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Glycobiology Advance Access published online on December 17, 2002
Glycobiology, doi:10.1093/glycob/cwg030
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Submitted on July 9, 2002
Revised on November 12, 2002
Accepted on November 12, 2002

© 2002 Oxford University Press

ORIGINAL ARTICLES

Characterization of the rat {alpha}(1,3)Galactosyltransferase:- evidence for two independent genes encoding glycosyltransferases which synthesize Gal{alpha}(1,3)Gal by two separate glycosylation pathways

Simon G Taylor 1, Ian F C McKenzie 1, Mauro S Sandrin 1*

1 John Connell Laboratory for Glycobiology, The Austin Research Institute, Austin and Repatriation Medical Centre, HEIDELBERG, VIC, 3084, Australia

* To whom correspondence should be addressed. E-mail: m.sandrin{at}ari.unimelb.edu.au.

Abstract

The important xenoepitope Gal{alpha}(1,3)Gal was thought to be exclusively synthesized by a single {alpha}(1,3)galactosyltransferase. However, the cloning of the distance family member, rat iGb3 synthase which is also capable of synthesizing Gal{alpha}(1,3)Gal, as the glycolipid structure iGb3, challenges the notion that {alpha}(1,3)galactosyltransferase is the sole Gal{alpha}(1,3)Gal synthesizing enzyme. Here we describe the cloning of the rat homolog of {alpha}(1,3)galactosyltransferase showing that indeed the rat expresses two distinct {alpha}(1,3)galactosyltransferases, {alpha}(1,3)GT and iGb3 synthase. Rat {alpha}(1,3)galactosyltransferase shows a high amino acid sequence identity with the {alpha}(1,3)galactosyltransferase of mouse (90%), pig (76%) and ox (75%), in contrast to the low amino acid sequence identity (42%) with iGb3 synthase. The rat {alpha}(1,3)galactosyltransferase is expressed in heart, brain spleen, kidney and liver, and has a similar intron/exon structure to the mouse {alpha}(1,3)galactosyltransferase. Transfection studies show that in contrast to the iGb3 synthase, rat {alpha}(1,3)galactosyltransferase can synthesize Gal{alpha}(1,3)Gal on glycoproteins but cannot synthesize the glycolipid iGb3, defining two separate glycosylation pathways for the synthesis of Gal{alpha}(1,3)Gal. Furthermore iGb3 synthase was found to be distinct with its capability of synthesizing poly-{alpha}-Gal glycolipid structures.


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