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Different Distributions of Glycosphingolipids in Mouse and Rabbit Skeletal Muscle Demonstrated by Biochemical and Immunohistological Analyses

The expression of neutral glycosphingolipids and gangliosides was investigated in mouse and rabbit skeletal muscle by means of biochemical and immunochemical techniques. Neutral glycosphingolipids from muscle of the inbred rabbit strain used in this study showed a simple TLC pattern, comprising main...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1994-02, Vol.115 (2), p.248-256
Main Authors: Müthing, Johannes, Maurer, Ulrich, Šoštarié, Ksenija, Neumann, Ulrich, Brandt, Heike, Duvar, Sevim, Peter-Katalinié, Jasna, Weber-Schurholz, Sabine
Format: Article
Language:English
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Summary:The expression of neutral glycosphingolipids and gangliosides was investigated in mouse and rabbit skeletal muscle by means of biochemical and immunochemical techniques. Neutral glycosphingolipids from muscle of the inbred rabbit strain used in this study showed a simple TLC pattern, comprising mainly monohexosylceramide. In addition to this compound, lactosylceramide, lacto-N-neotetraosylceramide, globoside and Forssman GSL were detected in mouse muscle. The major ganglioside in both species was GM3; GM3(Neu5Ac) and GM3(Neu5Gc) were found in a 3: 1 ratio in mouse muscle, whereas the absence of GM3(Neu5Gc) is characteristic of rabbit muscle. As a general structural feature of all muscle GM3 gangliosides investigated, a C18 fatty acid and C18 sphingosine were the major components besides minor C22 and C24 1 fatty acids of the respective ceramide portions, as revealed by positive and negative ion FAB-MS. α2–3 sialylated lacto-N-neotetraosyl-ceramide (sialylparagloboside) was expressed in both species, whereas the α2–6 sialylated isomeric compound was found only in mouse muscle. Minute quantities of ganglio-series GM1, GD1a, GD1b, and GT1b were detected in muscles from both species. Glycosphingolipid expression could be confirmed immunohistochemically by examining transverse and longitudinal cryosections of skeletal muscle samples. The results provide the basis for the investigation of muscle specific glycosphingolipids that might modulate membrane protein functions in muscle.
ISSN:0021-924X
DOI:10.1093/oxfordjournals.jbchem.a124326