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O-Linked Chain Glycosyltransferases

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Book cover Glycoprotein Methods and Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 125))

Abstract

The complex O-linked oligosaccharide chains (O-glycans) attached to the polypeptide backbone of mucins are assembled by glycosyltransferases. These enzymes act in the Golgi apparatus in a controlled sequence that is determined by their substrate specificities, their localization in Golgi compartments, and their relative catalytic activities (1). Activities are controlled by many factors, including the membrane environment, metal ions, concentrations of donor and acceptor substrates, cofactors, and, in some cases, posttranslational modifications of enzymes. Cloning of glycosyltransferases has revealed the existence of families of homologous glycosyltransferases with similar actions but encoded by different genes. Thus, many steps in the pathways of O-glycosylation appear to be catalyzed by several related glycosyltransferases that may show slight differences in properties and substrate specificities. The relative expression levels of these enzymes is cell typespecific and appears to be regulated during the growth and differentiation of cells and, during tissue development, and is altered in many disease states (2,3).

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Authors and Affiliations

  1. Division of Rheumatology, Department of Medicine, Queen’s University, Kingston, Ontario, Canada

    Inka Brockhausen

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  1. Inka Brockhausen
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Editors and Affiliations

  1. Bristol Royal Infirmary, Bristol, UK

    Anthony P. Corfield

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Brockhausen, I. (2000). O-Linked Chain Glycosyltransferases. In: Corfield, A.P. (eds) Glycoprotein Methods and Protocols. Methods in Molecular Biology™, vol 125. Humana Press. https://doi.org/10.1385/1-59259-048-9:273

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  • DOI: https://doi.org/10.1385/1-59259-048-9:273

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-720-5

  • Online ISBN: 978-1-59259-048-3

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