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Titolo:
Subunit structure of the high and low affinity human interleukin-15 receptors
Autore:
Lehours, P; Raher, S; Dubois, S; Guo, J; Godard, A; Jacques, Y;
Indirizzi:
INSERM, Inst Biol, U463, Grp Rech Cytokines Recepteurs & Transduct, F-44035 Nantes 01, France INSERM Nantes France 01 ecepteurs & Transduct, F-44035 Nantes 01, France CHU Nantes, F-44035 Nantes, France CHU Nantes Nantes France F-44035CHU Nantes, F-44035 Nantes, France Johns Hopkins Univ, Sch Med, Baltimore, MD 21287 USA Johns Hopkins Univ Baltimore MD USA 21287 ch Med, Baltimore, MD 21287 USA
Titolo Testata:
EUROPEAN CYTOKINE NETWORK
fascicolo: 2, volume: 11, anno: 2000,
pagine: 207 - 215
SICI:
1148-5493(200006)11:2<207:SSOTHA>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED KILLER-CELLS; HUMAN IL-2 RECEPTOR; BETA-CHAIN; ALPHA-CHAIN; GAMMA-CHAIN; 3-DIMENSIONAL STRUCTURE; GROWTH-FACTOR; CYTOKINE; EXPRESSION; CLONING;
Keywords:
interleukin-15; interleukin-2; cell-surface receptors; monoclonal antibodies; cross-linking; immunoprecipitation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Jacques, Y INSERM, Inst Biol, U463, Grp Rech Cytokines Recepteurs & Transduct, 9 QuaiMoncousu, F-44035 Nantes 01, France INSERM 9 Quai Moncousu Nantes France 01 4035 Nantes 01, France
Citazione:
P. Lehours et al., "Subunit structure of the high and low affinity human interleukin-15 receptors", EUR CYTOKIN, 11(2), 2000, pp. 207-215

Abstract

Radio-iodinated cytokines and monoclonal antibodies directed at the IL-2R beta- and gamma-chains were used to analyze the structure of the cell-surface IL-15 and IL-2 receptors expressed by the human lymphoma cell clone YT-2C2, YT-2C2 cells are IL-2R alpha negative and express IL-2R gamma (15,000 molecules/cell) in excess of IL-2R beta (11,000 molecules/cell). Accordingly, they display a number of beta/gamma complexes of intermediate affinity for IL-2 and IL-15 which is equivalent to the number of beta-chains. Both cytokines compete for binding to this beta/gamma complex, There are about 800 high affinity IL-15 receptors, suggesting the presence of a similar number of IL-15R alpha-chains, Within the common intermediate affinity beta/gamma-complex, the anti-beta-chain A41 mAb defines an epitope which is similarly engaged in IL-2 and IL-15 binding, whereas the anti-beta-chain 284 mAb defines an epitope which does not display similar interaction with either cytokines, Thus, although IL-2 and IL-15 compete for binding to this beta/gamma-complex, they do not use similar binding areas, Cross-linking and immunoprecipitation experiments have shown that the high affinity IL-15 receptors comprises IL-2R beta/gamma, in association with IL-15R alpha and that the three chains can be efficiently cross-linked to IL-15 and co-immunoprecipitated. Contrary to the intermediate affinity situation, high affinity IL-15 binding and subunit cross-linking were not affected by excess amounts of IL-2,A41 or 284 mAb, suggesting that when engaged in the IL-15 high affinity complex, the beta- and gamma-chains adopt different conformations, at least with respect to IL-15 binding, Finally, we provide evidence for the participation of a novel 35 kDa component within the high affinity structure, This component is immunoprecipitated with anti-IL-2R gamma mAb but not with anti-IL-2R beta mAb and might correspond to a truncated form of IL-2R gamma-chain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 15:05:10