Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mouse kidney beta-glucuronidase production is under multihormonal control. In normal mice, kidney glucuronidase is induced over 100-fold by testosterone. However, hypophysectomy reduces this induction to about 5% of normal. This loss in inducibility was in part restored by growth hormone. Simultaneous administration to hypophysectomized female mice of growth hormone and testosterone, but not of prolactin and testosterone, restored kidney glucuronidase concentration to half that found in testosterone-treated normal female mice. Growth hormone alone had no effect in hypophysectomized females nor did it enhance glucuronidase activity in testosterone-treated normal females. Radiolabeling experiments demonstrated that the enhancement by growth hormone of glucuronidase activity was accompanied by a corresponding increase in its rate of synthesis. Kidney hypertrophy and kidney glucuronidase production may be under common hormonal regulation. Testosterone or growth hormone treatment alone of hypophysectomized mice had little or no effect on either process, but combined treatment with the two hormones significantly enhanced both. The rate of synthesis of kidney glucuronidase is controlled by the Gur gene. Relative differences in kidney glucuronidase synthesis in mice of different Gur genotype were maintained in testosterone-treated hypophysectomized mice. This suggests that control of glucuronidase synthesis by the Gur locus is exerted by interaction with androgens rather than pituitary products.
Mol Cell Endocrinol 1978 Nov
PMID:Roles of growth hormone and testosterone in the synthesis of mouse kidney glucuronidase. 72 3

Injection of the opiate antagonist naloxone completely prevented the rise of serum prolactin induced by ether stress in intact male rats. Naloxone also led to a 50--95% inhibition of the marked elevation of plasma prolactin levels induced by suckling. These data suggest that endogenous opiates (endorphins) are involved in the stimulation of prolactin release induced by both stress and suckling in the rat.
Mol Cell Endocrinol 1978 Dec
PMID:Evidence for a role of endorphins in stress- and suckling-induced prolactin release in the rat. 73 23

Intravenous (iv) administration of 5 microgram of arginine vasotocin (AVT) into urethane-anesthetized, castrated male rats had no effect on plasma prolactin titers as compared to the rise in prolactin levels observed in intact AVT-treated rats. However, when castrated rats were first treated for two days with 2.5 mg/day of testosterone propionate and then challenged with a 5-microgram dose of AVT, the prolactin surge values obtained were comparable to those seen in intact AVT-treated rats. Conversely, treatment of intact rats for two days with 25 mg/day of the anti-androgen, cyproterone acetate, blocked the prolactin-releasing activity of AVT. In a separate experiment, treatment of castrated rats for two days with 2.5 mg/day of testosterone, androsterone or 50 microgram of estradiol benzoate and 25 mg progesterone, completely restored the prolactin-releasing activity of AVT. Similar treatment with 2.5 mg/day of androstenedione or dihydrotestosterone was without effect in restoring this response to AVT. It is concluded that the presence of gonadal steroids is essential to the action of AVT in provoking the release of prolactin in urethane-anesthetized male rats.
Mol Cell Endocrinol 1978 Dec
PMID:Effect of several androgens, cyproterone acetate or estrogen-progesterone on the prolactin-releasing activity of arginine vasotocin in castrated male rats. 73 24

A kinetic study of the influence of thyreotrope-releasing hormone (TRH) on prolactin turnover and synthesis by a new rat pituitary prolactin cell line (SD1) has been performed by means of pulse-chase experiments. After a 10-min [3H]leucine pulse, the chase was carried out in the presence or absence of TRH (54 nM), cycloheximide (3.6 X 10(-5)M) and/or [14C]-proline. The prolactin content of the cells in the medium was estimated using a radioimmunoassay technique. The specific radioactivity of prolactin in the medium was estimated after its isolation by disc gel electrophoresis. This kinetic study demonstrated, firstly, a rapid intracellular transit of newly synthesized prolactin (15 + 10 min or less); secondly, the existence of at least two intracellular prolactin pools; thirdly, a rapid effect of TRH on release of stored prolactin, which is independent of de novo protein synthesis, and fourthly, a delayed stimulating effect of TRH on prolactin synthesis.
Mol Cell Endocrinol 1975 Nov
PMID:Effect of thyreotrope-releasing hormone (TRH) on prolactin turnover in culture. 81 96

The prostate glands of rats, mice, guinea pigs and hamsters were found to be a rich source of enzymes catalyzing the Mn2+-dependent transfer of galactose from UDP-galactose to glycoprotein acceptors such as ovomucoid and ovalbumin. The ventral prostate was also very active in promoting transfer of fucose from GDP-fucose to ovomucoid. The prostatic enzymes promoting both galactosyl and fucosyl transfers to glycoproteins were very largely membrane-bound, and were markedly activated by the non-ionic detergent Triton X-100. Castration of adult male resulted in a many-fold and roughly parallel decline in both glycosyltransferase activities over a period of two weeks, which was reversed by subsequent daily treatment with testosterone for 8 days. The very low galactosyltransferase of the ventral prostate of hypophysectomized rats was markedly enhanced by testosterone administration, whereas prolactin alone or in combination with androgen had no significant effect.
Mol Cell Endocrinol
PMID:Glycoprotein glycosyltransferases in male reproductive organs and their hormonal regulation. 82 97

