SEARCH:   Advanced

Prepublished online as a Blood First Edition Paper on July 25, 2002; DOI 10.1182/blood-2002-04-1007. This Article Full Text (PDF) All Versions of this Article: 2002-04-1007v1 100/10/3618    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Ellies, L. G Articles by Marth, J. D Search for Related Content PubMed PubMed Citation Articles by Ellies, L. G Articles by Marth, J. D Social Bookmarking                   What's this? Submitted April 1, 2002 Accepted July 2, 2002 Sialyltransferase specificity in selectin ligand formation Lesley G Ellies, Markus Sperandio, Gregory H Underhill, James Yousif, Michael Smith, John J Priatel, Geoffrey S Kansas, Klaus Ley, and Jamey D Marth* Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, Howard Hughes Medical Institute, University of California San Diego, San Diego, CA, USA; UCSD Cancer Center, University of California, San Diego, CA, USA Cardiovascular Research Center and Department of Biomedical Engineering, University of Virginia Health Sciences Center, Charlottesville, VA, USA Department of Biomedical Engineering, Northwestern University Medical School, Chicago, IL, USA Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, Howard Hughes Medical Institute, University of California San Diego, San Diego, CA, USA Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, IL, USA * Corresponding author; email: jmarth{at}ucsd.edu. Selectin ligands are glycan structures that participate in leukocyte trafficking and inflammation. At least six ST3Gal sialyltransferases (I-VI) have been identified that may contribute to selectin ligand formation. However, it is not known which of these sialyltransferases are involved in vivo and whether they may differentially regulate selectin function. We have produced and characterized mice genetically deficient in ST3Gal-I, ST3Gal-II, ST3Gal-III, and ST3Gal-IV. Unlike mice bearing severe defects in selectin ligand formation, there was no finding of leukocytosis with these single ST3Gal deficiencies. Among neutrophils, only ST3Gal-IV was found to play a role in the synthesis of selectin ligands. In vitro rolling of marrow-derived neutrophils on E- or P-selectins presented by Chinese Hamster Ovary cells was reduced in the absence of ST3Gal-IV. However, in a TNF- induced inflammation model in vivo, no defect among P-selectin ligands was observed. Nevertheless, the number of leukocytes rolling on postcapillary venules in an E-selectin-dependent manner was decreased while E-selectin-dependent rolling velocity was increased. We propose that multiple ST3Gal sialyltransferases contribute to selectin ligand formation as none of these ST3Gal deficiencies recapitulated the degree of E- and P-selectin ligand deficit observed upon neuraminidase treatment of intact neutrophils. Our findings indicate a high degree of functional specificity among sialyltransferases and a significant role for ST3Gal-IV in selectin ligand formation. