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PubMed2003

Different biological effects of unmodified prolactin and a molecular mimic of phosphorylated prolactin involve different signaling pathways.

Previous work has shown that naturally phosphorylated prolactin antagonizes the growth-promoting activities of unmodified prolactin (U-PRL) and that this effect is duplicated by a molecular mimic, S179D PRL. At the same time, the S179D PRL is a superagonist with regard to expression of some PRL-regulated genes. We have asked whether the different activities of U-PRL and S179D PRL are the result of differential signaling. HC11 cells (a normal mouse mammary cell line) were grown to confluence, primed with hydrocortisone, and then exposed to the PRLs. A 15 min incubation of PRL-naive cells led to substantial tyrosine phosphorylation of Jak 2 and Stat 5a by U-PRL and an essentially equivalent Jak 2 activation by S179D PRL. The latter, however, was accompanied by reduced tyrosine phosphorylation of Stat 5a. EMSA analysis using a Stat 5 binding site showed both PRLs to cause equivalent binding of nuclear proteins and that most of what bound was complexed through Stat 5a. Phosphoamino acid analysis of Stat 5 showed S179D PRL to double the amount of serine phosphorylation versus that seen with U-PRL. Analysis of the MAP kinase pathway showed U-PRL capable of activation of ERKs 1 and 2 but that signaling via ERKs 1 and 2 was greater with S179D PRL. A 7-day incubation in either PRL increased beta-casein mRNA levels, but S179D PRL caused a 2-fold increase over that seen with U-PRL. The increase, over that seen with U-PRL, was blocked by the MAP kinase inhibitor, PD98059. After 7 days of treatment with S179D PRL, expression of the short PRL receptor was doubled, and signaling showed a greater dependence on the MAP kinase pathway (2.9-fold increase in ERK 1 and 2 activation). We conclude that although both PRLs use both pathways to some extent, U-PRL signals primarily through Jak 2-Stat 5 whereas S179D PRL signals primarily through the MAP kinase pathway especially after prolonged exposure. This is the first demonstration of differential involvement of signaling pathways by different forms of PRL.

Animals↗

PubMed1994

Inhibition of gonadotropin hormone-releasing hormone release by prolactin from GT1 neuronal cell lines through prolactin receptors.

High levels of prolactin (PRL) are associated with inhibition of luteinizing hormone secretion in several mammalian species. We asked whether this phenomenon could be explained by a direct inhibitory action of PRL on hypothalamic gonadotropin hormone-releasing hormone (GnRH) neurons. The ability of PRL to suppress GnRH release and expression was tested in the highly differentiated GT1 GnRH cell lines. In static culture, nanomolar concentrations of either rat or mouse PRL inhibited the release of GnRH in a dose-dependent fashion. PRL treatment for 24 hr also decreased GnRH mRNA levels determined by Northern analysis. The cells were shown to express the PRL receptor gene, and the mRNAs for both the short and long forms were present by Northern and PCR analysis, although the short form was more abundant. In Western blots with monoclonal antibody against the rat liver PRL receptor, the short 42-kDa form of the receptor was observed. These results demonstrate that PRL inhibits GnRH release and possibly gene expression in GnRH neurons. This action appears to be mediated through prolactin receptors expressed by the cells.

Animals↗

PubMed1999

Regulation of prolactin receptor (PRLR) gene expression in insulin-producing cells. Prolactin and growth hormone activate one of the rat prlr gene promoters via STAT5a and STAT5b.

