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Titolo:
Cartilage-specific autoimmunity in rheumatoid arthritis: characterization of a triple helical B cell epitope in the integrin-binding-domain of collagen type II
Autore:
Kraetsch, HG; Unger, C; Wernhoff, P; Schneider, C; Kalden, JR; Holmdahl, R; Burkhardt, H;
Indirizzi:
Univ Erlangen Nurnberg, Dept Internal Med 3, Inst Clin Immunol, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Erlangen Germany D-91054 -91054 Erlangen, Germany Univ Erlangen Nurnberg, Inst Clin Immunol & Rheumatol, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Erlangen Germany D-91054 -91054 Erlangen, Germany Univ Lund, CMB, Sect Med Inflammat Res, Lund, Sweden Univ Lund Lund Sweden v Lund, CMB, Sect Med Inflammat Res, Lund, Sweden
Titolo Testata:
EUROPEAN JOURNAL OF IMMUNOLOGY
fascicolo: 6, volume: 31, anno: 2001,
pagine: 1666 - 1673
SICI:
0014-2980(200106)31:6<1666:CAIRAC>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYNOVIAL-FLUID; ANTIBODIES; TISSUE;
Keywords:
autoimmunity; collagen type II; B cell epitope; collagen-induced arthritis; rheumatoid arthritis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
15
Recensione:
Indirizzi per estratti:
Indirizzo: Burkhardt, H Univ Erlangen Nurnberg, Dept Internal Med 3, Inst Clin Immunol, Krankenhausstr 12, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Krankenhausstr 12 Erlangen Germany D-91054
Citazione:
H.G. Kraetsch et al., "Cartilage-specific autoimmunity in rheumatoid arthritis: characterization of a triple helical B cell epitope in the integrin-binding-domain of collagen type II", EUR J IMMUN, 31(6), 2001, pp. 1666-1673

Abstract

Cartilage-specific proteins are considered potential autoantigens that could continuously fuel autoimmune responses directed to the joints in rheumatoid arthritis (RA). Using recombinant chimeric collagen type II we have identified one major type II collagen (CII) epitope (denoted U1) recognized byRA sera. The U1 epitope is a triple helical structure formed by 11 amino acids (triple helical position 494-504) and colocalizes with the recently described alpha1 beta1/alpha2 beta1 integrin binding site. It is a major epitope, found in 14/22 RA sera positive for antibodies to CII. One individual could be followed for a long time and the results showed that IgG antibodies specific for the U1 epitope were maintained along the chronic disease course but suppressed during periods of cyclosporin A and anti-CD4 treatment. We also found that the U1 epitope was recognized in rats susceptible to collagen-induced arthritis. A monoclonal autoantibody (mAb 126.30) was raised from DA rats, which bound the same epitope. The antibodies bound the cartilage in vivo showing that the epitope is exposed to the immune system for immune complex formation in the intact joint.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 17:41:12