scholarly journals PRL Gene

2020 ◽  
Author(s):  
Keyword(s):  
Prl Gene

scholarly journals Fibroblast Growth Factors Regulate Prolactin Transcription via an Atypical Rac-Dependent Signaling Pathway

2003 ◽  
Vol 17 (10) ◽  
pp. 1921-1930 ◽  
Author(s):  
Twila A. Jackson ◽  
David M. Koterwas ◽  
Melissa A. Morgan ◽  
Andrew P. Bradford
Keyword(s):  
Gene Expression ◽  
Growth Factors ◽  
Signaling Pathway ◽  
Promoter Activity ◽  
Fibroblast Growth Factors ◽  
Dominant Negative ◽  
Pituitary Cells ◽  
Dependent Manner ◽  
Fibroblast Growth ◽  
Prl Gene

Abstract Fibroblast growth factors (FGFs) play a critical role in pituitary development and in pituitary tumor formation and progression. We have previously characterized FGF signal transduction and regulation of the tissue-specific rat prolactin (rPRL) promoter in GH4 pituitary cells. FGF induction of rPRL transcription is independent of Ras, but mediated by a protein kinase C-δ (PKCδ)-dependent activation of MAPK (ERK). Here we demonstrate a functional role for the Rho family monomeric G protein, Rac1, in FGF regulation of PRL gene expression via an atypical signaling pathway. Expression of dominant negative Rac, but not RhoA or Cdc42, selectively inhibited FGF-induced rPRL promoter activity. Moreover, expression of dominant negative Rac also attenuated FGF-2 and FGF-4 stimulation of MAPK (ERK). However, in contrast to other Rac-dependent signaling pathways, FGF activation of rPRL promoter activity was independent of the c-Jun N-terminal kinase (JNK) and phosphoinositide 3-kinase/Akt cascades. FGFs failed to activate JNK1 or JNK2, and expression of dominant negative JNK or Akt constructs did not block FGF-induced PRL transcription. Consistent with the role of PKCδ in FGF regulation of PRL gene expression, activation of the rPRL promoter was blocked by an inhibitor of phospholipase Cγ (PLCγ) activity. FGF treatment also induced rapid tyrosine phosphorylation of PLCγ in a Rac-dependent manner. These results suggest that FGF-2 and FGF-4 activate PRL gene expression via a novel Rac1, PLCγ, PKCδ, and ERK cascade, independent of phosphoinositol-3-kinase and JNK.

scholarly journals Regulated expression of the prolactin gene in rat pituitary tumor cells.

1980 ◽  
Vol 87 (1) ◽  
pp. 6-13 ◽  
Author(s):  
B A Brennessel ◽  
D K Biswas
Keyword(s):  
Tumor Cells ◽  
Pituitary Tumor ◽  
Rna Sequences ◽  
Gh Cells ◽  
Prolactin Gene ◽  
Rat Pituitary ◽  
Cell Strains ◽  
Rat Pituitary Tumor Cells ◽  
Prl Gene ◽  
Specific Mrna

Prolactin (PRL) gene expression in three strains of GH cells (rat pituitary tumor cells) has been quantitated by measurement of: (a) intracellular and extracellular PRL, (b) cytoplasmic translatable PRL-specific mRNA (mRNAPRL), and (c) molecular hybridization of cytoplasmic poly(A) RNA to cDNAPRL (DNA complementary to mRNAPRL). Three GH cell lines utilized in this investigation were a PRL-producing (PRL+) strain, GH4C1, a PRL nonproducing 5-bromo-deoxyuridine resistnat (PRL- BrdUrdr) strain, F1BGH12C1, and a new strain, 928-9b, derived by fusion of PRL+ cells with a nuclear monolayer of the PRL-, BrdUrdr GH cell strain. PRL production is a characteristic of 928-9b cells, but the level of PRL production (2-4 micrograms/mg protein/24 h) is much lower than that of the PRL+ strain, GH4C1 (15-25 micrograms/mg protein/24 h). Levels of cytoplasmic translatable mRNAPRL and cytoplasmic PRL-RNA sequences quantitated with a cDNAPRL probe were also much lower in 928-9b as compared to the PRL+ parent. PRL-RNA sequences could not be detected in the PRL- strain. Thyrotopin-releasing hormone (TRH) stimulates PRL synthesis about threefold and inhibit a growth hormone (GH) synthesis 72% in the PRL+ strain. TRH has no effect on the synthesis of either PRL or GH in the 928-9b strain, although TRH receptors could be detected in these cells. Stimulation of PRL synthesis in the PRL+ strain by TRH could be correlated with increases in levels of cytoplasmic translatable mRNAPRL and increases in cytoplasmic PRL-RNA sequences. These results demonstrate that the graded expression of the PRL gene at the basal level, and in response to TRH, is caused by the regulated production of specific mRNA, i.e., mRNAPRL in these three GH cell strains.

