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PubMed1980

Mechanism of prolactin action.

Most experimental information regarding the mechanism of action of prolactin in its diverse array of target tissues has been discovered using mammary tissues. Evidence has recently been presented that suggests that prolactin may be "internalized" into its target cells and have intracellular actions. Accordingly, it has been reported that prolactin stimulates RNA synthesis in isolated nuclei from mammary tissues; and by immunoflorescent studies, prolactin has been located within its target cells. It has been further suggested from additional experimental studies that the primary action of prolactin may involve its initial interaction with fixed plasma membrane receptor sites. Subsequent actions of prolactin may involve the following: a) an increased intracellular concentration of potassium and a reduced level of sodium, b) an increased level of cGMP and a reduced level of cAMP, c) an enhanced rate of prostaglandin biosyntheesis mediated by a stimulation of phospholipase A2 activity, and d) a stimulation of polyamine synthesis. It has also been shown that the actions of prolactin require calcium ions in the extracellular environment. Laboratory studies have thus indicated that the actions of prolactin may be carried out by a number of processes; but a single, primary action of this hormone that accounts for all of its actions has not yet been proven.

Animals↗
PubMed1980

Role of prolactin in regulating gonadotropin secretion and gonad function in female rats.

The role of prolactin in female reproduction has been studied extensively in two systems; in the regulation of corpus luteum function, and in the regulation of gonadotropin secretion. In the rat, prolactin is an essential component of the luteotropic complex since it is the hormone responsible for transforming a corpus luteum of the estrous cycle into a corpus luteum of pseudopregnancy or pregnancy, which allows progesterone secretion to be maintained. The biphasic surges of prolactin initiated by cervical stimulation at the time of ovulation continue to be important throughout pseudopregnancy to maintain elevated levels of progesterone. During pregnancy, the luteotropic requirements change so that prolactin is no longer required after midpregnancy. In addition to its luteotropic effects, prolactin also has antigonadotropic effects that contribute significantly to the suppression of gonadotropin secretion during lactation. Suckling-induced prolactin secretion contributes to the suppression of both basal gonadotropin secretion and the postcastration rise in gonadotropins during lactation. Prolactin may have some effect at the pituitary to suppress responsiveness to luteinizing hormone-releasing hormone (LHRH), but its primary site of action appears to be the hypothalamus. Prolactin may be acting at the hypothalamus either to cause a decrease in LHRH secretion or to cause the release of substances that inhibit pituitary gonadotropin secretion directly.

Animals↗
PubMed1982

[Concentration and forms of prolactin in circulating blood and lymph of lactating goats during milking and injections of exogenous hormone].

Using the radioimmunological method, the dynamics of concentration as well as the content of monomeric and dimeric prolactin forms in the blood and lymph of the goat mammary gland were studied in the course of milking and after i.v. administration of exogenous hormone. The maximum prolactin concentration in lymph was lower than that in blood by 57.7 +/- 0.9 ng/ml. This difference is due to disappearance of the monomeric prolactin form, possibly as a result of binding of the hormone with receptors. The injections of 0.4 mg prolactin caused a two-fold increase in the peak of hormone concentration in comparison with that usually observed during milking. After 3-4 hormone injections the ratio of the maximum prolactin concentrations in lymph and blood approximated 1. This effect is associated with the negative regulation of prolactin receptors. When injecting prolactin between milkings, the difference of the maximum prolactin concentrations in lymph and in blood was two times lesser than during milking.

Animals↗
PubMed1982

[Plasma prolactin in middle-aged and elderly, hypertension patients over 60 and in persons with hyperlipoproteinemia].

Plasma prolactin level was studied in 92 practically healthy subjects, distributed into three age groups--20-44, 60-74 and 75-90 as well as in 25 patients with hypertonic disease (HD) aged over 60 and 30 subjects with hyperlipoproteinemia. Plasma prolactin was determined radioimmunologically. The results obtained show that plasma prolactin level is not essentially changed with age advancing. A tendency of plasma prolactin reduction in elderly and aged people is observed but the difference versus the control group is statistically insignificant. The females from the young age group, show significantly higher values of prolactin versus the males. In the elderly and aged people, the differences according to sex in prolactin level disappears, most likely due to dying out of ovarian function of the females and reduction of the stimulating effect of estrogens upon prolactin secretion. The patients with hypertonic disease over 60 and the males with hyperlipoproteinemia show a significant elevation of plasma prolactin as compared with the subjects from the control group.