20alpha-Hydroxysteroid dehydrogenase (20 alpha-SDH) activity increases in the cycling corpus luteum of the rat, beginning at 14.00 h on the day of diestrus, but remains low in corpora lutea of pregnancy throughout the first 19 days of gestation. When cells derived from 7-day-old corpora lutea of pregnant rats were cultured for 7 or 12 days, there was a spontaneous rise in 20 alpha-SDH activity from an initial value of 0.44 +/- 0.27 to 4.1 +/- 0.7 units/mg supernatant protein. Addition of LH (NIH-S-18; 2.0 mug/ml) or prostaglandin F2alpha (2.8 X 10(-5) M) to the medium from day 4 to the end of incubation period caused a slight but significant reduction in 20 alpha-SDH activity (20%, P less than 0.05). Supplementation of the medium with ovine prolactin (HIH-P-S11; 10.0 mug/ml) from the time of seeding or from the 2nd to 4th day of culture reduced the activity of 20 alpha-SDH measured on day 12 by 61% (P less than 0.001). This finding suggests that the suppression of 20 alpha-SDH by prolactin, hitherto demonstrated only in vivo results from a direct action of the hormone on the luteal cell.
Mol Cell Endocrinol 1977 Feb
PMID:Suppression of 20 alpha-hydroxysteroid dehydrogenase activity in cultured rat luteal cells by prolactin. 83 17

Mouse mammary epithelial cells in confluent primary monolayer cultures retain responsiveness to the specific hormones that induce mammary growth in vivo. Simultaneous stimulation by prolactin, progesterone and estrogen, in the presence of 5 percent fetal calf serum, is required to induce an increase in both thymidine uptake into DNA and in cell replication (as judged by mitotic indexes) over the hormone-free control. This increase in mitogenic response could not be elicited in either mouse fibroblasts or in mouse mammary tumor cells, the latter known to be hormone insensitive.
Mol Cell Endocrinol 1977 Aug
PMID:Response to prolactin and ovarian steroids of normal mammary epithelial cell cultures. 92 11

An analysis of primary structures for local similarities has been performed for a number of protein hormones. The statistical MacLachlan's technique and three matrices of amino acids similarities: in respect to the genetic code (M1), physico-chemical properties (M2), interchangeability of amino acids in homologous proteins (M3) have been used. When comparing prolactin and growth hormones, four zones of high structural similarity have been found. Comparison of beta-subunits of interstitial-cell and thyroid-stimulating hormones has shown two zones of high similarity. Using M3 matrice, non-homogeneity of the self local similarity of structure has been shown for prolactin, growth hormone, beta-lipotropin, proinsulin and parathormone. For the latter three hormones, the high evolutionary conservative regions coincide with the active sites of structure. It is suggested that such regions in the structures of prolactin and growth hormone also provide the active function.
Mol Biol (Mosk)
PMID:[An analysis of local similarities in the primary structures of protein hormones]. 94 64

The effect of ovine prolactin on the renal 25-hydroxycholecalciferol-1-hydroxylase was studied in the chick. Prolactin was found to increase the activity of this enzyme in both long-term and short-term experiments. In the long term, 7 days treatment with prolactin caused a marked stimulation of the 1-hydroxylase activity, however this effect was only seen when the enzyme was assayed 2-3 hours after the final injection of prolactin. A single subcutaneous injection of prolactin was also effective in increasing the 1-hydroxylase activity, this effect was maximal at one hour and had largely disappeared 3 hours after prolactin administration.
Mol Cell Endocrinol
PMID:Effect of prolactin on vitamin D metabolism. 95 48

Total polysomal RNA or poly(A)-containing RNA isolated from membrane-bound polysomes of normal lactating rabbits directed the synthesis of casein in a reticulocyte lysate. Casein was identified by immunoprecipitation followed by SDS-polyacrylamide gel electrophoresis of the immunoprecipitate. The poly(A)-containing RNA was heterogeneous with one major peak corresponding to a 12-S sedimentation coefficient as determined by polyacrylamide gel electrophoresis. Using the same procedure, mRNAs isolated from the non-secreting tissue of pseudopregnant rabbits were found not to contain the 12-S peak and were unable to direct the synthesis of casein in vitro. Prolactin injected into pseudopregnant rabbits induced the synthesis of proteins immunoprecipitable by anti-casein anti-serum and induced the simultaneous appearance of the 12-S mRNA. Progesterone injected with prolactin prevented the induction of casein synthesis and the appearance of mRNA for casein. A close relationship was established between the ability of the tissue to synthesize immunoprecipitable casein and the corresponding mRNA content of polysomes.
Mol Cell Endocrinol 1975 Jul
PMID:Regulation of casein synthesis in the rabbit mammary gland. Titration of mRNA activity for casein under prolactin and progesterone treatments. 114 19


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