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Characterisation of the human hemostatic O-glycoproteome

ABSTRACT: The hemostatic system comprises platelet aggregation, coagulation and fibrinolysis, and is critical to the maintenance of vascular integrity. Multiple studies indicate that glycans play an important role in maintaining the hemostatic system, however, most investigations have focused on N-glycans and little is known about the location and function of O-glycans. Here we performed the first systematic analysis of hemostatic O-glycosylation using lectin affinity chromatography coupled to LC-MS/MS to determine the precise location of O-glycans in human plasma, platelets, and endothelial cells. We identified the hitherto largest O-glycoproteome from native tissue, demonstrating that O-glycosylation is a ubiquitous modification of hemostatic proteins.

INSTRUMENT(S): LTQ Orbitrap Velos, Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Umbilical Vein Endothelial Cell, Blood Platelet, Platelet, Blood Plasma, Endothelial Cell

SUBMITTER: Sarah King

LAB HEAD: Hans Wandall

PROVIDER: PXD004590 | Pride | 2017-03-15

REPOSITORIES: Pride

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			Action	DRS
	130129_KS_SerumHW_PNA_90_IEF_1_100_2h_5HCD_5ETD.raw	Raw
	130129_KS_SerumHW_PNA_90_IEF_2_100_2h_5HCD_5ETD.raw	Raw
	130129_KS_SerumHW_PNA_90_IEF_3_100_2h_5HCD_5ETD.raw	Raw
	130215_KS_SerumHW_PNA_90_IEF_10_100_2h_5HCD_5ETD.raw	Raw
	130215_KS_SerumHW_PNA_90_IEF_11_100_2h_5HCD_5ETD.raw	Raw

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