Expression of the prolactin receptor (PRLR) gene is increased in pancreatic islets during pregnancy and in vitro in insulin-producing cells by growth hormone (GH) and prolactin (PRL). The 5'-region of the rat PRLR gene contains at least three alternative first exons that are expressed tissue-specifically because of differential promoter usage. We show by reverse transcription-polymerase chain reaction analysis that both exon 1A- and exon 1C-containing PRLR transcripts are expressed in rat islets and that human (h)GH, ovine (o)PRL, and bovine (b)GH increase exon 1A expression 6.5 +/- 0. 8-fold, 6.8 +/- 0.7-fold, and 3.9 +/- 0.7-fold and exon 1C expression 4.8 +/- 0.4-fold, 4.4 +/- 0.6-fold, and 2.5 +/- 0.7-fold, respectively. Expression of exon 1B was not detectable. The transcriptional activities of reporter constructs containing the 1A, 1B, or 1C promoter were found to be 22.8-fold, 2.7-fold, and 8. 0-fold, respectively, above that of a promoterless reporter construct when transfected into the insulin-producing INS-1 cells. The transcriptional activity of the 1A promoter construct was increased 8.9 +/- 1.9-fold by 0.5 microgram/ml hGH. Responsiveness to hGH of the 1A promoter was localized to the region from -225 to +81 with respect to the transcription start site. This region contains the sequence TTCTAGGAA that by gel retardation experiments was shown to bind the transcription factors STAT5a and STAT5b in response to stimulation by hGH, oPRL, or bGH. Mutation of this gamma-activated sequence-like element completely abolished transcriptional induction of the 1A promoter by hGH. Our results suggest that GH and PRL increase the levels of exon 1A- and 1C-containing PRLR mRNA species and furthermore that the transcriptional activity of the 1A promoter is increased via activation of STAT5a and STAT5b.

Animals↗

PubMed2000

Prolactin-releasing peptide activation of the prolactin promoter is differentially mediated by extracellular signal-regulated protein kinase and c-Jun N-terminal protein kinase.

Regulation of the mitogen-activated protein kinase (MAPK) family by prolactin-releasing peptide (PrRP) in both GH3 rat pituitary tumor cells and primary cultures of rat anterior pituitary cells was investigated. PrRP rapidly and transiently activated extracellular signal-regulated protein kinase (ERK) in both types of cells. Both pertussis toxin, which inactivates G(i)/G(o) proteins, and exogenous expression of a peptide derived from the carboxyl terminus of the beta-adrenergic receptor kinase I, which specifically blocks signaling mediated by the betagamma subunits of G proteins, completely blocked the PrRP-induced ERK activation, suggesting the involvement of G(i)/G(o) proteins in the PrRP-induced ERK activation. Down-regulation of cellular protein kinase C did not significantly inhibit the PrRP-induced ERK activation, suggesting that a protein kinase C-independent pathway is mainly involved. PrRP-induced ERK activation was not dependent on either extracellular Ca(2+) or intracellular Ca(2+). However, the ERK cascade was not the only route by which PrRP communicated with the nucleus. JNK was also shown to be significantly activated in response to PrRP. JNK activation in response to PrRP was slower than ERK activation. Moreover, to determine whether a MAPK family cascade regulates rat prolactin (rPRL) promoter activity, we transfected the intact rPRL promoter ligated to the firefly luciferase reporter gene into GH3 cells. PrRP activated the rPRL promoter activity in a time-dependent manner. Co-transfection with a catalytically inactive form of a MAPK construct or a dominant negative JNK, partially but significantly inhibited the induction of the rPRL promoter by PrRP. Furthermore, co-transfection with a dominant negative Ets completely abolished the response of the rPRL promoter to PrRP. These results suggest that PrRP differentially activates ERK and JNK, and both cascades are necessary to elicit rPRL promoter activity in an Ets-dependent mechanism.

Animals↗

PubMed2003

CIS1 interacts with the Y532 of the prolactin receptor and suppresses prolactin-dependent STAT5 activation.