Adult↗
PubMed1980

Immunochemical isolation of prolactin messenger RNA.

Prolactin mRNA has been isolated using immunochemical techniques. Initial experiments demonstrated that 125I-labeled prolactin antibody was able to bind to pituitary polysomes but not to liver polysomes, suggesting that the binding is specific. Prolactin-synthesizing polysomes were immunoprecipitated by reaction with antiprolactin followed by anti-antibody. Immunoprecipitated polysomal RNA was chromatographed on oligo(dT)-cellulose, and the poly(A) RNA was sedimented through a sucrose gradient. This procedure resulted in a 320-fold purification of prolactin mRNA as determined by translation in a mRNA-dependent reticulocyte lysate assay. Translation analysis also suggested that the isolated prolactin mRNA is greater than 95% pure. The molecular weight of prolactin mRNA determined by electrophoresis on agarose gels containing 10 mM mercury hydroxide was 350,000. Purified prolactin mRNA was used to synthesize full-length cDNA by means of avian myeloblastosis reverse transcriptase. Use of this cDNA as a hybridization probe demonstrated that estrogen is able to increase the concentration of prolactin mRNA sequences in the pituitary.

Animals↗
PubMed1980

Interactions between hypothalamic and peripheral hormones in the control of prolactin secretion.

The absence of nerve terminals in the anterior pituitary gland offers the possibility of studying a pure population of dopamine (DA) receptors. This study is facilitated by the use of anterior pituitary cells in primary culture, which permit the measurement of a precise parameter under typical dopaminergic control, namely prolactin secretion. On the other hand, since DA is the main hypothalamic factor controlling prolactin secretion, in vivo changes of plasma prolactin levels can be used as an index of DA release from the hypothalamus. Treatment with estrogens not only stimulates basal prolactin secretion but also can reverse the inhibitory effect of DA on prolactin secretion in vivo and in vitro. As assessed by the increased plasma prolactin levels following administration of a maximal dose of the DA antagonist thioproperazine, estrogens increase DA release from the hypothalamus. Progesterone, although inactive alone, can reverse the effect of estrogens on prolactin secretion both in vivo and in vitro. Under the same experimental conditions, dihydrotestosterone exerts inhibitory effects on spontaneous prolactin secretion and can reverse the stimulatory effects of estrogens.

Animals↗
PubMed1995

[The influence of recombinant human erythropoietin (rHu-EPO) on circadian rhythm of prolactin secretion in patients with chronic renal failure treated with hemodialysis].

Patients with chronic renal failure (CRF) have high serum prolactin level. In healthy subjects the circadian rhythm of prolactin secretion is well known. This study aimed to investigate, if the circadian rhythm of prolactin was maintained in patients with CRF treated with haemodialysis despite hyperprolactinaemia, and how the treatment with erythropoietin influenced the circadian rhythm of prolactin. Serum prolactin was determined four times a day at 6:00, 12:00, 18:00, 24:00 in 30 patients with CRF and in 15 healthy subjects. In the patients with CRF this investigation was both done on the day with haemodialysis and on the day without haemodialysis. The patients were divided into two groups: the first one included patients treated with erythropoietin and the second one included patients not treated with erythropoietin. The results of the investigation were analysed using the Cosinor test. Serum concentration of hormones was determined by LIA. It was shown that the circadian rhythm of prolactin was maintained in patients with CRF both on the day with and without haemodialysis. Both in patients with CRF and in healthy subjects the circadian rhythm indicated the highest serum concentration of prolactin in the night hours i.e. 22:30-1:00. In patients treated with erythropoietin a significantly lower average day concentration of prolactin was observed in comparison with patients not treated with erythropoietin.

Adult↗
PubMed1979

Purification of pre-prolactin mRNA from bovine anterior pituitary glands.

