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This Article Full Text Full Text (PDF) 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 Citing Articles via Google Scholar Google Scholar Articles by Gallart, T. Articles by Barceló, J. Search for Related Content PubMed PubMed Citation Articles by Gallart, T. Articles by Barceló, J. Related Collections Immunobiology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Anti-Sia-lb (Anti-Gd) Cold Agglutinins Bind the Domain NeuNAc2-3Gal in Sialyl Lewisx, Sialyl Lewisa, and Related Carbohydrates on Nucleated Cells and in Soluble Cancer-Associated Mucins Teresa Gallart, Dieter Roelcke, Maite Blay, Arturo Pereira, Antonio Martínez, Oriol Massó, Odette Viñas, Mariona Cid, Jordi Esparza, Rafael Molina, and Juanjo Barceló From the Services of Immunology, Hemotherapy and Hemostasis, Internal Medicine, Clinical Biochemistry, Hospital Clínic Universitari, Barcelona, Spain; the Merck Bioresearch Laboratory, Merck Farma y Química S.A., Barcelona, Spain; and the Institute for Immunology, Heildelberg Universität, Heilderberg, Germany. Anti-Sia-lb (formerly anti-Gd) cold agglutinins (CAs) recognize sialylated carbohydrates on both adult and neonate red blood cells (RBCs). RBC CA activity inhibition experiments reported here indicate that the domain NeuNAc2-3Gal, as found in sialyllactose, synthetic sialyl(s) Lewis(Le)x and sLea, sialyllactosamine, sialyl-fucosyllactose, and nonfucosylated sLea, constitutes the minimal epitope for these CAs, implicating that these autoantibodies could be able to bind this domain in sLex and sLea and related carbohydrates expressed on nucleated cells and in soluble cancer-related mucins. The following data obtained with the previously characterized monoclonal IgMk anti-Sia-lb CA, GAS, show that this is the case. GAS epitope expression among leukocytes that lack sLea parallels that of sLex determinant as detected by mouse monoclonal antibodies (MoAbs), especially MoAb KM-93. It is also found on epithelial malignant cells bearing both sLex and sLea. GAS epitope on these nucleated cells, (1) like that present on RBC, is abolished by sialidase, unaffected by proteases, and inhibited by sialyllactose; and (2) is overlapping and/or proximal to that recognized by anti-sLex MoAb, CSLEX-1, and KM-93. Moreover, CAGAS binds soluble cancer-associated mucins bearing sLex and sLea determinants. This binding is inhibited by sialyllactose and these mucins inhibit the RBC CA activity of CAGAS. The possible significance of anti-Sia-lb (anti-Gd) CAs as autoantibodies directed to carbohydrate ligands of host adhesion molecules that might be receptors of microbial adhesins of some CA-inducing pathogens is discussed. Blood, Vol. 90 No. 4 (August 15), 1997: pp. 1576-1587 © 1997 by The American Society of Hematology. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. L. Alpaugh, J. S. Tomlinson, Y. Ye, and S. H. Barsky Relationship of Sialyl-Lewisx/a Underexpression and E-Cadherin Overexpression in the Lymphovascular Embolus of Inflammatory Breast Carcinoma Am. J. Pathol., August 1, 2002; 161(2): 619 - 628. [Abstract] [Full Text] [PDF]

	Copyright © 1997 by American Society of Hematology         Online ISSN: 1528-0020