Evidence for an involvement of vitellogenin in the steroidogenic activity of rainbow trout (Oncorhynchus mykiss) vitellogenic oocytes

Citation
Ma. Reis-henriques et al., Evidence for an involvement of vitellogenin in the steroidogenic activity of rainbow trout (Oncorhynchus mykiss) vitellogenic oocytes, GEN C ENDOC, 117(2), 2000, pp. 260-267
Citations number
27
Categorie Soggetti
Endocrinology, Nutrition & Metabolism
Journal title
GENERAL AND COMPARATIVE ENDOCRINOLOGY
ISSN journal
00166480 → ACNP
Volume
117
Issue
2
Year of publication
2000
Pages
260 - 267
Database
ISI
SICI code
0016-6480(200002)117:2<260:EFAIOV>2.0.ZU;2-A
Abstract
In vivo and in vitro the concentration of vitellogenin (VTG) inside the ooc yte can alter VTG production by the liver, modulating the synthesis of 17 b eta-estradiol (E-2) by the ovary. To gain a greater insight into this mecha nism, the in vitro production of free and conjugated testosterone (T), E-2, and androstenedione (A) by rainbow trout oocytes from the early and middle vitellogenic stage was measured by radioimmunoassay. There was a decreased E-2 production that was greater in September (40%) than October (30%), by the oocytes incubated with the vitellogenic fraction. The production of E-2 conjugated as glucuronide was lower than sulfate (P < 0.05), but similar i n control and VTG-incubated oocytes. levels of free T increased from Septem ber to October, and conjugates were both produced at low levels, and no dif ferences were detected between control and incubated VTG oocytes. The decre ased synthesis of E-2 by oocytes incubated with VTG was not followed by an increase in the amount of T or conjugated E-2, because there were no differ ences under the two circumstances. However, there was a reduced synthesis o f A with oocytes producing low levels of E-2. These results suggest that th e presence of high levels of VTG in the oocyte suppresses the synthesis of A and E-2, affecting the activities of the enzymes C17,20 lyase and aromata se and probably interfering with the heme protein cytochrome P450 which in the ovary catalyses C 17,20 lyase (P450 c17) and aromatase (P450arom). (C) 2000 Academic Press.