Total cytoplasmic RNA, isolated from bovine anterior pituitary glands, directed the synthesis of primarily two proteins in a wheat germ cell-free system. Analysis of wheat germ cell-free products by sodium dodecyl sulfate-slab gel electrophoresis, direct immunoprecipitation with prolactin aatibody, and prolactin- and growth hormone-specific radioimmunoassay indicated that the two proteins were pre-prolactin and pre-growth hormone. Agarose-urea-gel electrophoresis of poly(A)-containing RNA revealed the presence of a large symmetrical RNA peak with an estimated size of approximately 15 S. The RNA contained in this peak was eluted from the gel and translated in the wheat germ cell-free system. Analysis of the translation products by electrophoresis, direct immunoprecipitation, and radioimmunoassay resulted in the detection of only pre-prolactin. The extent of pre-prolactin mRNA purification was assessed by synthesizing DNA complementary to gel-purified pre-prolactin mRNA and then following the hybridization of this cDNA to gel purified pre-prolactin mRNA. The result of this hybridization is consistent with the cell-free translation studies, namely that pre-prolactin mRNA is the predominant mRNA component of pituitary poly(A)-containing RNA.

Animals↗
PubMed1994

Opioids and the pulsatile prolactin secretory pattern: effects of hyperprolactinemia.

It is well known that opioids regulate prolactin secretion through unknown mechanisms. The present study describes the effects of morphine and naloxone administration on pulsatile prolactin secretion in adult sham-operated and pituitary-grafted female rats. Animals were rendered hyperprolactinemic by transplanting 2 pituitary glands beneath the kidney capsule. Naloxone (2 mg/kg/h), morphine (50 mg/kg/h)+naloxone or saline (0.5 ml/h) were administered i.v. through a jugular cannula and bled at 7-min intervals for a period of 3 h. Pituitary grafting increased mean serum prolactin levels, the absolute amplitude and the duration of the pulses, but decreased their frequency. Naloxone, in sham-operated rats, reduced mean serum prolactin levels, the absolute amplitude and the frequency of the pulses. However, morphine+naloxone administration increased mean serum prolactin levels and the absolute amplitudes of prolactin pulses in pituitary-grafted rats. Naloxone administration did not decrease previously increased mean serum levels of prolactin in pituitary-grafted rats. These results suggest that opioids synchronize the pulsatile pattern of prolactin and that these effects are blunted in pituitary-grafted animals.

Animals↗
PubMedDate not supplied

Effects of prolactin and estrogen on cell proliferation of the mouse liver induced by partial hepatectomy.

Estrogen or prolactin suppresses mouse hepatocellular tumorigenesis induced by carcinogens through inhibition of the growth of preneoplastic hepatocytes. In the present study, we investigated whether estrogen or prolactin inhibits proliferation of normal hepatocytes as well as preneoplastic hepatocytes in mice. The proliferation of mouse hepatocytes was induced by partial hepatectomy, and DNA synthesis of the liver was evaluated by measurement of 5-[125I]iododeoxyuridine ([125I]IdUrd) uptake/mg liver DNA after an injection of [125I]IdUrd into mice. For acute treatment with estrogen or prolactin, estradiol-17 beta (E2) (1 micrograms) or ovine prolactin (140 micrograms) was injected into ovariectomized mice twice a day from the day of partial hepatectomy. For chronic treatment with estrogen, ovariectomized mice received implants of E2 pellets containing 100 micrograms E2 40 days before partial hepatectomy, and for chronic treatment with prolactin, hyperprolactinemia was induced by pituitary graft under the renal capsule of ovariectomized mice 40 days before partial hepatectomy or by daily injections of perphenazine (150 micrograms/day) beginning 40 days before partial hepatectomy. The acute treatment with either estrogen or prolactin did not affect the hepatocyte proliferation induced by partial hepatectomy. Chronic hyperprolactinemia induced by the pituitary graft or by injections of perphenazine, and the chronic treatment with E2 pellets did not suppress either basal or partial hepatectomy-induced proliferation of hepatocytes. The present results show that acute and chronic treatments with estrogen or prolactin do not inhibit proliferation of mouse normal hepatocytes, and suggest that the effects of estrogen and prolactin on proliferation of mouse hepatocytes are different from those on proliferation of preneoplastic hepatocytes.

Animals↗
PubMed2001

Expression of prolactin receptors in normal, benign, and malignant breast tissue: an immunohistological study.

