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1

Liu, Lixin, Carlton E. Dean, and Tom E. Porter. "Thyroid Hormones Interact with Glucocorticoids to Affect Somatotroph Abundance in Chicken Embryonic Pituitary Cells in Vitro." Endocrinology 144, no. 9 (2003): 3836–41. http://dx.doi.org/10.1210/en.2003-0160.

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Abstract Our laboratory has reported that somatotroph differentiation occurs between d 14 and d 16 of chicken embryonic development and that corticosterone (CORT) can induce somatotroph differentiation at an earlier age in vitro and in vivo. The objective of the present study was to test for thyroid hormone-CORT interactions on somatotroph differentiation in vitro. Pituitary cells from d 11 chicken embryos were treated with CORT and thyroid hormones, and GH-producing somatotrophs were detected by reverse hemolytic plaque assays and immunocytochemistry. We found that thyroid hormones can act sy
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2

Liu, L., and TE Porter. "Endogenous thyroid hormones modulate pituitary somatotroph differentiation during chicken embryonic development." Journal of Endocrinology 180, no. 1 (2004): 45–53. http://dx.doi.org/10.1677/joe.0.1800045.

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Growth hormone cell differentiation normally occurs between day 14 and day 16 of chicken embryonic development. We reported previously that corticosterone (CORT) could induce somatotroph differentiation in vitro and in vivo and that thyroid hormones could act in combination with CORT to further augment the abundance of somatotrophs in vitro. The objective of the present study was to test our hypothesis that endogenous thyroid hormones regulate the abundance of somatotrophs during chicken embryonic development. Plasma samples were collected on embryonic day (e) 9-14. We found that plasma CORT a
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3

Kraemer, William J., Shawn D. Flanagan, Jeff S. Volek, et al. "Resistance exercise induces region-specific adaptations in anterior pituitary gland structure and function in rats." Journal of Applied Physiology 115, no. 11 (2013): 1641–47. http://dx.doi.org/10.1152/japplphysiol.00687.2013.

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The anterior pituitary gland (AP) increases growth hormone (GH) secretion in response to resistance exercise (RE), but the nature of AP adaptations to RE is unknown. To that end, we examined the effects of RE on regional AP somatotroph GH release, structure, and relative quantity. Thirty-six Sprague-Dawley rats were assigned to one of four groups: 1) no training or acute exercise (NT-NEX); 2) no training with acute exercise (NT-EX); 3) resistance training without acute exercise (RT-NEX); 4) resistance training with acute exercise (RT-EX). RE incorporated 10, 1 m-weighted ladder climbs at an 85
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4

Porter, TE, CE Dean, MM Piper, KL Medvedev, S. Ghavam, and J. Sandor. "Somatotroph recruitment by glucocorticoids involves induction of growth hormone gene expression and secretagogue responsiveness." Journal of Endocrinology 169, no. 3 (2001): 499–509. http://dx.doi.org/10.1677/joe.0.1690499.

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Prior research indicates that growth hormone (GH) cell differentiation can be induced prematurely by treatment with glucocorticoids in vitro and in vivo. However, the nature of these responses has not been fully characterized. In this study, the time course of corticosterone induction of GH-secreting cells in cultures of chicken embryonic pituitary cells, responsiveness of differentiated somatotrophs to GH secretagogues, localization of somatotroph precursor cells within the pituitary gland, and the effect of corticosterone on GH gene expression were determined to better define the involvement
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5

Kovacs, K., L. Stefaneanu, A. Mayerhofer, T. E. Wagner, and A. Bartke. "Ultrastructural comparison of pituitary somatotrophs and lactotrophs in mice transgenic for bovine and human growth hormone." Proceedings, annual meeting, Electron Microscopy Society of America 49 (August 1991): 258–59. http://dx.doi.org/10.1017/s0424820100085599.

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Acromegaly and gigantism are due to prolonged oversecretion of growth hormone (GH) most often caused by a somatotroph adenoma of the pituitary. Although the morphologic features of various types of somatotroph adenomas have been extensively investigated by electron microscopy, very little information is available on the ultrastructural changes of non-tumorous somatotrophs in cases of protracted GH excess. Transgenic mice with foreign GH gene incorporated into their genome secrete ectopically increased quantities of GH, have elevated serum GH levels and develop gigantism; thus it seemed conceiv
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6

Bossis, Ioannis, Shotaro Nishimura, Michael Muchow, and Tom E. Porter. "Pituitary Expression of Type I and Type II Glucocorticoid Receptors during Chicken Embryonic Development and Their Involvement in Growth Hormone Cell Differentiation." Endocrinology 145, no. 7 (2004): 3523–31. http://dx.doi.org/10.1210/en.2004-0155.

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Abstract Glucocorticoids can induce somatotroph differentiation in vitro and in vivo during chick embryonic and rat fetal development. In the present study, we identified the nuclear receptors involved in somatotroph differentiation and examined their ontogeny and cellular distribution during pituitary development in the chicken embryo. Several steroids were tested for their ability to induce GH cell differentiation. Only glucocorticoids and aldosterone were effective at low nanomolar concentrations, suggesting involvement of both type I (mineralocorticoid) and type II (glucocorticoid) recepto
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7

Tierney, T., and IC Robinson. "Increased lactotrophs despite decreased somatotrophs in the dwarf (dw/dw) rat: a defect in the regulation of lactotroph/somatotroph cell fate?" Journal of Endocrinology 175, no. 2 (2002): 435–46. http://dx.doi.org/10.1677/joe.0.1750435.

