Glycopeptide profiling of beta-2-glycoprotein I by mass spectrometry reveals attenuated sialylation in patients with antiphospholipid syndrome

• Published in: Journal of proteomics Vol. 73; no. 1; pp. 123 - 133
• Main Authors: Kondo, Akira, Miyamoto, Toshiaki, Yonekawa, Osamu, Giessing, Anders M., Østerlund, Eva C., Jensen, Ole N.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier B.V 02.11.2009; Elsevier
• Subjects: Adult; Algorithms; Antiphospholipid syndrome; Antiphospholipid Syndrome - metabolism; beta 2-Glycoprotein I - analysis; beta 2-Glycoprotein I - chemistry; beta 2-Glycoprotein I - metabolism; Biological and medical sciences; Case-Control Studies; Chymotrypsin - metabolism; Diverse techniques; Down-Regulation; Female; Fundamental and applied biological sciences. Psychology; Glycopeptides - analysis; Glycopeptides - metabolism; Glycosylation; Humans; In-source decay; LC-ESI-MS; MALDI-MS; Male; Mass Spectrometry - methods; Models, Biological; Molecular and cellular biology; N-glycan; Peptide Mapping - methods; Protein Processing, Post-Translational; Sialic Acids - metabolism; β2-glycoprotein I; In-source decay; APS; LC-ESI-MS; ZIC-HILIC; MALDI; PNGase F; IgG; MALDI-MS; aCL; β2-GPI; NH 4HCO 3; anti-β2-GPI; ESI; N-glycan; FA; ISD; β2-glycoprotein I; DHB; Antiphospholipid syndrome; Human; Antiphospholipid antibody syndrome; Glycoprotein; Patient; Glycan; Chenopodiaceae; Beta; Glycopeptide; Dicotyledones; Angiospermae; Spermatophyta; Mass spectrometry; Sialylation

β2-glycoprotein I (β2GPI) is a five-domain protein associated with the antiphospholipid syndrome (APS), however, its normal biological function is yet to be defined. β2GPI is N-glycosylated at several asparagine residues and the glycan moiety conjugated to residue 143 has been proposed to interact w...