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).
Aparicio-Siegmund, S, Moll, JM, Lokau, J, Grusdat, M, Schröder, J, Plöhn, S, Rose-John, S, Grötzinger, J, Lang, PA, Scheller, J, Garbers, C
Ling, P, Gately, MK, Gubler, U, Stern, AS, Lin, P, Hollfelder, K, Su, C, Pan, YC, Hakimi, J
Martens, E, Alloza, I, Scott, CJ, Billiau, A, Vandenbroeck, K
protein disulfide isomerase activity of P4HB [endoplasmic reticulum lumen]
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