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The dwarf (dw/dw) rat differs from all other rodent models of GH deficiency in that its pituitary prolactin (PRL) content is normal or even increased. We have now studied this throughout postnatal development, using a combination of immunocytochemistry, RIA and fluorescence-activated cell sorting (FACS) and analysis. Compared with normal Albino Swiss (AS) rats, adult dw/dw rats showed a profound reduction in pituitary GH content accompanied by increased PRL content, significantly so in females (AS vs dw/dw; P<0.01). Somatotroph hypoplasia was evident in the adult dw/dw rats, with most GH(+v
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8

Fedotov, V. P., V. I. Gudoshnikov, and T. V. Mamayeva. "Role of calcium ions and cyclic nucleotides in regulation of somatotroph functional activity in rats of different age." Problems of Endocrinology 40, no. 4 (1994): 42–45. http://dx.doi.org/10.14341/probl12145.

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Somatotropic hormone (STH) biosynthesis and secretion were studied in primary adenohypophyseal cultures of neonatal, prepubertal, and adult rats. It was shown by disc PAAG electrophorqsiS of products synthesized in incubation of neonatal rat hypophyseal cells that L-'4C leucin incorporates predominantly in the STH containing fraction. The share of prelabeled STH secreted into the culture virtually did not depend on the age of animals, this indicating the maturity of mechanisms of basal somatotroph secretion as early as in the neonatal period of development. Ca-regulating agents (ionophore A231
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9

Leite, V., E. A. Cardoso, M. E. Bock, L. G. Sobrinho, and P. A. Cattini. "A possible role for D8/PSF-A-like sequences in lactotroph versus somatotroph expression of the human prolactin gene." Journal of Endocrinology 149, no. 3 (1996): 473–83. http://dx.doi.org/10.1677/joe.0.1490473.

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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 me
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10

Hull, K. L., A. Murphy, and S. Harvey. "Avian somatotrophs: differentiation, morphology, distribution, and regulation." Canadian Journal of Physiology and Pharmacology 78, no. 12 (2000): 994–1002. http://dx.doi.org/10.1139/y00-094.

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Growth hormone (GH) is primarily synthesized, stored, and released by pituitary somatotrophs. These cells comprise a highly labile population that continuously undergoes proliferation, differentiation, and morphogenesis in response to changing physiological stimuli. They are also functionally and morphologically heterogeneous with distinct spatial and temporal distribution within the pituitary gland. The characteristics of these cells are discussed in this brief review.Key words: somatotroph, aves, growth hormone, adenohypophysis.
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11

Zhou, Hong, Xinyan Wang, Wendy K. W. Ko, and Anderson O. L. Wong. "Evidence for a Novel Intrapituitary Autocrine/Paracrine Feedback Loop Regulating Growth Hormone Synthesis and Secretion in Grass Carp Pituitary Cells by Functional Interactions between Gonadotrophs and Somatotrophs." Endocrinology 145, no. 12 (2004): 5548–59. http://dx.doi.org/10.1210/en.2004-0362.

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Abstract Gonadotropin (GTH) and GH released from the pituitary are known to interact at multiple levels to modulate the functions of the gonadotrophic and somatotrophic axes. However, their interactions at the pituitary level have not been fully characterized. In this study, autocrine/paracrine regulation of GH synthesis and secretion by local interactions between gonadotrophs and somatotrophs was examined using grass carp pituitary cells as a cell model. Exogenous GTH and GH induced GH release and GH mRNA expression in carp pituitary cells. Removal of endogenous GTH and GH by immunoneutraliza
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12

Gorar, Suheyla, Doga Turkkahraman, and Kanay Yararbas. "A Large PROP1 Gene Deletion in a Turkish Pedigree." Case Reports in Endocrinology 2018 (2018): 1–5. http://dx.doi.org/10.1155/2018/2403430.

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Pituitary-specific paired-like homeodomain transcription factor, PROP1, is associated with multiple pituitary hormone deficiency. Alteration of the gene encoding the PROP1 may affect somatotropes, thyrotropes, and lactotropes, as well as gonadotropes and corticotropes. We performed genetic analysis of PROP1 gene in a Turkish pedigree with three siblings who presented with short stature. Parents were first degree cousins. Index case, a boy, had somatotrope, gonadotrope, thyrotrope, and corticotrope deficiency. However, two elder sisters had somatotroph, gonadotroph, and thyrotroph deficiency an
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13

Avtanski, Dimiter, Horacio J. Novaira, Sheng Wu та ін. "Both Estrogen Receptor α and β Stimulate Pituitary GH Gene Expression". Molecular Endocrinology 28, № 1 (2014): 40–52. http://dx.doi.org/10.1210/me.2013-1245.

