Glycosphingolipids of skeletal muscle: I. Subcellular distribution of neutral glycosphingolipids and gangliosides in rabbit skeletal muscle

Carbohydrate Research

Volumn 307, Issue 1-2, 1998, Pages 135-145

  Müthing, Johannes ^a   Maurer, Ulrich ^a   Neumann, Ulrich ^b   Kniep, Bernhard ^c   Weber Schürholz, Sabine ^a  

^a BIELEFELD UNIVERSITY   (Germany)

^b Clin for Poultry of the Hannover S   (Germany)

^c DRESDEN UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

Antibodies; Immunohistochemistry; Membrane fractions; Subcellular localization; TLC immunostaining

Indexed keywords

GANGLIOSIDE; GLYCOSPHINGOLIPID;

ANIMAL TISSUE; ARTICLE; CARBOHYDRATE ANALYSIS; CELLULAR DISTRIBUTION; CONTROLLED STUDY; IMMUNOHISTOCHEMISTRY; LIPID COMPOSITION; MITOCHONDRIAL MEMBRANE; NONHUMAN; PRIORITY JOURNAL; RABBIT; SARCOLEMMA; SARCOPLASMIC RETICULUM; SKELETAL MUSCLE; THIN LAYER CHROMATOGRAPHY; TRANSVERSE TUBULAR SYSTEM;

ANIMALS; ANTIGENS, CD; CARBOHYDRATE CONFORMATION; CARBOHYDRATE SEQUENCE; CELL FRACTIONATION; CHROMATOGRAPHY, THIN LAYER; G(M1) GANGLIOSIDE; GANGLIOSIDES; GLUCOSYLCERAMIDES; GLYCOSPHINGOLIPIDS; INTRACELLULAR MEMBRANES; LACTOSYLCERAMIDES; MICROTUBULES; MITOCHONDRIA, MUSCLE; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; RABBITS; SARCOLEMMA; SARCOPLASMIC RETICULUM;

EID: 0032004159     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6215(98)00027-5     Document Type: Article

References (81)

