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Prepublished online as a Blood First Edition Paper on August 29, 2002; DOI 10.1182/blood-2002-06-1799. This Article Full Text (PDF) All Versions of this Article: 2002-06-1799v1 100/13/4485    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 Kobzdej, M. M Articles by McEver, R. P Search for Related Content PubMed PubMed Citation Articles by Kobzdej, M. M Articles by McEver, R. P Social Bookmarking                   What's this? Submitted June 19, 2002 Accepted July 23, 2002 Discordant expression of selectin ligands and Sialyl Lewis x-related epitopes on murine myeloid cells Marcin M Kobzdej, Anne Leppanen, Vishwanath Ramachandran, Richard D Cummings, and Rodger P McEver* Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA Department of Biochemistry and Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA; Department of Biochemistry and Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA * Corresponding author; email: rodger-mcever{at}omrf.ouhsc.edu. Murine leukocytes are thought to express 2-3-sialylated and 1-3-fucosylated selectin ligands such as sialyl Lewis x (sLex), although monoclonal antibodies (mAbs) to sLex or Lex reportedly do not bind to murine leukocytes. We observed that P- and E-selectin bound to pronase-sensitive ligands on murine monocytic WEHI-3 cells and murine neutrophils, indicating that the ligands for both selectins are glycoproteins. CSLEX-1, HECA-452, and other widely used mAbs to sLex and Lex did not bind to WEHI-3 cells and bound at very low levels to murine neutrophils. Only the anti-sLex mAbs 2H5 and KM93, which also recognize non-fucosylated glycans, bound to WEHI-3 cells. 2H5 and KM93 bound to pronase-resistant structures, indicating that the mAbs did not identify selectin ligands. Treatment of WEHI-3 cells with glycosidases or chlorate demonstrated that sialic acid modifications, 1-3-galactosylation, or sulfation did not mask epitopes for mAbs to sLex or Lex. Compared to human promyelocytic HL-60 cells, WEHI-3 cells and murine neutrophils expressed low 1-3-fucosyltransferase activities. Consistent with very low endogenous fucosylation, forced fucosylation of intact WEHI-3 cells or murine neutrophils by exogenous 1-3-fucosyltransferase FTVI and GDP-fucose created many new epitopes for anti-sLex mAbs such as HECA-452 and CSLEX-1. Nevertheless, forced fucosylation of intact cells did not significantly augment their ability to bind to fluid-phase P- or E-selectin or to roll on immobilized P- or E-selectin under flow. These data suggest that murine myeloid leukocytes fucosylate only a few specific glycans, which interact preferentially with P- and E-selectin. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Z. S Kawar, T. K Johnson, S. Natunen, J. B Lowe, and R. 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