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Journal articles on the topic 'Thyrotropin releasing hormone – Receptors'

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Published: 4 June 2021

Last updated: 12 February 2022

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1

ROBERTSON, ROBERT G., JULIE A. KELLY, and EWAN GRIFFITHS. "Thyrotrophin-releasing hormone analogue binding to central thyrotropin-releasing hormone receptors." Biochemical Society Transactions 14, no. 6 (December 1, 1986): 1245–46. http://dx.doi.org/10.1042/bst0141245.

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2

Sun, Y., X. Lu, and MC Gershengorn. "Thyrotropin-releasing hormone receptors -- similarities and differences." Journal of Molecular Endocrinology 30, no. 2 (April 1, 2003): 87–97. http://dx.doi.org/10.1677/jme.0.0300087.

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Thyrotropin-releasing hormone (TRH) initiates its effects by interacting with cell-surface membrane receptors. Two G protein-coupled receptors for TRH, TRH receptor type 1 (TRH-R1) and TRH receptor type 2 (TRH-R2), have been cloned from mammals. In this review, we compare TRH-R1 and TRH-R2 with regard to their tIssue distribution, binding affinities for TRH and TRH analogs, basal and activated signaling activities and characteristics of internalization. TRH-R1 and TRH-R2 are distributed differently in the brain and peripheral tIssues, but exhibit indistinguishable binding affinities for TRH and TRH analogs. Although they both can be stimulated by TRH to similar maximal signaling levels, TRH-R2 exhibits higher basal signaling activity and is more rapidly internalized than TRH-R1. These differences in signaling and internalization properties are probably important in the distinct parts that TRH-R1 and TRH-R2 may play in mammalian physiology.

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3

YU, RUN, RACHEL ASHWORTH, and PATRICIA M. HINKLE. "Receptors for Thyrotropin-Releasing Hormone on Rat Lactotropes and Thyrotropes." Thyroid 8, no. 10 (October 1998): 887–94. http://dx.doi.org/10.1089/thy.1998.8.887.

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4

Villalobos, Carlos, Lucía Núñez, and Javier García-Sancho. "Anterior pituitary thyrotropes are multifunctional cells." American Journal of Physiology-Endocrinology and Metabolism 287, no. 6 (December 2004): E1166—E1170. http://dx.doi.org/10.1152/ajpendo.00194.2004.

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Anterior pituitary (AP) contains some unorthodox multifunctional cells that store and secrete two different AP hormones (polyhormonal cells) and/or respond to several hypothalamic-releasing hormones (HRHs; multiresponsive cells). Multifunctional cells may be involved in paradoxical secretion (secretion of a given AP hormone evoked by a noncorresponding HRH) and transdifferentiation (phenotypic switch between different mature cell types without cell division). Here we combine calcium imaging (to assess responses to the four HRHs) and multiple sequential immunoassay of the six AP hormones to perform a single-cell phenotypic study of thyrotropes in normal male and female mice. Surprisingly, most of the thyrotropes were polyhormonal, containing, in addition to thyrotropin (TSH), luteinizing hormone (40–42%) and prolactin (19–21%). Thyrotropes costoring growth hormone and/or ACTH were found only in females (24% of each type). These results suggest that costorage of the different hormones does not happen at random and that gender favors certain hormone combinations. Our results indicate that thyrotropes are a mosaic of cell phenotypes rather than a single cell type. The striking promiscuity of TSH storage should originate considerable mix-up of AP hormone secretions on stimulation of thyrotropes. However, response to thyrotropin-releasing hormone was much weaker in the polyhormonal thyrotropes than in the monohormonal ones. This would limit the appearance of paradoxical secretion under physiological conditions and suggests that timing of hormone and HRH receptor expression during the transdifferentiation process is finely and differentially regulated.

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5

Lotti, Victor J., Raymond S. L. Chang, Deborah J. Cerino, Paul J. Kling, Daniel F. Veber, and Ruth F. Nutt. "Thyrotropin-releasing hormone receptors in gut tissues resemble pituitary receptors." Neuroscience Letters 64, no. 2 (February 1986): 173–76. http://dx.doi.org/10.1016/0304-3940(86)90095-9.

