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Study of O-glycan sialylation in C6 cultured glioma cells: Evidence for post-translational regulation of Aβ-galactoside α2,3 sialyltransferase activity by N-glycosylation

Abstract : We have studied the Gal beta 1-3GalNAc-R alpha 2,3 sialyltransferase from C6 glioma cells transferring Neu5Ac from CMP-Neu5Ac onto O-glycans of glycoproteins. Using synchronized C6 glioma cells, we showed that the alpha 2,3 sialyltransferase activity was inhibited by tunicamycin to a greater extend than DNA and protein biosynthesis suggesting inhibition of N-glycosylation of this enzyme. Additional demonstration of N-glycosylation of the alpha 2,3 sialytransferase was provided through ConA-Sepharose binding. Treatment of partially purified alpha 2,3 sialytransferase by peptide-N-glycosidase F showed a significative inhibition demonstrating that N-glycan moiety is required for complete activity of the C6 glioma cell alpha 2,3 sialyltransferase.
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https://hal.univ-lorraine.fr/hal-01705236
Contributor : Pascal Reboul <>
Submitted on : Friday, February 9, 2018 - 11:15:44 AM
Last modification on : Monday, February 12, 2018 - 5:23:17 PM

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Pierre Broquet, Pascal George, Jocelyne Geoffroy, Pascal Reboul, Pierre Louisot. Study of O-glycan sialylation in C6 cultured glioma cells: Evidence for post-translational regulation of Aβ-galactoside α2,3 sialyltransferase activity by N-glycosylation. Biochemical and Biophysical Research Communications, Elsevier, 1991, 178 (3), pp.1437 - 1443. ⟨10.1016/0006-291X(91)91054-G⟩. ⟨hal-01705236⟩

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