文摘
Ovarian pieces containing postvitellogenic follicles were incubated in vitro with different concentrations of the catecholestrogen 2-hydroxyestradiol-17¦Â (2-OHE2) to evaluate its effects on steroid production and germinal vesicle breakdown (GVBD) in the catfish Heteropneustes fossilis. The incubation with 2-OHE2 induced a shift in steroidogenic pattern: the C19 and C18 steroids testosterone (T) and estradiol-17¦Â (E2), respectively were significantly decreased with a concomitant significant increase in the C21 steroids progesterone (P4), 17-hydroxyprogesterone (17-OHP), 17,20¦Â-dihydroxy-4-pregnen-3-one (17,20¦Â-DP), 17,20¦Á-dihydroxy-4-pregnen-3-one (17,20¦Á-DP) and cortisol (F). Concomitantly, the catecholestrogen induced dose-dependently GVBD response, the first sign of meiosis resumption. The co- and pre-incubations of the ovarian pieces with 2-OHE2, and adrenergic (phentolamine, ¦Á-blocker and propranolol, ¦Â-blocker) or estrogen (tamoxifen) receptor blockers resulted in inhibition of the stimulatory effect of the catecholestrogen on C21 steroids and reversed the inhibition of testosterone and E2. The ¦Á-blocker was more effective than the ¦Â-blocker. Our results suggest that 2-OHE2 appears to employ both adrenergic (¦Á-type) and estrogen receptor mechanisms in mediating the effects. The co- or pre-incubation of ovarian pieces with IBMX (a cAMP elevating drug), H89 (a protein kinase A inhibitor), and PD098059 (a MAP kinase kinase inhibitor) significantly inhibited the stimulatory effect of 2-OHE2 on the C21 steroids. The effect of chelerythrine (a protein kinase C inhibitor), on the other hand, varied with the incubation condition. In the co-incubation, the steroids showed varied effects: 17,20¦Â-DP, testosterone and E2 were elevated, and P4 and 17-OHP were decreased. In the pre-incubation set up, all the steroids were inhibited except E2. The inhibition by the blockers was higher in the pre-incubation groups. Taken together, the data suggest the involvement cAMP-protein kinase A, protein kinase C and MAP kinase pathways in the modulation of the steroidogenic activity.