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Glycobiology Advance Access published online on July 28, 2004
Glycobiology, doi:10.1093/glycob/cwh133
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Received April 7, 2004
Revised July 6, 2004
Accepted July 26, 2004

ORIGINAL ARTICLES

Sialyltransferase mRNA abundances in B cells are strictly controlled, correlated with cognate lectin binding, and differentially responsive to immune signaling in vitro

Julie H. Marino 1, Matt Hoffman 1, Megan Meyer 1, Kenton S. Miller 1*

1 Faculty of Biological Science and The Mervin Bovaird Center for Studies in Molecular Biology and Biotechnology, The University of Tulsa, Tulsa, OK 74104, USA

* To whom correspondence should be addressed. E-mail: Kenton-Miller{at}utulsa.edu.


  Abstract

Mouse gene knockout studies have provided unimpeachable evidence of immune-relevantn functions for several sialyltransferase enzymes including ST6Gal I, ST3Gal I and ST3Gal IV. Such studies cannot, however, identify cellular mechanisms for regulating such activities. In this study we provide evidence that murine B lymphocytes respond to specific immune signals in vitro with tightly regulated changes in the sialic acid composition of the cell surface glycocalyx. These changes are both quantitative and qualitative in nature, and are apparently regulated at both the transcriptional and post-transcriptional levels. We have used lectin binding and flow cytometry combined with relative real-time PCR to show that MAH and PNA binding are tightly correlated with the abundance of ST3Gal IV and ST3Gal I mRNA, respectively, under several different conditions of B cell stimulation. Finally, we show that while SNA binding and the expression of ST6Gal I coding sequence are not tightly correlated, there is a clear differential control of 5'UTR exon usage in response to different immune signals.

Keywords: B lymphocyte; lectin; sialyltransferase; Q-RT PCR; glycocalyx.
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