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Abstract Although sex steroids have been implicated in the control of mammalian growth, their direct effect on GH synthesis is less clear. The aim of this study was to establish whether estradiol (E2) directly affects GH synthesis in somatotrophs. Somatotroph GH3 and MtT/S cells were used as in vitro models. At physiological doses of E2 stimulation, GH mRNA levels were increased and the ER antagonist ICI 182,780 completely abolished this effect. Estrogen receptor (ER) α– and ERβ-selective agonists, propylpyrazole triol (PPT), and 2,3-bis(4-hydroxyphenyl) propionitrile (DPN), respectively, augm
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14

Wade, Alisha N., Jennifer Baccon, M. Sean Grady, Kevin D. Judy, Donald M. O’Rourke, and Peter J. Snyder. "Clinically silent somatotroph adenomas are common." European Journal of Endocrinology 165, no. 1 (2011): 39–44. http://dx.doi.org/10.1530/eje-11-0216.

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ObjectiveSomatotroph adenomas are typically recognized when they secrete GH excessively and cause acromegaly. Both ‘silent’ somatotroph adenomas (immunohistochemical evidence of GH excess without biochemical or clinical evidence) and ‘clinically silent’ somatotroph adenomas (immunohistochemical and biochemical evidence but no clinical evidence) have occasionally been reported. The relative frequency of each presentation is unknown. The goal of this study was, therefore, to determine the frequency of clinically silent somatotroph adenomas, a group that is potentially recognizable in vivo.Design
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15

Honda, J., Y. Manabe, R. Matsumura, S. Takeuchi, and S. Takahashi. "IGF-I regulates pro-opiomelanocortin and GH gene expression in the mouse pituitary gland." Journal of Endocrinology 178, no. 1 (2003): 71–82. http://dx.doi.org/10.1677/joe.0.1780071.

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IGF-I is expressed in somatotrophs, and IGF-I receptors are expressed in most somatotrophs and some corticotrophs in the mouse pituitary gland. Our recent study demonstrated that IGF-I stimulates the proliferation of corticotrophs in the mouse pituitary. These results suggested that somatotrophs regulate corticotrophic functions as well as somatotrophic functions by the mediation of IGF-I molecules. The present study aimed to clarify factors regulating pituitary IGF-I expression and also the roles exerted by IGF-I within the mouse anterior pituitary gland. Mouse anterior pituitary cells were i
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16

Zhao, Sida, Jianhua Li, Jie Feng, et al. "Identification of Serum miRNA-423-5p Expression Signature in Somatotroph Adenomas." International Journal of Endocrinology 2019 (July 17, 2019): 1–12. http://dx.doi.org/10.1155/2019/8516858.

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Circulating miRNAs are novel disease biomarkers that are valuable for diagnosis and prognosis. But the circulating miRNAs profile in somatotroph adenomas is still unknown. Therefore, serum exosomal miRNAs expression profiling in somatotroph adenomas was performed on 6 somatotroph adenomas and 6 normal controls. From the exosomal miRNAs expression profiling, we found 169 miRNAs differently expressed between somatotroph adenomas and healthy pituitary samples (p< 0.05, FC > 2). Among the 169 miRNAs, miR-423-5p was expressed lower in somatotroph adenomas than in healthy pituitary samples, wh
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17

Matsuno, Akira, Hideki Katakami, Naoko Sanno, et al. "Pituitary Somatotroph Adenoma Producing Growth Hormone (GH)-Releasing Hormone (GHRH) with an Elevated Plasma GHRH Concentration: A Model Case for Autocrine and Paracrine Regulation of GH Secretion by GHRH1." Journal of Clinical Endocrinology & Metabolism 84, no. 9 (1999): 3241–47. http://dx.doi.org/10.1210/jcem.84.9.6008.

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An acromegalic patient with a pituitary somatotroph adenoma associated with an extremely elevated plasma GHRH concentration is presented. The preoperatively high concentration of plasma GHRH returned to the normal level after successful removal of the adenoma. GHRH production and GHRH gene expression were confirmed in the adenoma by studies including immunohistochemistry and in situ hybridization. Expression of GHRH receptor messenger ribonucleic acid was verified by in situ hybridization. Immunohistochemical double staining for GH and GHRH revealed their colocalization in single adenoma cells
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18

Kovacs, Kalman, Eva Horvath, Lucia Stefaneanu, et al. "Pituitary adenoma producing growth hormone and adrenocorticotropin: a histological, immunocytochemical, electron microscopic, and in situ hybridization study." Journal of Neurosurgery 88, no. 6 (1998): 1111–15. http://dx.doi.org/10.3171/jns.1998.88.6.1111.

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✓ The authors report on the morphological features of a pituitary adenoma that produced growth hormone (GH) and adrenocorticotropic hormone (ACTH). This hormone combination produced by a single adenoma is extremely rare; a review of the available literature showed that only one previous case has been published. The tumor, which was removed from a 62-year-old man with acromegaly, was studied by histological and immunocytochemical analyses, transmission electron microscopy, immunoelectron microscopy, and in situ hybridization. When the authors used light microscopy, the tumor appeared to be a bi
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19

Sartin, J. L., R. J. Kemppainen, E. S. Coleman, B. Steele, and J. C. Williams. "Cortisol inhibition of growth hormone-releasing hormone-stimulated growth hormone release from cultured sheep pituitary cells." Journal of Endocrinology 141, no. 3 (1994): 517–25. http://dx.doi.org/10.1677/joe.0.1410517.

