Thrombomodulatory effect of anti ß-2 glycoprotein I antibodies on crystalline annexin A5 on phospholipid bilayers, as observed by atomic force microscopy
Irman, Špela (Author), Škarabot, Miha (Author), Muševič, Igor (Author), Rozman, Blaž (Author), Božič, Borut (Author)

URLURL - Presentation file, Visit http://www.ifcc.org/media/58903/ejifcc_v21_04_02.pdf This link opens in a new window

Antibodies against ß2-glycoprotein I are a subset of very heterogeneous family of antiphospholipid antibodies. It is well recognised that anti ß2-glycoprotein I antibodies are the main pathogenic players in the autoimmune disease known as antiphospholipid syndrome. Many mechanisms have been proposed through which these autoantibodies could cause microplacental, arterial or venous thrombosis. One of the suggested mechanisms is an antiphospholipid antibody-mediated disruption of annexin A5 protective crystalline shield on negatively charged phospholipid membranes. In current report the study of Ž2Žglycoprotein I, antiß2-glycoprotein I antibodies and annexin A5 interactions was performed on in vitro model of planar solidŽsupported phospholipid bilayers and visualized by atomic force microscopy. Planar phospholipid bilayers comprised 30 % LŽŽŽphosphatidylserineand 70 % L[alpha] phosphatidylcholine. For the study of interactions 10 mg/l annexin A5, 0.15 g/l ß2-glycoprotein I, 10 g/l of IgG fraction from healthy blood donor, 10 g/l of IgG fraction from a patient with anti ß2-glycoprotein I antibodies and 0.4 g/l of isolated IgG anti ß2-glycoprotein I antibodies from the same patients in Hepes buffered saline with 1.5 mM Ca2+ were used. We confirmed the clustering of ß2-glycoprotein I on planar phospholipid bilayers. We also found that in the presence of annexin A5, ß2-glycoprotein I does not bind to planar phospholipid bilayers. However, when adding the anti ß2-glycoprotein I antibodies, the growth of ß2-glycoprotein I-anti-ß2-glycoprotein I antibodies complexes in the presence of incompletely crystallized annexin A5 on planar phospholipid bilayers was observed. Results confirm the possible thrombomodulatory activity of anti-ß2-glycoprotein antibodies through their effect on crystalline annexin A5. In addition, the hypothesis that the presence of possibly pathologic antigen-antibody pair itself is not sufficientto start the pathological process is confirmed and visualized for the first time.

Keywords:anti beta glikoproteini, atomska mikroskopija, protitelesa, fosfolipidi
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:FFA - Faculty of Pharmacy
Number of pages:13 str.
Numbering:Vol. 21, no. 4
ISSN on article:1650-3414
COBISS.SI-ID:3208305 Link is opened in a new window
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Shortened title:eJIFCC
COBISS.SI-ID:22363609 This link opens in a new window

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