β2-Glycoprotein I as a 'cofactor' for anti-phospholipid reactivity with endothelial cells

P. L. Meroni, N. Del Papa, E. Raschi, P. Panzeri, M. O. Borghi, A. Tincani, G. Balestrieri, Ma Khamashta, G. R V Hughes, T. Koike, S. A. Krilis

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

β2-glycoprotein I (β2GPI) is a cofactor for anti-phospholipid (aPL) binding to cardiolipin (CL)-coated plates. β2GPI is also able to bind to endothelial cell (EC) membranes as supported by in-vivo as well as by in-vitro studies. The PL-binding site in the fifth domain of the molecule is involved in the adhesion to endothelium. Actually, specific mutations in this molecular portion abolish endothelium binding and a synthetic peptide spanning the sequence Glu274-Cys288 of the CL-binding site displays comparable adhesion to EC monolayers. Heparan sulphate appears to be one of the anionic EC membrane structures with which cationic β2GPI interacts, as supported by studies with heparitinase-treated EC. β2GPI binding to EC might be related to its activity as endothelial growth factor or as a lipid-carrying glycoprotein. Adhesion of β2GPI to endothelial membranes offers suitable epitopes for circulating aPL that, once bound, can induce cell activation.

Original languageEnglish
JournalLupus
Volume7
Issue numberSUPPL. 2
Publication statusPublished - 1998

Fingerprint

Phospholipids
Glycoproteins
Endothelial Cells
Cardiolipins
heparitinsulfate lyase
Endothelium
Binding Sites
Cell Membrane Structures
Endothelial Growth Factors
Heparitin Sulfate
Epitopes
Cell Membrane
Lipids
Peptides
Mutation
Membranes

Keywords

  • β2-glycoprotein I
  • Anti-phospholipid antibodies
  • Endothelial cells
  • Heparan sulphate

ASJC Scopus subject areas

  • Immunology
  • Rheumatology

Cite this

β2-Glycoprotein I as a 'cofactor' for anti-phospholipid reactivity with endothelial cells. / Meroni, P. L.; Del Papa, N.; Raschi, E.; Panzeri, P.; Borghi, M. O.; Tincani, A.; Balestrieri, G.; Khamashta, Ma; Hughes, G. R V; Koike, T.; Krilis, S. A.

In: Lupus, Vol. 7, No. SUPPL. 2, 1998.

Research output: Contribution to journalArticle

Meroni, PL, Del Papa, N, Raschi, E, Panzeri, P, Borghi, MO, Tincani, A, Balestrieri, G, Khamashta, M, Hughes, GRV, Koike, T & Krilis, SA 1998, 'β2-Glycoprotein I as a 'cofactor' for anti-phospholipid reactivity with endothelial cells', Lupus, vol. 7, no. SUPPL. 2.
Meroni, P. L. ; Del Papa, N. ; Raschi, E. ; Panzeri, P. ; Borghi, M. O. ; Tincani, A. ; Balestrieri, G. ; Khamashta, Ma ; Hughes, G. R V ; Koike, T. ; Krilis, S. A. / β2-Glycoprotein I as a 'cofactor' for anti-phospholipid reactivity with endothelial cells. In: Lupus. 1998 ; Vol. 7, No. SUPPL. 2.
@article{9846093d52a64008a0fcfc507ef8016a,
title = "β2-Glycoprotein I as a 'cofactor' for anti-phospholipid reactivity with endothelial cells",
abstract = "β2-glycoprotein I (β2GPI) is a cofactor for anti-phospholipid (aPL) binding to cardiolipin (CL)-coated plates. β2GPI is also able to bind to endothelial cell (EC) membranes as supported by in-vivo as well as by in-vitro studies. The PL-binding site in the fifth domain of the molecule is involved in the adhesion to endothelium. Actually, specific mutations in this molecular portion abolish endothelium binding and a synthetic peptide spanning the sequence Glu274-Cys288 of the CL-binding site displays comparable adhesion to EC monolayers. Heparan sulphate appears to be one of the anionic EC membrane structures with which cationic β2GPI interacts, as supported by studies with heparitinase-treated EC. β2GPI binding to EC might be related to its activity as endothelial growth factor or as a lipid-carrying glycoprotein. Adhesion of β2GPI to endothelial membranes offers suitable epitopes for circulating aPL that, once bound, can induce cell activation.",
keywords = "β2-glycoprotein I, Anti-phospholipid antibodies, Endothelial cells, Heparan sulphate",
author = "Meroni, {P. L.} and {Del Papa}, N. and E. Raschi and P. Panzeri and Borghi, {M. O.} and A. Tincani and G. Balestrieri and Ma Khamashta and Hughes, {G. R V} and T. Koike and Krilis, {S. A.}",
year = "1998",
language = "English",
volume = "7",
journal = "Lupus",
issn = "0961-2033",
publisher = "SAGE Publications Ltd",
number = "SUPPL. 2",