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6

Golubeva, M. G. "Thyrotropin-releasing hormone: structure, synthesis, receptors, and basic effects." Neurochemical Journal 7, no. 2 (April 2013): 98–102. http://dx.doi.org/10.1134/s1819712413020037.

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7

Gershengorn, M. C., and R. Osman. "Molecular and cellular biology of thyrotropin-releasing hormone receptors." Physiological Reviews 76, no. 1 (January 1, 1996): 175–91. http://dx.doi.org/10.1152/physrev.1996.76.1.175.

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Thyrotropin-releasing hormone (TRH) receptor (TRH-R) complementary DNAs have been cloned from several species. The deduced amino acid sequences are compatible with TRH-R being a seven-transmembrane-spanning G protein-coupled receptor. These complementary DNAs and reagents derived from them have permitted detailed study of TRH-R biology at the molecular and cellular levels. Studies that have been performed since 1990 are reviewed in this article under the following headings: TRH-R gene, tissue distribution of TRH-R, primary structure of TRH-Rs, three-dimensional structure of the TRH-R binding pocket, TRH-R and G proteins, TRH-R activation, TRH desensitization, TRH-R endocytosis, and regulation of TRH-R number. It is evident that many new insights into the structure, function, and regulation of TRH-Rs have been gained in the last several years but that our understanding of these processes is incomplete. We look forward to even greater progress in the future.

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8

Ertek, Sibel. "Molecular economy of nature with two thyrotropins from different parts of the pituitary: pars tuberalis thyroid-stimulating hormone and pars distalis thyroid-stimulating hormone." Archives of Medical Science 17, no. 1 (January 5, 2021): 189–95. http://dx.doi.org/10.5114/aoms/102476.

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Thyrotropin (TSH) is classically known to be regulated by negative feedback from thyroid hormones and stimulated by thyrotropin-releasing hormone (TRH) from the hypothalamus. At the end of the 1990s, studies showed that thyrotroph cells from the pars tuberalis (PT) did not have TRH receptors and their TSH regulation was independent from TRH stimulation. Instead, PT-thyrotroph cells were shown to have melatonin-1 (MT-1) receptors and melatonin secretion from the pineal gland stimulates TSH- subunit formation in PT. Electron microscopy examinations also revealed some important differences between PT and pars distalis (PD) thyrotrophs. PT-TSH also have low bioactivity in the peripheral circulation. Studies showed that they have different glycosylations and PT-TSH forms macro-TSH complexes in the periphery and has a longer half-life. Photoperiodism affects LH levels in animals via decreased melatonin causing increased TSH- subunit expression and induction of deiodinase-2 (DIO-2) in the brain. Mammals need a light stimulus carried into the suprachiasmatic nucleus (which is a circadian clock) and then transferred to the pineal gland to synthesize melatonin, but birds have deep brain receptors and they are stimulated directly by light stimuli to have increased PT-TSH, without the need for melatonin. Photoperiodic regulations via TSH and DIO 2/3 also have a role in appetite, seasonal immune regulation, food intake and nest-making behaviour in animals. Since humans have no clear seasonal breeding period, such studies as recent ‘’domestication locus’’ studies in poultry are interesting. PT-TSH that works like a neurotransmitter in the brain may become an important target for future studies about humans.

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9

Ertek, Sibel. "Molecular economy of nature with two thyrotropins from different parts of the pituitary: pars tuberalis thyroid-stimulating hormone and pars distalis thyroid-stimulating hormone." Archives of Medical Science 17, no. 1 (January 5, 2021): 189–95. http://dx.doi.org/10.5114/aoms/102476.

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Thyrotropin (TSH) is classically known to be regulated by negative feedback from thyroid hormones and stimulated by thyrotropin-releasing hormone (TRH) from the hypothalamus. At the end of the 1990s, studies showed that thyrotroph cells from the pars tuberalis (PT) did not have TRH receptors and their TSH regulation was independent from TRH stimulation. Instead, PT-thyrotroph cells were shown to have melatonin-1 (MT-1) receptors and melatonin secretion from the pineal gland stimulates TSH- subunit formation in PT. Electron microscopy examinations also revealed some important differences between PT and pars distalis (PD) thyrotrophs. PT-TSH also have low bioactivity in the peripheral circulation. Studies showed that they have different glycosylations and PT-TSH forms macro-TSH complexes in the periphery and has a longer half-life. Photoperiodism affects LH levels in animals via decreased melatonin causing increased TSH- subunit expression and induction of deiodinase-2 (DIO-2) in the brain. Mammals need a light stimulus carried into the suprachiasmatic nucleus (which is a circadian clock) and then transferred to the pineal gland to synthesize melatonin, but birds have deep brain receptors and they are stimulated directly by light stimuli to have increased PT-TSH, without the need for melatonin. Photoperiodic regulations via TSH and DIO 2/3 also have a role in appetite, seasonal immune regulation, food intake and nest-making behaviour in animals. Since humans have no clear seasonal breeding period, such studies as recent ‘’domestication locus’’ studies in poultry are interesting. PT-TSH that works like a neurotransmitter in the brain may become an important target for future studies about humans.

