Expression of sialyltransferase activity on intact human neutrophils.
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.
Rifat
Salahaldin
S
Department of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Kang
Tae Jin
TJ
Mann
Dean
D
Zhang
Lei
L
Puche
Adam C
AC
Stamatos
Nicholas M
NM
Goldblum
Simeon E
SE
Brossmer
Reinhard
R
Cross
Alan S
AS
D002465:Cell Movement / Q000187:drug effects; D004912:Erythrocytes / Q000201:enzymology; D005786:Gene Expression Regulation; D006801:Humans; D016209:Interleukin-8 / Q000494:pharmacology; D018613:Microscopy, Confocal; D009439:Neuraminidase; D009504:Neutrophils / Q000201:enzymology* / Q000648:ultrastructure; D012799:Sialyltransferases / Q000037:antagonists & inhibitors / Q000097:blood / Q000235:genetics*; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D016209:Interleukin-8; D012799:Sialyltransferases; D009439:Neuraminidase; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase