The binding of 125I-labeled ovine prolactin (125I-oPRL) to membranes from the kidney, epidermis, liver, and testis of Xenopus laevis adult specimens either kept in an aquatic environment or exposed for 2 weeks to dehydrating conditions was studied. Prolactin binding specificity was assayed through competition with several unlabeled hormones (oPRL, hGH, rGH, rLH, and porcine insulin). In the animal exposed to dehydrating conditions a statistically highly significant reduction in prolactin binding to the membranes from the kidney and epidermis was recorded. No significant variations were revealed by the membranes from the liver and testis. The reduction detected in the binding of 125I-oPRL is not related to the dissociation constant, but to the number of PRL binding sites. Since PRL ranks among the few peptide hormones whose rise in the bloodstream promotes an increase in the number of their own receptors, the reduction of its binding sites in Xenopus specimens exposed to dehydration might lend some support to our earlier hypothesis that transfer to a dehydrating environment may bring about, in this totally aquatic species, some decrease in the blood PRL levels.
Prolactin binding sites in Xenopus laevis tissues: comparison between normal and dehydrated animals
MUCCIOLI, Giampiero;PATTONO, Paola Maria;
1987-01-01
Abstract
The binding of 125I-labeled ovine prolactin (125I-oPRL) to membranes from the kidney, epidermis, liver, and testis of Xenopus laevis adult specimens either kept in an aquatic environment or exposed for 2 weeks to dehydrating conditions was studied. Prolactin binding specificity was assayed through competition with several unlabeled hormones (oPRL, hGH, rGH, rLH, and porcine insulin). In the animal exposed to dehydrating conditions a statistically highly significant reduction in prolactin binding to the membranes from the kidney and epidermis was recorded. No significant variations were revealed by the membranes from the liver and testis. The reduction detected in the binding of 125I-oPRL is not related to the dissociation constant, but to the number of PRL binding sites. Since PRL ranks among the few peptide hormones whose rise in the bloodstream promotes an increase in the number of their own receptors, the reduction of its binding sites in Xenopus specimens exposed to dehydration might lend some support to our earlier hypothesis that transfer to a dehydrating environment may bring about, in this totally aquatic species, some decrease in the blood PRL levels.
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