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10

Hugues, Jean-Noel, Bryan Wolf, Jacques Sebaoun, Nicole Buisson, and Danièle Gourdji. "Is thyrotropin-releasing hormone receptor involved in thyrotrope adaptation to starvation?" Acta Endocrinologica 115, no. 3 (July 1987): 353–56. http://dx.doi.org/10.1530/acta.0.1150353.

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Abstract. The aim of the present study was to delineate the involvement of TRH receptors in the thyrotrope adaptation to starvation (i.e. plasma TSH and thyroid hormone decrease, increased sensitivity to T3) by measuring [3H]TRH binding in euthyroid, hypothyroid and T3-substituted rats (175 ng/100 g body weight). Our results show that in euthyroid rats, starvation does not significantly modify either the affinity or the number of pituitary binding sites. In hypothyroid and T3-substituted rats, starvation does not alter the negative control exerted by T3 on the number of TRH binding sites. Our data indicate that the adaptation of thyrotrope to starvation does not primarily result from alterations of TRH binding sites.

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11

De Groef, Bert, Sylvia V. H. Grommen, and Veerle M. Darras. "Increasing plasma thyroxine levels during late embryogenesis and hatching in the chicken are not caused by an increased sensitivity of the thyrotropes to hypothalamic stimulation." Journal of Endocrinology 189, no. 2 (May 2006): 271–78. http://dx.doi.org/10.1677/joe.1.06492.

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The hatching process in the chicken is accompanied by dramatic changes in plasma thyroid hormones. The cause of these changes, though crucial for hatching and the onset of endothermy, is not known. One hypothesis is that the pituitary gland becomes more sensitive to hypothalamic stimulation during this period. We have tested whether the responsiveness of the thyrotropes to hypothalamic stimuli changes throughout the last week of embryonic development and hatching by studying the mRNA expression of receptors involved in the control of the secretory activity of this cell type. We used a real-time PCR set-up to quantify whole pituitary mRNA expression of the β subunit of thyrotrophin (TSH-β), type 1 thyrotrophin-releasing hormone receptor (TRH-R1), corticotrophin-releasing hormone receptors (CRH-R1 and CRH-R2) and somatostatin subtype receptor 2 (SSTR2) on every day of the last week of embryonic development, including the day of hatch and the first day of posthatch life. The thyrotrope-specific expression was investigated by a combination of in situ hybridization with immunohistochemistry at selected ages. Although TSH-β mRNA levels increased towards day 19 of incubation (E19), the expression of CRH-R2 and TRH-R1 mRNA by the thyrotropes tended to decrease during this period, suggesting a lower sensitivity of the thyrotropes to the stimulatory factors CRH and TRH. CRH-R1, which is not involved in the control of TSH secretion, increased steadily throughout the period tested. The expression of SSTR2 mRNA by the thyrotropes was low during embryonic development and increased just before hatching. We have concluded that the sensitivity of the pituitary thyrotropes to hypothalamic stimulation decreases throughout the last week of embryonic development, so that the higher expression of TSH-β mRNA around E16–E19, and hence the increasing plasma thyroxine level, is unlikely to be the result of an increased stimulation by either TRH or CRH.

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12

Donoso, M. Veronica, and J. Pablo Huidobro-Toro. "Gastrointestinal neurotensin receptors: lack of modulation by thyrotropin releasing hormone." Journal of Pharmacy and Pharmacology 37, no. 6 (June 1985): 425–28. http://dx.doi.org/10.1111/j.2042-7158.1985.tb03029.x.

