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Blood, 16 July 2009, Vol. 114, No. 3, pp. 733-741. Prepublished online as a Blood First Edition Paper on April 9, 2009; DOI 10.1182/blood-2009-03-210237. This Article Full Text Full Text (PDF) Supplemental Methods and Figure All Versions of this Article: blood-2009-03-210237v1 114/3/733    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Google Scholar Articles by Mir, G. H. Articles by Leppänen, A. PubMed PubMed Citation Articles by Mir, G. H. Articles by Leppänen, A. Related Collections Vascular Biology Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  VASCULAR BIOLOGY Glycoforms of human endothelial CD34 that bind L-selectin carry sulfated sialyl Lewis x capped O- and N-glycans Gerard Hernandez Mir1, Jari Helin2, Kari-Pekka Skarp1, Richard D. Cummings3, Antti Mäkitie4, Risto Renkonen5, and Anne Leppänen1 1 Department of Biological and Environmental Sciences, Division of Biochemistry, University of Helsinki, Helsinki, Finland; 2 Glykos Finland, Helsinki, Finland; 3 Department of Biochemistry, Emory University School of Medicine, Atlanta, GA; 4 Department of Otolaryngology–Head and Neck Surgery, Helsinki University Central Hospital, Helsinki, Finland; and 5 Transplantation Laboratory & Infection Biology Research Program, Haartman Institute, University of Helsinki, Helsinki, Finland Endothelial sialomucin CD34 functions as an L-selectin ligand mediating lymphocyte extravasation only when properly glycosylated to express a sulfated carbohydrate epitope, 6-sulfo sialyl Lewis x (6-sulfo SLex). It is thought that multivalent 6-sulfo SLex expression promotes high-affinity binding to L-selectin by enhancing avidity. However, the reported low amount of 6-sulfo SLex in total human CD34 is inconsistent with this model and prompted us to re-evaluate CD34 glycosylation. We separated CD34 into 2 glycoforms, the L-selectin–binding and nonbinding glycoforms, L-B-CD34 and L-NB-CD34, respectively, and analyzed released O- and N-glycans from both forms. L-B-CD34 is relatively minor compared with L-NB-CD34 and represented less than 10% of total tonsillar CD34. MECA-79, a mAb to sulfated core-1 O-glycans, bound exclusively to L-B-CD34 and this form contained all sulfated and fucosylated O-glycans. 6-Sulfo SLex epitopes occur on core-2 and extended core-1 O-glycans with approximately 20% of total L-B-CD34 O-glycans expressing 6-sulfo SLex. N-glycans containing potential 6-sulfo SLex epitopes were also present in L-B-CD34, but their removal did not abolish binding to L-selectin. Thus, a minor glycoform of CD34 carries relatively abundant 6-sulfo SLex epitopes on O-glycans that are important for its recognition by L-selectin. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: "Home sweet home" for lymphocytes Steven D. Rosen and Hanayo Arata-Kawai Blood 2009 114: 499-500. [Full Text] [PDF] This article has been cited by other articles: S. D. Rosen and H. Arata-Kawai "Home sweet home" for lymphocytes Blood, July 16, 2009; 114(3): 499 - 500. [Full Text] [PDF]

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