Prolactin (PRL) interacts with a single-chain prolactin-specific receptor of the cytokine receptor superfamily. PRL triggers the activation of JAK2 kinase, which phosphorylates the PRL receptor itself, and of STAT5, a member of the family of signal transducers and activators of transcription (STAT). We have shown that the STAT5-dependent immediate early gene, CIS1 (Cytokine-Inducible SH2 domain-containing protein-1), suppresses PRL-induced STAT5 activation in vitro as well as in transgenic mice. To facilitate the study of the interactions between CIS1 and the PRL receptor, we have developed the yeast tri-hybrid system, a modification of the yeast two-hybrid system. We expressed CIS1 fused to the DNA-binding domain and PRL receptor cytoplasmic domain fused to the transcription activation domain in the presence or absence of the tyrosine kinase domain of JAK2 in yeast. CIS1 bound to the PRL receptor cytoplasmic domain in a JAK2-dependent manner. Moreover, we determined that the phosphorylated Y532 of the murine PRL receptor is the binding site for CIS1. Interestingly, Y532 has been shown to be unnecessary for STAT5 activation, although CIS1 overexpression suppressed PRL-induced STAT5 activation. These data suggest that the suppression of STAT5 activation by CIS1 is not due to a simple competition with STAT5 but rather to a modification of the receptor by CIS1 binding.

Animals↗

PubMed2005

Association of polymorphisms for prolactin and prolactin receptor genes with broody traits in chickens.

Prolactin (PRL) is generally accepted as crucial to the onset and maintenance of broodiness in avian species. The prolactin receptor (PRLR) plays an important role in the PRL signal transduction cascade. Two candidate genes, PRL and PRLR, were screened for polymorphisms in the chicken, and their genetic effects on broodiness were evaluated. Pedigreed hens (n = 155) of the Blue-shell chicken, a Chinese local breed, were observed for phenotypic broody traits including nesting days, broody days, repeats of broody cycles, and duration of broodiness. For polymorphism analysis, White Leghorns, Hy-Line brown egg layers, Avian broilers, and some other Chinese local breeds were included. Fifteen sets of primers were used to amplify the nucleotide sequences of the promotor of PRL and exons of PRLR. The PCR products were screened for polymorphisms using single-stranded conformational polymorphism protocol. Sequencing revealed a 24-bp insertion occurring in the promotor, -377 approximately -354, of PRL (GenBank accession no. AB011434). A single nucleotide polymorphism (SNP), A9026G (GenBank accession no. AY237377), in exon 3 of PRLR was also detected, which led to a nucleotide transition in the 5'-untranslated region (5'-UTR) of PRLR cDNA. Two SNP, T14771C and G14820A (GenBank accession no. AY237376), were detected in exon 6 of the PRLR. The T14771C transition led to an amino acid variation, Leu340Ser, in PRLR, whereas the G14820A transition was a synonymous mutation. An association analysis showed that the genetic polymorphisms at PRLR3 and PRLR6 were not related to broodiness (P > 0.05), whereas the individuals without the insertion sequence at PRLpro2 were associated with broody traits (P < 0.05) and the incidence (>30%) of typical broody of genotypes +/- and -/- was higher (P < 0.01) than that of +/+. In addition, all White Leghorns were +/+ for PRLpro2, whereas local breeds with very strong broodiness were nearly all -/-. Homozygous insertion of the 24-bp sequence in the PRL promoter may decrease the expression of PRL, leading to nonbroodiness. The results suggested that PRLpro2 could be a genetic marker in breeding against broodiness in chickens.

Animals↗

PubMed2002

Characterization of a prolactin-regulated gene in reproductive tissues using the prolactin receptor knockout mouse model.

Prolactin (PRL) exerts pleiotropic physiological effects in various cells and tissues, although it is mainly considered as a regulator of reproduction and cell growth. Null mutation of the prolactin receptor (PRLR) gene leads to female sterility due to a failure of embryo implantation. Using this mouse model and the method of mRNA differential display, we identified PRL target genes that are regulated during the peri-implantation period. We characterized 1 among the 45 isolated genes, UA-3, which is regulated in the uterus as well as in the ovary during early pregnancy. This gene corresponds to a P311 mouse cDNA that was originally identified for its high expression in late-stage embryonic brain and adult cerebellum. We report here that UA-3 is present in numerous tissues as well as in ovary and uterus at the site of blastocyst apposition, and that its expression is hormonally regulated. Moreover, in situ hybridization reveals high expression in ovarian granulosa cells and in uterine epithelium. Recently, it has been suggested that P311 expression is tightly regulated at several levels by mechanisms that control cellular growth, transformation, motility, or a combination of these. Taken together, these results suggest that P311 could be involved in these processes during pregnancy, although its function remains to be clearly established.

