Glycobiology Advance Access originally published online on March 24, 2004
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Glycobiology vol 14 no 6 pp. 481-494, 2004
Glycobiology vol. 14 no. 6 © Oxford University Press 2004; all rights reserved.
Mobilization of neutrophil sialidase activity desialylates the pulmonary vascular endothelial surface and increases resting neutrophil adhesion to and migration across the endothelium
3 Department of Medicine, Division of Infectious Diseases, University of Maryland School of Medicine Baltimore, MD 21201; 4 Immunology and Disease Resistance Laboratory, USDA-Agricultural Research Service, Beltsville, MD 20705; 5 Program in Oncology Greenebaum Cancer Center, University of Maryland School of Medicine Baltimore, MD 21201; and 6 Department of Veterans Affairs Medical Center, Mucosal Biology Research Center, 10 North Greene Street, University of Maryland School of Medicine Baltimore, MD 21201
Received on January 5, 2003; revised on February 18, 2004; accepted on February 19, 2004
The amount of sialic acid on the surface of the neutrophil (PMN) influences its ability to interact with other cells. PMN activation with various stimuli mobilizes intracellular sialidase to the plasma membrane, where it cleaves sialic acid from cell surfaces. Because enhanced PMN adherence, spreading, deformability, and motility each are associated with surface desialylation and are critical to PMN diapedesis, we studied the role of sialic acid on PMN adhesion to and migration across pulmonary vascular endothelial cell (EC) monolayers in vitro. Neuraminidase treatment of either PMN or EC increased adhesion and migration in a dose-dependent manner. Neuraminidase treatment of both PMNs and ECs increased PMN adhesion to EC more than treatment of either PMNs or ECs alone. Moreover, neuraminidase treatment of ECs did not change surface expression of adhesion molecules or release of IL-8 and IL-6. Inhibition of endogenous sialidase by either cross-protective antineuraminidase antibodies (45.5% inhibition) or competitive inhibition with pseudo-substrate (41.2% inhibition) decreased PMN adhesion to ECs; the inhibitable sialidase activity appeared to be associated with activated PMNs. Finally, EC monolayers preincubated with activated PMNs became hyperadhesive for subsequently added resting PMNs, and this hyperadhesive state was mediated through endogenous PMN sialidase activity. Blocking anti-E-selectin, anti-CD54 and anti-CD18 antibodies decreased PMN adhesion to tumor necrosis factor–activated ECs but not to PMN-treated ECs. These data implicate desialylation as a novel mechanism through which PMN-EC adhesion can be regulated independent of de novo protein synthesis or altered adhesion molecule expression. The ability of activated PMNs, through endogenous sialidase activity, to render the EC surface hyperadherent for unstimulated PMNs may provide for rapid amplification of the PMN-mediated host response.
1 Present address: Department of Medicine, Division of Microbiology and Infectious Diseases, Adnan Menderes University School of Medicine, Aydin, Turkey
2 To whom correspondence should be addressed; e-mail: simeon.goldblum{at}med.va.gov
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