ArticleGlycobiology2018
Glycosylation profiling of dog serum reveals differences compared to human serum.
Article in Glycobiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Differences in canine serum N-glycosylation pattern during infection and pregnancy.Scientific reports · 2026Article
- Leishmania Infection: A Bioorganic Model Under the Light of Benchtop Low Field Nuclear Magnetic Resonance.Biological procedures online · 2026Article
- Structural and functional characterization of IdeC, a novel IgG-specific protease ofInfection and immunity · 2025Article
- Pregnancy-related changes in the canine serum N-glycosylation pattern studied by Rapifluor HILIC-UPLC-FLR-MS.Scientific reports · 2024Article
- Human extracellular matrix (ECM)-like collagen and its bioactivity.Regenerative biomaterials · 2024Article
- Detection of N-glycolyl-neuraminic acid-containing glycolipids in human skin.Frontiers in immunology · 2023Article
- Alteration of rhesus macaque serum N-glycome during infection with the human parasitic filarial nematode Brugia malayi.Scientific reports · 2022Article
- Serum metabolomic profiles in dogs with chronic enteropathy.Journal of veterinary internal medicine · 2022Article
- Insights into the effects of N-glycosylation on the characteristics of the VC1 domain of the human receptor for advanced glycation end products (RAGE) secreted by Pichia pastoris.Glycoconjugate journal · 2019Article
- Highly modified and immunoactive N-glycans of the canine heartworm.Nature communications · 2019Article
- Changes in canine serum N-glycosylation as a result of infection with the heartworm parasite Dirofilaria immitis.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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.
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