Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle.

Klietsch, Rhea; Ervasti, James M.; Arnold, W.; Campbell, Kevin P.; Jorgensen, A O

doi:10.1161/01.res.72.2.349

Cited by 117 publications

(83 citation statements)

References 50 publications

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“…Klietsch et al (1993) reported that dystrophin and its binding protein complex are localized to T-tubules in cardiac but not in skeletal muscles. We also confirmed the localization of dystrophin and found that caveolin-3 is present on the T-tubules of adult cardiac muscles.…”

Section: Discussionmentioning

confidence: 99%

Immunolocalization of Caveolin-1 and Caveolin-3 in Monkey Skeletal, Cardiac and Uterine Smooth Muscles.

Hagiwara

Nishina

Yorifuji

et al. 2002

Cell Struct. Funct.

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ABSTRACT. Caveolin, a 20-24 kDa integral membrane protein, is a principal component of caveolar domains. Caveolin-1 is expressed predominantly in endothelial cells, fibroblasts, and adipocytes, while the expression of caveolin-3 is confined to muscle cells. However, their localization in various muscles has not been well documented. Using double-immunofluorescence labeling and confocal laser microscopy, we examined the localization of caveolins-1 and 3 in adult monkey skeletal, cardiac and uterine smooth muscles and the co-immunolocalization of these caveolins with dystrophin, which is a product of the Duchenne muscular dystrophy gene. In the skeletal muscle tissue, caveolin-3 was localized along the sarcolemma except for the transverse tubules, and coimmunolocalized with dystrophin, whereas caveolin-1 was absent except in the blood vessels of the muscle tissue. In cardiac muscle cells, caveolins-1 and -3 and dystrophin were co-immunolocalized on the sarcolemma and transverse tubules. In uterine smooth muscle cells, caveolin-1, but not caveolin-3, was co-immunolocalized with dystrophin on the sarcolemma.

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Section: Discussionmentioning

confidence: 99%

Immunolocalization of Caveolin-1 and Caveolin-3 in Monkey Skeletal, Cardiac and Uterine Smooth Muscles.

Hagiwara

Nishina

Yorifuji

et al. 2002

Cell Struct. Funct.

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“…Similar Dp427 isoforms exist in both skeletal and cardiac muscle, although with a slightly different subcellular localization. In skeletal muscle, Dp427-M and its associated surface proteins are restricted to the sarcolemma (23,25) while, in cardiac fibres, Dp427-C is also found in the transverse-tubular region of the surface mermbrane (26,27). The gigantic 2.4-Mb dystrophin gene with a coding sequence of 79 exons was shown to correspond to a full-length 14-kb mRNA message.…”

Section: The Dystrophin-glycoprotein Complexmentioning

confidence: 95%

The pathobiochemical role of the dystrophin-dystroglycan complex and the Ca2+-handling apparatus in diabetes-related muscle weakness (Review)

