Dataset Information

N-glycosylation analysis of human complement component C3 LC-MS

ABSTRACT: The most abundant and central component, glycoprotein C3, contributes to the development of type 1 diabetes by enhancing the organ-specific autoimmune inflammatory processes. It is known that changes in glycosylation can modulate inflammatory responses and we recently showed that children at the onset of type 1 diabetes have a higher proportion of oligomannose glycans in plasma N-glycome compared to their healthy siblings. Due to fact that C3 contains two N-glycosylation sites occupied by this type of glycans, our aim was to develop a novel high-throughput and cost-effective glycoproteomic workflow for N-glycosylation analysis of human C3 to reveal the possible role of C3 glycosylation in type 1 diabetes development.

INSTRUMENT(S): maXis

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Dinko Šoić

LAB HEAD: Olga Gornik

PROVIDER: PXD034083 | Pride | 2023-03-10

REPOSITORIES: Pride

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Publications

High-Throughput Human Complement C3 N-Glycoprofiling Identifies Markers of Early Onset Type 1 Diabetes Mellitus in Children.

Šoić Dinko D Keser Toma T Štambuk Jerko J Kifer Domagoj D Pociot Flemming F Lauc Gordan G Morahan Grant G Novokmet Mislav M Gornik Olga O

Molecular & cellular proteomics : MCP 20220827 10

Recently, it was shown that children at the onset of type 1 diabetes (T1D) have a higher proportion of oligomannose glycans in their total plasma protein N-glycome compared to their healthy siblings. The most abundant complement component, glycoprotein C3, contains two N-glycosylation sites occupied exclusively by this type of glycans. Furthermore, complement system, as well as C3, was previously associated with T1D. It is also known that changes in glycosylation can modulate inflammatory respon ...[more]

PMID: 36031042

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			Action	DRS
	C3_MS_MS.baf	Other
	P010_2-A2_01_11357.baf	Other
	P011_2-A2_01_11493.baf	Other
	P012_2-A2_01_11429.baf	Other
	P013_2-A2_01_11361.baf	Other