ISSN:
1432-0533
Keywords:
Key words Ultrastructural localization
;
α-
;
β-
;
γ-Sarcoglycan
;
Dystrophin
;
β-Dystroglycan
;
Skeletal myofiber
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Abstract Ultrastructural localization of α-, β- and γ-sarcoglycan and their mutual relation, and their relation to dystrophin, β-dystroglycan and β-spectrin were investigated in normal skeletal myofibers. Single-immunogold labeling electron microscopy showed that the signals of rabbit and sheep polyclonal antibodies against the synthetic peptide of the cytoplasmic domain of α-, β or γ-sarcoglycan were present along the inside surface of muscle plasma membrane and at the sarcoplasmic side of plasma membrane invaginations and vesicular structures in subsarcolemmal areas. These localizations were similar to that of dystrophin, β-dystroglycan and β-spectrin. Double-immunogold labeling disclosed the close association of α-, β- and γ-sarcoglycan each other and α-, β-, γ-sarcoglycan with dystrophin or β-dystroglycan, and this was confirmed by statistical analysis. Monoclonal antibody against the extracellular domain of α-sarcoglycan was used with above-mentioned polyclonal anti-β- and -γ-sarcoglycan antibodies for triple-immunogold labeling, in which signals of α-sarcoglycan localized at the outer surface of muscle plasmalemma and those of β- and γ-sarcoglycans were present at the inside surface of plasma membrane. The triple immunolabeling showed an occasional closely associated presence of the three signals for α-, β- and γ-sarcoglycans, and a more frequent association for two signals out of α-, β- and γ-sarcoglycans. This study demonstrated that α-, β- and γ-sarcoglycan are closely located to one another and to dystrophin and β-dystroglycan at the muscle plasma membrane.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s004010050987
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