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Abstract Cortisol inhibits growth hormone (GH) release in short-term culture and is stimulatory in long-term cultures of rat and human pituitary cells. This study sought to determine the in vitro effects of cortisol on GH release and the signal transduction pathways mediating the effects of cortisol on GH release from cultured ovine somatotrophs. Pituitary cells were dispersed with collagenase and placed in culture medium for 4 days. The data indicate that cortisol inhibited growth hormone-releasing hormone (GHRH)-stimulated GH release by at least 2 h. In short-term culture GHRH-, forskolin- a
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20

Garcia, Edwin A., Giampaolo Trivellin, Elena D. Aflorei, et al. "Characterization of SNARE Proteins in Human Pituitary Adenomas: Targeted Secretion Inhibitors as a New Strategy for the Treatment of Acromegaly?" Journal of Clinical Endocrinology & Metabolism 98, no. 12 (2013): E1918—E1926. http://dx.doi.org/10.1210/jc.2013-2602.

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Context: Targeted secretion inhibitors (TSIs), a new class of recombinant biotherapeutic proteins engineered from botulinum toxin, represent a novel approach for treating diseases with excess secretion. They inhibit hormone secretion from targeted cell types through cleavage of SNARE (soluble N-ethylmaleimide-sensitive factor-activating protein receptor) proteins. qGHRH-LHN/D is a TSI targeting pituitary somatotroph through binding to the GHRH-receptor and cleavage of the vesicle-associated membrane protein (VAMP) family of SNARE proteins. Objective: Our objective was to study SNARE protein ex
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21

Zhou, Hong, Yonghua Jiang, Wendy K. W. Ko, Wensheng Li, and Anderson O. L. Wong. "Paracrine regulation of growth hormone gene expression by gonadotrophin release in grass carp pituitary cells: functional implications, molecular mechanisms and signal transduction." Journal of Molecular Endocrinology 34, no. 2 (2005): 415–32. http://dx.doi.org/10.1677/jme.1.01629.

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Growth hormone (GH) is known to stimulate luteinizing hormone (LH) release via paracrine interactions between somatotrophs and gonadotrophs. However, it is unclear if LH can exert a reciprocal effect to modulate somatotroph functions. Here we examined the paracrine effects of LH on GH gene expression using grass carp pituitary cells as a cell model. LH receptors were identified in grass carp somatotrophs and their activation by human chorionic gonadotropin (hCG) increased ‘steady-state’ GH mRNA levels. Removal of endogenous LH by immunoneutralization using LH antiserum inhibited GH release and
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22

Malamed, Sasha, Jean A. Gibney, Lisa D. Cain, Frank M. Perez, and Colin G. Scanes. "Immunocytochemical studies of chicken somatotrophs and somatotroph granules before and after hatching." Cell and Tissue Research 272, no. 2 (1993): 369–74. http://dx.doi.org/10.1007/bf00302741.

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23

Lekva, Tove, Jens Petter Berg, Robert Lyle, et al. "Epithelial Splicing Regulator Protein 1 and Alternative Splicing in Somatotroph Adenomas." Endocrinology 154, no. 9 (2013): 3331–43. http://dx.doi.org/10.1210/en.2013-1051.

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Somatotroph adenomas secrete supraphysiological amounts of GH, causing acromegaly. We have previously hypothesized that epithelial mesenchymal transition (EMT) may play a central role in the progression of these adenomas and that epithelial splicing regulator 1 (ESRP1) may function prominently as a master regulator of the EMT process in pituitary adenomas causing acromegaly. To further elucidate the role of ESRP1 in somatotroph adenomas and in EMT progression, we used RNA sequencing (RNAseq) to sequence somatotroph adenomas characterized by high and low ESRP1 levels. Transcripts identified by
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24

Kontogeorgos, George, Sylvia L. Asa, Kalman Kovacs, Harley S. Smyth, and William Singer. "Production of alpha-subunit of glycoprotein hormones by pituitary somatotroph adenomas in vitro." Acta Endocrinologica 129, no. 6 (1993): 565–72. http://dx.doi.org/10.1530/acta.0.1290565.

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Somatotroph adenomas of the pituitary secrete growth hormone in excess and are associated with acromegaly. Morphologically, they can be separated into two entities, densely and sparsely granulated variants. It has been shown that a number of somatotroph adenomas produce α-subunit of glycoprotein hormones; however, it is not clear whether α-subunit production correlates with tumor cell morphology. We studied 32 surgically removed pituitary somatotroph adenomas in tissue culture to determine structure-function correlations of growth hormone and α-subunit production. All tumors were classified on
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25

Sauer, J., U. Renner, U. Hopfner та ін. "Interleukin-1β Enhances Interleukin-1 Receptor Antagonist Content in Human Somatotroph Adenoma Cell Cultures1". Journal of Clinical Endocrinology & Metabolism 83, № 7 (1998): 2429–34. http://dx.doi.org/10.1210/jcem.83.7.4963.