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13

Peña, Pilar de la, Donato del Camino, Luis A. Pardo, Pedro Domínguez, and Francisco Barros. "GsCouples Thyrotropin-releasing Hormone Receptors Expressed inXenopusOocytes to Phospholipase C." Journal of Biological Chemistry 270, no. 8 (February 24, 1995): 3554–59. http://dx.doi.org/10.1074/jbc.270.8.3554.

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14

Hulchiy, Mariana, Hua Zhang, J. Mark Cline, Angelica Lindén Hirschberg, and Lena Sahlin. "Receptors for thyrotropin-releasing hormone, thyroid-stimulating hormone, and thyroid hormones in the macaque uterus." Menopause: The Journal of The North American Menopause Society 19, no. 11 (November 2012): 1253–59. http://dx.doi.org/10.1097/gme.0b013e318252e450.

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15

Cook, Laurie B., and Patricia M. Hinkle. "Fate of Internalized Thyrotropin-Releasing Hormone Receptors Monitored with a Timer Fusion Protein." Endocrinology 145, no. 7 (July 1, 2004): 3095–100. http://dx.doi.org/10.1210/en.2004-0304.

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Abstract Trafficking of TRH receptors was studied in a stable HEK293 cell line expressing receptor fused to a Timer protein (TRHR-Timer) that spontaneously changes from green to red over 10 h. Cells expressing TRHR-Timer responded to TRH with an 11-fold increase in inositol phosphate formation, increased intracellular free calcium, and internalization of 75% of bound [3H][N3-methyl-His2]TRH within 10 min. After a 20-min exposure to TRH at 37 C, 75–80% of surface binding sites disappeared as receptors internalized. When TRH was removed and cells incubated in hormone-free medium, approximately 75% of [3H][N3-methyl-His2]TRH binding sites reappeared at the surface over the next 2 h with or without cycloheximide. Trafficking of TRHR-Timer was monitored microscopically after addition and withdrawal of TRH. In untreated cells, both new (green) and old (red) receptors were seen at the plasma membrane, and TRH caused rapid movement of young and old receptors into cytoplasmic vesicles. When TRH was withdrawn, some TRHR-Timer reappeared at the plasma membrane after several hours, but much of the internalized receptor remained intracellular in vesicles that condensed to larger structures in perinuclear regions deeper within the cell. Strikingly, receptors that moved to the plasma membrane were generally younger (more green) than those that underwent endocytosis. There was no change in the red to green ratio over the course of the experiment in cells exposed to vehicle. The results indicate that, after agonist-driven receptor internalization, the plasma membrane is replenished with younger receptors, arising either from an intracellular pool or preferential recycling of younger receptors.

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16

Negrev, Negrin, Yuri Nyagolov, Margarita Stefanova, and Emiliya Stancheva. "Thyroid hormonal axis regulates protein C anticoagulation pathway in rats." Open Life Sciences 6, no. 4 (August 1, 2011): 518–23. http://dx.doi.org/10.2478/s11535-011-0031-y.

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AbstractEffects of the hormones of the hypothalamic-pituitary-thyroid axis on some basic parameters of the activity of protein C anticoagulation pathway in rats are studied. Thyrotropin-releasing hormone (0.06 mg/kg body mass), thyrotropin (1 IU/kg), triiodothyronine (T3) (0.08 mg/kg), thyroxine (T4) (0.08 mg/kg), administered subcutaneously for three consecutive days on four different groups of rats increased significantly activated protein C, free protein S and protein S activity, and reduced the soluble endothelial protein C receptor. Protein C antigen and total protein S were significantly elevated only by thyrotropin-releasing hormone and thyroid-stimulating hormone, but they were not affected by T3 and T4 treatment. The data indicate the hypothalamic-pituitary-thyroid axis is involved in the regulation of the protein C anticoagulation pathway in rats by activation of this system, suggesting a tendency of hypocoagulability.

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17

Bhargava, Hemendra N., Poduri Ramarao, Anil Gulati, George A. Matwyshyn, and Rameshwar Prasad. "Brain and Pituitary Receptors for Thyrotropin-Releasing Hormone in Hypothyroid Rats." Pharmacology 38, no. 4 (1989): 243–52. http://dx.doi.org/10.1159/000138543.

