Table of Contents Author Guidelines Submit a Manuscript
Journal of Immunology Research
Volume 2014 (2014), Article ID 195687, 8 pages
http://dx.doi.org/10.1155/2014/195687
Research Article

Optimization of Unnicked β2-Glycoprotein I and High Avidity Anti-β2-Glycoprotein I Antibodies Isolation

1Department of Rheumatology, University Medical Centre Ljubljana, Laboratory for Immunology, Vodnikova 62, 1000 Ljubljana, Slovenia
2Department of Molecular and Biomedical Sciences, Jožef Stefan Institute, 1000 Ljubljana, Slovenia
3Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia
4Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, 1000 Ljubljana, Slovenia
5Natural Sciences and Information Technologies, Faculty of Mathematics, University of Primorska, 6000 Koper, Slovenia
6Faculty of Pharmacy, University of Ljubljana, 1000 Ljubljana, Slovenia

Received 19 November 2013; Accepted 8 December 2013; Published 23 January 2014

Academic Editor: Jozélio Freire De Carvalho

Copyright © 2014 Andrej Artenjak et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. A. A. Mehdi, I. Uthman, and M. Khamashta, “Antiphospholipid syndrome: pathogenesis and a window of treatment opportunities in the future,” European Journal of Clinical Investigation, vol. 40, no. 5, pp. 451–464, 2010. View at Publisher · View at Google Scholar · View at Scopus
  2. B. de Laat, K. Mertens, and P. G. de Groot, “Mechanisms of disease: antiphospholipid antibodies—from clinical association to pathologic mechanism,” Nature Clinical Practice Rheumatology, vol. 4, no. 4, pp. 192–199, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. E. J. Favaloro and R. C. W. Wong, “Laboratory testing for the antiphospholipid syndrome: making sense of antiphospholipid antibody assays,” Clinical Chemistry and Laboratory Medicine, vol. 49, no. 3, pp. 447–461, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. J. Lozier, N. Takahashi, and F. W. Putnam, “Complete amino acid sequence of human plasma β2-glycoprotein I,” Proceedings of the National Academy of Sciences of the United States of America, vol. 81, no. 12, pp. 3640–3644, 1984. View at Google Scholar · View at Scopus
  5. F. Lin, R. Murphy, B. White et al., “Circulating levels of β2-glycoprotein I in thrombotic disorders and in inflammation,” Lupus, vol. 15, no. 2, pp. 87–93, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. J. E. Hunt, R. J. Simpson, and S. A. Krilis, “Identification of a region of β2-glycoprotein I critical for lipid binding and anti-cardiolipin antibody cofactor activity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 6, pp. 2141–2145, 1993. View at Google Scholar · View at Scopus
  7. R. Schwarzenbacher, K. Zeth, K. Diederichs et al., “Crystal structure of human β2-glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome,” EMBO Journal, vol. 18, no. 22, pp. 6228–6239, 1999. View at Publisher · View at Google Scholar · View at Scopus
  8. D. A. Horbach, E. Van Oort, T. Lisman, J. C. M. Meijers, R. H. W. M. Derksen, and P. G. De Groot, “β2-glycoprotein I is proteolytically cleaved in vivo upon activation of fibrinolysis,” Thrombosis and Haemostasis, vol. 81, no. 1, pp. 87–95, 1999. View at Google Scholar · View at Scopus
  9. Ç. Aǧar, G. M. A. Van Os, M. Mörgelin et al., “β2-Glycoprotein I can exist in 2 conformations: implications for our understanding of the antiphospholipid syndrome,” Blood, vol. 116, no. 8, pp. 1336–1343, 2010. View at Publisher · View at Google Scholar · View at Scopus
  10. B. De Laat, R. H. W. M. Derksen, M. Van Lummel, M. T. T. Pennings, and P. G. De Groot, “Pathogenic anti-β2-glycoprotein I antibodies recognize domain I of β2-glycoprotein I only after a conformational change,” Blood, vol. 107, no. 5, pp. 1916–1924, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. S. Miyakis, M. D. Lockshin, T. Atsumi et al., “International consensus statement on an update of the classification criteria for definite antiphospholipid syndrome (APS),” Journal of Thrombosis and Haemostasis, vol. 4, no. 2, pp. 295–306, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. S. Čučnik, B. Božič, T. Kveder, M. Tomšič, and B. Rozman, “Avidity of anti-β2-glycoprotein I and thrombosis or pregnancy loss in patients with antiphospholipid syndrome,” Annals of the New York Academy of Sciences, vol. 1051, pp. 141–147, 2005. View at Publisher · View at Google Scholar · View at Scopus
  13. B. de Laat, R. H. W. M. Derksen, and P. G. de Groot, “High-avidity anti-β2 glycoprotein I antibodies highly correlate with thrombosis in contrast to low-avidity anti-β2 glycoprotein I antibodies,” Journal of Thrombosis and Haemostasis, vol. 4, no. 7, pp. 1619–1621, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. S. Cucnik, T. Kveder, A. Artenjak et al., “Avidity of anti-beta2-glycoprotein I antibodies in patients with antiphospholipid syndrome,” Lupus, vol. 21, no. 7, pp. 764–765, 2012. View at Google Scholar
