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Involvement of lysosomes in substrate stabilization of tryptophan-2,3-dioxygenase in rat liver.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Sato A,Endo Y,Natori Y

doi

10.1016/0006-291x(92)91644-6

subject

Has Abstract

pub_date

1992-02-28 00:00:00

pages

306-11

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)91644-6

journal_volume

183

pub_type

杂志文章

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