Study ofO-sialylation of glycoproteins in C6 glioma cells treated with retinoic acid |
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Authors: | Pascal Reboul Pascal George Delphine Miquel Pierre Louisot Pierre Broquet |
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Affiliation: | (1) Laboratoire de Biochimie Génale et Médicale, INSERM-CNRS U.189, Faculté de Médecine Lyon-Sud, B.P.12, 69921 Oullins Cedex, France;(2) Present address: French Centre National de la Recherche Scientifique, France |
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Abstract: | When treated with retinoic acidin vivo, C6 glioma cells show an enhancement of CMP-Neu5Ac:Gal 1–3 GalNAc-R -2,3 sialyltransferase activity. A 300kDa glycoprotein was detected by lectin affinoblotting in retinoic acid-treated C6 cells which stained weakly or not at all in control cells. Comparative studies with different lectins demonstrated that this glycoprotein contains 2,3 Neu5Ac Gal-GalNAc O-glycan moieties. Cultures in the presence of an inhibitor of O-glycan synthesis (N-acetylgalactosaminide -O-benzyl) demonstrated that enhancement of staining of the 300 kDa glycoprotein was not due to the increase of the 2,3 sialyltransferase but to thede novo synthesis of the polypeptide chain of this glycoprotein.Abbreviations RA retinoic acid - Neu5Ac N-acetylneuraminic acid - CMP-Neu5Ac cytidine 5 monophosphosialate - 2,3 ST CMP-Neu5Ac:Gal 1–3 GalNAc-R -2,3 sialyltransferase - GalNAc-O-benzyl N-acetylgalactosaminide -O-benzyl - Gal1-3GalNAc-O-benzyl Galactosyl 1-3N-acetylgalactosaminide -O-benzyl - TBS Tris-HCl buffer 50mm pH 7.5 containing NaCl 0.15m and Tween 20 0.05% - B1 buffer TBS containing MgCl2 1mm, MnCl2 1mm and CaCl2 1mm |
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Keywords: | retinoic acid C6 glioma cells lectin-affinoblotting /content/k30851r2t5374t88/xxlarge945.gif" alt=" agr" align=" BASELINE" BORDER=" 0" >2,3 sialyltransferase |
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