Cross-reactivity between annexin A2 and Beta-2-glycoprotein I in animal models of antiphospholipid syndrome

Antiphospholipid syndrome (APS) affects coagulation and the brain by autoimmune mechanisms. The major antigen in APS is beta-2-glycoprotein I (?2-GPI) is known to complex with annexin A2 (ANXA2), and antibodies to ANXA2 have been described in APS. We measured these antibodies in mice with experiment...

Full description

Autores:
Tipo de recurso:
Fecha de publicación:
2017
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/24279
Acceso en línea:
https://doi.org/10.1007/s12026-016-8840-8
https://repository.urosario.edu.co/handle/10336/24279
Palabra clave:
Beta2 glycoprotein 1
Immunoglobulin g
Lipocortin 2
Beta2 glycoprotein 1
Immunoglobulin g
Lipocortin 2
Phospholipid antibody
Animal experiment
Animal model
Animal tissue
Antiphospholipid syndrome
Article
Chemoluminescence
Controlled study
Cross reaction
Enzyme linked immunosorbent assay
Female
Immobilized metal affinity chromatography
Immune response
Immunization
Immunoblotting
Immunoprecipitation
Mouse
Nonhuman
Priority journal
Protein expression
Radioimmunoprecipitation
Animal
Antiphospholipid syndrome
Bagg albino mouse
Blood
Brain
Cross reaction
Disease model
Immunology
Animals
Annexin a2
Antiphospholipid syndrome
Beta 2-glycoprotein i
Brain
Cross reactions
Enzyme-linked immunosorbent assay
Female
Immunoglobulin g
Annexin
Anticardiolipin
Antiphospholipid syndrome
Autoantibodies
Autoimmune
Beta-2-glycoprotein
inbred balb c
animal
antiphospholipid
Antibodies
Disease models
Mice
Rights
License
Abierto (Texto Completo)
Description
Summary:Antiphospholipid syndrome (APS) affects coagulation and the brain by autoimmune mechanisms. The major antigen in APS is beta-2-glycoprotein I (?2-GPI) is known to complex with annexin A2 (ANXA2), and antibodies to ANXA2 have been described in APS. We measured these antibodies in mice with experimental APS (eAPS) induced by immunization with ?2-GPI. Sera of these mice reacted significantly with recombinant ANXA2 by enzyme-linked immunosorbent assay (ELISA) and the eAPS mice had significantly high levels of immunoglobulin G (IgG) in the brain by immunoblot assays compared to adjuvant immunized controls. Immunoprecipitation performed by mixing eAPS brain tissue with protein-G beads resulted in identification of two autoantigens unique to the eAPS group, one of which was ANXA2. In order to study more directly and methodically the specific role of anti-ANXA2 antibodies in APS, we immunized mice with ?2-GPI which contained no ANXA2 or with ANXA2 and measured antibodies to these proteins. Levels of antibodies to ANXA2 measured by ELISA were 0.72 ± 0.007 arbitrary units (a.u), 0.24 ± 0.03 and 0.02 ± 0.01 a.u for sera from ANXA2, ?2-GPI and control mice, respectively (p  less than  0.0001 and p = 0.037 for the comparison of the ANXA2 and ?2-GPI groups to the controls). Purified IgG from ?2-GPI sera did not show cross-binding with ANXA2. Antibodies to ?2-GPI and phospholipids were found in the ?2-GPI immunized group only. The present study suggests an immune response to the ?2-GPI–ANXA2 complex in eAPS and provides a novel ANXA2 immunization model which will serve to study the role of ANXA2 antibodies in of APS. © 2016, Springer Science+Business Media New York.