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J Biol Chem, Vol. 273, Issue 50, 33644-33651, December 11, 1998

Characterization of a UDP-Gal:Gal1-3GalNAc 1,4-Galactosyltransferase Activity in a Mamestra brassicae Cell Line

Michel Lopez, Maud Gazon^§, Sylvie Juliant^§, Yves Plancke, Yves Leroy, Gérard Strecker, Jean-Pierre Cartron^¶, Pascal Bailly^¶, Martine Cerutti^§, André Verbert, and Philippe Delannoy

From the  Laboratoire de Chimie Biologique, Unité Mixte de Recherche du CNRS 111, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France, ^§ Station de Pathologie Comparée INRA/Unité de Recherche Associée du CNRS 2209, route d'Alès, F-30380 Saint Christol-les-Alès, France, and ^¶ INSERM U-76, Glycoconjugués des Cellules Sanguines, Institut National de Transfusion Sanguine, 6 rue Alexandre Cabanel, F-75739 Paris, France

The binding of Bandeiraea simplicifolia lectin-I isolectin B₄ on the endogenous glycoproteins of different insect cell lines led us to characterize for the first time a UDP-Gal:Gal1-3GalNAc 1,4-galactosyltransferase in a Mamestra brassicae cell line (Mb). The study of the acceptor specificity indicated that the Mb -galactosyltransferase prefers Gal1-3-R as acceptor, and among such glycans, the relative substrate activity V_max/K_m was equal to 20 µl·mg¹·h¹ for Gall-3GlcNAc1-O-octyl and to 330 µl·mg¹·h¹ for Gal1-3GalNAc-1-O-benzyl, showing clearly that Gal1-3GalNAc disaccharide was the more suitable acceptor substrate for Mb -galactosyltransferase activity. Nuclear magnetic resonance and mass spectrometry data allowed us to establish that the Mb -galactosyltransferase synthesizes one unique product, Gal1-4Gal1-3GalNAc1-O-benzyl. The Gal1-3GalNAc disaccharide is usually present on O-glycosylation sites of numerous asialoglycoproteins and at the nonreducing end of some glycolipids. We observed that Mb 1,4-galactosyltransferase catalyzed the transfer of galactose onto both natural acceptors. Finally, we demonstrated that the trisaccharide Gal1-4Gal1-3GalNAc1-O-benzyl was able to inhibit anti-P^K monoclonal antibody-mediated hemagglutination of human blood group P^K₁ and P^K₂ erythrocytes.

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