  15. Y. Shoenfeld, R. Gerli, A. Doria et al., “Accelerated atherosclerosis in autoimmune rheumatic diseases,” Circulation, vol. 112, no. 21, pp. 3337–3347, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. A. Artenjak, K. Lakota, M. Frank et al., “Antiphospholipid antibodies as non-traditional risk factors in atherosclerosis based cardiovascular diseases without overt autoimmunity. A critical updated review,” Autoimmunity Reviews, vol. 11, no. 12, pp. 873–882, 2012. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Cucnik, I. Krizaj, B. Rozman et al., “Concomitant isolation of protein C inhibitor and unnicked beta2-glycoprotein I,” Clinical Chemistry and Laboratory Medicine, vol. 42, no. 2, pp. 171–174, 2004. View at Google Scholar
  18. U. Žager, Š. Irman, M. Lunder et al., “Immunochemical properties and pathological relevance of anti-β2-glycoprotein I antibodies of different avidity,” International Immunology, vol. 23, no. 8, pp. 511–518, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. J. Omersel, U. Žager, T. Kveder, and B. Božič, “Alteration of antibody specificity during isolation and storage,” Journal of Immunoassay and Immunochemistry, vol. 31, no. 1, pp. 45–59, 2010. View at Publisher · View at Google Scholar · View at Scopus
  20. J. Omersel, I. Avberšek-Lužnik, P. A. Grabnar, T. Kveder, B. Rozman, and B. Božič, “Autoimmune reactivity of IgM acquired after oxidation,” Redox Report, vol. 16, no. 6, pp. 248–256, 2011. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Cucnik, A. Ambrozic, B. Bozic, M. Skitek, and T. Kveder, “Anti-β2-glycoprotein I ELISA: methodology, determination of cut-off values in 434 healthy Caucasians and evaluation of monoclonal antibodies as possible international standards,” Clinical Chemistry and Laboratory Medicine, vol. 38, no. 8, pp. 777–783, 2000. View at Google Scholar · View at Scopus
  22. T. Avcin, A. Ambrozic, B. Bozic et al., “Estimation of anticardiolipin antibodies, anti-beta2 glycoprotein I antibodies and lupus anticoagulant in a prospective longitudinal study of children with juvenile idiopathic arthritis,” Clinical and Experimental Rheumatology, vol. 20, no. 1, pp. 101–108, 2002. View at Google Scholar
  23. S. Čučnik, T. Kveder, I. Križaj, B. Rozman, and B. Božič, “High avidity anti-β2-glycoprotein I antibodies in patients with antiphospholipid syndrome,” Annals of the Rheumatic Diseases, vol. 63, no. 11, pp. 1478–1482, 2004. View at Publisher · View at Google Scholar · View at Scopus
  24. A. Artenjak, M. Kozelj, K. Lakota et al., “High avidity anti-b2-glycoprotein I antibodies activate human coronary artery endothelial cells and trigger peripheral blood mononuclear cell migration,” European Journal of Inflammation, vol. 11, no. 2, pp. 385–396, 2013. View at Google Scholar
  25. P. L. Meroni, M. O. Borghi, E. Raschi, and F. Tedesco, “Pathogenesis of antiphospholipid syndrome: understanding the antibodies,” Nature Reviews Rheumatology, vol. 7, no. 6, pp. 330–339, 2011. View at Publisher · View at Google Scholar · View at Scopus
  26. T. A. Brighton, Y.-P. Dai, P. J. Hogg, and C. N. Chesterman, “Microheterogeneity of beta-2 glycoprotein I: implications for binding to anionic phospholipids,” Biochemical Journal, vol. 340, no. 1, pp. 59–67, 1999. View at Publisher · View at Google Scholar · View at Scopus
  27. B. L. Steele, M. C. Alvarez-Veronesi, and T. A. Schmidt, “Molecular weight characterization of PRG4 proteins using multi-angle laser light scattering (MALLS),” Osteoarthritis Cartilage, vol. 21, no. 3, pp. 498–504, 2013. View at Google Scholar
  28. T. A. Schmidt, N. S. Gastelum, Q. T. Nguyen, B. L. Schumacher, and R. L. Sah, “Boundary lubrication of articular cartilage: role of synovial fluid constituents,” Arthritis and Rheumatism, vol. 56, no. 3, pp. 882–891, 2007. View at Publisher · View at Google Scholar · View at Scopus
  29. T. E. Ludwig, J. R. McAllister, V. Lun et al., “Diminished cartilage-lubricating ability of human osteoarthritic synovial fluid deficient in proteoglycan 4: restoration through proteoglycan 4 supplementation,” Arthritis & Rheumatism, vol. 64, no. 12, pp. 3963–3971, 2012. View at Google Scholar
  30. S. Čučnik, T. Kveder, G. Z. Ulcova et al., “The avidity of anti-β2-glycoprotein i antibodies in patients with or without antiphospholipid syndrome: a collaborative study in the frame of the European forum on antiphospholipid antibodies,” Lupus, vol. 20, no. 11, pp. 1166–1171, 2011. View at Publisher · View at Google Scholar · View at Scopus