Modulation of endothelial cell function by antiphospholipid antibodies

P. L. Meroni, N. Del Papa, B. Beltrami, A. Tincani, G. Balestrieri, S. A. Krilis

Research output: Contribution to journalArticle


β 2-glycoprotein I (β 2-GP-I) the plasma cofactor for anti-phospholipid antibodies adheres on the endothelial surfaces and can be recognized by anti-β 2-GP-I antibodies naturally occurring in patients with the anti-phospholipid syndrome. As for the cofactor binding to cardiolipin- or gamma irradiated-plates, the endothelial binding is mediated by the so-called phospholipid binding site, a cationic structure able to react with anionic molecules. Endothelial monolayers appear to represent a substrate able to bind β 2-GP-I and to present it in a suitable manner in order to allow the binding of anti-β 2-GP-I β 2 antibodies. The complex between β 2-GP-I and the respective antibodies induce an endothelial cell activation as demonstrated by the up-regulation of adhesion molecule expression, the secretion of proinflammatory cytokines and the modulation of arachidonic acid metabolism. Taken together these findings strongly sustain a pivotal role for β 2-GP-I in allowing antibody deposition on the endothelium and in affecting endothelial cell functions potentially responsible for a procoagulant state.

Original languageEnglish
Pages (from-to)448-450
Number of pages3
Issue number5
Publication statusPublished - 1996



  • Adhesion molecules
  • Anti-β -glycoprotein-I antibodies
  • Antiphospholipid antibodies
  • Cytokines
  • Endothelial cells
  • Prostacyclin
  • Thrombosis

ASJC Scopus subject areas

  • Rheumatology
  • Immunology

Cite this

Meroni, P. L., Del Papa, N., Beltrami, B., Tincani, A., Balestrieri, G., & Krilis, S. A. (1996). Modulation of endothelial cell function by antiphospholipid antibodies. Lupus, 5(5), 448-450.