N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.

Zacchi, Lucia F. and Schulz, Benjamin L. (2015) N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.. Glycoconjugate Journal, 1-18. doi:10.1007/s10719-015-9641-3

Author Zacchi, Lucia F.
Schulz, Benjamin L.
Title N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.
Journal name Glycoconjugate Journal   Check publisher's open access policy
ISSN 1573-4986
Publication date 2015-12-05
Year available 2015
Sub-type Article (original research)
DOI 10.1007/s10719-015-9641-3
Open Access Status Not yet assessed
Start page 1
End page 18
Total pages 18
Place of publication New York, United States
Publisher Springer
Collection year 2016
Language eng
Abstract Glycosylation is a co- and post-translational modification that is critical for the regulation of the biophysical properties and biological activities of diverse proteins. Biosynthetic pathways for protein glycosylation are inherently inefficient, resulting in high structural diversity in mature glycoproteins. Macroheterogeneity is the structural diversity due to the presence or absence of glycans at specific glycosylation sites, and is caused by inefficiency in the initial transfer of glycans to proteins. Here, we review the enzymatic and evolutionary mechanisms controlling macroheterogeneity, its biological consequences in physiological and disease states, its relevance to heterologous production and glycoengineering of glycoproteins, and mass spectrometry based methods for its analysis. We highlight the importance of the analysis of macroheterogeneity for a complete understanding of glycoprotein biosynthesis and function, and emphasize how advances in mass spectrometry glycoproteomics will enable analysis of this critical facet of glycoprotein structural diversity.
Keyword Glycosylation
Mass spectrometry
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 11 Dec 2015, 10:10:14 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences