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Volume 272, Number 41, Issue of October 10, 1997 pp. 25743-25752
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

An IgG Monoclonal Antibody against Dictyostelium discoideum Glycoproteins Specifically Recognizes Fuc1,6GlcNAc in the Core of N-Linked Glycans
LOCALIZED EXPRESSION OF CORE-FUCOSYLATED GLYCOCONJUGATES IN HUMAN TISSUES

(Received for publication, November 15, 1996, and in revised form, July 15, 1997)

Geetha Srikrishna , Nissi M. Varki ^§ , Peter C. Newell ^¶ , Ajit Varki ^§ and Hudson H. Freeze

From the  Burnham Institute, La Jolla, California 92037, the ^§ Glycobiology Program, Cancer Center, Department of Medicine, University of California, San Diego, La Jolla, California 92093, and the ^¶ Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom

Core fucosylation of N-linked oligosaccharides (GlcNAc1,4(Fuc1,6)GlcNAc1-Asn) is a common modification in animal glycans, but little is known about the distribution of core-fucosylated glycoproteins in mammalian tissues. Two monoclonal antibodies, CAB2 and CAB4, previously raised against carbohydrate epitopes of Dictyostelium discoideum glycoproteins (Crandall, I. E. and Newell, P. C. (1989) Development 107, 87-94), specifically recognize fucose residues in 1,6-linkage to the asparagine-bound GlcNAc of N-linked oligosaccharides. These IgG3 antibodies do not cross-react with glycoproteins containing -fucoses in other linkages commonly seen in N- or O-linked sugar chains. CAB4 recognizes core 1,6 fucose regardless of terminal sugars, branching pattern, sialic acid linkage, or polylactosamine substitution. This contrasts to lentil and pea lectins that recognize a similar epitope in only a subset of these structures. Additional GlcNAc residues found in the core of N-glycans from dominant Chinese hamster ovary cell mutants LEC14 and LEC18 progressively decrease binding. These antibodies show that many proteins in human tissues are core-fucosylated, but their expression is localized to skin keratinocytes, vascular and visceral smooth muscle cells, epithelia, and some extracellular matrix-like material surrounding subpopulations of lymphocytes. The availability of these antibodies now allows for an extended investigation of core fucose epitope expression in development and malignancy and in genetically manipulated mice.

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