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Vol. 27, Issue 1, 122-124, January 1999
Instituto de Fisiología Experimental, CONICET-Universidad
Nacional de Rosario, Facultad de Ciencias Bioquímicas y
Farmacéuticas, Suipacha 570, Rosario, Argentina (M.G.L., V.A.C.,
E.J.S.-P., A.D.M.); and
Department of Pharmacology, College of
Medicine, University of Kentucky, Lexington, Kentucky (M.V.)
Hepatic glutathione S-transferase (GST) activity is
increased in postpartum female rats, a phenomenon that depends on the lactation stimulus. Here we evaluated the effect of prolactin (PRL)
administration on hepatic enzyme activity and on the expression of the
major subunits of the
- (rGSTA1, rGSTA2, rGSTA3) and µ-classes (rGSTM1, rGSTM2). A similar study was conducted in lactating (LM) and
in nonlactating (NLM) mother rats 14 days after delivery and in virgin
female rats (V). Ovine PRL (oPRL) was administered to ovariectomized
rats at daily doses of 75, 150, 200, and 300 µg/100 g b.wt. (PRL1,
PRL2, PRL3, and PRL4, respectively) for 4 consecutive days. GST
activity was measured using 1-chloro-2,4-dinitrobenzene as substrate.
The relative content of the different subunits was determined by
Western blot. oPRL produced a dose-dependent increase in GST activity
(60% at the highest dose). Subunit analysis performed in PRL2 and PRL4
revealed a substantial enhancement in rGSTM2 and to a lesser extent in
rGSTM1, in response to oPRL. The effect was also dose-dependent.
-Class subunits were increased only slightly after hormone
treatment. A 60% increase in GST activity was observed for LM relative
to NLM and V. As was observed for PRL treatment, the increase was
associated with changes in the expression of µ-class subunits whereas
-class subunits were not affected by lactation. Taken together these
data would indicate a role of PRL in regulating GST activity postpartum
via an increase in the content of µ-class subunits, particularly rGSTM2.
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