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: D. Frommhold, A. Ludwig, M. G. Bixel, A. Zarbock, I. Babushkina, M. Weissinger, S. Cauwenberghs, L. G. Ellies, J. D. Marth, A. G. Beck-Sickinger, et al. Sialyltransferase ST3Gal-IV controls CXCR2-mediated firm leukocyte arrest during inflammation J. Exp. Med., June 9, 2008; 205(6): 1435 - 1446. [Abstract] [Full Text] [PDF] M. Tenno, K. Ohtsubo, F. K. Hagen, D. Ditto, A. Zarbock, P. Schaerli, U. H. von Andrian, K. Ley, D. Le, L. A. Tabak, et al. Initiation of Protein O Glycosylation by the Polypeptide GalNAcT-1 in Vascular Biology and Humoral Immunity Mol. Cell. Biol., December 15, 2007; 27(24): 8783 - 8796. [Abstract] [Full Text] [PDF] J. D. Hernandez, J. Klein, S. J. Van Dyken, J. D. Marth, and L. G. Baum T-cell activation results in microheterogeneous changes in glycosylation of CD45 Int. Immunol., July 2, 2007; (2007) dxm053v1. [Abstract] [Full Text] [PDF] E. M. Comelli, M. Sutton-Smith, Q. Yan, M. Amado, M. Panico, T. Gilmartin, T. Whisenant, C. M. Lanigan, S. R. Head, D. Goldberg, et al. Activation of Murine CD4+ and CD8+ T Lymphocytes Leads to Dramatic Remodeling of N-Linked Glycans J. Immunol., August 15, 2006; 177(4): 2431 - 2440. [Abstract] [Full Text] [PDF] P. R. Mangan, D. O'Quinn, L. Harrington, C. S. Bonder, P. Kubes, D. F. Kucik, D. C. Bullard, and C. T. Weaver Both Th1 and Th2 Cells Require P-Selectin Glycoprotein Ligand-1 for Optimal Rolling on Inflamed Endothelium Am. J. Pathol., December 1, 2005; 167(6): 1661 - 1675. [Abstract] [Full Text] [PDF] G. H. Underhill, D. G. Zisoulis, K. P. Kolli, L. G. Ellies, J. D. Marth, and G. S. Kansas A crucial role for T-bet in selectin ligand expression in T helper 1 (Th1) cells Blood, December 1, 2005; 106(12): 3867 - 3873. [Abstract] [Full Text] [PDF] J. S. Merzaban, J. Zuccolo, S. Y. Corbel, M. J. Williams, and H. J. Ziltener An Alternate Core 2 {beta}1,6-N-Acetylglucosaminyltransferase Selectively Contributes to P-Selectin Ligand Formation in Activated CD8 T Cells J. Immunol., April 1, 2005; 174(7): 4051 - 4059. [Abstract] [Full Text] [PDF] A. Hidalgo and P. S. Frenette Enforced fucosylation of neonatal CD34+ cells generates selectin ligands that enhance the initial interactions with microvessels but not homing to bone marrow Blood, January 15, 2005; 105(2): 567 - 575. [Abstract] [Full Text] [PDF] J. H. Marino, M. Hoffman, M. Meyer, and K. S. Miller Sialyltransferase mRNA abundances in B cells are strictly controlled, correlated with cognate lectin binding, and differentially responsive to immune signaling in vitro Glycobiology, December 1, 2004; 14(12): 1265 - 1274. [Abstract] [Full Text] [PDF] M. L. Smith, T. S. Olson, and K. Ley CXCR2- and E-Selectin-induced Neutrophil Arrest during Inflammation In Vivo J. Exp. Med., October 4, 2004; 200(7): 935 - 939. [Abstract] [Full Text] [PDF] S. Mathieu, M. Prorok, A.-M. Benoliel, R. Uch, C. Langlet, P. Bongrand, R. Gerolami, and A. El-Battari Transgene Expression of {alpha}(1,2)-Fucosyltransferase-I (FUT1) in Tumor Cells Selectively Inhibits Sialyl-Lewis x Expression and Binding to E-Selectin without Affecting Synthesis of Sialyl-Lewis a or Binding to P-Selectin Am. J. Pathol., February 1, 2004; 164(2): 371 - 383. [Abstract] [Full Text] [PDF] P. Gagneux, M. Cheriyan, N. Hurtado-Ziola, E. C. M. B. van der Linden, D. Anderson, H. McClure, A. Varki, and N. M. Varki Human-specific Regulation of {alpha}2-6-linked Sialic Acids J. Biol. Chem., November 28, 2003; 278(48): 48245 - 48250. [Abstract] [Full Text] [PDF] J. R. Brown, M. M. Fuster, T. Whisenant, and J. D. Esko Expression Patterns of {alpha}2,3-Sialyltransferases and {alpha}1,3-Fucosyltransferases Determine the Mode of Sialyl Lewis X Inhibition by Disaccharide Decoys J. Biol. Chem., June 20, 2003; 278(26): 23352 - 23359. [Abstract] [Full Text] [PDF]

	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020