Mulvey

Mullen²,

Ohlendieck³

2008

Mol Med Report

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Abstract. Serious diabetic complications affect millions of patients worldwide. Skeletal muscle represents the largest insulin-regulated glucose sink in the body, making insulin resistance and abnormal glucose disposal in muscle fibres a critical aspect of diabetes mellitus. Advances in the biomedical analysis of the molecular mechanisms underlying diabetic complications rely heavily on the study of suitable disease models. The Goto-Kakizaki (GK) rat is an established animal model of non-obese type 2 diabetes. This review discusses the recent finding that expression of the dystrophin-dystroglycan complex is drastically altered in diabetic GK skeletal muscle fibres. In normal muscle, the dystrophin-glycoprotein complex provides a stabilizing connection between the actin membrane cytoskeleton and the extracellular matrix component laminin. A reduction in dystrophin-associated proteins may be associated with a weakening of the fibre periphery, abnormal sarcolemmal signaling and/or a decreased cytoprotective mechanism in diabetic skeletal muscle. Stimulation by insulin might be altered due to impaired linkage between the dystrophin-anchored actin cytoskeleton and the intracellular pool of essential glucose transporters. The diminished recruitment of GLUT4 transporter molecules to the sarcolemma may be a key step in the development of insulin resistance in diabetic skeletal muscles. Thus, analogous to certain forms of muscular dystrophy, altered dystrophin levels may have pathological effects in type 2 diabetes. In contrast, the dystrophin-glycoprotein complex does not appear to be altered in diabetic cardiac muscle. However, reduced expression of the sarcoplasmic reticulum Ca 2+ -ATPase isoform SERCA2 is characteristic of cardiac abnormalities in type 2 diabetes. Reduced Ca 2+ removal from the sarcoplasm may be associated with impaired relaxation kinetics, and could therefore play a pathophysiological role in diabetic cardiomyopathy. Here, the potential impact of these molecular alterations in diabetic muscle tissues is discussed and critically examined with respect to the future design of alternative treatment strategies to counteract diabetes-associated muscle weakness.

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“…In particular, about dystrophin, some Authors showed that it is not uniquely distributed at costameres and is continuously and uniformly distributed at the cytoplasmic surface of the peripheral plasma membrane [6], while Kaprielian et al [7] have documented that dystrophin partially colocalizes with costameric vinculin in myocytes and it is absent from ICDs. Therefore, dystrophin also localizes at the Ttubules in cardiac muscle in contrast to its known absence in skeletal muscle T-tubules [8]. Our previous study carried out only on atrial myocytes, demonstrated that the DGC and talin-vinculin-integrin complexes had a costameric distribution and both complexes are present at the level of T tubules and ICDs [9].…”

Section: Introductionmentioning

confidence: 99%

Distribution of costameric proteins in normal human ventricular and atrial cardiac muscle.

Mauro

Gaeta²,

Arco³

et al. 2010

Folia Histochem Cytobiol.

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Abstract:In the mature heart, the intercalated disc and costameres provide the cell-cell and cell-matrix junctions respectively. Intercalated disc is situated at the bipolar ends of the cardiomyocytes and the myofibrils are anchored at this structure. The costameres mediate integration with the extracellular matrix that covers individual cardiomyocytes laterally. Costameres are considered as "proteic machinery" that appears to comprise two protein complexes: the dystrophin-glycoprotein complex (DGC) and the vinculin-talin-integrin system. There are structural differences between atrial and ventricular myocytes, but there have been relatively few studies that have analyzed costameres and focal adhesion function in cardiac cells. Our previous study carried out only on atrial myocytes, demonstrated that the DGC and talin-vinculin-integrin complexes had a costameric distribution that, unlike skeletal muscle, it localized only on the I band. We performed a further immunohistochemical analysis extending also the evaluation to the normal human cardiac muscle fibers obtained from ventricle and interventricular septum, in order to define the distribution and the spatial relationship between the proteins of the two complexes also in the other heart districts. Immunoconfocal microscopy of cardiac tissue revealed the costameric distribution of DGC and of vinculin-talin-integrin system, the association of all tested proteins in intercalated disks, in disagreement with other Authors, and in T-tubule with irregular spokelike extensions penetrating toward the center of the cell. Moreover, our data showed that all tested proteins colocalize between each other.

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Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle.

Cited by 117 publications

References 50 publications

Immunolocalization of Caveolin-1 and Caveolin-3 in Monkey Skeletal, Cardiac and Uterine Smooth Muscles.

Immunolocalization of Caveolin-1 and Caveolin-3 in Monkey Skeletal, Cardiac and Uterine Smooth Muscles.

The pathobiochemical role of the dystrophin-dystroglycan complex and the Ca2+-handling apparatus in diabetes-related muscle weakness (Review)

Distribution of costameric proteins in normal human ventricular and atrial cardiac muscle.

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