Cell Surface β1,4-Galactosyltransferase

A Signal Transducing Receptor?
  • Daniel H. Dubois
  • Barry D. Shur
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 376)


The carbohydrate components of membrane-bound and secreted glycoproteins are composed of a variety of simple and complex oligosaccharides that directly influence protein structure, intracellular targeting, biological activity, half-life, and/or specificity of action (1, 2). The enzymes responsible for the biosynthesis of these oligosaccharide chains are the glycosyltransferases, which demonstrate exquisite specificity by recognizing specific glycoside structures on maturing proteins and lipids. It is generally thought that each glycosyl-transferase is responsible for catalyzing one specific glycosidic linkage. From the variety of known carbohydrate linkages, it is speculated that there are more than 100 glycosyltransferases (3), only a few of which have been cloned and well characterized (4, 5).


Cytoplasmic Domain Zona Pellucida Acrosome Reaction Mouse Sperm Uterine Epithelial Cell 
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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Daniel H. Dubois
    • 1
  • Barry D. Shur
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyUniversity of Texas, M. D. Anderson Cancer CenterHoustonUSA

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