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PubMed1982

Dopaminergic mechanisms regulating prolactin secretion in patients with prolactin-secreting pituitary adenoma. Long-term studies after selective transsphenoidal surgery.

Twenty-seven female patients with prolactin-secreting pituitary microadenoma, were studied at different intervals following selective transsphenoidal removal of the tumor. Postoperatively, all patients had normal prolactin (PRL) levels and regular menstrual cycles were restored. Sixteen of 27 patients showed positive responses to TRH and metoclopramide (MCP) within 1 mo after surgery. On the contrary, 9 patients showed evaluation of these patients demonstrated that normal neuroendocrine relationships were restored after several months since positive PRL responses to TRH and MCP could be elicited in such patients. The remaining 2 patients who showed basal PRL levels in the upper range of normal, exhibited negative responses to TRH and MCP. These patients had progressively to TRH and MCP exhibited 10-20 mo after surgery a normal decrease in PRL levels following administration of carbidopa plus L-Dopa. Negative responses to carbidopa plus L-Dopa were instead obtained in 6 postoperative patients with elevated PRL levels and negative responses to TRH and MCP. These results suggest that: 1) Hyperprolactinemia induced by "autonomous" pituitary adenomas increases hypothaLamic dopamine (DA) secretion, which in turn inhibits PRL secretion by nonadenomatous lactotropes. 2) Total selective removal of the microadenoma acutely decreases PRL concentration, but a functional inhibition of the normal lactotrope can persist for a period of few months following surgery in a certain number of patients. 3) Prolonged reduction of PRL concentration is accompanied to a normal DA tone with reestablishment of normal neuroendocrine relationships.

Adenoma↗

PubMed1991

Determination of the primary and secondary structures of the dromedary (Camelus dromedarius) prolactin and comparison with prolactins from other species.

A non-glycosylated form of camel prolactin (camPRL), isolated from one-humped camel (Camelus dromedarius) pituitaries, was totally sequenced. A glycosylated form, separated by affinity chromatography on ConA-Sepharose, was partially sequenced. The comparison of the N-terminal amino acid sequences of the glycosylated and non-glycosylated forms showed that the only putative site of N-glycosylation (Asn-31) was indeed glycosylated. The far ultraviolet (UV) circular dichroism (CD) spectra of the two isohormones were identical, suggesting that the carbohydrate moiety had no effect on the global camPRL secondary structure. The far UV circular dichroism spectra of the two isohormones were analyzed in order to determine their relative proportions of periodic secondary structure, 60% of which was found to be in alpha-helix, as in prolactins of other species. The dromedary sequence was compared to those of other species and interpreted in term of evolutionary process. As already found for gonadotropins, the closest species to the dromedary was found to be the pig.

Amino Acid Sequence↗

PubMed1992

Prolactin and prolactin secretagogues reverse immunosuppression in mice treated with cysteamine, glucocorticoids, or cyclosporin-A.

Suppression of prolactin (PRL) secretion with the dopamine agonist, bromocriptine, has been shown in rodents to diminish a variety of immunologic responses, including delayed type hypersensitivity, primary antibody response, T-cell dependent macrophage activation, and ex vivo T- and B-lymphocyte proliferation in response to mitogens. These same responses can be suppressed by endogenous or exogenous glucocorticosteroids and, in large measure, the immunosuppressant peptide cyclosporin A. The sulfhydryl reducing agent cysteamine (2-aminoethanethiol) is known to reduce pituitary and plasma prolactin levels. Treatment of mice with cysteamine at doses which suppressed circulating PRL levels resulted in suppression of ex vivo blastogenic responses of lymphocytes from treated mice. The T-cell-dependent primary IgM response to immunization with sheep red blood cells was also suppressed by cysteamine treatment. Treatment of mice with drugs stimulating the release of endogenous PRL, or with exogenous ovine PRL, was found to antagonize the suppression of lymphocyte proliferative responses to mitogens induced in mice by glucocorticoid or cyclosporin treatment. These data suggest that many drugs in common clinical use could have potential immunomodulatory actions due to suppression or stimulation of pituitary PRL secretion. Furthermore, lactogenic hormones appear to exert counterregulatory actions which may modify glucocorticosteroid actions on immune and other target issues.