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In addition to the well-known modulation of immune and inflammatory responses, the interleukin-1 (IL-1) system has been shown to be involved in the regulation of anterior pituitary hormone secretion and growth. We previously demonstrated that IL-1 receptor antagonist (IL-1ra) is expressed in human pituitary adenomas cultured in vitro. In the present study, we investigated the regulation of IL-1ra protein by IL-1β (1–100 U/mL) in human somatotroph adenomas (n = 9) cultured for 12–48 h. IL-1β significantly enhanced the concentration of IL-1ra dose dependently in the somatotroph adenoma cell lysa
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26

Pagesy, P., J. Y. Li, M. Kujas, et al. "Apparently Silent Somatotroph Adenomas." Pathology - Research and Practice 187, no. 8 (1991): 950–56. http://dx.doi.org/10.1016/s0344-0338(11)81066-6.

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27

Aylwin, S. J. B., J. P. Welch, C. L. Davey, et al. "The Relationship between Steroidogenic Factor 1 and DAX-1 Expression and in Vitro Gonadotropin Secretion in Human Pituitary Adenomas1." Journal of Clinical Endocrinology & Metabolism 86, no. 6 (2001): 2476–83. http://dx.doi.org/10.1210/jcem.86.6.7531.

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The orphan nuclear receptors, steroidogenic factor 1 (SF-1) and DAX-1, are involved in gonadotroph differentiation, and SF-1 has been shown to activate the LH-β and glycoprotein hormone α-subunit (αGSU) gene promoters. Pituitary adenomas from 34 patients [13 somatotroph tumors, 4 prolactinomas, and 17 clinically nonfunctioning pituitary adenomas (NFPAs)] were enzymatically dispersed and cultured in vitro for 48 h. Tissue culture medium was collected and assayed for LH, FSH, and αGSU; messenger RNA was extracted from adherent cells, and expression of SF-1 and DAX-1 messenger RNA was determined
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28

Halliday, W. C., S. L. Asa, K. Kovacs, and B. W. Scheithauer. "Intermediate Filaments in the Human Pituitary Gland: An Immunohistochemical Study." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 17, no. 2 (1990): 131–36. http://dx.doi.org/10.1017/s0317167100030328.

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ABSTRACT:Normal pituitaries, pituitaries showing CHC and selected adenomas were assessed for their possible content of intermediate filaments (IF), using immunohistochemical techniques. Normal pituitaries were stained for each of the five known IF (Cytokeratins (CK), glial fibrillary acidic protein (GFAP), desmin, vimentin, and neurofilaments (NF)). Desmin could not be demonstrated, and NF staining was limited to processes in the posterior gland. In serial sections, CK was demonstrated in some corticotrophs, somatotrophs, and lactotrophs. Vimentin was limited to processes in the posterior glan
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29

Chinezu, Laura, Alexandre Vasiljevic, Jacqueline Trouillas, Marion Lapoirie, Emmanuel Jouanneau, and Gérald Raverot. "Silent somatotroph tumour revisited from a study of 80 patients with and without acromegaly and a review of the literature." European Journal of Endocrinology 176, no. 2 (2017): 195–201. http://dx.doi.org/10.1530/eje-16-0738.

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Background Silent somatotroph tumours are growth hormone (GH) immunoreactive (IR) pituitary tumours without clinical and biological signs of acromegaly. Their better characterisation is required to improve the diagnosis. Materials and methods Twenty-one silent somatotroph tumours were compared to 59 somatotroph tumours with acromegaly. Tumours in each group were classified into GH and plurihormonal (GH/prolactin (PRL)/±thyroid-stimulating hormone (TSH)) and into densely granulated (DG) and sparsely granulated (SG) types. The two groups were then compared with regards to proliferation (Ki-67, p
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30

Petit, Audrey, Catherine Bleicher, and Benoît T. Lussier. "Intracellular calcium stores are involved in growth hormone-releasing hormone signal transduction in rat somatotrophs." Canadian Journal of Physiology and Pharmacology 77, no. 7 (1999): 520–28. http://dx.doi.org/10.1139/y99-048.

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In rat pituitary somatotrophs, the stimulation of growth hormone secretion by growth hormone-releasing hormone (GHRH) is a Ca2+-dependent event involving Ca2+ influx. The presence of calcium-induced calcium release (CICR) Ca2+ stores has been suggested in these cells. The aim of our study was to demonstrate the presence of CICR stores in rat somatotrophs and to determine their function in GHRH Ca2+ signalling. To this end we measured cytosolic free Ca2+ concentration ([Ca2+]i), using indo-1 in purified rat somatotrophs in primary culture, while altering intracellular Ca2+ stores. Ionomycin (10
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31

Mayr, Bernhard, Rolf Buslei, Marily Theodoropoulou, Günter K. Stalla, Michael Buchfelder, and Christof Schöfl. "Molecular and functional properties of densely and sparsely granulated GH-producing pituitary adenomas." European Journal of Endocrinology 169, no. 4 (2013): 391–400. http://dx.doi.org/10.1530/eje-13-0134.

