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Originally published online as doi:10.1189/jlb.0706462 on July 29, 2008

Published online before print July 29, 2008
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(Journal of Leukocyte Biology. 2008;84:1075-1081.)
© 2008 by Society for Leukocyte Biology

Expression of sialyltransferase activity on intact human neutrophils

Salahaldin Rifat*, Tae Jin Kang*, Dean Mann{dagger}, Lei Zhang*, Adam C. Puche{ddagger}, Nicholas M. Stamatos§, Simeon E. Goldblum*, Reinhard Brossmer|| and Alan S. Cross*,1

* Departments of Medicine,
{dagger} Pathology,
{ddagger} Anatomy and Neurobiology, and
§ Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA; and
|| Biochemistry Center of Heidelberg, University of Heidelberg, Heidelberg, Germany

1 Correspondence: Center for Vaccine Development, University of Maryland School of Medicine, 685 W. Baltimore Street, HSF I 480, Baltimore, MD 21201, USA. E-mail: across{at}medicine.umaryland.edu

Endogenous polymorphonuclear leukocyte (PMN)-associated sialidase activity enhances PMN adhesion to and migration across the endothelium through the removal of sialylated cell-surface residues. We tested the hypothesis that PMNs also express sialyltransferase (ST) activity that restores sialyl residues to the PMN surface. We developed a highly sensitive fluorometric assay to demonstrate that intact human PMNs can mediate and accept sialyl residue transfer. This ST activity is inhibited by a ST inhibitor, CMP, which also inhibits the transendothelial migration of PMNs in response to IL-8 in vitro and in vivo. We conclude that intact PMNs express sialidase and ST activities that permit rapid modulation of their surface sialylation and their ability to adhere to and migrate across the endothelium.

Key Words: sialic acid cell trafficking • inflammation