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Titolo:
ANALYSIS OF THE MULTIPLE INTERACTIONS BETWEEN IL-12 AND THE HIGH-AFFINITY IL-12 RECEPTOR COMPLEX
Autore:
PRESKY DH; MINETTI LJ; GILLESSEN S; WILKINSON VL; WU CY; GUBLER U; CHIZZONITE R; GATELY MK;
Indirizzi:
HOFFMANN LA ROCHE INC,DEPT INFLAMMAT AUTOIMMUNE DIS,340 KINGSLAND ST,123-4 NUTLEY NJ 07110
Titolo Testata:
The Journal of immunology
fascicolo: 5, volume: 160, anno: 1998,
pagine: 2174 - 2179
SICI:
0022-1767(1998)160:5<2174:AOTMIB>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL STIMULATORY FACTOR; LYMPHOCYTE MATURATION FACTOR; ACTIVATED HUMAN LYMPHOBLASTS; HETERODIMERIC CYTOKINE; FACTOR INTERLEUKIN-12; MOUSE INTERLEUKIN-12; BIOLOGIC ACTIVITY; GAMMA PRODUCTION; P40 HOMODIMER; T-CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
D.H. Presky et al., "ANALYSIS OF THE MULTIPLE INTERACTIONS BETWEEN IL-12 AND THE HIGH-AFFINITY IL-12 RECEPTOR COMPLEX", The Journal of immunology, 160(5), 1998, pp. 2174-2179

Abstract

IL-12 is a heterodimeric cytokine, composed of a p40 and a p35 subunit, that exerts its biological effects by binding to specific cell surface receptors, Two IL-12R proteins, designated human IL-12 (huIL-12) receptor beta 1 (huIL-12R beta 1) and huIL-12R beta 2, have been previously identified, These IL-12R individually bind huIL-12 with low affinity and in combination bind huIL-12 with high affinity and confer IL-12 responsiveness, In this study the interactions of huIL-12 with thesetwo identified human IL-12R protein subunits are examined, The heterodimer-specific anti-huIL-12 mAb 20C2, which neutralizes huIL-12 bioactivity but does not block I-125-huIL-12 binding to huIL-12R beta 1, blocked binding of huIL-12 to huIL-12R beta 2. In contrast, anti-huIL-12Rbeta 1 mAb 2B10 and mouse IL-12 p40 subunit homodimer (mo(p40)(2)) blocked I-125-huIL-12 binding to huIL-12R beta 1, but not to huIL-12R beta 2. Therefore, two classes of IL-12 inhibitors can he identified that differ in their ability to block huIL-12 interaction with either huIL-12R beta 1 or huIL-12R beta 2. Both mo(p40)(2) and 20C2 blocked highaffinity binding to huIL-12R beta 1/beta 2-cotransfected COS-7 cells,although, as previously reported, mo(p40)(2) does not block high affinity binding to IL-12R on PHA-activated human lymphoblasts, Furthermore, these two classes of IL-12 inhibitors synergistically decreased huIL-12-stimulated proliferation and IFN-gamma production, Therefore, IL-12, in binding to the high affinity IL-12R, interacts with IL-12R beta1 primarily via regions on the IL-12 p40 subunit and with IL-12R beta2 via 20C2-reactive, heterodimer-specific regions of IL-12 to which the p35 and p10 subunits both contribute.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 04:07:43