Interleukin 23

IL12B
Crystal structure of IL-12B
Identifiers
Symbol	IL12B
Alt. symbols	CLMF2, NKSF2, p40
Entrez	3593
HUGO	5970
OMIM	161561
PDB	1F42
RefSeq	NM_002187
UniProt	P29460
Other data
Locus	Chr. 5 q31.1-33.1

Interleukin-23 (IL-23) is a heterodimeric cytokine composed of an IL12B ( IL-12p40 )subunit (that is shared with IL12 ) and the IL23A ( IL-23p19 ) subunit. A functional receptor for IL-23 (the IL-23 receptor) has been identified and is composed of IL-12R β1 and IL-23R.

IL-23 was first described by Robert Kastelein and colleagues at the DNAX research institute using a combination of computational, biochemical and cellular immunology approaches.

Prior to the discovery of IL-23, IL-12 had been proposed to represent a key mediator of inflammation in mouse models of inflammation. However, many studies aimed at assessing the role of IL-12 had blocked the activity of IL-12p40, and were therefore not as specific as thought. Studies which blocked the function of IL-12p35 did not produce the same results as those targeting IL-12p40 as would have been expected if both subunits formed part of IL-12 only.

The discovery of an additional potential binding partner for IL-12p40 led to a reassessment of this role for IL-12. Seminal studies in experimental autoimmune encephalomyelitis, a mouse model of multiple sclerosis, showed that IL-23 was responsible for the inflammation observed, not IL-12 as previously thought. Subsequently, IL-23 was shown to facilitate development of inflammation in numerous other models of immune pathology where IL-12 had previously been implicated including models of arthritis, intestinal inflammation, and psoriasis.