Animals↗

PubMed2002

Expression of prolactin receptors and regulation of cell proliferation by prolactin, corticotropin-releasing factor, and corticosterone in a neuroblastoma cell line.

The aetiology of neuroblastoma remains obscure, although a number of neuropeptides have been implicated in its pathogenesis. Using the mouse neuroblastoma cell line Neuro2a as a model, we have investigated the mitogenic actions of prolactin (PRL) and two hypothalamo-pituitary-adrenal stress axis hormones, corticotropin-releasing factor (CRF) and corticosterone. Using established polyclonal PRL receptor antisera with immunofluorescence cytochemistry, we show that the Neuro2a cells possess immunoreactive forms of both the long and short forms of the receptor. PRL and CRF were effective as mitogens in Neuro2a cell cultures, where a 10(-7) M concentration of PRL or CRF elicited a two-fold increase in the numbers of cells after 72 h (p < 0.0001). Corticosterone, however, attenuated their proliferation. These data suggest that prolactin may act to increase the proliferation and regulation of neuroblastomas and that the effects of PRL may be modified by hypothalamo-pituitary-adrenal hormones.

Animals↗

PubMed2001

Prolactin and prolactin receptor expression in rat, small intestine, intraepithelial lymphocytes during neonatal development.

Intraepithelial lymphocytes (IEL) are specialized T cells found between the epithelial cells of the small intestine. Because of their location, IEL are the first lymphocytes to contact intestinal bacteria and food antigens. In the neonate, IEL may be the first cells of the immune system to interact with milk-borne hormones including prolactin (PRL). PRL, an endocrine hormone abundant in breast milk, interacts with cells through surface receptors. PRL has been shown to function as an immunoregulator and may affect the development of the newborn's immune system. To determine if PRL plays a role in IEL development, small intestine IEL from rats of various ages were examined for the presence of surface prolactin receptor (PRL-R) and several lymphoid markers by flow cytometry. Between birth and 96 days of age about 80% of IEL were found to express PRL-R. These same cells also expressed the mRNA for PRL. Additionally, all of the IEL subpopulations examined were found to express PRL-R. Analysis of the normal development of rat IEL revealed an age related increase in total IEL, CD4 positive cells as well as a peak in interleukin-2 receptor (IL-2R) expression at weaning. In summary, the results indicate that IEL express PRL and PRL-R. In addition, an activation marker, IL-2R, changes in expression during neonatal development.

Animals↗

PubMed2005

Prolactin, the prolactin receptor and uncoupling protein abundance and function in adipose tissue during development in young sheep.

A primary role of the prolactin receptor (PRLR) during fetal and postnatal development has been suggested to be the regulation of uncoupling protein (UCP) expression. We, therefore, determined whether: (1) the rate of loss of UCP1 from brown adipose tissue after birth was paralleled by the disappearance of PRLR; and (2) administration of either pituitary extract prolactin (PRL) containing a mixture of posttranslationally modified forms or its pseudophosphorylated form (S179D PRL) improved thermoregulation and UCP1 function over the first week of neonatal life. PRLR abundance was greatest in adipose tissue 6 h after birth before declining up to 30 days of age, a trend mirrored by first a gain and then a loss of UCP1. In contrast, in the liver--which does not possess UCPs--a postnatal decline in PRLR was not observed. Administration of PRL resulted in an acute increase in colonic temperature in conjunction with increased plasma concentrations of non-esterified fatty acids and, as a result, the normal postnatal decline in body temperature was delayed. S179D PRL at lower concentrations resulted in a transient rise in colonic temperature at both 2 and 6 days of age. In conclusion, we have demonstrated a close relationship between the ontogeny of UCP1 and the PRLR. Exogenous PRL administration elicits a thermogenic effect suggesting an important role for the PRLR in regulating UCP1 function.

