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Induction of cytochrome p450 1A1 and 1B1 by photooxidized tryptophan in transformed human keratinocytes.

L-Tryptophan was oxidized by UVA, UVB, or UVC irradiation and the effect of oxidized tryptophan (OT) was investigated for its ability to induce CYP1A1 and 1B1 in a human keratinocyte cell line (HaCat). The results obtained demonstrate that tryptophan oxidized by UVA, UVB, or UVC produced photoproducts which caused a significant induction of 7-ethoxyresorufin O-deethylase (EROD) activity in HaCat cells. The induction of EROD activity by UVB-OT was studied in greater detail. The results demonstrate that induction of EROD activity by UVB-OT was dose- and time-dependent. Results with immunoblot analyses showed that administration of UVB-OT, but not unoxidized tryptophan, caused a marked induction of CYP1A1 and 1B1 proteins in HaCat cells.[1]

References

  1. Induction of cytochrome p450 1A1 and 1B1 by photooxidized tryptophan in transformed human keratinocytes. Sindhu, R.K., Wagner, F.E., Kikkawa, Y. Adv. Exp. Med. Biol. (2003) [Pubmed]
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