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ObjectiveGH-producing pituitary adenomas display two distinct morphological patterns of cytoplasmic GH-containing secretory granules, namely the densely and sparsely granulated somatotroph adenoma subtype. It is unknown whether these morphological variants reflect distinct pathophysiological entities at the molecular level.MethodsIn 28 GH-producing adenoma tissues from a consecutive set of patients undergoing pituitary surgery for acromegaly, we studied the GH granulation pattern, the expression of somatostatin receptor subtypes (SSTR) as well as the calcium, cAMP and ZAC1 pathways in primary
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32

Larkin, Sarah J., Francesco Ferraù, Niki Karavitaki, et al. "Sequence analysis of the catalytic subunit of PKA in somatotroph adenomas." European Journal of Endocrinology 171, no. 6 (2014): 705–10. http://dx.doi.org/10.1530/eje-14-0545.

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ObjectiveThe pathogenetic mechanisms of sporadic somatotroph adenomas are not well understood, but derangements of the cAMP pathway have been implicated. Recent studies have identified L206R mutations in the alpha catalytic subunit of protein kinase A (PRKACA) in cortisol-producing adrenocortical adenomas and amplification of the beta catalytic subunit of protein kinase A PRKACB in acromegaly associated with Carney complex. Given that both adrenocortical adenomas and somatotroph adenomas are known to be reliant on the cAMP signalling pathway, we sought to determine the relevance of the L206R m
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33

Romanet, Pauline, Justine Galluso, Peter Kamenicky, et al. "Somatotroph Tumors and the Epigenetic Status of the GNAS Locus." International Journal of Molecular Sciences 22, no. 14 (2021): 7570. http://dx.doi.org/10.3390/ijms22147570.

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Forty percent of somatotroph tumors harbor recurrent activating GNAS mutations, historically called the gsp oncogene. In gsp-negative somatotroph tumors, GNAS expression itself is highly variable; those with GNAS overexpression most resemble phenotypically those carrying the gsp oncogene. GNAS is monoallelically expressed in the normal pituitary due to methylation-based imprinting. We hypothesize that changes in GNAS imprinting of gsp-negative tumors affect GNAS expression levels and tumorigenesis. We characterized the GNAS locus in two independent somatotroph tumor cohorts: one of 23 tumors p
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34

Fu, Xiaoqin, Shotaro Nishimura, and Tom E. Porter. "Evidence that lactotrophs do not differentiate directly from somatotrophs during chick embryonic development." Journal of Endocrinology 183, no. 2 (2004): 417–25. http://dx.doi.org/10.1677/joe.1.05799.

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It is generally accepted that, in mammals, lactotrophs differentiate from somatotrophs through an intermediate cell type, the mammosomatotroph. However, little information exists about mammosomatotrophs and their relationship with lactotroph development in non-mammalian vertebrates. We reported previously that corticosterone (CORT) can induce both somatotroph and lactotroph differentiation in cultures of chicken embryonic pituitary cells. Our current objectives were to determine the abundance of mammosomatotrophs during chicken pituitary development, to identify mammosomatotrophs during CORT i
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35

Schernthaner-Reiter, Marie Helene, Giampaolo Trivellin, Thomas Roetzer, Johannes A. Hainfellner, Matthew F. Starost, and Constantine A. Stratakis. "Prkar1a haploinsufficiency ameliorates the growth hormone excess phenotype in Aip-deficient mice." Human Molecular Genetics 29, no. 17 (2020): 2951–61. http://dx.doi.org/10.1093/hmg/ddaa178.

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Abstract Mutations of the regulatory subunit (PRKAR1A) of the cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA), leading to activation of the PKA pathway, are the genetic cause of Carney complex which is frequently accompanied by somatotroph tumors. Aryl hydrocarbon receptor-interacting protein (AIP) mutations lead to somatotroph tumorigenesis in mice and humans. The mechanisms of AIP-dependent pituitary tumorigenesis are still under investigation and evidence points to a connection between the AIP and PKA pathways. In this study, we explore the combined effects of Aip and P
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36

Ferrante, E., C. Pellegrini, S. Bondioni, et al. "Octreotide promotes apoptosis in human somatotroph tumor cells by activating somatostatin receptor type 2." Endocrine-Related Cancer 13, no. 3 (2006): 955–62. http://dx.doi.org/10.1677/erc.1.01191.

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Somatostatin analogs currently used in the treatment of acromegaly and other neuroendocrine tumors inhibit hormone secretion and cell proliferation by binding to somatostatin receptor type (SST) 2 and 5. The antiproliferative pathways coupled to these receptors have been only partially characterized. The aim of this study was to evaluate the effect of octreotide and super selective SST2 (BIM23120) and SST5 (BIM23206) analogs on apoptotic activity and apoptotic gene expression in human somatotroph tumor cells. Eight somatotroph tumors expressing similar levels of SST2 and SST5 evaluated by real
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37

Pankova, S. S., Т. I. Buraya, and N. Р. Goncharov. "Use of dexamethasone for the differential diagnosis of dwarfism." Problems of Endocrinology 41, no. 1 (1995): 12–13. http://dx.doi.org/10.14341/probl11330.