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18

Blanchard, Louise, and Nicholas Barden. "Ontogeny of receptors for thyrotropin-releasing hormone in the rat brain." Developmental Brain Research 24, no. 1-2 (January 1986): 85–88. http://dx.doi.org/10.1016/0165-3806(86)90175-6.

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19

Zemkova, Hana, Marek Kucka, Shuo Li, Arturo E. Gonzalez-Iglesias, Melanija Tomic, and Stanko S. Stojilkovic. "Characterization of purinergic P2X4 receptor channels expressed in anterior pituitary cells." American Journal of Physiology-Endocrinology and Metabolism 298, no. 3 (March 2010): E644—E651. http://dx.doi.org/10.1152/ajpendo.00558.2009.

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Anterior pituitary cells express cation-conducting P2X receptor channels (P2XRs), but their molecular identity, electrophysiological properties, cell-specific expression pattern, and physiological roles have been only partially characterized. In this study, we show by quantitative RT-PCR that mRNA transcripts for the P2X4 subunit are the most abundant in rat anterior pituitary tissue and confirm the P2X4R protein expression by Western blot analysis. Single-cell patch-clamp recordings show that extracellular ATP induced an inward depolarizing current in a majority of thyrotropin-releasing hormone-responsive pituitary cells, which resembled the current profile generated by recombinant P2X4R. The channels were activated and desensitized in a dose-dependent manner and deactivated rapidly. Activation of these channels led to stimulation of electrical activity and promotion of voltage-gated and voltage-insensitive Ca2+ influx. In the presence of ivermectin, a specific allosteric modulator of P2X4Rs, there was an approximately fourfold increase in the maximum amplitude of the ATP-induced inward current, accompanied by an increase in the sensitivity of receptors for ATP, slowed deactivation of receptors, and enhanced ATP-induced prolactin release. These results indicate that thyrotropin-releasing hormone-responsive cells, including lactotrophs, express homomeric and/or heteromeric P2X4Rs, which facilitate Ca2+ influx and hormone secretion.

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20

KAJI, HIDESUKE, and PATRICIA M. HINKLE. "Regulation of Thyroid Hormone Receptors and Responses by Thyrotropin-Releasing Hormone in GH4C1 Cells*." Endocrinology 121, no. 5 (November 1987): 1697–704. http://dx.doi.org/10.1210/endo-121-5-1697.

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21

Chiamolera, Maria Izabel, and Fredric E. Wondisford. "Thyrotropin-Releasing Hormone and the Thyroid Hormone Feedback Mechanism." Endocrinology 150, no. 3 (January 29, 2009): 1091–96. http://dx.doi.org/10.1210/en.2008-1795.

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Thyroid hormone (TH) plays a critical role in development, growth, and cellular metabolism. TH production is controlled by a complex mechanism of positive and negative regulation. Hypothalamic TSH-releasing hormone (TRH) stimulates TSH secretion from the anterior pituitary. TSH then initiates TH synthesis and release from the thyroid gland. The synthesis of TRH and TSH subunit genes is inhibited at the transcriptional level by TH, which also inhibits posttranslational modification and release of TSH. Although opposing TRH and TH inputs regulate the hypothalamic-pituitary-thyroid axis, TH negative feedback at the pituitary was thought to be the primary regulator of serum TSH levels. However, study of transgenic animals showed an unexpected, dominant role for TRH in regulating the hypothalamic-pituitary-thyroid axis and an unanticipated involvement of the thyroid hormone receptor ligand-dependent activation function (AF-2) domain in TH negative regulation. These results are summarized in the review. The thyrotropin-releasing hormone neuron is well-positioned to integrate information about the environment as well as circulating TH levels and ultimately affect metabolism in response to these physiological changes.

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22

De Groef, Bert, Nesya Goris, Lutgarde Arckens, Eduard R. Kühn, and Veerle M. Darras. "Corticotropin-Releasing Hormone (CRH)-Induced Thyrotropin Release Is Directly Mediated through CRH Receptor Type 2 on Thyrotropes." Endocrinology 144, no. 12 (December 1, 2003): 5537–44. http://dx.doi.org/10.1210/en.2003-0526.

