Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
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 ISI Web of Science
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 arrow Search for citing articles in:
ISI Web of Science (13)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Loveless, R. W.
Right arrow Articles by Feizi, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Loveless, R. W.
Right arrow Articles by Feizi, T.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, Vol 8, 1237-1242, Copyright © 1998 by Society for Glycobiology


ORIGINAL ARTICLES

Monoclonal antibody 91.9H raised against sulfated mucins is specific for the 3'-sulfated Lewisa tetrasaccharide sequence

RW Loveless, CT Yuen, H Tsuiji, T Irimura and T Feizi
The Glycosciences Laboratory, Imperial College School of Medicine, Northwick Park Hospital, Harrow, Middlesex, HA1 3UJ, United Kingdom.

The IgG1hybridoma antibody, 91.9H, was originally raised against sulfated mucins isolated from normal human colonic mucosa. Previous studies have shown that the 91.9H antigen is expressed on normal colonic epithelial cells and the sulfomucins that they produce, but not in the normal small intestine and stomach. Tissue-specific changes occur in 91.9H antigen expression in disease: the antigen diminishes in colonic carcinomas, whereas in regions of gastric mucosa showing intestinal metaplasia and in gastric carcinomas, the antigen is expressed as a "neo-antigen." This report is concerned with elucidation, by the neoglycolipid technology, of the determinant recognized by antibody 91.9H using sulfated and sialyl oligosaccharides of Lewisa(Lea) and Lextypes, and analogs that lack sulfate, sialic acid, or fucose. Binding experiments with the lipid-linked oligosaccharides immobilized on chromatograms or on microwells, and inhibition of binding experiments with free oligosaccharides based on di-, tri- and tetrasaccharide backbones, show that the 91.9H antigenic determinant is based on a trisaccharide backbone, and consists of the 3'-sulfated Leatetrasaccharide sequence, which is a potent ligand for the E- and L-selectins. The antibody gives a relatively low signal with the 3'-sulfated non-fucosylated backbone, and has no detectable cross- reaction with the 3'-sulfated Lexisomer, nor with sialyl-Leaand - Lexanalogues. Antibody 91.9H is a valuable addition, therefore, to the repertoire of reagents for mapping details of the distribution, and determining the relative importance of sulfated and sialyl oligosaccharides as ligands for the selectins, in normal and pathological epithelia and endothelia.
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. Clin. Pathol.Home page
K Bodger, F Campbell, and J M Rhodes
Detection of sulfated glycoproteins in intestinal metaplasia: a comparison of traditional mucin staining with immunohistochemistry for the sulfo-Lewisa carbohydrate epitope
J. Clin. Pathol., September 1, 2003; 56(9): 703 - 708.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
N. Ikeda, H. Eguchi, S. Nishihara, H. Narimatsu, R. Kannagi, T. Irimura, M. Ohta, H. Matsuda, N. Taniguchi, and K. Honke
A Remodeling System of the 3'-Sulfo-Lewis a and 3'-Sulfo-Lewis x Epitopes
J. Biol. Chem., October 12, 2001; 276(42): 38588 - 38594.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
A. Seko, J.-i. Sumiya, S. Yonezawa, K. Nagata, and K. Yamashita
Biochemical differences between two types of N-acetylglucosamine:->6sulfotransferases in human colonic adenocarcinomas and the adjacent normal mucosa: specific expression of a GlcNAc:->6sulfotransferase in mucinous adenocarcinoma
Glycobiology, September 1, 2000; 10(9): 919 - 929.
[Abstract] [Full Text] [PDF]


Home page
JEMHome page
C. Leteux, W. Chai, R. W. Loveless, C.-T. Yuen, L. Uhlin-Hansen, Y. Combarnous, M. Jankovic, S. C. Maric, Z. Misulovin, M. C. Nussenzweig, et al.
The Cysteine-Rich Domain of the Macrophage Mannose Receptor Is a Multispecific Lectin That Recognizes Chondroitin Sulfates a and B and Sulfated Oligosaccharides of Blood Group Lewisa and Lewisx Types in Addition to the Sulfated N-Glycans of Lutropin
J. Exp. Med., April 3, 2000; 191(7): 1117 - 1126.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Seko, S. Hara-Kuge, and K. Yamashita
Molecular Cloning and Characterization of a Novel Human Galactose 3-O-Sulfotransferase That Transfers Sulfate to Galbeta 1right-arrow3GalNAc Residue in O-Glycans
J. Biol. Chem., July 6, 2001; 276(28): 25697 - 25704.
[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.