Adrenocorticotropic Hormone↗

PubMed2005

Prolactin in the brushtail possum (Trichosurus vulpecula): development of homologous radioimmunoassay using recombinant possum prolactin.

We report the production of recombinant possum prolactin (posPrl), and its use in the development and validation of a highly specific homologous radioimmunoassay for the measurement of prolactin (Prl) in brushtail possums. This enabled the subsequent investigation of some basic mechanisms involved in the regulation of Prl secretion in this species. Recombinant posPrl spanning the entire coding region was expressed in Escherichia coli, resulting in a 199 amino acid protein with a molecular weight approximately 23 kDa. The potency of posPrl was 45.3 +/- 4.8% that of ovine Prl in a radioreceptor assay using possum mammary gland receptors and induced a 3.4 +/- 0.8-fold increase in progesterone secretion in primary possum granulosa cells. Antiserum (G27) was raised against recombinant posPrl and was highly specific for possum Prl (approximately 30% binding at 1:60,000 final dilution), and exhibited negligible cross-reactivity (<0.0001%) with possum growth hormone. Serial dilutions of pituitary gland extracts, and plasma samples from male and female possums gave parallel inhibition curves to recombinant posPrl standards in the assay. Biological validation of the RIA included treating possums with drugs known to alter Prl secretion in other mammals. In seasonally anoestrous female possums, administration of 20 microg thyrotropin-releasing hormone (TRH) resulted in a 15-fold increase (P < 0.01) in plasma Prl concentrations. In mid-late lactating female possums, a bolus of cabergoline (dopamine agonist; 75 microg) reduced (P < 0.05) plasma Prl levels to baseline for 24 h, while repeated administration (6 x 75 microg at 12 h intervals) suppressed (P < 0.01) plasma Prl concentrations until 24h after the last injection. Prolonged inhibition of Prl levels subsequently caused marked (P < 0.01) attenuation in rate of bodyweight increase of pouch young. The amplitude of the Prl surge in response to a bolus of TRH (15 microg) was 5-fold lower in cabergoline-treated, compared to control mid-late lactating possums. In conclusion, we report the development and validation of a robust and sensitive RIA for measuring Prl concentrations in the plasma of brushtail possums.

Animals↗

PubMed2005

Comparison of mammalian prolactin-releasing peptide and Carassius RFamide for feeding behavior and prolactin secretion in chicks.

Prolactin-releasing peptide (PrRP) was named for its originally reported effects as a prolactin (PRL) secretagogue in mammals. Carassius RFamide (C-RFa) is an orthologous PRL secretagogue in fishes and a gene encoding a 20-amino acid peptide of identical sequence is present in the chicken. These facts suggest that C-RFa is a putative chicken PrRP. However, no information is available for the physiological effects of C-RFa in chickens. Therefore, in the present study, we compared the effect of intracerebroventricular (ICV) injection of C-RFa and mammalian PrRP (mPrRP) on feeding behavior and plasma PRL, growth hormone (GH), and corticosterone (CORT) concentrations. ICV injection of C-RFa did not affect feeding behavior of chicks while mPrRP was stimulatory. The injection of C-RFa also did not significantly affect plasma PRL, GH, and CORT concentrations. In contrast, ICV injection of mPrRP exerted similar effects to those reported in mammals by increasing plasma CORT and decreasing GH concentrations. Additionally, the peptide induced an unexpected inhibitory effect on plasma PRL concentrations. Overall, these data suggest that an as yet unidentified peptide that shares some functional similarities with mPrRP is present in birds, but that the physiological role of the avian 20-amino acid C-RFa peptide remains to be determined.

Animals↗

PubMed1998

Identification in the rat prolactin gene of sequences homologous to the distal promoter of the human prolactin gene.

The goal of the present study was to test the hypothesis that a second, more distal, promoter exists upstream from the rat prolactin (PRL) gene (rPrl) that is homologous to that identified upstream from the human prolactin gene (hPrl). The nucleotide sequence of the rat genome extending from 7.4 to 2.5 kb upstream from the proximal rPrl promoter was determined, revealing significant sequence homology to the hPrl distal promoter and its 5'-flanking domain. Using reverse transcription-polymerase chain reaction, novel rPrl transcripts that originate upstream from the proximal rPrl promoter were detected in rat uterus, spleen, pons medulla, anterior pituitary and the GH4C1 pituitary tumor cell line. Further characterization of these novel 5'-extended rPrl transcripts from GH4C1 cells indicated that they were full length, polyadenylated and properly spliced. However, data from primer extension (5'-RACE) experiments strongly suggested that the 5'-extended rPrl transcripts originate, not at the distal promoter-like motif, but at scattered sites located 60-153 bp upstream from the proximal promoter. Therefore, it appears improbable that the rat sequences homologous to the hPrl distal promoter comprise a functional promoter.