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Abstract CRH is known as the main stimulator of ACTH release. In representatives of all nonmammalian vertebrates, CRH has also been shown to induce TSH secretion, acting directly at the level of the pituitary. We have investigated which cell types and receptors are involved in CRH-induced TSH release in the chicken (Gallus gallus). Because a lack of CRH type 1 receptors (CRH-R1) on the chicken thyrotropes has been previously reported, two hypotheses were tested using in situ hybridization and perifusion studies: 1) TSH secretion might be induced in a paracrine way involving melanocortins from the corticotropes; and 2) thyrotropes might express another type of CRH-R. For the latter, we have cloned a partial cDNA encoding the chicken CRH-R2. Neither α-melanotropin (α-MSH) nor its powerful analog Nle4,d-Phe7-MSH could mimic the in vitro TSH-releasing effect of ovine CRH. The nonselective melanocortin receptor blocker SHU91199 did not influence CRH- or TRH-induced TSH secretion. On the other hand, we have found that thyrotropes express CRH-R2 mRNA. The involvement of this CRH receptor in the response of thyrotropes to CRH was further confirmed by the fact that TSH release was stimulated by human urocortin III, a CRH-R2-specific agonist, whereas the TSH response to CRH was completely blocked by the CRH-R blocker astressin and the CRH-R2-specific antagonist antisauvagine-30. We conclude that CRH-induced TSH secretion is mediated by CRH-R2 expressed on thyrotropes.

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23

Phillips, William J., John J. Enyeart, and Patricia M. Hinkle. "Pituitary Thyrotropin-Releasing Hormone Receptors: Local Anesthetic Effects on Binding and Responses." Molecular Endocrinology 3, no. 9 (September 1989): 1345–51. http://dx.doi.org/10.1210/mend-3-9-1345.

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24

Manaker, S., A. Winokur, C. H. Rhodes, and T. C. Rainbow. "Autoradiographic localization of thyrotropin-releasing hormone (TRH) receptors in human spinal cord." Neurology 35, no. 3 (March 1, 1985): 328. http://dx.doi.org/10.1212/wnl.35.3.328.

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25

Pack, Alison M., S. Barak Caine, Andrew Winokur, Scott Manaker, and Alfred P. Fishman. "Autoradiographic distribution of thyrotropin-releasing hormone receptors in the african lungfishProtopterus annectens." Journal of Comparative Neurology 287, no. 1 (September 1, 1989): 19–27. http://dx.doi.org/10.1002/cne.902870103.

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26

Itadani, Hiraku, Takao Nakamura, Junko Itoh, Hisashi Iwaasa, Akio Kanatani, Joseph Borkowski, Masaki Ihara, and Masataka Ohta. "Cloning and Characterization of a New Subtype of Thyrotropin-Releasing Hormone Receptors." Biochemical and Biophysical Research Communications 250, no. 1 (September 1998): 68–71. http://dx.doi.org/10.1006/bbrc.1998.9268.

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27

Schwartzentruber, R. Steven, and Robert J. Omeljaniuk. "Thyrotropin-Releasing Hormone Receptors in the Pituitary of Rainbow Trout (Oncorhynchus mykiss)." General and Comparative Endocrinology 97, no. 2 (February 1995): 209–19. http://dx.doi.org/10.1006/gcen.1995.1020.

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28

KLINGLER, W., G. VON POSTEL, and J. REICHEL. "Influence of oestradiol-17β and testosterone on pituitary thyrotropin-releasing hormone receptors." Acta Endocrinologica 113, no. 1_Suppl (August 1986): S39. http://dx.doi.org/10.1530/acta.0.111s039.

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29

KLINGLER, W., J. REICHEL, G. VON POSTEL, and R. KNUPPEN. "Influence of different oestrogens and catecholoestrogens on pituitary thyrotropin-releasing hormone receptors." Acta Endocrinologica 116, no. 3_Suppl (August 1987): S67—S68. http://dx.doi.org/10.1530/acta.0.114s067.

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30

Funatsu, Kunihiko S., and Kazutoyo Inanaga. "Modulation of dopamine receptors by thyrotropin-releasing hormone in the rat brain." Peptides 8, no. 2 (March 1987): 319–25. http://dx.doi.org/10.1016/0196-9781(87)90107-0.

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31

Bhargava, Hemendra N., and Sumantra Das. "Evidence for opiate action at the brain receptors for thyrotropin-releasing hormone." Brain Research 368, no. 2 (March 1986): 262–67. http://dx.doi.org/10.1016/0006-8993(86)90570-6.