AIMS: Prolactin plays an important role in the proliferation and differentiation of normal breast epithelium, and possibly in the development of breast carcinoma. The effects of prolactin are mediated by its receptor; thus, alteration in the expression of this receptor could be important in studying the biology of breast cancer. This investigation was aimed at comparing the expression of prolactin receptors in normal, benign, and malignant breast tissue. MATERIAL/METHODS: The expression of prolactin receptors was studied in paraffin wax embedded sections of 102 breast biopsies (93 female and nine male), using the monoclonal antibody B6.2, and the avidin-biotin immunoperoxidase technique. Six biopsies were normal, 34 had benign lesions, and 62 were malignant. RESULTS: In normal cases, prolactin receptor positivity was seen only on the luminal borders of the epithelial cells lining ducts and acini. In most benign lesions, variable degrees of luminal and cytoplasmic staining were seen. Cells showing apocrine metaplasia and florid regular ductal epithelial hyperplasia were mostly negative. In malignant cases, the staining pattern was mostly cytoplasmic and heterogeneous. Forty one of the 59 carcinomas in women showed a degree of positivity involving 10-100% of the tumour cells. A significant direct correlation was found between prolactin receptor and oestrogen receptor staining when only cases that scored more than 100/300 for the latter receptor, using the H scoring system, were considered (p = 0.0207). No correlation was found between prolactin receptors and progesterone receptors, patient's age, tumour size, tumour grade, or axillary lymph node status. CONCLUSIONS: Prolactin receptors seem to be expressed at different cellular sites in normal, benign, and malignant breast epithelial cells. The receptor is expressed in more than two thirds of female breast carcinomas, suggesting that it may play a role in the pathogenesis of the disease. The positivity is correlated with moderate and strong staining for oestrogen receptors in tissue sections, but not with other prognostic factors.

Adult↗
PubMed2006

Toxic effects of methoxychlor on the episodic prolactin secretory pattern: possible mediated effects of nitric oxide production.

BACKGROUND: This work addresses the issue of whether methoxychlor (MTX) exposure may modify the ultradian secretion of prolactin through changes in the synthesis of nitric oxide (NO) induced by Nomega-nitro-L-arginine methyl ester (L-NAME) in the hypothalamic-pituitary axis. Associated changes in dopamine (DA) content in the anterior (AH), mediobasal (MBH) and posterior hypothalamus (PH) and median eminence (ME) were evaluated. METHODS: Two groups of animals (MTX and MTX+L-NAME treated) received subcutaneous (sc) injections of MTX at a dose of 25 mg/kg/day for one month. The other two groups of animals (control and L-NAME treated) received sc vehicle injections (0.5 mL/day of sesame oil), during the same period of time to be used as controls. Forty hours before the day of the experiment, animals were anaesthetized with intrapritoneal injections of 2.5% tribromoethanol in saline and atrial cannulas were implanted through the external jugular vein. Plasma was continuously extracted in Hamilton syringes coupled to a peristaltic bomb in tubes containing phosphate-gelatine buffer (to increase viscosity). The plasma was obtained by decantation and kept every 7 minutes for the measurement of plasma prolactin levels through a specific radioimmnunoassay and DA concentration by high-pressure liquid chromatography (HPLC). RESULTS: Prolactin release in animals from all experimental groups analyzed was episodic. Mean plasma prolactin levels during the bleeding period, and the absolute pulse amplitude were increased after MTX or Nomega-nitro-L-arginine methyl ester (L-NAME) administration. However MTX and L-NAME did not modify any other parameter studied with the exception of relative pulse amplitude in MTX treated rats. L-NAME administration to rats treated with the pesticide reduced mean plasma prolactin levels and the absolute amplitude of prolactin peaks. Peak duration, frequency and relative amplitude of prolactin peaks were not changed in the group of rats treated with MTX plus L-NAME as compared to either control or MTX treated rats. Whereas MTX decreased DA content in the ME and increased it in the AH, its content did not change in the MBH or PH, as compared to the values found in controls. Also, L-NAME administration decreased DA content in the ME as compared to controls. However, L- NAME administration to MTX exposed rats, markedly increased DA content in the ME as compared to either MTX treated or control rats. L-NAME administration increased DA content in the AH as compared to the values found in non-treated rats. However L-NAME administration to MTX exposed rats did not modify DA content as compared to either MTX treated or control rats. L-NAME administration did not modify DA content at the MBH nor in saline treated nor in MTX treated rats. However, the values of DA in the MBH in MTX plus L-NAME treated animals were statistically decreased as compared to L-NAME treated rats. In the PH, L-NAME administration increased DA content as compared to the values found in non-treated animals. L-NAME administration to MTX exposed rats also increased DA content as compared to either MTX treated or control rats. CONCLUSION: The results suggest the existence of an interaction between MTX and L-NAME in the modulation of the ultradian prolactin secretion at the pituitary levels. The possibility of an indirect effect mediated by changes in DA content at the ME requires further examination.

