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Titolo:
Immunosuppressive activities of recombinant glycosylation-inhibiting factor mutants
Autore:
Tomura, T; Watarai, H; Honma, N; Sato, M; Iwamatsu, A; Kato, Y; Kuroki, R; Nakano, T; Mikayama, T; Ishizaka, K;
Indirizzi:
Kirin Brewery Co Ltd, Pharmaceut Res Lab, Gunma 3711295, Japan Kirin Brewery Co Ltd Gunma Japan 3711295 t Res Lab, Gunma 3711295, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan , Yokohama, Kanagawa, Japan La Jolla Inst Allergy & Immunol, San Diego, CA 92121 USA La Jolla Inst Allergy & Immunol San Diego CA USA 92121 iego, CA 92121 USA
Titolo Testata:
JOURNAL OF IMMUNOLOGY
fascicolo: 1, volume: 162, anno: 1999,
pagine: 195 - 202
SICI:
0022-1767(19990101)162:1<195:IAORGF>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
SUPPRESSOR T-CELLS; TCR ALPHA-CHAIN; BIOCHEMICAL-CHARACTERIZATION; FACTOR MIF; FACTOR PEPTIDE; IGE ANTIBODY; MURINE IGE; MACROPHAGE; LYMPHOCYTES; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Ishizaka, K Kirin Brewery Co Ltd, Pharmaceut Res Lab, 3 Miyahara, Gunma 3711295, Japan Kirin Brewery Co Ltd 3 Miyahara Gunma Japan 3711295 95, Japan
Citazione:
T. Tomura et al., "Immunosuppressive activities of recombinant glycosylation-inhibiting factor mutants", J IMMUNOL, 162(1), 1999, pp. 195-202

Abstract

We have shown previously that glycosylation-inhibiting factor (GIF) in culture supernatants of suppressor T cell (Ts) hybridomas had bioactivity, while the same cells contained a substantial quantity of inactive GIF in cytosol, Mass-spectrometric analysis of GIF in the culture supernatant and cytosol of a Ts hybridoma provided direct evidence that GIF protein was posttranslationally modified in the Ts cells, and that the GIF bioactivity is associated with the posttranslationally modified species. Assuming that conformational changes induced by the posttranslational modifications are responsible for generation of bioactivity, we constructed cysteine mutants of human rGIF (rhGIF) in which cysteine at position 57, 60, or 81 was replaced with Ala, and the mutants were expressed in Escherichia coli. Replacement of Cys(57) or Cys(60) with Ala resulted in generation of bioactivity, while replacement of Cys(81) with Ala failed to do so. It was also found that replacement of Cys(57) with Ala and carboxymethylation of a sulfhydryl group in Cys(60) synergistically increased the GIF bioactivity of the GIF derivatives. A mutated GIF protein, in which Cys(57) and Asn(106) in the rhGIF were replaced with Ala and Ser, respectively, had immunosuppressive effects on the IgE and IgG1 Ab responses of BDF1 mice to DNP-OVA, while wild-type rhGIF didnot. Evidence was obtained that the mutated GIF suppressed Ag priming of Th cells for the Ab responses and proliferative response.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 02:41:51