Animals↗

PubMed1990

Effects of prolactin and glycosylated prolactin on (pro)insulin synthesis and insulin release from cultured rat pancreatic islets.

In order to study the possible differential effects of the nonglycosylated and glycosylated forms of prolactin on insulin content and secretion in pancreatic islets, neonatal rat pancreatic islets were exposed for 6 days in vitro to 2 micrograms/ml of nonglycosylated ovine prolactin (oPRL), or to 2 micrograms/ml of glycosylated oPRL (G-oPRL). oPRL stimulated a significant increase (p less than 0.01) in the total amount of insulin released into the medium over the 6 day culture period; however, G-oPRL had no effect. Islets cultured for 6 days in the presence of oPRL showed no increase in the amount of DNA per islet. However, there was a significant (p less than 0.007) increase in the amount of total protein synthesized by the islets exposed to oPRL. These findings suggest that the effect of oPRL on neonatal rat pancreatic islet cells is a nonspecific effect. The nonglycosylated form of PRL may play a role in B-cell function by promoting protein synthesis, which results in augmented insulin synthesis.

Animals↗

PubMed1981

Abnormal regulation of prolactin secretion after successful surgery for prolactin-secreting pituitary tumours.

Patients with prolactin-secreting pituitary tumours have a diminished prolactin (PRL) response after administration of a variety of stimulatory agents, including thyrotrophin-releasing hormone (TRH), chlorpromazine (CPZ) and insulin-induced hypoglycaemia. We examined responses to these agents in sixty-seven women with PRL-secreting tumours before and after trans-sphenoidal surgery. Twenty-nine of the women were cured as defined by restoration of normal serum PRL concentrations and resumption of regular menses. One year following trans-sphenoidal surgery, patients with normal PRL concentrations and regular menses had normal PRL responses to TRH, while the responses to CPZ and insulin hypoglycaemia were not improved. The reversible impairment of PRL response to TRH reflects suppressed function of normal PRL-secreting cells, and the persistence of abnormal PRL responses to provocative stimuli after successful tumour removal may reflect some fundamental defect in the regulation of PRL secretion in patients with PRL-secreting adenomas. When growth hormone (GH) reserve after insulin hypoglycaemia was represented as the mean absolute increment above the basal concentration and compared with normal subjects, women with PRL-secreting tumours had a diminished response that returned to normal after successful surgery. This reversible impairment of GH secretion is not adequately reflected by standard criteria for GH response and suggests that PRL may have a role in the regulation of GH secretion.

Adenoma↗

PubMed2000

Prolactin-releasing peptides do not stimulate prolactin release in vivo.

The prolactin (PRL)-releasing activity of the novel prolactin-releasing peptides (PrRPs) was studied in vivo using male and lactating female rats. Whereas thyrotropin-releasing hormone effectively stimulated PRL and thyrotropin release as expected, PrRP in both animal models neither stimulated PRL secretion nor affected the release of other pituitary hormones. At the anterior pituitary level, in situ hybridization (ISH) histochemistry and Northern blot analysis revealed significantly higher expression levels of PrRP receptor (UHR-1) transcripts in female compared to male rats but not between lactating and nonlactating animals. By ISH, expression of UHR-1 mRNA was also detected in the intermediate lobe but not in the posterior pituitary. UHR-1 transcripts were also readily detectable in various hypothalamic brain areas whereas expression of PrRP mRNA was restricted to the ventral part of the dorsomedial hypothalamic nucleus but was not detected in neuroendocrine hypothalamic nuclei (e.g. PVN, SON). We thus assume that in the central nervous system, PrRP may likely have functions as a neuromodulator. However, together with the detailed cytochemical studies of various investigators that failed to detect PrRP-immunopositive nerve endings in the median eminence, our results strongly suggest that the hypothalamic PrRPs cannot be classified as hypophysiotrophic factors.

