| First Author | Oppmann B | Year | 2000 |
| Journal | Immunity | Volume | 13 |
| Issue | 5 | Pages | 715-25 |
| PubMed ID | 11114383 | Mgi Jnum | J:65966 |
| Mgi Id | MGI:1927676 | Doi | 10.1016/s1074-7613(00)00070-4 |
| Citation | Oppmann B, et al. (2000) Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12. Immunity 13(5):715-25 |
| abstractText | A novel sequence discovered in a computational screen appears distantly related to the p35 subunit of IL-12. This factor, which we term p19, shows no biological activity by itself; instead, it combines with the p40 subunit of IL-12 to form a novel, biologically active, composite cytokine, which we term IL-23. Activated dendritic cells secrete detectable levels of this complex. IL-23 binds to IL-12Rbeta1 but fails to engage IL-12Rbeta2; nonetheless, IL-23 activates Stat4 in PHA blast T cells. IL-23 induces strong proliferation of mouse memory (CD4(+)CD45Rb(low)) T cells, a unique activity of IL-23 as IL-12 has no effect on this cell population. Similar to IL-12, human IL-23 stimulates IFN-gamma production and proliferation in PHA blast T cells, as well as in CD45RO (memory) T cells. |