1. [1] G. Reuter and R. Schauer, Glycoconjugate J., 5 (1988) 133-135.
2. [2] IUPAC-IUB Commission on Biochemical Nomenclature, Eur. J. Biochem., 79 (1977) 11-21.
3. [3] L. Svennerholm, J. Neurochem., 10 (1963) 613-623.
4. [4] R.K. Yu and M. Saito, Structures and Localization of Gangliosides, in R.U. Margolis and R.K. Margolis (Eds.), Neurobiology of Glycoconjugates, Plenum Press, New York, 1989, pp 1-42.
5. [5] R.W. Ledeen, Biosynthesis, Metabolism and Biological Effects of Gangliosides, in R.U. Margolis and R.K. Margolis (Eds.), Neurobiology of Gycoconjugates, Plenum Press, New York, 1989, pp 43-83.
6. [6] S.-I. Hakomori, J. Biol. Chem., 265 (1990) 18713-18716.
7. [7] G. Schwarzmann and K. Sandhoff, Biochemistry, 29 (1990) 10865-10871.
8. [8] R.L. Schnaar, Glycobiology, 1 (1991) 477-485.
9. [9] C.B. Zeller and R.B. Marchase, Am. J. Physiol., 262 (1992) C1341-C1355.
10. [10] G. van Echten and K. Sandhoff, J. Biol. Chem., 268 (1993) 5341-5344.
11. [11] A. Varki, Glycobiology, 2 (1992) 25-40.
12. [12] R. Schauer, S. Kelm, G. Reuter, P. Roggentin, and L. Shaw, Biochemistry and Role of Sialic Acids, in A. Rosenberg (Ed.), Biology of the Sialic Acids, Plenum Press, New York, 1995, pp 7-67.
13. [13] T.E. Thompson and T.W. Tillack, Ann. Rev. Biophys. Biophys. Chem., 14 (1985) 361-386.
14. [14] B.K. Gillard, L.T. Thurmon, and D.M. Marcus, Glycobiology, 3 (1993) 57-67.
15. [15] F.W. Symington, W.A. Murray, S.I. Bearman, and S.-I. Hakomori, J. Biol. Chem., 262 (1987) 11356-11363.
16. [16] H.R. Katz and K.F. Austen, J. Immunol., 136 (1986) 3819-3824.
17. [17] I.L. van Genderen, G. van Meer, J.W. Slot, H.J Geuze, and W.F. Voorhout, J. Cell Biol., 115 (1991) 1009-1019.
18. [18] M. Sekine, T. Ariga, T. Miyatake, Y. Kuroda, A. Suzuki, and T. Yamakawa, J. Biochem., 95 (1984) 155-160.
19. [19] G.R. Matyas and D.J. Morré, Biochim. Biophys. Acta, 921 (1987) 599-614.
20. [20] K.H. Chou, C.E. Nolan, and F.B. Jungalwala, J. Neurochem., 44 (1985) 1898-1912.
21. [21] P. Palestini, M. Masserini, A. Fiorilli, E. Calappi, and G. Tettamanti, J. Neurochem., 61 (1993) 955-960.
22. [22] R.W. Ledeen, M.-F. Diebler, G. Wu, Z.-H. Lu, and H. Varoqui, Neurochem. Res., 18 (1993) 1151-1155.
23. [23] V. Chigorno, M. Valsecchi, D. Acquotti, S. Sonnino, and G. Tettamanti, FEBS Lett., 263 (1990) 329-331.
24. [24] K.-F.J. Chan and Y. Liu, Glycobiology, 1 (1991) 193-203.
25. [25] B.K. Gillard, J.P. Heath, L.T. Thurmon, and D.M. Marcus, Exp. Cell. Res., 192 (1991) 433-444.
26. [26] B.K. Gillard, L.T. Thurmon, and D.M. Marcus, Cell Motil. Cytoskel, 21 (1992) 255-271.
27. [27] J. Müthing, U. Maurer, and S. Weber-Schürholz, Carbohydr. Res., 307 (1998) 147-157.
28. [28] K. Nakamura, M. Nagashima, M. Sekine, M. Igarashi, T. Ariga, T. Atsumi, T. Miyatake, A. Suzuki, and T. Yamakawa, Biochim. Biophys. Acta, 752 (1983) 291-300.
29. [29] T. Ariga, M. Sekine, K. Nakamura, M. Igarashi, M. Nagashima, T. Miyatake, A. Suzuki, and T. Yamakawa, J. Biochem., 93 (1983) 889-893.
30. [30] L. Svennerholm, Å. Bruce, J.E. Månsson, B.-M. Rynmark, and M.-T. Vanier, Biochim. Biophys. Acta, 280 (1972) 626-636.
31. [31] Y.-T. Li, J.-E. Månsson, M.-T. Vanier, and L. Svennerholm, J. Biol. Chem., 248 (1973) 2634-2636.
32. [32] K.C. Leskawa, P.E. Buse, E.L. Hogan, and A.J. Garvin, Neurochem. Pathol., 2 (1994) 19-29.
33. [33] M. Cacić, J. Müthing, I. Kracun, U. Neumann, and S. Weber-Schürholz, Glycoconjugate J., 11 (1994) 477-485.
34. [34] J. Müthing and M. Cacić, Glycoconjugate J., 14 (1997) 19-28.
35. [35] F.E. Lassaga, I. Albarracin de Lassaga, and R. Caputto, J. Lipid Res., 13 (1972) 810-815.
36. [36] M. Iwamori and Y. Nagai, J. Biochem., 84 (1978) 1609-1615.
37. [37] M. Iwamori and Y. Nagai, Biochim. Biophys. Acta, 665 (1981) 214-220.
38. [38] K. Nakamura, T. Ariga, T. Yahagi, T. Miyatake, A. Suzuki, and T. Yamakawa, J. Biochem., 94 (1983) 1359-1365.
39. [39] J. Müthing, U. Maurer, K. Sostarić, U. Neumann, H. Brandt, S. Duvar, J. Peter-Katalinić, and S. Weber-Schürholz, J. Biochem., 115 (1994) 248-256.
40. [40] L.H. Wang, Y.P. Tu, X.Y. Yang, Z.C. Tsui, and F.Y. Yang, FEBS Lett., 388 (1996) 128-130.
