PMID- 15904931
OWN - NLM
STAT- MEDLINE
DCOM- 20050818
LR  - 20141120
IS  - 0022-1759 (Print)
IS  - 0022-1759 (Linking)
VI  - 300
IP  - 1-2
DP  - 2005 May
TI  - Oxidation and biotinylation of beta 2 glycoprotein I glycan chains induce an 
      increase in its affinity for anionic phospholipids similar to that obtained by 
      the addition of anti-beta 2 glycoprotein I or anti-cardiolipin antibodies.
PG  - 160-78
AB  - Binding of beta 2 glycoprotein I (beta2GPI) to apoptotic cells plays a key role 
      in the opsonization of apoptotic bodies and the formation of antiphospholipids 
      antibodies. Here, we describe the binding of beta2GPI to apoptotic cells using 
      beta2GPI labelled with biotin-hydrazide (beta2GPI-bh) after oxidation of its 
      glycan chains. Flow cytometry analyses and confocal microscopy showed that 
      beta2GPI-bh, contrary to native beta(GPI, bound to apoptotic cells, either 
      permeable or non-permeable to propidium iodide (PI), as did annexin-V-FITC. But, 
      in the absence of divalent ions, beta2GPI-bh, contrary to annexin V, was still 
      able to bind to apoptotic cells. Binding equilibrium studies, performed on 
      solid-state anionic phospholipids (AnPL), revealed that beta2GPI-bh had a greater 
      apparent affinity for AnPL than native beta2GPI. In presence of the anti-beta2GPI 
      mAb 8C3, the ability of native beta2GPI to bind to AnPL was increased and binding 
      to apoptotic PI+ and PI- CEM cells was observed whereas binding of beta2GPI-bh 
      was barely affected by the addition of 8C3. However, the 8C3-enhanced ability of 
      native beta2GPI to bind to AnPL was still weaker than that of beta2GPI-bh. It is 
      not clear why the oxidation and biotinylation of glycan chains of beta2GPI 
      increases its affinity for AnPL, but it seems that if such oxidative process 
      occurs naturally, it could participate in enhancing antiphospholipid formation.
FAU - d'Angeac, Arnaud Dupuy
AU  - d'Angeac AD
AD  - Laboratoire de Chimie Biomoleculaire, UMR CNRS 5032, UM II, ENSCM, 8 rue de 
      l'Ecole Normale 34296 Montpellier Cedex 5, France. dangeac@univ-montp2.fr
FAU - Stefas, Ilias
AU  - Stefas I
FAU - Duperray, Christophe
AU  - Duperray C
FAU - Rucheton, Marcel
AU  - Rucheton M
FAU - Graafland, Hubert
AU  - Graafland H
FAU - Montero, Jean-Louis
AU  - Montero JL
FAU - Chicheportiche, Robert
AU  - Chicheportiche R
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - J Immunol Methods
JT  - Journal of immunological methods
JID - 1305440
RN  - 0 (Antibodies, Anticardiolipin)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycoproteins)
RN  - 0 (Phospholipids)
RN  - 0 (Polysaccharides)
RN  - 0 (Recombinant Proteins)
RN  - 0 (beta 2-Glycoprotein I)
SB  - IM
MH  - Animals
MH  - Antibodies, Anticardiolipin/*metabolism
MH  - Antibodies, Monoclonal/metabolism
MH  - Apoptosis
MH  - Binding Sites
MH  - Biotinylation
MH  - Cell Line
MH  - Glycoproteins/*chemistry/immunology/*metabolism
MH  - Humans
MH  - In Vitro Techniques
MH  - Kinetics
MH  - Oxidation-Reduction
MH  - Phospholipids/*metabolism
MH  - Polysaccharides/chemistry/metabolism
MH  - Recombinant Proteins/chemistry/immunology/metabolism
MH  - beta 2-Glycoprotein I
EDAT- 2005/05/21 09:00
MHDA- 2005/08/19 09:00
CRDT- 2005/05/21 09:00
PHST- 2004/06/23 00:00 [received]
PHST- 2005/02/01 00:00 [revised]
PHST- 2005/03/05 00:00 [accepted]
PHST- 2005/05/21 09:00 [pubmed]
PHST- 2005/08/19 09:00 [medline]
PHST- 2005/05/21 09:00 [entrez]
AID - S0022-1759(05)00087-6 [pii]
AID - 10.1016/j.jim.2005.03.016 [doi]
PST - ppublish
SO  - J Immunol Methods. 2005 May;300(1-2):160-78. doi: 10.1016/j.jim.2005.03.016.