J. Biochem, 1994, Vol. 115, No. 2 248-256
© 1994 Japanese Biochemical Society
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Different Distributions of Glycosphingolipids in Mouse and Rabbit Skeletal Muscle Demonstrated by Biochemical and Immunohistological Analyses1
o
tarié**
*Institute for Cell Culture Technology, University of Bielefeld Germany
**Department of Chemistry and Biochemistry, School of Medicine, University of Zagreb Croatia
***Clinic for Poultry of the Hannover School of Veterinary Medicine Hannover, Germany
****Institute for Physiological Chemistry, University of Bonn Germany
*****Institute for Developmental Biology, University of Bielefeld Germany
To whom correspondence should be addresed at: Universiät Bielefeld, Technische Fakultät, Arbeitagruppe Zellkulmrtechnik, Posifach 100131, 33501 Bielefeld, Germany
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. 
2–3 sialylated lacto-N-neotetraosyl-ceramide (sialylparagloboside) was expressed in both species, whereas the 2–6 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.
1This work was financed by the Deutsche Forschungsgemeinschaft SFB 223 "Pathomechamsms of Cellular Interactions," Project C 06
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