Adipose Tissue↗

PubMedDate not supplied

Prolactin regulation of prolactin binding sites in pancreatic islets and adrenal glands of ovariectomized rats.

The role of prolactin (Prl) in the regulation of Prl binding to its specific binding sites was studied in the Langerhans islets, adrenal gland and liver of adult ovariectomized female rats. Animals were sc injected twice daily during 10 days with ovine Prl (1 mg/kg BW), sulpiride (30 mg/kg BW) and bromocriptine (3 mg/kg BW). At the end of the treatment period, the animals were killed and serum was collected for Prl assay. Total Prl binding sites were measured in the membrane fraction of tissue by desaturating the occupied membrane receptors in vitro with 4M MgCl2. Serum levels of Prl were significantly higher in sulpiride-treated animals, whereas bromocriptine administration rendered undetectable values. Prolactin and sulpiride treatment significantly reduced Prl binding to the adrenal gland and Langerhans islets, whereas it greatly increased Prl binding to the liver. On the other hand, bromocriptine increased Prl binding sites in the adrenal gland and Langerhans islets, but in the liver caused no apparent effect. The binding affinity (Ka) in each tissue remained unchanged under the different experimental conditions. In addition, the binding of Prl to pancreas islets membranes was lower in late pregnancy when compared with control rats. All of these data provide strong evidence in favor of a role for Prl in regulating the number of its own tissue binding sites.

Adrenal Glands↗

PubMed1995

Influence of thyroxine and thyroxine with growth hormone and prolactin on splenocyte subsets and on the expression of interleukin-2 and prolactin receptors on splenocyte subsets of Snell dwarf mice.

A number of immune parameters were examined in Snell dwarf mice and compared with normal littermates. The number of splenocytes per gram of body weight were significantly decreased in dwarf animals, and the decrease was distributed throughout the CD4, CD8, B220, and MAC-1 subsets. The percentage of CD4 and CD8 splenocytes was markedly increased, and the percentage of B220 and MAC-1 splenocytes markedly decreased, in dwarf animals. In addition, the percentage of splenocyte T cells constitutively expressing interleukin-2 (IL-2) receptors and prolactin (PRL) receptors was decreased, with the CD4 subset presenting the most dramatic effect. The effects of replacing the hormones deficient in the Snell dwarf mouse (i.e., growth hormone [GH], prolactin [PRL], and thyroxine [T4] on the above immune parameters were also examined. The administration of T4 alone for 10 days corrected the defect in splenocyte cell numbers per grams body weight for both the CD4 and CD8 subsets, but only partially corrected the defect for the B220 and MAC-1 subsets. The addition of rbGH and rbPRL for the last 3 days of T4 injection had little additive effect on the number of CD4 and CD8 cells but increased the number of B220 and MAC-1 subsets to values comparable to those of normal animals on the basis of body weight. The decrease in the percentage of CD4 splenocytes in dwarf animals constitutively expressing IL-2R was partially corrected by T4 injection and completely corrected by the addition of rbGH and rbPRL for the last 3 days. The decrease in CD4 splenocytes constitutively expressing PRLR was partially corrected by T4 injection alone and the addition of rbGH and rPRL resulted in percentages comparable to that of normal animals. The results indicate that Snell dwarf animals are deficient in immune parameters and that the administration of the hormones lacking in this animal can correct the deficiencies.

Analysis of Variance↗

PubMed1999

Inhibition of rat corneal angiogenesis by 16-kDa prolactin and by endogenous prolactin-like molecules.

