Abstract
The addition of oligosaccharides to proteins is a significant posttranslational modification that modulates protein structure, function and localization. Glycans are vital for development in all eukaryotes and are profoundly connected to a large number of human diseases, ranging from glycan genetic diseases to autoimmune disorders and cancer. Glycans present a difficult challenge in the analytical field because of the intricate dynamics of their synthesis as well as the complexity of the structures themselves. In addition to the role of glycans in development and disease, they are of great interest in the biotherapeutic industry where modification of glycosylation can significantly enhance therapeutic efficacy and biological activity in a range of glycoprotein products. However, glycosylation on a global scale in humans is yet to be fully appreciated as researchers are discovering that glycosylation is not only protein, cell or tissue specific, but is additionally influenced by individual genetics and environmental factors. Functional glycomics and glycoproteomics are emerging as a central field in systems biology and will continue to be a key focus in discerning health and disease.
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Abbreviations
- ADCC:
-
antibody-dependent cell mediated cytotoxicity
- AFP:
-
α-fetoprotein
- AGP:
-
α1-acid glycoprotein
- CCD:
-
cross reactive carbohydrate determinant
- CDG:
-
congenital disorders of glycosylation
- CE:
-
capillary electrophoresis
- CEA:
-
carcinoembryonic antigen
- CHO:
-
Chinese hamster ovary
- CID:
-
collision induced dissociation
- DMB:
-
1,2-diamino-4,5-methylene-dioxybenzene
- EAATs:
-
excitatory amino acid transporters
- EGFR:
-
epidermal growth factor receptor
- EPO:
-
erythropoietin
- ER:
-
endoplasmic reticulum
- ERT:
-
enzyme replacement therapy
- ESI:
-
electrospray ionization
- FcγR:
-
Fc-gamma receptor
- FDA:
-
Food and Drug Administration
- Fuc:
-
fucose
- FucT:
-
α(1,6)-fucosyltransferse
- Fuc-TIII:
-
α(1,3/4)-fucosyltransferase
- Gal:
-
galactose
- GalNAc:
-
N-acetylgalactosamine
- Gal-T:
-
β(1,4)galactosyltransferase
- Glc:
-
glucose
- GlcNAc:
-
N-acetylglucosamine
- GnT-I:
-
N-acetylglucosaminyltransferase-I
- GnT-III:
-
N-acetylglucosaminyltransferase-III
- GnT-V:
-
N-acetylglucosaminyltransferase-V
- GU:
-
glucose unit
- GWAS:
-
genome-wide association study
- HA:
-
hemagglutinin
- HCC:
-
hepatocellular carcinomas
- β-HCG:
-
β-human chorionic gonadotrophin
- HILIC:
-
Hydrophilic interaction chromatography
- HPLC:
-
high performance liquid chromatography
- IgG:
-
immunoglobulin G
- LacNAc:
-
N-acetyllactosamine
- Lex :
-
Lewisx
- LLO:
-
lipid-linked oligosaccharide
- LSD:
-
lysosomal storage disease
- MALDI:
-
matrix assisted laser desorption ioziation
- Man:
-
mannose
- MBL:
-
mannose-binding lectin
- MS:
-
mass spectrometry
- MSn :
-
sequential mass spectrometry
- Neu5Gc:
-
N-glycolylneuraminic acid
- Neu5Nac:
-
N-acetylneuraminic acid
- NK:
-
natural killer
- NMR:
-
nuclear magnetic resonance
- OST:
-
oligosacchryltransferase
- PGC:
-
porous graphitized carbon
- PNGase F:
-
peptide-N-glycosidase F
- PSA:
-
prostate specific antigen
- RA:
-
rheumatoid arthritis
- RNase 1:
-
ribonuclease 1
- RP-HPLC:
-
reverse phase-HPLC
- SLE:
-
systemic lupus erythematosus
- sLea :
-
sialyl Lewisa
- sLey :
-
sialyl Lewisy
- ST3GalIV:
-
β-galactoside α(2,3)-sialyltransferase
- ST8Sia II:
-
α(2,8)-sialyltransferase II
- ST8Sia IV:
-
α(2,8)-sialyltransferase IV
- TGFβR:
-
transforming growth factor-β receptor
- TOF:
-
time of flight
- WAX:
-
weak anion exchange
- Xyl:
-
xylose
- Xyl-T:
-
β(1,2)-xylosyltransferase
- 2-AB:
-
2-aminobenzamide
- 2D-DIGE:
-
2D difference gel electrophoresis
- 2-DE:
-
2D gel electrophoresis
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Struwe, W.B., Cosgrave, E.F., Byrne, J.C., Saldova, R., Rudd, P.M. (2010). Glycoproteomics in Health and Disease. In: Owens, R., Nettleship, J. (eds) Functional and Structural Proteomics of Glycoproteins. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-9355-4_1
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