Glycosylation profiling of dog serum reveals differences compared to human serum.

Abstract:

:Glycosylation is the most common post-translational modification of serum proteins, and changes in the type and abundance of glycans in human serum have been correlated with a growing number of human diseases. While the glycosylation pattern of human serum is well studied, little is known about the profiles of other mammalian species. Here, we report detailed glycosylation profiling of canine serum by hydrophilic interaction chromatography-ultraperformance liquid chromatography (HILIC-UPLC) and mass spectrometry. The domestic dog (Canis familiaris) is a widely used model organism and of considerable interest for a large veterinary community. We found significant differences in the serum N-glycosylation profile of dogs compared to that of humans, such as a lower abundance of galactosylated and sialylated glycans. We also compare the N-glycan profile of canine serum to that of canine IgG - the most abundant serum glycoprotein. Our data will serve as a baseline reference for future studies when performing serum analyses of various health and disease states in dogs.

journal_name

Glycobiology

journal_title

Glycobiology

authors

Behrens AJ,Duke RM,Petralia LM,Harvey DJ,Lehoux S,Magnelli PE,Taron CH,Foster JM

doi

10.1093/glycob/cwy070

subject

Has Abstract

pub_date

2018-11-01 00:00:00

pages

825-831

issue

11

eissn

0959-6658

issn

1460-2423

pii

5076956

journal_volume

28

pub_type

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