Journal Article↗
PubMed1978

Purification of rat prolactin releasing factor by gel filtration.

Pregnant rat hypothalamic fragments were extracted with 30 mM Tris-HCl buffer at pH 7.8, subjected to enzymatic digestion, and applied to gel filtration on Sephadex G-25 for purification of the prolactin releasing factor. Effect of the eluted fractions on the release of prolactin were tested by the determination of serum and pituitary prolactin after the injection in lactating rats. Prolactin was estimated by radioimmunoassay. One fraction (tube number 61--73) eluted later than synthetic ACTH enhanced release of prolactin 30 min after injection, but other fractions had no effect on the release of prolactin. Prolactin releasing factor would be quantitatively predominant over prolactin inhibiting factor in pregnant rat.

Animals↗
PubMed1994

Prolactin induces phosphorylation of Tyr694 of Stat5 (MGF), a prerequisite for DNA binding and induction of transcription.

Mammary gland factor (MGF) is a transcription factor discovered initially in the mammary epithelial cells of lactating animals. It confers the lactogenic hormone response to the milk protein genes. We reported recently the isolation of the cDNA encoding MGF. MGF is a novel member of the cytokine-regulated transcription factor gene family. Members of this gene family mediate interferon alpha/beta and interferon gamma induction of gene transcription, as well as the response to epidermal growth factor and interleukin-6, and have been named signal transducers and activators of transcription (Stat). The name Stat5 has been assigned to MGF. We studied the mechanisms involved in the prolactin activation of Stat5 in COS cells co-transfected with cDNA encoding Stat5 and the prolactin receptor. Prolactin treatment of the transfected cells caused activation of Stat5 within 5-10 min. This activation does not require ongoing protein synthesis. Tyrosine kinase inhibitors prevent Stat5 activation in transfected COS cells. Treatment of recombinant Stat5 with a tyrosine-specific protein phosphatase in vitro abolishes its DNA binding activity. Prolactin stimulation of transfected cells induces Stat5 phosphorylation on tyrosine. Phosphorylation of in vitro transcribed and translated Stat5 with the Jak2 tyrosine kinase, but not with fyn, lyn or lck, confers DNA binding activity. The prolactin response of the beta-casein milk protein gene promoter can be observed in COS cells transfected with cDNA vectors encoding Stat5 and the long form of the prolactin receptor. The short form of the prolactin receptor is unable to promote Stat5 phosphorylation and confer transcriptional induction in COS cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Alkaloids↗
PubMed1982

Regional variations in the testicular dependence of prolactin binding and its possible relationship to castration-induced involution in rat prostate gland.

Prolactin binding sites of ventral, lateral, and dorsal lobes of rat prostate were examined immunohistochemically 1, 2, 4, and 8 days after castration or sham operation. In sham-operated rats each lobe exhibited a distinct pattern of intracellular and intraluminal prolactin binding. A loss in prolactin binding from epithelial cells of ventral prostate, which was visualized postcastration, was quantitated with the aid of an image analyzer and then statistically evaluated. The proportion of ventral prostate epithelial cells devoid of prolactin binding increased from approximately 13% in sham-operated rats to approximately 29% 1 day after castration, and reached a peak level of about 71% 4 days postcastration. No loss of prolactin binding was evident in either lateral or dorsal prostate up to 8 days postcastration. Direct measurement of epithelial cell heights and subsequent statistical evaluation revealed similar regional differences in the rates and extent of prostate involution. Eight days after castration ventral prostate epithelial cell heights decreased by 56% whereas lateral and dorsal lobe epithelial cells heights decreased about 25% and 14%, respectively. The apparent relationship between testicular dependence of prostatic prolactin binding and castration-induced prostatic involution are discussed in terms of possible regional variations in the prolactin-androgen interplay in prostate.