Animals↗

PubMed1986

Restraint stress decreases afternoon plasma prolactin levels in female rats. Influence of neural antagonists and agonists on restraint-induced changes in plasma prolactin and corticosterone.

Female Sprague-Dawley rats were ovariectomized, given estrogen, and blood samples were obtained via an atrial catheter in the afternoon during the prolactin (PRL) surge. Restraint stress applied at 16.00 h and continued for 3 h resulted in marked decrease in plasma prolactin (PRL) and an increase in plasma corticosterone (B). The neural mechanism(s) involved in the plasma PRL decrease to restraint stress in the afternoon were examined using neural agonists and antagonists. The administration of pimozide, a dopamine antagonist, increased plasma PRL and completely prevented the restraint-induced decrease in PRL. This result suggested that an increase in dopamine secretion mediated the stress-induced decrease of PRL in the afternoon. In unrestrained animals, the intravenous administration of atropine (a muscarinic cholinergic antagonist), arecoline (a muscarinic cholinergic agonist), propranolol (a beta-adrenergic antagonist) and morphine (a beta-endorphin agonist) at 16.00 h decreased plasma PRL from that of vehicle-injected animals. Bicuculline (a GABAergic antagonist) had no effect while phentolamine (an alpha-adrenergic antagonist) and phenoxybenzamine (an alpha-adrenergic antagonist) initially increased and then decreased plasma PRL. Naloxone (a beta-endorphin antagonist) initially decreased and then increased plasma PRL in unrestrained animals. In restrained animals, the intravenous administration of atropine and naloxone had no effect on the decrease in plasma PRL. Bicuculline and propranolol decreased plasma PRL below that observed for restrained animals alone, while phentolamine and morphine slightly retarded the course of the decrease. Arecoline did not alter the PRL decrease to restraint in the early sample periods but was followed by a rebound increase at later times.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed2005

Cloning and expression of two new prolactin-related proteins, prolactin-related protein-VIII and -IX, in bovine placenta.

BACKGROUND: Prolactin-related proteins (PRPs) are specific proteins of the growth hormone/prolactin (GH/PRL) family in bovine placenta. This study reports the identification and sequencing of a full-length cDNA for two new members of bovine PRPs, bPRP-VIII and -IX, and their localization and quantitative expression in bovine placenta. METHODS: New bPRP-VIII and -IX were identified from bovine placentome. Localization and quantitative gene expression in the placenta were respectively investigated by in situ hybridization and real-time RT-PCR methods. Recombinant proteins of these genes were produced by a mammalian HEK293 cell expression system. RESULTS: Full-length bPRP-VIII and -IX cDNA were respectively cloned with 909 and 910 nucleotide open-reading-frames corresponding to proteins of 236 and 238 amino acids. The predicted bPRP-VIII amino acid sequence shared about 40 to 70% homology with other bPRPs, and bPRP-IX had about 50 to 80% homology of others. The two new bPRPs were detected only in the placenta by RT-PCR. mRNA was primarily expressed in the cotyledon and intercotyledonary tissues throughout gestation. An in situ hybridization analysis revealed the presence of bPRP-VIII and -IX mRNA in the trophoblastic binucleate and/or trinucleate cells. bPRP-VIII mRNA was observed in the extra-embryonic membrane on Day 27 of gestation, however, no bPRP-IX mRNA was observed in the extra-embryonic membrane in the same stage of pregnancy by quantitative real-time RT-PCR analysis. Both new bPRP genes were possible to translate a mature protein in a mammalian cell expression system with approximately 28 kDa in bPRP-VIII and 38 kDa in bPRP-IX. CONCLUSION: We identified the new members of bovine prolactin-related protein, bPRP-VIII and -IX. Localization and quantitative expression were confirmed in bovine placenta by in situ hybridization or real-time PCR. Their different temporal and spatial expressions suggest a different role for these genes in bovine placenta during gestation.

Amino Acid Sequence↗

PubMed2004

Neuroendocrine dopaminergic regulation of prolactin release in systemic lupus erythematosus: a possible role of lymphocyte-derived prolactin.