}

TY - JOUR

T1 - β2-Glycoprotein I as a 'cofactor' for anti-phospholipid reactivity with endothelial cells

AU - Meroni, P. L.

AU - Del Papa, N.

AU - Raschi, E.

AU - Panzeri, P.

AU - Borghi, M. O.

AU - Tincani, A.

AU - Balestrieri, G.

AU - Khamashta, Ma

AU - Hughes, G. R V

AU - Koike, T.

AU - Krilis, S. A.

PY - 1998

Y1 - 1998

N2 - β2-glycoprotein I (β2GPI) is a cofactor for anti-phospholipid (aPL) binding to cardiolipin (CL)-coated plates. β2GPI is also able to bind to endothelial cell (EC) membranes as supported by in-vivo as well as by in-vitro studies. The PL-binding site in the fifth domain of the molecule is involved in the adhesion to endothelium. Actually, specific mutations in this molecular portion abolish endothelium binding and a synthetic peptide spanning the sequence Glu274-Cys288 of the CL-binding site displays comparable adhesion to EC monolayers. Heparan sulphate appears to be one of the anionic EC membrane structures with which cationic β2GPI interacts, as supported by studies with heparitinase-treated EC. β2GPI binding to EC might be related to its activity as endothelial growth factor or as a lipid-carrying glycoprotein. Adhesion of β2GPI to endothelial membranes offers suitable epitopes for circulating aPL that, once bound, can induce cell activation.

AB - β2-glycoprotein I (β2GPI) is a cofactor for anti-phospholipid (aPL) binding to cardiolipin (CL)-coated plates. β2GPI is also able to bind to endothelial cell (EC) membranes as supported by in-vivo as well as by in-vitro studies. The PL-binding site in the fifth domain of the molecule is involved in the adhesion to endothelium. Actually, specific mutations in this molecular portion abolish endothelium binding and a synthetic peptide spanning the sequence Glu274-Cys288 of the CL-binding site displays comparable adhesion to EC monolayers. Heparan sulphate appears to be one of the anionic EC membrane structures with which cationic β2GPI interacts, as supported by studies with heparitinase-treated EC. β2GPI binding to EC might be related to its activity as endothelial growth factor or as a lipid-carrying glycoprotein. Adhesion of β2GPI to endothelial membranes offers suitable epitopes for circulating aPL that, once bound, can induce cell activation.

KW - β2-glycoprotein I

KW - Anti-phospholipid antibodies

KW - Endothelial cells

KW - Heparan sulphate

UR - http://www.scopus.com/inward/record.url?scp=0032245795&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032245795&partnerID=8YFLogxK

M3 - Article

C2 - 9814672

AN - SCOPUS:0032245795

VL - 7

JO - Lupus

JF - Lupus

SN - 0961-2033

IS - SUPPL. 2

ER -