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Titolo:
A FUNCTIONAL INTERLEUKIN-12 RECEPTOR COMPLEX IS COMPOSED OF 2 BETA-TYPE CYTOKINE RECEPTOR SUBUNITS
Autore:
PRESKY DH; YANG H; MINETTI LJ; CHUA AO; NABAVI N; WU CY; 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:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 24, volume: 93, anno: 1996,
pagine: 14002 - 14007
SICI:
0027-8424(1996)93:24<14002:AFIRCI>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL STIMULATORY FACTOR; LYMPHOCYTE MATURATION FACTOR; ACTIVATED HUMAN LYMPHOBLASTS; INTERFERON-GAMMA PRODUCTION; IL-12 RECEPTOR; HETERODIMERIC CYTOKINE; T-CELLS; EXPRESSION; CLONING; PROLIFERATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
D.H. Presky et al., "A FUNCTIONAL INTERLEUKIN-12 RECEPTOR COMPLEX IS COMPOSED OF 2 BETA-TYPE CYTOKINE RECEPTOR SUBUNITS", Proceedings of the National Academy of Sciences of the United Statesof America, 93(24), 1996, pp. 14002-14007

Abstract

We have identified a cDNA from a human phytohemagglutinin-activated lymphoblast library encoding a protein that binds I-125-labeled human interleukin 12 (I-125-huIL-12) with a K-d of about 5 nM when expressed in COS-7 cells, When coexpressed in COS-7 cells with the previously identified IL-12 beta receptor (IL-12R beta) protein, two classes of I-125-huIL-12 binding sites were measured with K(d)s of about 55 pM and 8nM, corresponding to the high- and low-affinity binding sites seen onphytohemagglutinin-activated lymphoblasts, This newly identified huIL-12R subunit is a member of the cytokine receptor superfamily, with closest resemblance to the beta-type cytokine receptor gp130 and the receptors for leukemia inhibitory factor and granulocyte colony-stimulating factor, Consequently, we have reclassified the previously identified IL-12R beta subunit as huIL-12R beta 1 and designated the newly identified subunit as huIL-12R beta 2, huIL-12R beta 2 is an 862-amino acid type I transmembrane protein with a 595-amino-acid-long extracellular domain and a cytoplasmic tail of 216 amino acids that contains threetyrosine residues, A cDNA encoding the mouse homolog of the huIL12R beta 2 protein has also been isolated, Human and mouse IL-12R beta 2 proteins show a 68% amino acid sequence identity, When expressed in COS-7 cells, huIL-12R beta 2 exists as a disulfide-linked oligomer with anapparent monomeric molecular weight of 130 kDa, Coexpression of the two identified IL-12R subunits in Ba/F3 cells conferred IL-12 responsiveness, and clones of these cotransfected Ba/F3 cells that grew continuously in the presence of IL-12 were isolated and designated LJM-1 cells, LJM-1 cells exhibited dose-dependent proliferation in response to huIL-12, with an ED(50) of about 1 pM huIL-12, Interestingly, Ba/F3 cells transfected with IL-12R beta 2 alone proliferated In response to huIL-12 with an ED(50) of about 50 pM, although a role for endogenous mouse IL-12R beta 1 in IL-12 signal transduction in these transfectants cannot be ruled out, These results demonstrate that the functional high-affinity IL-12R is composed of at least two beta-type cytokine receptor subunits, each independently exhibiting a low affinity for IL-12.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/10/20 alle ore 04:37:13