2. Academic Validation
  3. Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12

Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12

  • Immunity. 2000 Nov;13(5):715-25. doi: 10.1016/s1074-7613(00)00070-4.
B Oppmann 1,  R Lesley,  B Blom,  J C Timans,  Y Xu,  B Hunte,  F Vega,  N Yu,  J Wang,  K Singh,  F Zonin,  E Vaisberg,  T Churakova,  M Liu,  D Gorman,  J Wagner,  S Zurawski,  Y Liu,  J S Abrams,  K W Moore,  D Rennick,  R de Waal-Malefyt,  C Hannum,  J F Bazan,  R A Kastelein
Affiliations

Affiliation

  • 1 DNAX Research Institute, Palo Alto, CA 94304, USA.
PMID: 11114383 DOI: 10.1016/s1074-7613(00)00070-4
Abstract

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-12R beta 1 but fails to engage IL-12R beta 2; 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.

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