Association of prolactin polymorphism with milk fat content in Iranian Sarabi cows

2007 ◽  
Vol 2007 ◽  
pp. 160-160
Author(s):  
A. Heravi Moussavi ◽  
M.R. Nassiry ◽  
M. Tahmoores Pour ◽  
A. Javadmanesh ◽  
M.H. Sekhavati
Keyword(s):  
Dairy Cattle ◽  
Candidate Gene ◽  
Milk Fat ◽  
Anterior Pituitary ◽  
Fat Content ◽  
Genetic Differences ◽  
Biological Functions ◽  
Milk Traits ◽  
Polypeptide Hormones ◽  
Prl Gene

Prolactin (PRL) is a polypeptide hormones produced by cells of the anterior pituitary. The bovine PRL gene consists of 4 introns and 5 exons, located on chromosome 23. Different biological functions of PRL were subdivided into five broad categories: reproduction, osmoregulation, growth, integument, and synergism with steroids. Also, It has been shown to be important for control of mammary growth, lactogenesis and lactation (Skinkyteet al., 2005). Chung et al, (1996) showed that PRL-RsaI locus had a significant effect on milk fat percent in dairy cattle. Therefore the PRL gene was chosen as a candidate gene for milk traits in dairy cattle. The objective of this study was to evaluate the association of genetic differences in bovine PRL gene and milk fat content in Iranian Sarabi cows.

MILK PRODUCTIVITY OF BLACK-AND-WHITE CATTLE WITH DIFFERENT GENOTYPES OF PROLACTIN AND SOMATOTROPIN

2021 ◽  
pp. 21-25
Author(s):  
Л.Р. ЗАГИДУЛЛИН ◽  
Р.Р. ШАЙДУЛЛИН ◽  
Т.М. АХМЕТОВ ◽  
С.В. ТЮЛЬКИН ◽  
А.Б. МОСКВИЧЕВА
Keyword(s):  
Protein Content ◽  
Milk Yield ◽  
Milk Fat ◽  
Milk Protein ◽  
Milk Productivity ◽  
Black And White ◽  
Gh Gene ◽  
White Cattle ◽  
Fat Yield ◽  
Prl Gene

Изучена взаимосвязь аллельных вариантов генов пролактина и соматотропина с показателями молочной продуктивности коров черно-пестрой породы по 1 и 3 лактации. У первотелок, как и у полновозрастных животных,  наиболее высокий удой (4642 и 6240 кг), количество молочного жира (174,1 и 215,0 кг) и молочного белка (149,0 и 182,5 кг) достигнуты в группе с генотипом PRL АА. По массовой доле жира и белка в молоке коровы с генотипом PRL ВВ достоверно превосходили животных с генотипом PRL АА на 0,12% (Р<0,05) и 0,05% (Р<0,05) соответственно. По гену соматотропина наибольший уровень молочной продуктивности выявлен у коров с генотипом GH LL при достоверном преимуществе над GH VV у первотелок по удою на 439 кг (Р<0,01), выходу молочного жира — на 13,6 кг (Р<0,001), выходу молочного белка — на 15,3 кг (Р<0,01). У полновозрастных коров превышение над остальными группами было только по удою — на 219—548 кг (Р<0,05). Наибольшая жирномолочность характерна животным с генотипом GH VV по 1 лактации — 3,83% и по 3 лактации — 3,82%, а лучшая белковомолочность — коровам, имеющим аллель V гена GH:  3,21 и 3,23% соответственно. Полученные данные свидетельствуют о более высоком уровне молочной продуктивности у коров с генотипом PRL АА и GH LL, но лучшая жирномолочность и белковомолочность отмечены у особей, имеющих в своем генотипе аллели В гена PRL и V гена GH. The interrelation of allelic variants of prolactin and somatotropin genes with indicators of milk productivity of black-and-white cows for the 1st and 3rd lactation was studied. The highest milk yield (4642 and 6240 kg) amount of milk fat (174.1 and 215.0 kg) and milk protein (149.0 and 182.5 kg) were in the group with the PRL AA genotype in first-calf heifers as well as in full-age animals. In terms of the mass fraction of fat and protein of milk, the cows with the PRL BB genotype significantly exceeded animals with the PRL AA genotype by 0.12% (P<0.05) and 0.05% (P<0.05), respectively. According to the somatotropin gene, the highest level of milk productivity was revealed in cows with the GH LL genotype with a significant advantage over GH VV in first-calf heifers in milk yield by 439 kg (P<0.01), milk fat yield by 13.6 kg (P<0.001), milk protein yield by 15.3 kg (P<0.01). The excess over the other groups in full-age cows was only in terms of milk yield that was by 219-548 kg (P<0.05). The highest protein content of milk is a characteristic of animals with the GH VV genotype, 3.83% is for the 1st lactation and 3.82% is for the 3rd lactation, and the best protein content of milk in cows with V allele of the GH gene is 3.21 and 3.23%, respectively. The obtained data  indicated a higher level of milk productivity in cows with the PRL AA and GH LL genotypes but the best fat and milk content was noted in cows with alleles B of the PRL gene and V of the GH gene in their genotype.