Animals↗
PubMed1977

Evaluation of research on control of prolactin secretion.

At least three substances have been reported to be present in the hypothalamus that can inhibit prolactin release, namely a PIF, catecholamines and acetylcholine. At least four substances have been reported to be present in the hypothalamus that can stimulate prolactin release, namely PRF, TRH, serotonin and prostaglandins. Neither the existence of a distinctive PIF or PRF in the hypothalamus can be considered as definitely established. The predominant action of the mammalian hypothalamus on prolactin release is inhibitory under most conditions, and is stimulatory in avian species. In addition to control by the hypothalamus, several hormones and drugs can act directly on the pituitary to alter prolactin release. The interrelationships of these agents within and without the hypothalamus on prolactin secretion are complex, and there are many questions about their mode of action. Studies on the regulation of prolactin secretion have resulted in development of many methods for either increasing or decreasing release of this important hormone, and thereby have provided opportunities for influencing lactation, growth of mammary and pituitary tumors and other tissues responsive to prolactin.

Animals↗
PubMed1984

Modulation of prolactin binding sites in vitro by membrane fluidizers. II. Age-dependent effects on rat ventral prostatic membranes.

The objectives of this study were to determine (i) if the age-related changes in 125I-labeled ovine prolactin specific binding of rat ventral prostate was correlated with changes in membrane lipid microviscosity and (ii) if membrane fluidizers produced age-dependent effects on prolactin binding of prostatic membranes. The degree of fluidization was monitored by a fluorescence polarization method using 1,6-diphenylhexatriene. Membrane preparations of ventral prostate glands obtained from immature (24-25 days old), young-adult (80-90 days old) and aged (550-610 days old) male rats were used for prolactin binding and membrane lipid microviscosity measurements. Relative to immature rats, prostatic prolactin binding decreased approximately 50% in young-adult rats and 75% in aged rats. Membrane lipid microviscosity, relative to immature rats, was increased 72% in young-adult rats and 140% in aged rats. Prostatic membranes obtained from immature animals exhibited no significant effects of in vitro alcohol treatment on prolactin binding, whereas, those obtained from aged animals exhibited maximal increase in prolactin binding. The value of the microviscosity parameter, after in vitro alcohol exposure, exhibited no significant changes in immature animals, whereas, this parameter was decreased approximately 15% in young-adults and approximately 30% in aged animals. These data suggest that in vitro fluidization of prostatic membrane exhibits an age-dependent modification of prolactin binding.

1-Propanol↗
PubMed1983

Modulation of prolactin binding sites in vitro by membrane fluidizers. I. Effects on adult rat ventral prostatic membranes.

The objective of this study was to determine if aliphatic alcohols, known fluidizers of certain membranes, could increase in vitro the apparent fluidity and prolactin binding capacity of membrane preparations obtained from ventral prostate glands of adult male rats. The degree of fluidization was monitored by a fluorescence polarization method using 1,6-diphenylhexatriene. Membrane preparations were either incubated with varying concentrations of ethanol, 1-propanol or 1-butanol and 125I-oPRL overnight at room temperature or were exposed to the alcohols for 15 min at room temperature and washed prior to the overnight incubation with ligand. Regardless of the conditions of incubation, alcohol exposure produced the same effects, a dose-dependent elevation and then decline in specific prolactin binding. Butanol produced a maximal 37-42% increase in prolactin binding at a concentration of 1.0%, propanol produced a maximal 40-56% increase in prolactin binding at a concentration of 3.8%, and ethanol produced a maximal 54-77% increase in prolactin binding at concentration of 4.8%. Scatchard analysis of the oPRL binding of ventral prostatic membranes indicated that the in vitro treatment of these membrane fluidizers increased the number of oPRL binding sites rather than the apparent affinity constant. The value of the microviscosity parameter decreased by 10-13%, 13-15% and 21-25%, after a 15 min exposure of prostatic membranes to 1.0% butanol, 3.8% propanol and 4.8% ethanol, respectively. These data suggest that in vitro fluidization of prostatic membrane modifies prolactin binding capacity and are consistent with in vivo prostatic prolactin receptor level-membrane fluidity relationships observed in earlier studies.

1-Butanol↗