Mouse beta 1,3-galactosyltransferase (GA1/GM1/GD1b synthase): protein characterization, tissue expression, and...

The composition of cell surface gangliosides is largely dependent on the relative activities of Golgi resident glycosyltransferases. In the brain of birds and mammals, complex gangliosides (GM2, GM1, GD1a, GD1b, GT1b) abound at late stages of development and in the adult, due to the relatively high activities of the UDP-GalNAc:LacCer/GM3/GD3 beta 1,4-N-acetylgalactosaminyltransferase (GalNAc-T) and the UDP-Gal: GA2/GM2/GD2 beta 1, 3-galactosyltransferase (Gal-T2) relative to that of CMP-NeuAc:GM3 alpha 2,8-sialyltransferase (Sial-T2). Unlike brain, the mature mammalian neural retina abundantly expresses the simple ganglioside GD3, in relation to complex gangliosides, due to the low activity of GalNAc-T and Gal-T2 relative to Sial-T2. Here we describe the isolation and characterization of a mouse Gal-T2 cDNA that drives the synthesis of an epitope-tagged protein of molecular mass 43 kDa, which was enzymatically active and localized to the Golgi complex in transfected cell lines. Using this cDNA as a probe, it was found that Gal-T2 is coded by a single gene located in chromosome 17, and that the coding sequence is contained in a single exon. The expression of the specific Gal-T2 mRNA (approximately 1.8 kb) was highest in testis, which also showed elevated Gal-T2 activity. In the postnatal neural retina, Gal-T2 mRNA increased after day 3, maintained high levels of expression by days 4-7, and then decreased to initial values by day 10. The developmental pattern of mRNA expression was temporally coincident with that of Gal-T2 activity expression, indicating that this enzyme is under transcriptional control in the neural retina.