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Published on: May 4, 2012
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Human plasma protein N-glycosylation
Florent Clerc1, Karli R Reiding1, Bas C Jansen1
1Center for Proteomics and Metabolomics, Leiden University Medical Center, P.O. Box 9600, 2300 RC, Leiden, The Netherlands.
Glycoconjugate Journal
|November 12, 2015
Summary
Protein glycosylation impacts biological processes and biopharmaceutical quality. This review details N-glycosylation of major plasma glycoproteins, crucial for disease biomarkers and drug development.
Area of Science:
- Biochemistry
- Glycobiology
- Proteomics
Background:
- Glycosylation is a complex protein modification influencing structure, function, and biological roles.
- It is a critical quality attribute for biopharmaceuticals and a target for disease biomarker discovery.
- Plasma glycoproteins are key targets for understanding glycosylation's role in health and disease.
Purpose of the Study:
- To review the current knowledge on N-glycosylation of major human plasma glycoproteins.
- To provide site-specific glycosylation data where available.
- To discuss the contribution of individual protein glycosylation to the overall plasma N-glycome.
Main Methods:
- Literature review of scientific publications.
- Analysis of existing data on plasma glycoprotein glycosylation.
- Site-specific mapping of N-glycosylation sites.
Main Results:
- Comprehensive overview of N-glycosylation for 24 major and minor plasma glycoproteins.
- Detailed site-specific glycosylation information presented for several proteins.
- Discussion on the collective impact of individual protein glycosylation on the plasma N-glycome.
Conclusions:
- Understanding plasma glycoprotein N-glycosylation is vital for biopharmaceutical development and disease diagnostics.
- Site-specific glycosylation analysis provides deeper insights into protein function and biomarker potential.
- The collective plasma N-glycome profile offers a holistic view of biological states.
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