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Eukaryotic protein glycosylation: a primer for histochemists and cell biologists.

Authors
  • Corfield, Anthony1
  • 1 Mucin Research Group, School of Clinical Sciences, Bristol Royal Infirmary, University of Bristol, Bristol, BS2 8HW, UK. [email protected]
Type
Published Article
Journal
Histochemistry and cell biology
Publication Date
Feb 01, 2017
Volume
147
Issue
2
Pages
119–147
Identifiers
DOI: 10.1007/s00418-016-1526-4
PMID: 28012131
Source
Medline
Keywords
License
Unknown

Abstract

Proteins undergo co- and posttranslational modifications, and their glycosylation is the most frequent and structurally variegated type. Histochemically, the detection of glycan presence has first been performed by stains. The availability of carbohydrate-specific tools (lectins, monoclonal antibodies) has revolutionized glycophenotyping, allowing monitoring of distinct structures. The different types of protein glycosylation in Eukaryotes are described. Following this educational survey, examples where known biological function is related to the glycan structures carried by proteins are given. In particular, mucins and their glycosylation patterns are considered as instructive proof-of-principle case. The tissue and cellular location of glycoprotein biosynthesis and metabolism is reviewed, with attention to new findings in goblet cells. Finally, protein glycosylation in disease is documented, with selected examples, where aberrant glycan expression impacts on normal function to let disease pathology become manifest. The histological applications adopted in these studies are emphasized throughout the text.

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