UDP-GlcNAc 2-Epimerase: A Regulator of Cell Surface Sialylation

Author:

Keppler Oliver T.1,Hinderlich Stephan2,Langner Josmar1,Schwartz-Albiez Reinhard3,Reutter Werner2,Pawlita Michael1

Affiliation:

1. Applied Tumor Virology Program,

2. Institut für Molekularbiologie und Biochemie, Freie Universität Berlin, Arnimallee 22, D-14195 Berlin-Dahlem, Germany.

3. Tumor Immunology Program, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference81 articles.

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3. Foxall C., et al., J. Cell Biol. 117, 895 (1992).

4. Erbe D. V., et al., ibid. 120, 1227 (1993);

5. Pilatte Y., Bignon J., Lambre C. R., Glycobiology 3, 201 (1993);

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