Possible mechanism for the first response to short captivity stress in the water frog, Rana esculenta.
J Endocrinol
; 148(2): 233-9, 1996 Feb.
Article
em En
| MEDLINE
| ID: mdl-8699137
ABSTRACT
To clarify the endocrine mechanism involved in the short captivity stress in the water frog, Rana esculenta, the activity of 9-ketoreductase, the enzyme which converts prostaglandin E2 (PGE2) into prostaglandin F2 alpha (PGF2 alpha), and aromatase, which converts testosterone into oestradiol-17 beta, were studied. Adult male and female frogs were sacrificed 0, 1.5, 3, 6, 12, 24, 48, 72, 168 and 336 h after capture in the field. PGE2, PGF2 alpha, progesterone, testosterone, oestradiol-17 beta and corticosterone plasma levels were detected by RIA at each time point. 9-Ketoreductase (conversion of [3H]PGE2 into [3H]PGF2 alpha) and aromatase (conversion of [3H]testosterone into [3H]oestradiol-17 beta) activities in the brain, testis, ovary and interrenal were also determined at each time point. After capture, levels of plasma PGF2 alpha increased (male 228%; female 288%) and PGE2 decreased (male 68%; female 81%) at 1.5 h, oestradiol-17 beta increased (male 399%; female 425%) and testosterone decreased (male 87%; female 83%) at 6 h, and corticosterone increased (male 421%; female 426%) at 72 h. 9-Ketoreductase activity in the brain was enhanced at 1.5 h after capture (male 249%; female 262%); aromatase activity increased at 6 h in the testis (261%), ovary (273%) and interrenal (male 227%; female 267%). These results indicate that short captivity stress could induce an increase in plasma PGF2 alpha through activation of brain 9-ketoreductase. In turn, PGF2 alpha might enhance the levels of circulating oestradiol-17 beta through activation of gonadal and interrenal aromatase.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Rana esculenta
/
Estresse Psicológico
/
Encéfalo
/
Aromatase
/
Hidroxiprostaglandina Desidrogenases
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Ano de publicação:
1996
Tipo de documento:
Article