Prolactin (PRL) secretion by the pituitary is under the control of dopamine. Hyperprolactinemia has been found in patients with systemic lupus erythematosus (SLE) and seems to be associated with clinical activity. T-lymphocytes express PRL and those from SLE patients appear to secrete more PRL than controls. In this study, immuno-(RIA) and bio-(BIO) assayable PRL in both serum and culture media of peripheral blood mononuclear cells (PBMNC) from SLE and control subjects were evaluated in the basal state and in response to 10 mg oral administration of metoclopramide, a dopamine receptor antagonist. Prolactin size heterogeneity in serum and culture media and PRL gene transcription in PBMNC were also studied. Basal serum RIA-PRL, BIO-PRL and the BIO/RIA ratio were similar in both groups. The serum BIO-PRL response after metoclopramide was higher than RIA-PRL in SLE, and this increment was also greater than in control subjects. PBMNC from SLE subjects secreted and produced more BIO-PRL. After metoclopramide, secretion and production of PRL increased only in PBMNC from control women and not in those from SLE patients. Our results demonstrated an increased central dopaminergic tone in SLE and suggest that lymphocyte-derived PRL might contribute to alter the functional activity of the hypothalamic dopaminergic system in SLE attempting to maintain serum PRL within a physiological range.

Adult↗

PubMed1992

Prolactin message in brain and pituitary of adult male rats is identical: PCR cloning and sequencing of hypothalamic prolactin cDNA from intact and hypophysectomized adult male rats.

Prolactin (PRL), or a PRL-like molecule has been identified in the central nervous system and other tissues by numerous investigators. The previous finding of PRL in brain persisting for weeks following hypophysectomy led us, and others, to conclude the brain and central nervous system PRL is synthesized locally. Also, our previous results showing PRL mRNA in hypothalamic and extra-hypothalamic brain regions using reverse transcription-polymerase chain reaction (RT-PCR) techniques, along with this report that the sequence of the PRL message in the brain is identical to that found in the anterior pituitary solidifies our, and others, hypothesis that PRL is synthesized in many locations other than the traditional one (anterior pituitary). The actual sequencing of hypothalamic PRL cDNA produced from RT-PCR of mRNA from intact or hypophysectomized rats demonstrates unequivocally that brain PRL mRNA is identical to anterior pituitary prolactin mRNA.

Amino Acid Sequence↗

PubMed1978

A heterologous radioimmunoassay for avian prolactin: application to the measurement of prolactin in the turkey.

A specific heterologous double-antibody radioimmunoassay has been developed to measure turkey prolactin (PRL) using a guinea pig anti-hPRL antiserum and 125I-labelled ovine PRL [125I]oPRL. Turkey pituitary prolactin and serum give parallel dose-response curves and no cross-reaction is seen with turkey growth hormone, LH or FSH, or mammalian LH, FSH, TSH, GH or placental lactogens. The RIA is accurate and precise and is sufficiently sensitive to measure PRL in all physiological situations investigated in the turkey. The RIA will measure PRL in several avian species including the chicken, duck, goose, pheasant, pheasant X chicken F1 hybrid, pigeon, quail and rock. Plasma PRL concentrations in laying and broody turkey hens were not significantly different (46.5 +/- 2.5 vs. 39.7 +/- 3.8 ng/ml) but both were significantly higher (P less than 0.001) than in non-laying turkey hens (4.6 +/- 0.7 ng/ml). Oestradiol injection into laying hens did not alter PRL levels while the same injection in non-laying hens caused a significant three-fold increase in plasma PRL levels.

Animals↗

PubMed1994

Correlation of the antibody titers with serum prolactin levels and their clinical course in patients with anti-prolactin autoantibody.

