Skip Navigation



Glycobiology Advance Access published online on March 24, 2004
Glycobiology, doi:10.1093/glycob/cwh065
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
14/6/481    most recent
cwh065v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Sakarya, S.
Right arrow Articles by Goldblum, S. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sakarya, S.
Right arrow Articles by Goldblum, S. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Submitted on January 5, 2003
Revised on February 18, 2004
Accepted on February 19, 2004

© 2004 Glycobiology © Oxford University Press 2004; all rights reserved.

ORIGINAL ARTICLES

Mobilization of neutrophil sialidase activity desialylates the pulmonary vascular endothelial surface and increases resting neutrophil adhesion to and migration across the endothelium

Serhan Sakarya 1, Salahaldin Rifat 1, Jie Zhou 1, Douglas D. Bannerman 2, Nicholas M. Stamatos 1, Alan S. Cross 3, and Simeon E. Goldblum 4*

1 Department of Medicine, Division of Infectious Diseases, University of Maryland School of Medicine, Baltimore, MD 21201
2 Immunology and Disease Resistance Laboratory, USDA-Agricultural Research Service, Beltsville, MD 20705
3 Department of Medicine, Division of Infectious Diseases, University of Maryland School of Medicine, Baltimore, MD 21201; Program in Oncology, Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201
4 Department of Medicine, Division of Infectious Diseases, University of Maryland School of Medicine, Baltimore, MD 21201; Department of Veterans Affairs Medical Center, Mucosal Biology Research Center, University of Maryland School of Medicine, Baltimore, MD 21201

* To whom correspondence should be addressed. E-mail: simeon.goldblum{at}med.va.gov.

Abstract

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. Since 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 PMN and EC increased PMN adhesion to EC greater than treatment of either PMN or EC alone. Moreover, neuraminidase treatment of EC did not change surface expression of adhesion molecules or release of IL-8 and IL-6. Inhibition of endogenous sialidase by either cross-protective anti-neuraminidase antibodies (45.5% inhibition) or competitive inhibition with pseudosubstrate (41.2% inhibition) decreased PMN adhesion to EC; the inhibitable sialidase activity appeared to be associated with activated PMN. 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 TNF-activated EC but not to PMN-treated EC. These data implicate desialylation as a novel mechanism through which PMN-EC adhesion can be regulated independent of de novoprotein 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.


adhesion molecules, endothelial cells, neuraminidase, neutrophils, sialidase
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Leukoc. Biol.Home page
S. Rifat, T. J. Kang, D. Mann, L. Zhang, A. C. Puche, N. M. Stamatos, S. E. Goldblum, R. Brossmer, and A. S. Cross
Expression of sialyltransferase activity on intact human neutrophils
J. Leukoc. Biol., October 1, 2008; 84(4): 1075 - 1081.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
B. K. Sohanpal, S. El-Labany, M. Lahooti, J. A. Plumbridge, and I. C. Blomfield
Integrated regulatory responses of fimB to N-acetylneuraminic (sialic) acid and GlcNAc in Escherichia coli K-12
PNAS, November 16, 2004; 101(46): 16322 - 16327.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.