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Titolo:
STRUCTURE-FUNCTION ANALYSIS OF THE P35 SUBUNIT OF MOUSE INTERLEUKIN-12
Autore:
ZOU JJ; SCHOENHAUT DS; CARVAJAL DM; WARRIER RR; PRESKY DH; GATELY MK; GUBLER U;
Indirizzi:
HOFFMANN LA ROCHE INC,DEPT INFLAMMAT AUTOIMMUNE DIS,340 KINGSLAND ST NUTLEY NJ 07110 HOFFMANN LA ROCHE INC,DEPT INFLAMMAT AUTOIMMUNE DIS NUTLEY NJ 07110
Titolo Testata:
The Journal of biological chemistry
fascicolo: 11, volume: 270, anno: 1995,
pagine: 5864 - 5871
SICI:
0021-9258(1995)270:11<5864:SAOTPS>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL STIMULATORY FACTOR; LYMPHOCYTE MATURATION FACTOR; ACTIVATED HUMAN LYMPHOBLASTS; RECEPTOR-BINDING; FACTOR NKSF; EXPRESSION; PROTEINS; PURIFICATION; MUTAGENESIS; CYTOKINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
J.J. Zou et al., "STRUCTURE-FUNCTION ANALYSIS OF THE P35 SUBUNIT OF MOUSE INTERLEUKIN-12", The Journal of biological chemistry, 270(11), 1995, pp. 5864-5871

Abstract

Mouse IL-12 acts on both mouse and human cells; human IL-12 acts onlyon human cells. This species specificity is determined by the p35 subunit of the IL-12 heterodimer. Since mouse and human p35 sequences are60% identical, the determinants for the species specificity most likely reside in the nonhomologous sequences of mouse p35. To identify theregions on the p35 subunit interacting with the mouse IL-12 receptor,we constructed a series of chimeric mouse-human p35 molecules by replacing mouse sequences with the nonhomologous human counterparts. An IL-12 heterodimer containing a mouse-human p35 chimera with five residues changed in three discontinuous sites had drastically reduced (750-3000-fold) bioactivities on mouse cells. However, the competitive binding activity of the same mutant IL-12 heterodimer on mouse cells was only reduced 30-fold relative to wild-type IL-12. These findings therefore suggest that 1) the mouse p35 subunit participates in both receptor binding and signaling, 2) the mutations introduced into p35 affect signaling to a much greater extent than receptor binding, and 3) the fiveresidues identified on p35 are required for interacting with the mouse, but not with the human IL-12 receptor and as such contribute extensively to the observed species specificity of IL-12.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 20:28:29