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Glycobiology Advance Access published online on August 3, 2005
Glycobiology, doi:10.1093/glycob/cwj024
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org
Received May 30, 2005
Revised July 8, 2005
Accepted July 22, 2005

Article

Differential Expression and Enzymatic Properties of GalNAc-4-Sulfotransferase-1 and GalNAc-4-Sulfotransferase-2 GLYCO-2005-00086

Rajeev K. Boregowda 1, YiLing Mi 1, Hongyin Bu 1, and Jacques U. Baenziger 1*

1 Department of Pathology Washington University School of Medicine St. Louis, MO 63110

* To whom correspondence should be addressed.
Jacques U. Baenziger, E-mail: Baenziger{at}pathology.wustl.edu


  Abstract

We have cloned two GalNAc-4-sulfotransferases, GalNAc-4-ST1 and GalNAc-4-ST2, that transfer sulfate to terminal {beta}1,4-linked GalNAc. In conjunction with the action of protein-specific {beta}1,4GalNAc-transferases, GalNAc-4-ST1 and GallNAc-4-ST2 account for the presence of terminal {beta}1,4-linked GalNAc-4-SO4 on glycoproteins such as lutropin, thyrotropin, proopiomelanocortin, carbonic anhydratase VI, and tenascin-R. GalNAc-4-ST1 and GalNAc-4-ST2 can be distinguished by their differing specificity for oligosaccharide acceptors and temperature lability. The differences in properties have been used to show that the levels of GalNAc-4-ST1 and GalNAc-4-ST2 activity are proportionate to the levels of their respective transcripts. Furthermore, we have found that both transcript and activity levels of GalNAc-4-ST1 and GalNAc-4-ST2 vary widely among different tissues indicating that the regulation of their expression differs. Differences in specificity and the regulation of expression may account for existence of two GalNAc-4-sulfotransferases in vivo. The highest levels of both GalNAc-4-ST1 and GalNAc-4-ST2 transcripts are present in the pituitary of the mouse with multiple cell types that produce glycoproteins terminating with GalNAc-4-SO4. Genetic ablation of both GalNAc-4-ST1 and GalNAc-4-ST2 may be necessary to alter the pattern and/or extent of sulfate addition to terminal {beta}1,4GalNAc in tissues such as pituitary.


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D. Fiete, Y. Mi, E. L. Oats, M. C. Beranek, and J. U. Baenziger
N-Linked Oligosaccharides on the Low Density Lipoprotein Receptor Homolog SorLA/LR11 Are Modified with Terminal GalNAc-4-SO4 in Kidney and Brain
J. Biol. Chem., January 19, 2007; 282(3): 1873 - 1881.
[Abstract] [Full Text] [PDF]


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