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The capacity of somatotrophs to respond with secretion of growth hormones to dexamethasone administration was studied in children with different forms of dwarfism. In cases of growth delay caused by deficiency of growth hormone the content of STH during dexamethasone test was at the basal level. In the rest cases blood plasma (serum) STH levels increased at the 180th min after dexamethasone administration. A 6 to 50-fold increase of blood STH level was observed in the presence of intact somatotropic function of the hypophysis. Dexamethasone is recommended for the assessment, of the function of
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38

Jenkins, S. A., M. Muchow, M. P. Richards, J. P. McMurtry, and T. E. Porter. "Administration of Adrenocorticotropic Hormone during Chicken Embryonic Development Prematurely Induces Pituitary Growth Hormone Cells." Endocrinology 148, no. 8 (2007): 3914–21. http://dx.doi.org/10.1210/en.2006-1102.

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Treatment of fetal rats and embryonic chickens with exogenous glucocorticoids induces premature GH cell differentiation. However, it is unknown whether the developing adrenal gland is capable of mounting this response autonomously. The present study determined whether stimulation of the adrenal gland in developing chicken embryos through administration of ACTH could induce a premature increase in GH cells. We found that plasma corticosterone and ACTH levels increased between embryonic day (e) 11 and e17, consistent with GH cell (somatotroph) ontogeny. Injection of ACTH into eggs on e9, e10, or
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39

Delgrange, Etienne, and Julian Donckier. "Proliferation Activity in Somatotroph Pituitary Adenomas." Mayo Clinic Proceedings 73, no. 10 (1998): 1027. http://dx.doi.org/10.4065/73.10.1027.

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40

Matted, Robert L., and Jeffery A. Carroll. "Somatotroph function in the neonatal pig." Domestic Animal Endocrinology 14, no. 4 (1997): 241–49. http://dx.doi.org/10.1016/s0739-7240(97)00022-2.

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41

Apel, Robyn L., Robert J. Wilson, and Sylvia L. Asa. "A composite somatotroph-corticotroph pituitary adenoma." Endocrine Pathology 5, no. 4 (1994): 240–46. http://dx.doi.org/10.1007/bf02921493.

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42

Langlois, Fabienne, Randall Woltjer, Justin S. Cetas, and Maria Fleseriu. "Silent somatotroph pituitary adenomas: an update." Pituitary 21, no. 2 (2018): 194–202. http://dx.doi.org/10.1007/s11102-017-0858-y.

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43

Nasr, Christian, Alexander Mason, Marc Mayberg, Susan M. Staugaitis, and Sylvia L. Asa. "Acromegaly and Somatotroph Hyperplasia with Adenomatous Transformation Due to Pituitary Metastasis of a Growth Hormone-Releasing Hormone-Secreting Pulmonary Endocrine Carcinoma." Journal of Clinical Endocrinology & Metabolism 91, no. 12 (2006): 4776–80. http://dx.doi.org/10.1210/jc.2006-0610.

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Abstract Context: GHRH excess from extracranial endocrine tumors is known to cause somatotroph hyperplasia and acromegaly. Hypothalamic gangliocytomas producing GHRH are also known to be associated with pituitary adenomas causing acromegaly. Objectives: The objective of this study was to describe a case of acromegaly due to a pulmonary GHRH-secreting endocrine carcinoma with metastasis to the pituitary gland and to look at the peculiar histological features of this case. Subject: The patient was a 44-yr-old woman who was diagnosed with a biopsy-proven metastatic pulmonary endocrine tumor durin
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44

Diaz-Rodriguez, Esther, Angela R. Garcia-Rendueles, Alejandro Ibáñez-Costa, et al. "Somatotropinomas, But Not Nonfunctioning Pituitary Adenomas, Maintain a Functional Apoptotic RET/Pit1/ARF/p53 Pathway That Is Blocked by Excess GDNF." Endocrinology 155, no. 11 (2014): 4329–40. http://dx.doi.org/10.1210/en.2014-1034.

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Abstract Acromegaly is caused by somatotroph cell adenomas (somatotropinomas [ACROs]), which secrete GH. Human and rodent somatotroph cells express the RET receptor. In rodents, when normal somatotrophs are deprived of the RET ligand, GDNF (Glial Cell Derived Neurotrophic Factor), RET is processed intracellularly to induce overexpression of Pit1 [Transcription factor (gene : POUF1) essential for transcription of Pituitary hormones GH, PRL and TSHb], which in turn leads to p19Arf/p53-dependent apoptosis. Our purpose was to ascertain whether human ACROs maintain the RET/Pit1/p14ARF/p53/apoptosis
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Alba, Maria, Danilo Fintini, Cyril Y. Bowers, A. F. Parlow, and Roberto Salvatori. "Effects of long-term treatment with growth hormone-releasing peptide-2 in the GHRH knockout mouse." American Journal of Physiology-Endocrinology and Metabolism 289, no. 5 (2005): E762—E767. http://dx.doi.org/10.1152/ajpendo.00203.2005.