Changes in PRL Gene Expression During Upstream Movement of the Japanese Eel, Anguilla japonica

2019 ◽  
Vol 36 (6) ◽  
pp. 521
Author(s):  
Takashi Yada ◽  
Nobuto Fukuda ◽  
Michihisa Abe ◽  
Katsumi Tsukamoto
Keyword(s):  
Gene Expression ◽  
Anguilla Japonica ◽  
Japanese Eel ◽  
Prl Gene

scholarly journals Role of Specific Protein Kinase C Isozymes in Mediating Epidermal Growth Factor, Thyrotropin-Releasing Hormone, and Phorbol Ester Regulation of the Rat Prolactin Promoter in GH4/GH4C1 Pituitary Cells

2002 ◽  
Vol 16 (12) ◽  
pp. 2840-2852 ◽  
Author(s):  
Cheryl A. Pickett ◽  
Nicole Manning ◽  
Yoshiko Akita ◽  
Arthur Gutierrez-Hartmann
Keyword(s):  
Gene Transcription ◽  
Promoter Activity ◽  
The Novel ◽  
Calphostin C ◽  
Kinase C ◽  
Epidermal Growth ◽  
Pkc Isozymes ◽  
Pkc Inhibitors ◽  
Prl Gene

Abstract Epidermal growth factor (EGF) and TRH both produce enhanced prolactin (PRL) gene transcription and PRL secretion in GH4 rat pituitary tumor cell lines. These agents also activate protein kinase C (PKC) in these cells. Previous studies have implicated the PKCε isozyme in mediating TRH-induced PRL secretion. However, indirect studies using phorbol ester down-regulation to investigate the role of PKC in EGF- and TRH-induced PRL gene transcription have been inconclusive. In the present study, we examined the role of multiple PKC isozymes on EGF- and TRH-induced activation of the PRL promoter by utilizing general and selective PKC inhibitors and by expression of genes for wild-type and kinase-negative forms of the PKC isozymes. Multiple nonselective PKC inhibitors, including staurosporine, bisindolylmaleimide I, and Calphostin C, inhibited both EGF and TRH induced rat PRL promoter activity. TRH effects were more sensitive to Calphostin C, a competitive inhibitor of diacylglycerol, whereas Go 6976, a selective inhibitor of Ca2+-dependent PKCs, produced a modest inhibition of EGF but no inhibition of TRH effects. Rottlerin, a specific inhibitor of the novel nPKCδ isozyme, significantly blocked both EGF and TRH effects. Overexpression of genes encoding PKCs α, βΙ, βΙΙ, δ, γ, and λ failed to enhance either EGF or TRH responses, whereas overexpression of nPKCη enhanced the EGF response. Neither stable nor transient overexpression of nPKCε produced enhancement of EGF- or TRH-induced PRL promoter activity, suggesting that different processes regulate PRL transcription and hormone secretion. Expression of a kinase inactive nPKCδ construct produced modest inhibition of EGF-mediated rPRL promoter activity. Taken together, these data provide evidence for a role of multiple PKC isozymes in mediating both EGF and TRH stimulated PRL gene transcription. Both EGF and TRH responses appear to require the novel isozyme, nPKCδ, whereas nPKCη may also be able to transmit the EGF response. Inhibitor data suggest that the EGF response may also involve Ca2+-dependent isozymes, whereas the TRH response appears to be more dependent on diacylglycerol.

