NDLI: Human plasma protein N-glycosylation

Content Provider	Springer Nature Link
Author	Clerc, Florent Reiding, Karli R. Jansen, Bas C. Kammeijer, Guinevere S. M. Bondt, Albert Wuhrer, Manfred
Copyright Year	2016
Abstract	Glycosylation is the most abundant and complex protein modification, and can have a profound structural and functional effect on the conjugate. The oligosaccharide fraction is recognized to be involved in multiple biological processes, and to affect proteins physical properties, and has consequentially been labeled a critical quality attribute of biopharmaceuticals. Additionally, due to recent advances in analytical methods and analysis software, glycosylation is targeted in the search for disease biomarkers for early diagnosis and patient stratification. Biofluids such as saliva, serum or plasma are of great use in this regard, as they are easily accessible and can provide relevant glycosylation information. Thus, as the assessment of protein glycosylation is becoming a major element in clinical and biopharmaceutical research, this review aims to convey the current state of knowledge on the N-glycosylation of the major plasma glycoproteins alpha-1-acid glycoprotein, alpha-1-antitrypsin, alpha-1B-glycoprotein, alpha-2-HS-glycoprotein, alpha-2-macroglobulin, antithrombin-III, apolipoprotein B-100, apolipoprotein D, apolipoprotein F, beta-2-glycoprotein 1, ceruloplasmin, fibrinogen, immunoglobulin (Ig) A, IgG, IgM, haptoglobin, hemopexin, histidine-rich glycoprotein, kininogen-1, serotransferrin, vitronectin, and zinc-alpha-2-glycoprotein. In addition, the less abundant immunoglobulins D and E are included because of their major relevance in immunology and biopharmaceutical research. Where available, the glycosylation is described in a site-specific manner. In the discussion, we put the glycosylation of individual proteins into perspective and speculate how the individual proteins may contribute to a total plasma N-glycosylation profile determined at the released glycan level.
Starting Page	309
Ending Page	343
Page Count	35
File Format	PDF
ISSN	02820080
Journal	Glycoconjugate Journal
Volume Number	33
Issue Number	3
e-ISSN	15734986
Language	English
Publisher	Springer US
Publisher Date	2015-11-10
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	N-glycosylation Plasma Serum Glycoproteins Glycoproteomics Immunoglobulins Biochemistry Pathology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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