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Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Authors
  • Bhide, Gaurang P.1
  • Colley, Karen J.1
  • 1 The University of Illinois at Chicago, 900 S. Ashland Avenue, MC669, Chicago, IL, 60607, USA , Chicago (United States)
Type
Published Article
Journal
Histochemistry and Cell Biology
Publisher
Springer Berlin Heidelberg
Publication Date
Dec 14, 2016
Volume
147
Issue
2
Pages
149–174
Identifiers
DOI: 10.1007/s00418-016-1520-x
Source
Springer Nature
Keywords
License
Yellow

Abstract

Sialylated N-glycans play essential roles in the immune system, pathogen recognition and cancer. This review approaches the sialylation of N-glycans from three perspectives. The first section focuses on the sialyltransferases that add sialic acid to N-glycans. Included in the discussion is a description of these enzymes’ glycan acceptors, conserved domain organization and sequences, molecular structure and catalytic mechanism. In addition, we discuss the protein interactions underlying the polysialylation of a select group of adhesion and signaling molecules. In the second section, the biosynthesis of sialic acid, CMP-sialic acid and sialylated N-glycans is discussed, with a special emphasis on the compartmentalization of these processes in the mammalian cell. The sequences and mechanisms maintaining the sialyltransferases and other glycosylation enzymes in the Golgi are also reviewed. In the final section, we have chosen to discuss processes in which sialylated glycans, both N- and O-linked, play a role. The first part of this section focuses on sialic acid-binding proteins including viral hemagglutinins, Siglecs and selectins. In the second half of this section, we comment on the role of sialylated N-glycans in cancer, including the roles of β1-integrin and Fas receptor N-glycan sialylation in cancer cell survival and drug resistance, and the role of these sialylated proteins and polysialic acid in cancer metastasis.

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