paradigm change, I was fortunately able to work as an active researcher on its frontiers for 12 years. After we discovered that dystrophin is located on the cell membrane in 1988, we studied the architecture of dystrophin and dystrophin-associated proteins (DAPs) complex in order to investigate the function of dystrophin and pathomechanism of DMD. During the conduct of these studies, we came to consider that the dystrophin–DAP complex serves to transmembranously connect the subsarcolemmal cytoskeleton networks and basal lamina to protect the lipid bilayer. It then became our working hypothesis that injury of the lipid bilayer upon muscle contraction is the cause of DMD. During this process, we predicted that subunits of the sarcoglycan (SG) complex are responsible for respective types of DMD-like muscular dystrophy with autosomal recessive inheritance. Our prediction was confirmed to be true by many researchers including ourselves. In this review, I will try to explain what we observed and how we considered concerning the architecture and function of the dystrophin–DAP complex, and the pathomechanisms of DMD and related muscular dystrophies.

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“…In collaboration with him, we 55) showed that δ-SG (glycoprotein) is also contained in the purified SG complex preparation. Therefore, the SG complex is composed of four subunits.…”

Section: Dystrophin and The Dystrophin-associated Protein (Dap) Complmentioning

confidence: 89%

Section: The Second Stage Of the Dystrophin Eramentioning

confidence: 92%

Our trails and trials in the subsarcolemmal cytoskeleton network and muscular dystrophy researches in the dystrophin era

Ozawa

2010

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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“…It has been shown that ·-sarcoglycan is not tightly associated with other sarcoglycans [Yoshida et al, 1994;Yoshida et al, 1997]. Some authors have proposed a molecular model in which the sarcoglycan complex is identifiable in two subunits, one made up of ·-sarcoglycan, a type I transmembrane protein, and the other of ß-, Á-and ‰-sarcoglycans, type II transmembrane proteins, with a strong link be tween ß-and ‰-sarcoglycan [Chan et al, 1998].…”

Section: Discussionmentioning

confidence: 99%

Sarcoglycans in Human Skeletal Muscle and Human Cardiac Muscle: A Confocal Laser Scanning Microscope Study

Anastasi

Cutroneo²,

Trimarchi³

et al. 2003

Cells Tissues Organs

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Sarcoglycans are a subcomplex of transmembrane proteins which are part of the dystrophin-glycoprotein complex. They are expressed in the skeletal, cardiac and smooth muscle. Although numerous studies have been conducted on the sarcoglycan subcomplex in skeletal and cardiac muscle, the manner of the distribution and localization of these proteins along the nonjunctional sarcolemma is not clear. We therefore carried out an indirect immunofluorescence study on surgical biopsies of normal human skeletal muscle and of healthy human atrial myocardium biopsies of patients affected by valvulopathy. Our results indicate that, in skeletal muscle, sarcoglycans have a costameric distribution and all colocalize with each other. Only in a few cases did the α-sarcoglycan not colocalize with other sarcoglycans. In addition, these glycoproteins can be localized in different fibers either in the regions of the sarcolemma over band I or band A. In cardiac muscle, our results show a costameric distribution of all proteins examined and, unlike in skeletal muscle, they show a constant colocalization of all sarcoglycans with each other, along with a consistent localization of these proteins in the region of the sarcolemma over band I. In our opinion, this situation seems to confirm the hypothesis of a correlation between the region of the sarcolemma occupied by costameric proteins and the metabolic type, fast or slow, of the muscular fibers. These data, besides opening a new line of research in understanding interactions between the sarcoglycans and other transmembrane proteins, could also be extended to skeletal and cardiac muscles affected by neuromuscular and cardiovascular pathologies to understand possible structural alterations.

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“…Previous studies have demonstrated differential expression of sarcoglycans in non-muscle tissues: ␣-and ␥-sarcoglycan are expressed exclusively in skeletal and cardiac muscle (25); ␤-and ␦-sarcoglycan are selectively expressed in skeletal and cardiac muscle, but are also detectable in other tissues (21,22,34,35); and ⑀-sarcoglycan is widely expressed (19,20). We began the present study by asking how these differences arise, focusing on the three muscle lineages: skeletal, cardiac, and smooth.…”

Section: Early Embryonic Appearance Of ⑀-Sarcoglycan In All Musclementioning

confidence: 97%

“…In striated (skeletal and cardiac) muscle fibers, ␣-sarcoglycan is associated with three other sarcoglycans (␤, ␥, and ␦), forming a subcomplex within the DGC (21,22). The sarcoglycan subcomplex may strengthen the binding of dystroglycan and dystrophin to the sarcolemma, thereby stabilizing the link between the inside and the outside of the cell (23).…”

mentioning

confidence: 99%

ε-Sarcoglycan Replaces α-Sarcoglycan in Smooth Muscle to Form a Unique Dystrophin-Glycoprotein Complex

Straub

Ettinger

Durbeej

et al. 1999

Journal of Biological Chemistry

122

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The sarcoglycan complex has been well characterized in striated muscle, and defects in its components are associated with muscular dystrophy and cardiomyopathy. Here, we have characterized the smooth muscle sarcoglycan complex. By examination of embryonic muscle lineages and biochemical fractionation studies, we demonstrated that ⑀-sarcoglycan is an integral component of the smooth muscle sarcoglycan complex along with ␤-and ␦-sarcoglycan. Analysis of genetically defined animal models for muscular dystrophy supported this conclusion. The ␦-sarcoglycan-deficient cardiomyopathic hamster and mice deficient in both dystrophin and utrophin showed loss of the smooth muscle sarcoglycan complex, whereas the complex was unaffected in ␣-sarcoglycan null mice in agreement with the finding that ␣-sarcoglycan is not expressed in smooth muscle cells. In the cardiomyopathic hamster, the smooth muscle sarcoglycan complex, containing ⑀-sarcoglycan, was fully restored following intramuscular injection of recombinant ␦-sarcoglycan adenovirus. Together, these results demonstrate a tissue-dependent variation in the sarcoglycan complex and show that ⑀-sarcoglycan replaces ␣-sarcoglycan as an integral component of the smooth muscle dystrophin-glycoprotein complex. Our results also suggest a molecular basis for possible differential smooth muscle dysfunction in sarcoglycan-deficient patients.

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The fourth component of the sarcoglycan complex

Cited by 25 publications

References 20 publications

Our trails and trials in the subsarcolemmal cytoskeleton network and muscular dystrophy researches in the dystrophin era

Our trails and trials in the subsarcolemmal cytoskeleton network and muscular dystrophy researches in the dystrophin era

Sarcoglycans in Human Skeletal Muscle and Human Cardiac Muscle: A Confocal Laser Scanning Microscope Study

ε-Sarcoglycan Replaces α-Sarcoglycan in Smooth Muscle to Form a Unique Dystrophin-Glycoprotein Complex

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