2014
DOI: 10.1016/j.bbrc.2014.09.064
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The role of β2-glycoprotein I (β2GPI) carbohydrate chains in the reactivity of anti-β2GPI antibodies from patients with primary antiphospholipid syndrome and in the activation and differentiation of U937 cells

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Cited by 4 publications
(2 citation statements)
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“…Human β2-GP I is a glycosylated protein present in plasma. It has been reported that the affinity of aβ2-GP I against partially glycosylated β2-GP I and completely de-glycosylated β2-GPI is increased compared with native β2-GP I ( 15 ). Based on these results, the present study used a prokaryotic expression system for obtaining β2-GP I protein to ensure lack of glycosylation.…”
Section: Resultsmentioning
confidence: 99%
“…Human β2-GP I is a glycosylated protein present in plasma. It has been reported that the affinity of aβ2-GP I against partially glycosylated β2-GP I and completely de-glycosylated β2-GPI is increased compared with native β2-GP I ( 15 ). Based on these results, the present study used a prokaryotic expression system for obtaining β2-GP I protein to ensure lack of glycosylation.…”
Section: Resultsmentioning
confidence: 99%
“…Variations of the carbohydrate chains of β2-GPI correlate to some clinical manifestations [52] [53]. The pathogenic key role of the β2-GPI domain I is further highlighted by the report, in a β2-GPI immunized mouse-model of APS, of a better oral tolerance when mice were fed with β2-GPI-D1 instead of complete β2-GPI or with β2-GPI-D5 [54].…”
Section: β2-gpi and Cryptic Epitopesmentioning
confidence: 95%