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Glycoproteomics in Health and Disease

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Functional and Structural Proteomics of Glycoproteins

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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  1. National Institute for Bioprocessing Research and Training, Dublin-Oxford Glycobiology Group, Conway Institute for Biomolecular and Biomedical Sciences, University College Dublin, Belfield, Dublin 4, Dublin, Ireland

    Weston B. Struwe, Eoin F.J. Cosgrave, Jennifer C. Byrne, Radka Saldova & Pauline M. Rudd

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  2. Eoin F.J. Cosgrave
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Correspondence to Weston B. Struwe .

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  1. Oxford Protein Production Facility, Roosevelt DR, Oxford, OX3 7BN, United Kingdom

    Raymond Owens

  2. Oxford Protein Production Facility, Roosevelt Dr, Oxford, OX3 7BN, United Kingdom

    Joanne Nettleship

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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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