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Study ofO-sialylation of glycoproteins in C6 glioma cells treated with retinoic acid

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Abstract

When treated with retinoic acidin vivo, C6 glioma cells show an enhancement of CMP-Neu5Ac:Galβ 1–3 GalNAc-R α-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 α2,3 Neu5Ac Gal-GalNAc O-glycan moieties. Cultures in the presence of an inhibitor of O-glycan synthesis (N-acetylgalactosaminide α-O-benzyl) demonstrated that enhancement of staining of the 300 kDa glycoprotein was not due to the increase of the α2,3 sialyltransferase but to thede novo synthesis of the polypeptide chain of this glycoprotein.

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Abbreviations

RA:

retinoic acid

Neu5Ac:

N-acetylneuraminic acid

CMP-Neu5Ac:

cytidine 5′ monophosphosialate

α2,3 ST:

CMP-Neu5Ac:Galβ 1–3 GalNAc-R α-2,3 sialyltransferase

GalNAcα-O-benzyl:

N-acetylgalactosaminide α-O-benzyl

Galβ1-3GalNAcα-O-benzyl:

Galactosyl β1-3N-acetylgalactosaminide α-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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Author notes

  1. Pierre Broquet (Chargé de Recherche)

    Present address: French “Centre National de la Recherche Scientifique”, France

Authors and Affiliations

  1. Laboratoire de Biochimie Génale et Médicale, INSERM-CNRS U.189, Faculté de Médecine Lyon-Sud, B.P.12, 69921, Oullins Cedex, France

    Pascal Reboul, Pascal George, Delphine Miquel, Pierre Louisot & Pierre Broquet (Chargé de Recherche)

Authors
  1. Pascal Reboul
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  2. Pascal George
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  3. Delphine Miquel
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  4. Pierre Louisot
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  5. Pierre Broquet
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Reboul, P., George, P., Miquel, D. et al. Study ofO-sialylation of glycoproteins in C6 glioma cells treated with retinoic acid. Glycoconjugate J 13, 69–79 (1996). https://doi.org/10.1007/BF01049682

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  • DOI: https://doi.org/10.1007/BF01049682

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