PURPOSE: The cornea is an avascular organ, where induction of new blood vessels involves the turn-on of proangiogenic factors and/or the turn-off of antiangiogenic regulators. Prolactin (PRL) fragments of 14 kDa and 16 kDa bind to endothelial cell receptors and inhibit angiogenesis. This study was designed to determine whether antiangiogenic PRL-like molecules are involved in cornea avascularity. METHODS: Sixteen-kDa PRL and basic fibroblast growth factor (bFGF) or anti-PRL antibodies were placed into rat cornea micropockets and neovascularization evaluated by the optical density associated with capillaries stained by the peroxidase reaction and by the number of vessels growing into the implants. Prolactin receptors in corneal epithelium were investigated by immunocytochemistry. RESULTS: bFGF induced a dose-dependent stimulation of corneal neovascularization. This effect was inhibited by coadministration of 16-kDa PRL, as indicated by a 65% reduction in vessel density and a 50% decrement in the incidence of angiogenic responses. Corneal angiogenic reactions of different intensities were induced by implantation of polyclonal and monoclonal anti-PRL antibodies. Corneal epithelial cells were labeled by several anti-PRL receptor monoclonal antibodies. CONCLUSIONS: These findings show that exogenous 16-kDa PRL inhibits bFGF-induced corneal neovascularization and suggest that PRL-like molecules with antiangiogenic actions function in the cornea. PRL receptors in the corneal epithelium may imply that PRL in the cornea derives from lacrimal PRL internalized through an intracellular pathway. These observations are consistent with the notion that members of the PRL family are potential regulators of corneal angiogenesis.

Animals↗

PubMed2003

Opposite effects of unmodified prolactin and a molecular mimic of phosphorylated prolactin on morphology and the expression of prostate specific genes in the normal rat prostate.

BACKGROUND: In the current study, we have investigated the individual roles of unmodified, wild-type prolactin (WT PRL) and a molecular mimic of phosphorylated prolactin (S179D PRL) in the normal rat prostate. METHODS: In the first animal experiment, recombinant WT PRL and S179D PRL were delivered to adult male rats at a rate of 14 microg/kg per day for 3 weeks. In the second animal experiment, two subcutaneous (200 microg/kg) injections of long-acting forms of the two PRLs were given to adult male rats on day 1 and day 22 for a total of 5.5 weeks of treatment. RESULTS: The different forms of PRL had opposite effects on the normal rat prostate, independently of androgens. WT PRL promoted morphologic changes in prostate epithelium consistent with preparation for cell proliferation, whereas S179D PRL produced morphologic evidence of a more differentiated epithelium. Northern blot analysis of expression of the two major prostate specific proteins, prostatein and probasin, showed that WT PRL decreased, whereas S179D PRL increased, the expression of the mRNAs for these two proteins. At the same time, S179D PRL reduced both testosterone and dihydrotestosterone levels. CONCLUSION: We conclude that PRL is an important modulator of normal rat prostate biology and that different forms of PRL have specific functions. The molecular mimic of phosphorylated PRL, S179D PRL, is the most important in terms of epithelial cell differentiation.

Animals↗

PubMed1988

Prolactin in patients with major depressive disorder and in healthy subjects. III. Investigation of basal and post-TRH prolactin during different forms of acute and chronic psychological stress.

Prolactin (PRL) levels after thyrotropin-releasing hormone (TRH) (delta PRL) were determined 4 times and basal prolactin levels 6 times in 10 healthy medical students before, during, and after a major examination in medicine. No significant differences in basal or delta PRL levels occurred during the examination period. Basal PRL was also measured in 14 doctors of medicine after delivering a paper at a clinical conference and a further 9 doctors both before and after delivering a paper. PRL was measured serially at 20-min intervals in 4 doctors on the day on which they presented the paper. No significant differences in PRL levels were found in any of the tests conducted during this kind of stress as compared with the corresponding values obtained under nonstressful conditions. Increases in PRL before delivering the paper were seen in 3 subjects, but such increases also occurred completely independently of stress. An 18-hr fast did not influence PRL secretion in 11 healthy volunteers. Both the information obtained from a review of the literature on the influence of stress on PRL secretion and our own results strongly suggest that contrary to common opinion, there is no evidence at all that psychological stress affects PRL secretion in man.