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Growth hormone (GH) secretagogues (GHS) stimulate GH secretion in vivo in humans and in animals. They act on the ghrelin receptor, expressed in both the hypothalamus and the pituitary. It is unknown whether GHSs act predominantly by increasing the release of hypothalamic GH-releasing hormone (GHRH) or by acting directly on the somatotroph cells. We studied whether a potent GHS could stimulate growth in the absence of endogenous GHRH. To this end, we used GHRH knockout (GHRH-KO) mice. These animals have proportionate dwarfism due to severe GH deficiency (GHD) and pituitary hypoplasia due to red
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46

Hage, Mirella, Clément Janot, Sylvie Salenave, Philippe Chanson, and Peter Kamenický. "MANAGEMENT OF ENDOCRINE DISEASE: Etiology and outcome of acromegaly in patients with a paradoxical GH response to glucose." European Journal of Endocrinology 184, no. 6 (2021): R261—R268. http://dx.doi.org/10.1530/eje-20-1448.

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To gain more insight on the pathogenesis of somatotroph pituitary adenomas, recent studies have focused on a subgroup of patients with acromegaly displaying a paradoxical growth hormone (GH) response during oral glucose tolerance test (OGTT). The paradoxical rise of GH after oral glucose intake occurs in about one-third of acromegaly patients and has been pathogenetically linked, by analogy to glucose-dependent insulinotropic polypeptide (GIP)-dependent Cushing's syndrome, to the ectopic expression of GIP receptor (GIPR) in somatotroph adenoma cells. GIPR-expressing adenomas are negative for a
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47

Gardner, M. J., and D. J. Flint. "Long-term reductions in GH, insulin-like growth factor-I and body weight gain in rats treated neonatally with antibodies to rat GH." Journal of Endocrinology 124, no. 3 (1990): 381–86. http://dx.doi.org/10.1677/joe.0.1240381.

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ABSTRACT Treatment of neonatal rats on days 2–5 with antibodies against rat GH (rGH) markedly reduced body weight gain and serum concentrations of insulin-like growth factor-I for 6–8 weeks in both females and males, after which weight gain normalized without evidence of catch-up growth. There were no significant effects on serum prolactin, tri-iodothyronine or corticosterone. Testis and ovarian weights were reduced, although only in proportion to body size. In females, but not males, the treated rats, though lighter, had increased fat deposition in the parametrial depot. Pituitary weight was
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48

Wettschureck, N., A. Moers, B. Wallenwein, A. F. Parlow, C. Maser-Gluth, and S. Offermanns. "Loss of Gq/11 Family G Proteins in the Nervous System Causes Pituitary Somatotroph Hypoplasia and Dwarfism in Mice." Molecular and Cellular Biology 25, no. 5 (2005): 1942–48. http://dx.doi.org/10.1128/mcb.25.5.1942-1948.2005.

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ABSTRACT Heterotrimeric G proteins of the Gq/11 family transduce signals from a variety of neurotransmitter and hormone receptors and have therefore been implicated in various functions of the nervous system. Using the Cre/loxP system, we generated mice which lack the genes coding for the α subunits of the two main members of the Gq/11 family, gnaq and gna11, selectively in neuronal and glial precursor cells. Mice with defective gnaq and gna11 genes were morphologically normal, but they died shortly after birth. Mice carrying a single gna11 allele survived the early postnatal period but died w
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Mear, Yves, Marie-Pierre Blanchard, Céline Defilles, et al. "Ghrelin Receptor (GHS-R1a) and Its Constitutive Activity in Somatotroph Adenomas: A New Co-targeting Therapy Using GHS-R1a Inverse Agonists and Somatostatin Analogs." Journal of Clinical Endocrinology & Metabolism 99, no. 12 (2014): E2463—E2471. http://dx.doi.org/10.1210/jc.2014-2753.

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Context: The ghrelin receptor GHS-R1a is highly expressed in human somatotroph adenomas and exhibits unusually high basal signaling activity. In humans, the suppression of this constitutive activity by mutation induces a short stature. Objective: Using a GHS-R1a inverse agonist, modified substance P (MSP), we explored the role of GHS-R1a constitutive activity in GH hypersecretion from somatotroph adenomas and as a putative therapeutic target. Design: The effects of MSP were assessed on GH secretion from 19 human somatotroph tumors in vitro. Moreover, these effects were compared with those of o
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Somm, Emmanuel, Nicolas Bonnet, Philippe Zizzari, et al. "Comparative Inhibition of the GH/IGF-I Axis Obtained With Either the Targeted Secretion Inhibitor SXN101959 or the Somatostatin Analog Octreotide in Growing Male Rats." Endocrinology 154, no. 11 (2013): 4237–48. http://dx.doi.org/10.1210/en.2013-1427.

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Abnormally high GH/IGF-I levels, most often caused by adenomas arising from pituitary somatotrophs, generate deleterious effects. We recently described a targeted secretion inhibitor (SXN101742) comprising a GHRH domain and the endopeptidase domain of botulinum toxin serotype D (GHRH-light chain endopeptidase type D domain [LC/D] associated to a heavy chain translocation domain [HN]) able to down-regulate the GH/IGF-I axis. In the present study, we compared the effect of a single iv bolus of a related molecule developed for clinical studies (SXN101959, 1 mg/kg) with a sc infusion of the somato
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