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32

Klingler, W., G. von Postel, J. Reichel, and R. Knuppen. "Influences of oestradiol-17β and testosterone to pituitary thyrotropin-releasing hormone receptors." Journal of Steroid Biochemistry 25 (January 1986): 78. http://dx.doi.org/10.1016/0022-4731(86)90673-4.

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33

de la Peña, P., L. M. Delgado, D. del Camino, and F. Barros. "Cloning and expression of the thyrotropin-releasing hormone receptor from GH3 rat anterior pituitary cells." Biochemical Journal 284, no. 3 (June 15, 1992): 891–99. http://dx.doi.org/10.1042/bj2840891.

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Functional thyrotropin-releasing hormone (TRH) receptors have been expressed in Xenopus laevis oocytes following the microinjection of total and poly(A)+ RNA from GH3 rat anterior pituitary tumour cells. Under voltage-clamp conditions, application of the peptide induced a biphasic Ca(2+)-dependent chloride current. The amplitude of the initial, fast, component of the response was dependent on the concentration of the hormone and on the amount of mRNA injected. Size fractionation of poly(A)+ RNA on a continuous sucrose gradient and Northern blot analysis indicated that the receptor was encoded by an mRNA of approx. 3.5 kb. A 3.28 kbp cDNA encoding the TRH receptor has been cloned and sequenced. Full functionality of the predicted 412-amino-acid receptor protein was demonstrated by functional expression of cell surface receptors in Xenopus oocytes after both cytoplasmic injection of sense RNA transcribed in vitro from this cDNA and nuclear injection of the cDNA under the control of the Herpes simplex virus thymidine kinase promoter. The predicted protein contains seven putative membrane-spanning domains and shows significant sequence identify with some G-protein-coupled receptors. RNA blot analysis indicates that the mRNA for the TRH receptor is exclusively expressed in the pituitary gland. Expression studies performed with clones in which the 3′ region of the mRNA has been successively shortened indicate that the 3′ terminal region is not an important determinant for efficient functional expression in oocytes.

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34

Nakashima, Makoto, Saburo Kajita, and Saburo Otsuki. "Reduction of rat striatal thyrotropin-releasing hormone receptors produced by repeated methamphetamine administration." Biological Psychiatry 25, no. 2 (January 1989): 191–99. http://dx.doi.org/10.1016/0006-3223(89)90163-7.

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35

Engel, Stanislav, and Marvin C. Gershengorn. "Thyrotropin-releasing hormone and its receptors — A hypothesis for binding and receptor activation." Pharmacology & Therapeutics 113, no. 2 (February 2007): 410–19. http://dx.doi.org/10.1016/j.pharmthera.2006.09.004.

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36

Manaker, S., A. Winokur, WH Rostene, and TC Rainbow. "Autoradiographic localization of thyrotropin-releasing hormone receptors in the rat central nervous system." Journal of Neuroscience 5, no. 1 (January 1, 1985): 167–74. http://dx.doi.org/10.1523/jneurosci.05-01-00167.1985.

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37

Joels, Lesley A., and Alan H. Drummond. "The interaction of benzodiazepines with thyrotropin-releasing hormone receptors on clonal pituitary cells." British Journal of Pharmacology 96, no. 2 (February 1989): 450–56. http://dx.doi.org/10.1111/j.1476-5381.1989.tb11837.x.

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38

Manaker, S., L. H. Shulman, A. Winokur, and T. C. Rainbow. "Autoradiographic localization of thyrotropin-releasing hormone receptors in amyotrophic lateral sclerosis spinal cord." Neurology 35, no. 11 (November 1, 1985): 1650. http://dx.doi.org/10.1212/wnl.35.11.1650.

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39

Zhu, Chang-Cheng, Laurie B. Cook, and Patricia M. Hinkle. "Dimerization and Phosphorylation of Thyrotropin-releasing Hormone Receptors Are Modulated by Agonist Stimulation." Journal of Biological Chemistry 277, no. 31 (May 22, 2002): 28228–37. http://dx.doi.org/10.1074/jbc.m204221200.

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40

Rahmani, Nafasat H., Anil Gulati, and Hemendra N. Bhargava. "Spinal cord thyrotropin releasing hormone receptors of morphine tolerant-dependent and abstinent rats." Peptides 11, no. 4 (July 1990): 693–95. http://dx.doi.org/10.1016/0196-9781(90)90182-5.

