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      Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis.

      Science (New York, N.Y.)

      Animals, Asparagine, Carbohydrate Conformation, Cell Line, Cell Transformation, Neoplastic, Glucosyltransferases, metabolism, Glycosylation, Lysosome-Associated Membrane Glycoproteins, Membrane Glycoproteins, Membrane Proteins, Mice, Mutation, N-Acetylglucosaminyltransferases, Neoplasm Metastasis, Neoplasms, Experimental, genetics, Oligosaccharides, biosynthesis, Structure-Activity Relationship

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          Neoplastic transformation has been associated with a variety of structural changes in cell surface carbohydrates, most notably increased sialylation and beta 1-6-linked branching of complex-type asparagine (Asn)-linked oligosaccharides (that is, -GlcNAc beta 1-6Man alpha 1-6Man beta 1-). However, little is known about the relevant glycoproteins or how these transformation-related changes in oligosaccharide biosynthesis may affect the malignant phenotype. Here it is reported that a cell surface glycoprotein, gp 130, is a major target of increased beta 1-6-linked branching and that the expression of these oligosaccharide structures is directly related to the metastatic potential of the cells. Glycosylation mutants of a metastatic tumor cell line were selected that are deficient in both beta 1-6 GlcNAc transferase V activity and metastatic potential in situ. Moreover, induction of increased beta 1-6 branching in clones of a nonmetastatic murine mammary carcinoma correlated strongly with acquisition of metastatic potential. The results indicate that increased beta 1-6-linked branching of complex-type oligosaccharides on gp 130 may be an important feature of tumor progression related to increased metastatic potential.

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