Murine cells have been shown to produce Interleukin-12 homodimer (IL-12p80) (Gillessen et al. 1995). In a cell-free system porcine Interleukin 12 homodimer (IL-12p80) is formed from two subunits of Interleukin 12 subunit beta (IL12B, IL-12p40), stabilized by a disulfide link. The cysteine in position 197 of IL12B is required for homodimer formation. Prolyl 4-hydroxylase subunit beta (P4HB), in this article referred to as protein disulfide isomerase (PDI), can act as a chaperone to induce homodimer formation (Martens et al. 2000). Human cells do not produce IL-12p80 under normal conditions (Ling et al. 1995), when however expressed acts as an antagonist of Interleukin-12 signaling, competing with the Interleukin 12 heterodimer (IL12) for its receptor (Ling et al. 1995).
Stern, AS, Hollfelder, K, Su, C, Hakimi, J, Gubler, U, Gately, MK, Lin, P, Pan, YC, Ling, P
Garbers, C, Plöhn, S, Lang, PA, Grötzinger, J, Lokau, J, Moll, JM, Aparicio-Siegmund, S, Scheller, J, Schröder, J, Grusdat, M, Rose-John, S
Vandenbroeck, K, Billiau, A, Alloza, I, Scott, CJ, Martens, E
protein disulfide isomerase activity of P4HB [endoplasmic reticulum lumen]
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