Abstract
Modification of cell surface molecules with sialic acid is crucial for their function in many biological processes, including cell adhesion and signal transduction. Uridine diphosphate-N-acetylglucosamine 2-epimerase (UDP-GlcNAc 2-epimerase) is an enzyme that catalyzes an early, rate-limiting step in the sialic acid biosynthetic pathway. UDP-GlcNAc 2-epimerase was found to be a major determinant of cell surface sialylation in human hematopoietic cell lines and a critical regulator of the function of specific cell surface adhesion molecules.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antigens, CD / metabolism
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Antigens, Differentiation, B-Lymphocyte / metabolism
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Carbohydrate Epimerases / genetics
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Carbohydrate Epimerases / metabolism
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Cell Adhesion Molecules / metabolism
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Cell Membrane / metabolism*
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Culture Media
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Escherichia coli Proteins*
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Glycoconjugates / metabolism*
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HL-60 Cells
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Histocompatibility Antigens Class I / biosynthesis
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Humans
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Lectins / metabolism
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Lewis X Antigen / biosynthesis
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Lipopolysaccharide Receptors / biosynthesis
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Oligosaccharides / biosynthesis
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Rats
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Sialic Acid Binding Ig-like Lectin 2
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Sialic Acids / biosynthesis*
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Sialyl Lewis X Antigen
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Transcription, Genetic
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Transfection
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Tumor Cells, Cultured
Substances
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Antigens, CD
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Antigens, Differentiation, B-Lymphocyte
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CD22 protein, human
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Cell Adhesion Molecules
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Culture Media
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Escherichia coli Proteins
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Glycoconjugates
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Histocompatibility Antigens Class I
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Lectins
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Lewis X Antigen
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Lipopolysaccharide Receptors
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Oligosaccharides
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Sialic Acid Binding Ig-like Lectin 2
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Sialic Acids
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Sialyl Lewis X Antigen
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Carbohydrate Epimerases
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UDP acetylglucosamine-2-epimerase
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wecB protein, E coli