Involvement of lysosomes in substrate stabilization of tryptophan-2,3-dioxygenase in rat liver.
Administration of tryptophan or hydrocortisone to rats caused a several-fold increase in tryptophan-2,3-dioxygenase activity in the liver. Highly purified lysosomes were isolated from livers of tryptophan- or hydrocortisone-treated animals as well as the control rats. Immunoblotting of lysosomal proteins with anti-tryptophan-2,3-dioxygenase showed 48 kDa band, corresponding to the subunit molecular weight of the enzyme. The relative amount of the immuno-reactive substance in the lysosomes from hydrocortisone-treated rats was 3 times higher than the control while the value in the lysosomes from tryptophan-treated rats was essentially the same as in the control. These results indicate that administration of tryptophan renders cytosolic tryptophan-2,3-dioxygenase less vulnerable to lysosomal uptake and causes an accumulation of the enzyme in the cytosol.[1]References
- Involvement of lysosomes in substrate stabilization of tryptophan-2,3-dioxygenase in rat liver. Sato, A., Endo, Y., Natori, Y. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
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