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Titolo:
Surface expression of a glycolytic enzyme, alpha-enolase, recognized by autoantibodies in connective tissue disorders
Autore:
Moscato, S; Pratesi, F; Sabbatini, A; Chimenti, D; Scavuzzo, M; Passantino, R; Bombardieri, S; Giallongo, A; Migliorini, P;
Indirizzi:
Univ Pisa, Dept Internal Med, Clin Immunol Unit, I-56126 Pisa, Italy Univ Pisa Pisa Italy I-56126 Med, Clin Immunol Unit, I-56126 Pisa, Italy Natl Res Council, Ist Biol Sviluppo, Palermo, Italy Natl Res Council Palermo Italy uncil, Ist Biol Sviluppo, Palermo, Italy
Titolo Testata:
EUROPEAN JOURNAL OF IMMUNOLOGY
fascicolo: 12, volume: 30, anno: 2000,
pagine: 3575 - 3584
SICI:
0014-2980(200012)30:12<3575:SEOAGE>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
CANDIDATE PLASMINOGEN RECEPTOR; ANTICYTOPLASMIC ANTIBODIES; WEGENERS GRANULOMATOSIS; MIXED CRYOGLOBULINEMIA; MEMBRANE-PROTEINS; ENDOTHELIAL-CELLS; PHASE-SEPARATION; TARGET ANTIGEN; IDENTIFICATION; BINDING;
Keywords:
alpha-enolase; plasminogen receptor; autoimmunity; autoantibody;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Migliorini, P Univ Pisa, Dept Internal Med, Clin Immunol Unit, Via Roma 67, I-56126 Pisa, Italy Univ Pisa Via Roma 67 Pisa Italy I-56126 -56126 Pisa, Italy
Citazione:
S. Moscato et al., "Surface expression of a glycolytic enzyme, alpha-enolase, recognized by autoantibodies in connective tissue disorders", EUR J IMMUN, 30(12), 2000, pp. 3575-3584

Abstract

In systemic autoimmune diseases, autoantibodies specific for alpha -enolase are detected more frequently in patients with active renal involvement. To analyze the properties of anti-alpha -enolase antibodies and the distribution of the enzyme in the cell, mouse monoclonal and polyclonal antibodies were obtained from mice immunized with a glutathione-S-transferase-alpha -enolase fusion protein. Anti-alpha -enolase antibodies were purified from patient sera on enolase from human kidney. Using these antibodies, the distribution of alpha -enolase in the cell was analyzed in subcellular fractions and in the cell membrane by flow cytometry and immunoprecipitation, Plasminogen binding was studied by an immunoenzymatic assay. We observed that alpha -enolase was present in the cytosol and membrane fractions obtained from kidney and U937 cells. By flow cytometry, mouse polyclonal anti-enolase antibodies, one monoclonal and 7/9 human anti-enolase antibodies bound the membrane of U937 cells. One monoclonal antibody and mouse polyclonal anti-enolase antibodies immunoprecipitated a 48-kDa molecule from surface-labeled U937 cells and this molecule was recognized by rabbit anti-enolase antibodies. Both immunization-induced antibodies and 7/9 autoantibodies from patient sera inhibited the binding of plasminogen to alpha -enolase. The results show that alpha -enolase, an autoantigen in connective tissue diseases, is a cytoplasmic enzyme which is also expressed on the cell membrane, with whichit is strongly associated. Anti-alpha -enolase autoantibodies isolated from patient sera recognize the membrane-associated form of the enzyme and/or interfere with its receptor function, thus inhibiting the binding of plasminogen. Autoantibodies specific for alpha -enolase could play a pathogenic role, either by a cytopathic effect or by interfering with membrane fibrinolytic activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 08:31:56