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Cell Surface β1,4-Galactosyltransferase

A Signal Transducing Receptor?

  • Chapter
Glycoimmunology

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 376))

Abstract

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).

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Texas, M. D. Anderson Cancer Center, Box 117, 1515 Holcombe Blvd, Houston, Texas, 77030, USA

    Daniel H. Dubois & Barry D. Shur

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  1. Daniel H. Dubois
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  1. St. George’s Hospital Medical School, University of London, London, England

    Azita Alavi  & John S. Axford  & 

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Dubois, D.H., Shur, B.D. (1995). Cell Surface β1,4-Galactosyltransferase. In: Alavi, A., Axford, J.S. (eds) Glycoimmunology. Advances in Experimental Medicine and Biology, vol 376. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1885-3_9

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  • DOI: https://doi.org/10.1007/978-1-4615-1885-3_9

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