41. [41] S. Weber-Schürholz, E. Wischmeyer, M. Laurien, H. Jockusch, T. Schürholz, D.W. Landry, and Q. Al-Awqati, J. Biol. Chem., 268 (1993) 547-551.
42. [42] J. Müthing, J. Chromatogr. A, 720 (1996) 3-25.
43. [43] T. Imagawa, A.T. Leung, and K.P. Campbell, J. Biol. Chem., 62 (1987) 8333-8339.
44. [44] V. Flockerzi, H.-J. Oeken, F. Hofmann, D. Pelzer, A. Cavalié, and W. Trautwein, Nature, 323 (1986) 66-68.
45. [45] J. Müthing and U. Neumann, Biomed. Chromatogr., 7 (1993) 158-161.
46. [46] J. Müthing, F. Unland, D. Heitmann, M. Orlich, F.-G. Hanisch, J. Peter-Katalinić, V. Knäuper, H. Tschesche, S. Kelm, R. Schauer, and J. Lehmann, Glycoconjugate J., 10 (1993) 120-126.
47. [47] M.N. Fukuda, A. Dell, J.E. Oates, P. Wu, J.C. Klock, and M. Fukuda, J. Biol. Chem., 260 (1985) 1067-1082.
48. [48] G. Wu and R. Ledeen, Anal. Biochem., 173 (1988) 368-375.
49. [49] K. Sandhoff and T. Kolter, Trends Cell. Biol., 6 (1996) 98-103.
50. [50] A.H. Futerman, Ceramide Metabolism - Compartmentalized in the Endoplasmic Reticulum and Golgi Apparatus, in D. Hoekstra (Ed.), Current Topics in Membranes, Vol. 40, Academic Press, San Diego, CA, 1994, pp 93-110.
51. [51] E.G. Mandon, I. Ehses, J. Rother, G. van Echten, and K. Sandhoff, J. Biol. Chem., 267 (1992) 11144-11148.
52. [52] K. Hirschberg, J. Rodger, and A.H. Futerman, Biochem. J., 290 (1993) 751-757.
53. [53] D. Jeckel, A. Karrenbauer, K.N.J. Burger, G. van Meer, and F. Wieland, J. Cell Biol., 7 (1992) 259-267.
54. [54] M. Trinchera, M. Fabbri, and R. Ghidoni, J. Biol. Chem., 266 (1991) 20907-20912.
55. [55] H. Lannert, C. Bünning, D. Jeckel, and F. Wieland, FEBS Lett., 342 (1994) 91-96.
56. [56] K.N.J. Burger, P. van der Bijl, and G. van Meer, J. Cell Biol., 133 (1996) 15-28.
57. [57] K.C. Leskawa, R.E. Erwin, P.E. Buse, and E.L. Hogan, Mol. Cell. Biochem., 83 (1988) 47-54.
58. [58] K.C. Leskawa and E.L. Hogan, Mol. Cell. Biochem., 96 (1990) 163-173.
59. [59] F.C. Clark and P.B. Smith, Biochim. Biophys. Acta, 755 (1983) 56-64.
60. [60] H. Kadowaki, L.A. Symanski, K.E. Rys-Sikora, and R.S. Koff, J. LipidRes., 30 (1989) 1789-1797.
61. [61] L.J. Melkerson-Watson and C.C. Sweeley, J. Biol. Chem., 266 (1991) 4448-4457.
62. [62] H. Kadowaki and M.A. Grant, J. Biol. Chem., 269 (1994) 14931-14938.
63. [63] H. Kadowaki and M.A. Grant, J. Lipid Res., 36 (1995) 1274-1282.
64. [64] G. Pohlentz, D. Klein, G. Schwarzmann, D. Schmitz, and K. Sandhoff, Proc. Natl. Acad. Sci. USA, 85 (1988) 7044-7048.
65. [65] H. Iber, C. Zacharias, and K. Sandhoff, Glycobiology, 2 (1992) 137-142.
66. [66] J.-L. Chien and E.L. Hogan, Biochim. Biophys. Acta, 620 (1980) 454-461.
67. [67] S. Dasgupta, J.-L. Chien, and E.L. Hogan, Biochim. Biophys. Acta, 1036 (1990) 11-17.
68. [68] R.D. Mitchell, P. Palade, and S. Fleischer, J. Cell Biol., 96 (1983) 1008-1016.
69. [69] P.K. Smith, R.I. Krohn, G.T. Hermanson, A.K. Mallia, F.H. Gartner, M.D. Provenzano, E.K. Fujimoto, N.M. Goeke, B.J. Olson, and D.C. Klenk, Anal. Biochem., 150 (1985) 76-85.
70. [70] C.C. Allain, L.S. Poon, C.S.G. Chan, W. Richmond, and P.C. Fu, Clin. Chem., 20 (1974) 470-475.
71. [71] S. Kara, Y. Takemori, M. Yamaguchi, M. Nakamura, and Y. Ohkura, Anal. Biochem., 164 (1987) 138-145.
72. [72] R.W. Ledeen and R.K. Yu, Methods Enzymol., 83 (1982) 139-191.
73. [73] K. Ueno, S. Ando, and R.K. Yu, J. Lipid Res., 19 (1978) 863-871.
74. [74] T. Saito and S.-I. Hakomori, J. Lipid Res., 12 (1971) 257-259.
75. [75] V.P. Skipsky, Methods Enzymol, 35 (1975) 396-425.
76. [76] L. Svennerholm, Biochim. Biophys. Acta, 24 (1957) 604-611.
77. [77] J.L. Magnani, B. Nilsson, M. Brockhaus, D. Zopf, Z. Steplewski, H. Koprowski, and V. Ginsburg, J. Biol. Chem., 257 (1982) 14365-14369.
78. [78] J. Müthing and P.F. Mühlradt, Anal. Biochem., 173 (1988) 10-17.
79. [79] J. Müthing, TLC in Structure and Recognition Studies of Glycosphingolipids, in E.F. Hounsell (Ed.), Glycoanalysis Protocols, Humana Press, Totowa, NJ, in press.
80. [80] J.L. Magnani, D.F. Smith, and V. Ginsburg, Anal. Biochem., 109 (1980) 399-402.
81. [81] A. Pörtner, J. Peter-Katalinić, H. Brade, F. Unland, H. Büntemeyer, and J. Müthing, Biochemistry, 32 (1993) 12685-12693.