Patients with anti-prolactin (PRL) autoantibody were surveyed among 208 patients with hyperprolactinemia (PRL > or = 30 micrograms/l) and 228 subjects with normal PRL levels, and the relationship of the antibody titers with serum PRL levels and their clinical course were studied. Diagnosis of possessing the anti-PRL autoantibody was based on the polyethylene glycol method, displacement of the binding of [125I]PRL with the serum by unlabeled PRL and the binding of PRL to protein G, the affinity gel for immunoglobulin G. Prolactin was measured by an immunoradiometric assay that we found was not affected by the anti-PRL autoantibody. A significantly high frequency of anti-PRL autoantibody in patients with idiopathic hyperprolactinemia (16%) and a positive correlation between titers of the autoantibody and serum PRL levels (r = 0.74, p < 0.01) may indicate that the anti-PRL autoantibody itself is another cause of hyperprolactinemia, probably owing to the delayed clearance of PRL. Most patients with anti-PRL autoantibody lacked the clinical symptoms of hyperprolactinemia, such as amenorrhea and galactorrhea, and spontaneous pregnancy occurred despite the marked hyperprolactinemic state, indicating that the biological activity of PRL was attenuated by the autoantibody. In addition, PRL levels and the titers of anti-PRL autoantibody were not changed significantly during the observation period of up to 5 years without any medical intervention. These results suggest that the anti-PRL autoantibody itself is one of the causes of hyperprolactinemia and that medical intervention is unnecessary for this type of hyperprolactinemia.

Adolescent↗

PubMed1984

Autofeedback effects of prolactin on basal, suckling-induced, and proestrous secretion of prolactin.

Subcutaneous injections of ovine prolactin (oPRL, 4 mg/kg) were utilized to study the negative feedback effect of PRL on its own secretion in lactating and 4-day estrous cycling female rats. Basal PRL secretion in the 10-day postpartum lactating rat is not suppressed by acute or 48 hr of exposure to oPRL. In contrast, basal PRL secretion on the morning of proestrus is inhibited following 48 hr of exposure to oPRL. Thus, the lactating rat appears to be unresponsive to the negative feedback action of PRL compared with the adult female rat in regards to basal PRL secretion. The suckling-induced PRL response is partially suppressed by exposure to oPRL in 10-day postpartum lactating rats. Considering the areas under the PRL response curves, the suckling-induced release is blunted by 6 (decreased 49%), 12 (decreased 46%), and 48 (decreased 77%) hr of oPRL exposure compared to controls. In contrast, in cycling animals, 48 hr of exposure to elevated oPRL levels dramatically abolished the proestrous PRL surge. Elevated PRL levels, by a direct action on the brain and/or indirectly by altering ovarian function, inhibit or override the hypothalamic mechanism(s) mediating the proestrous PRL surge while having a lesser effect on the mechanism(s) mediating the suckling-induced PRL response. Taken together, the present data point to probable differences in the mechanism(s) mediating basal, suckling-induced, and the proestrous secretion of prolactin.

Animals↗

PubMed1977

Plasma prolactin and prolactin release in liver cirrhosis.

A significant increase of basal plasma prolactin levels (radioimmunoassayed) in 75 patients with liver cirrhosis was found in comparison to 50 male controls (8.5+/-4.5 (SD) vs. 5.5+/-1.7 ng/ml p less than 0.001). The extent and incidence of hyperprolactinaemia in 48 patients with alcoholic cirrhosis was more pronounced than in 27 cases of cirrhosis of non-alcoholic aetiologies (mean 9.7+/-4.8 vs. 5.7+/-2.1 ng/ml). No relation to ascites formation as well as to the development of gynaecomastia was apparent. Prolactin release following thyrotropin-releasing hormone was markedly enhanced in alcoholic as compared to non-alcoholic cirrhosis. Possibly hyperprolactinaemia and increased pituitary hormone reserve reflects hyperoestrogenism but changes of the hypothalamic regulation cannot be excluded as yet.

Alcoholism↗

PubMed1984

Purification of rabbit mammary prolactin receptor by acidic elution from a prolactin affinity column.

Membrane-bound prolactin receptors from the mammary gland of 6-7-day postpartum lactating rabbits were solubilized using the zwitterionic detergent, Zwittergent 3-12 (3- dodecyldimethylammonio )-1-propanesulfonate). The solubilized receptor from one rabbit was bound to an ovine prolactin-agarose affinity gel and eluted at pH 4.2. The receptor appeared as a single band upon staining sodium dodecyl sulfate-polyacrylamide gels with Coomassie blue. The protein yield from one rabbit was about 8 micrograms and the overall yield of receptor was over 50%. The apparent molecular weight was 42,000 on sodium dodecyl sulfate gels but varied on molecular weight columns due to the type of detergent. Receptor inactivated by iodination had an apparent molecular weight of 21,000 on sodium dodecyl sulfate gels. The purified receptor did not bind to concanavalin A-agarose or Lens culinaris-agarose.

Animals↗