A possible role for D8/PSF-A-like sequences in lactotroph versus somatotroph expression of the human prolactin gene

1996 ◽  
Vol 149 (3) ◽  
pp. 473-483 ◽  
Author(s):  
V Leite ◽  
E A Cardoso ◽  
M E Bock ◽  
L G Sobrinho ◽  
P A Cattini
Keyword(s):  
Hela Cells ◽  
Upstream Region ◽  
Internal Deletion ◽  
Mobility Shift ◽  
Significant Stimulation ◽  
Prolactin Gene ◽  
Flanking Sequences ◽  
Promoter Specificity ◽  
Repressor Activity ◽  
Prl Gene

Abstract The transcription factor GHF-1/Pit-1 is essential for the expression of GH and prolactin (PRL) by somatotrophs and lactotrophs respectively. However, PRL is not expressed in mature somatotrophs despite the presence of GHF-1/Pit-1. A possible mechanism is the presence of a somatotroph-specific repressor in the 5′-flanking sequences of the PRL gene. The region −3500/−1750 of the human (h) PRL gene is associated with negative regulatory activity and contains an element, designated D8, that resembles repressor PSF-A sequences which are located in the distal upstream region of placental members of the human GH family. An internal deletion of D8 sequences resulted in a significant stimulation of promoter activity in somatotroph GC (P<0·005) and somatolactotroph-like GH3 and GH4C1 cells (P<0·05), but not lactotroph-like 235–1 cells after gene transfer. However, D8 binding was observed by nuclease protection with lactotroph- as well as somatotroph-like cell nuclear protein. Although proteins that bind to the D8 element appear ubiquitous, this element does yield tissuespecific complexes in mobility shift assays. Further, competition studies do not suggest an interaction between GHF-1/Pit-1 and D8 proteins. The hPRL D8 element was inserted upstream of a thymidine kinase promoter and used to transfect pituitary and non-pituitary HeLa cells, to assess intrinsic repressor activity and/or promoter specificity. Although no repression was observed, a significant ninefold increase in expression was observed in HeLa cells (P<0·001) which was at least twofold greater than observed in any of the pituitary cell lines tested. These results implicate D8 in the somatotroph-specific repression of hPRL; however, they also suggest that D8 can act as a stimulator as well as a repressor, depending on the interaction of a ubiquitous D8 factor forming promoter and cell-specific complexes with other elements/factors. Journal of Endocrinology (1996) 149, 473–483

scholarly journals A PIT-1 Homeodomain Mutant Blocks the Intranuclear Recruitment Of the CCAAT/Enhancer Binding Protein α Required for Prolactin Gene Transcription

2003 ◽  
Vol 17 (2) ◽  
pp. 209-222 ◽  
Author(s):  
John F. Enwright ◽  
Margaret A. Kawecki-Crook ◽  
Ty C. Voss ◽  
Fred Schaufele ◽  
Richard N. Day
Keyword(s):  
Gene Transcription ◽  
Binding Protein ◽  
Hormone Deficiency ◽  
Centromeric Heterochromatin ◽  
Pituitary Hormone ◽  
Homeodomain Protein ◽  
Pituitary Cells ◽  
Enhancer Binding Protein ◽  
Ccaat Enhancer Binding Protein ◽  
Prl Gene

Abstract The pituitary-specific homeodomain protein Pit-1 cooperates with other transcription factors, including CCAAT/enhancer binding protein α (C/EBPα), in the regulation of pituitary lactotrope gene transcription. Here, we correlate cooperative activation of prolactin (PRL) gene transcription by Pit-1 and C/EBPα with changes in the subnuclear localization of these factors in living pituitary cells. Transiently expressed C/EBPα induced PRL gene transcription in pituitary GHFT1–5 cells, whereas the coexpression of Pit-1 and C/EBPα in HeLa cells demonstrated their cooperativity at the PRL promoter. Individually expressed Pit-1 or C/EBPα, fused to color variants of fluorescent proteins, occupied different subnuclear compartments in living pituitary cells. When coexpressed, Pit-1 recruited C/EBPα from regions of transcriptionally quiescent centromeric heterochromatin to the nuclear regions occupied by Pit-1. The homeodomain region of Pit-1 was necessary for the recruitment of C/EBPα. A point mutation in the Pit-1 homeodomain associated with the syndrome of combined pituitary hormone deficiency in humans also failed to recruit C/EBPα. This Pit-1 mutant functioned as a dominant inhibitor of PRL gene transcription and, instead of recruiting C/EBPα, was itself recruited by C/EBPα to centromeric heterochromatin. Together our results suggest that the intranuclear positioning of these factors determines whether they activate or silence PRL promoter activity.

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