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

16 Citations (Scopus)

Abstract

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
JournalLupus
Volume5
Issue number5
Publication statusPublished - 1996

Fingerprint

Antiphospholipid Antibodies
Glycoproteins
Endothelial Cells
Antibodies
Phospholipids
Cardiolipins
Antiphospholipid Syndrome
Arachidonic Acid
Endothelium
Anti-Idiotypic Antibodies
Up-Regulation
Binding Sites
Cytokines

Keywords

  • 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.

Modulation of endothelial cell function by antiphospholipid antibodies. / Meroni, P. L.; Del Papa, N.; Beltrami, B.; Tincani, A.; Balestrieri, G.; Krilis, S. A.

In: Lupus, Vol. 5, No. 5, 1996, p. 448-450.

Research output: Contribution to journalArticle

Meroni, PL, Del Papa, N, Beltrami, B, Tincani, A, Balestrieri, G & Krilis, SA 1996, 'Modulation of endothelial cell function by antiphospholipid antibodies', Lupus, vol. 5, no. 5, pp. 448-450.
Meroni PL, Del Papa N, Beltrami B, Tincani A, Balestrieri G, Krilis SA. Modulation of endothelial cell function by antiphospholipid antibodies. Lupus. 1996;5(5):448-450.
Meroni, P. L. ; Del Papa, N. ; Beltrami, B. ; Tincani, A. ; Balestrieri, G. ; Krilis, S. A. / Modulation of endothelial cell function by antiphospholipid antibodies. In: Lupus. 1996 ; Vol. 5, No. 5. pp. 448-450.
@article{744b1acfbba1477b9e002c12e1cf9610,
title = "Modulation of endothelial cell function by antiphospholipid antibodies",
abstract = "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.",
keywords = "Adhesion molecules, Anti-β -glycoprotein-I antibodies, Antiphospholipid antibodies, Cytokines, Endothelial cells, Prostacyclin, Thrombosis",
author = "Meroni, {P. L.} and {Del Papa}, N. and B. Beltrami and A. Tincani and G. Balestrieri and Krilis, {S. A.}",
year = "1996",
language = "English",
volume = "5",
pages = "448--450",
journal = "Lupus",
issn = "0961-2033",
publisher = "SAGE Publications Ltd",
number = "5",

}

TY - JOUR

T1 - Modulation of endothelial cell function by antiphospholipid antibodies

AU - Meroni, P. L.

AU - Del Papa, N.

AU - Beltrami, B.

AU - Tincani, A.

AU - Balestrieri, G.

AU - Krilis, S. A.

PY - 1996

Y1 - 1996

N2 - 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.

AB - 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.

KW - Adhesion molecules

KW - Anti-β -glycoprotein-I antibodies

KW - Antiphospholipid antibodies

KW - Cytokines

KW - Endothelial cells

KW - Prostacyclin

KW - Thrombosis

UR - http://www.scopus.com/inward/record.url?scp=0029807892&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029807892&partnerID=8YFLogxK

M3 - Article

VL - 5

SP - 448

EP - 450

JO - Lupus

JF - Lupus

SN - 0961-2033

IS - 5

ER -