Adult↗

PubMed1983

Immunocytochemical identification of the prolactin-secreting cells in the teleost pituitary with an antiserum to chum salmon prolactin.

An antiserum raised to highly purified chum salmon (Oncorhynchus keta) prolactin (sPRL) was used to identify prolactin-producing cells in the adenohypophysis of 15 species of teleosts by the immunocytochemical peroxidase-antiperoxidase method. In the chum salmon, the only pituitary cells that reacted with sPRL antibody were the PRL cells organized as follicular structures in the rostral pars distalis. When the antiserum was absorbed with sPRL, on the other hand, no immunoreactive cell was observed in the pituitary, indicating the specificity of the antiserum. Furthermore, the antibody to sPRL reacted only with PRL cells in the pituitaries of three species of salmonids, a plecoglossid, eel, carp, goldfish, killifish, tilapia, and five species of marine fishes, thus showing no species specificity of the antibody among the teleosts tested. The PRL cells of the eel decreased in number and also in immunoreactivity after adaptation to seawater for 1 month. On the other hand, highly immunoreactive PRL cells were observed in the pituitaries of marine fishes, although the cells were much fewer in number than in eels and in other fishes in fresh water.

Animals↗

PubMed1990

Prolactin receptors in liver, kidney, and gill of the tilapia (Oreochromis mossambicus): characterization and effect of salinity on specific binding of iodinated ovine prolactin.

Specific binding of 125I-ovine prolactin (oPRL) to microsomal fractions from gill, kidney, and liver of adult tilapia was determined. Specific binding varied among tissues, the highest values being displayed by kidney membranes. In the liver, the binding of oPRL was not strongly displaced by tilapia prolactins (tPRL177 and tPRL188), although tPRL177 was six times more potent than tPRL188. On the other hand, in kidney and gill membranes, the two tPRLs were equipotent. Tilapia PRLs showed low potency in competing for oPRL-binding sites when pregnant rat liver membranes were utilized. Tilapia growth hormone (tGH) and human growth hormone (hGH) displaced 125I-oPRL from liver as well as did tPRL177 but were not recognized well by renal or branchial receptors. Two 125I-oPRL-binding sites were detected in every tissue tested. These binding sites are subject to physiological regulation since adaptation to seawater resulted in a significant decrease in specific binding.

Animals↗

PubMed1991

Cloning of a turkey prolactin cDNA: expression of prolactin mRNA throughout the reproductive cycle of the domestic turkey (Meleagris gallopavo).

A cDNA-encoding turkey prolactin (PRL) has been isolated from a turkey pituitary library. The 953-base pair cDNA clone contains a 229-amino acid open reading frame which consists of a 30-amino acid signal peptide followed by a 199-amino acid mature PRL. The deduced amino acid sequence of turkey PRL shows greater than 90% homology to chicken PRL and 54-78% homology to other mammalian prolactins. A mRNA of 1100 nucleotides was detected in total RNA extracted from turkey pituitaries. Levels of PRL mRNA increased approximately 10-, 20-, and 100-fold in photostimulated, laying, and incubating hens, respectively, relative to that found in nonphotostimulated hens. The corresponding increases in plasma PRL levels were 2-, 5.5-, and 50-fold and in pituitary PRL content were 2-, 4-, and 13.4-fold, respectively. The transition from incubation to the photorefractory phase resulted in a 10-fold reduction in PRL mRNA, a 3.7-fold decrease in pituitary PRL, and a dramatic 50-fold decrease in plasma PRL. The changes in the abundance of pituitary PRL mRNA appear to be related to the changes in PRL-releasing activity observed at each of the reproductive stages. This study provides the first characterization of pituitary PRL mRNA and its comparison with plasma and pituitary PRL levels during the avian reproductive cycle.

Amino Acid Sequence↗