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41

Petrou, C. P., and A. H. Tashjian. "Evidence that the thyrotropin-releasing hormone receptor and its ligand are recycled dissociated from each other." Biochemical Journal 306, no. 1 (February 15, 1995): 107–13. http://dx.doi.org/10.1042/bj3060107.

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We have examined the trafficking of the thyrotropin-releasing hormone receptor (TRHR) and its ligand, after TRHR-TRH internalization in rat pituitary GH4C1 cells. After rapid ligand-induced receptor sequestration, the cell surface receptor pool was replenished. Replenishment was insensitive to inhibition of protein synthesis and was dependent on the duration of internalization; therefore, the replenished receptors were not newly synthesized but recycled. The total amount of recycled receptors decreased with increasing internalization time, resulting in only partial replenishment of the cell-surface receptor pool after prolonged incubation with ligand. Thus, in addition to a receptor recycling pathway, a non-cycling route exists for TRHR sorting; this route became dominant with increasing internalization periods. TRHR entry into these pathways was not determined by the affinity of the receptor-ligand interaction, because the extent of receptor recycling was similar after TRH- and methyl-TRH (MeTRH)-induced internalization. Unlike results with the TRHR, the TRH recycling pool was not depleted by the noncycling pathway. After multiple rounds of [3H]MeTRH internalization, the amount of cell-associated radioactivity increased with increasing internalization time due to accumulation of the ligand or its metabolites in a non-cycling pathway, but the absolute amount of recycled ligand remained constant after short or long internalization times. The difference in the proportion of TRHR and MeTRH that were diverted into a noncycling pathway indicated intracellular dissociation of the internalized TRHR-TRH complex. Dissociation of the internalized TRHR-TRH complex was dependent on the acidic pH in an intracellular compartment. Although extracellular acidic pH did not enhance cell-surface receptor-ligand (RL) dissociation, bafilomycin A1 inhibited both receptor and ligand recycling. We conclude that the TRHR-TRH system is unique among recycling receptors because, after RL sequestration, the TRHR-TRH complex becomes dissociated intracellularly via a bafilomycin A1-sensitive, acidic pH-dependent mechanism, and both the unoccupied TRHR and TRH recycle disassociated from each other.

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42

Decroli, Eva, and Alexander Kam. "Dampak Klinis Thyroid-Stimulating Hormone." Jurnal Kesehatan Andalas 6, no. 1 (July 20, 2017): 222. http://dx.doi.org/10.25077/jka.v6i1.674.

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Thyroid-Stimulating Hormone (TSH), yang disebut juga dengan tirotropin, adalah glikoprotein yang disekresikan oleh bagian anterior dari kelenjar hipofisis. Sintesis dan sekresi dari TSH diatur oleh faktor dari hipotalamus yang didominasi oleh thyrotropin-releasing hormone (TRH) dan faktor perifer yang didominasi oleh kadar hormon tiroid. Setelah disintesis, TSH disekresikan, lalu akan berikatan dengan reseptor yang disebut Thyroid-Stimulating Hormone Receptor (TSHR). Ikatan TSH-TSHR akan memberikan dampak klinis terhadap jaringan dan organ tempat terjadinya ikatan tersebut. Ikatan tersebut bisa terjadi pada kelenjar tiroid dan jaringan ekstratiroid. Jaringan yang sudah dikenal mengekspresikan TSHR adalah jaringan adiposa, hipotalamus, hipofisis anterior, tulang, hati dan sistem imun.

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43

COOK, Laurie B., and Patricia M. HINKLE. "Agonist-dependent up-regulation of thyrotrophin-releasing hormone receptor protein." Biochemical Journal 380, no. 3 (June 15, 2004): 815–21. http://dx.doi.org/10.1042/bj20031467.

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To study the effect of agonist on the TRH (thyrotrophin-releasing hormone) receptor protein, an epitope-tagged receptor was stably expressed in HEK-293 cells (human embryonic kidney 293 cells) and receptor levels were measured by immunoblotting. TRH caused a 5–25-fold increase in receptor protein during 48 h, which was half-maximal at 1 nM and was slowly reversible after hormone withdrawal. Chlordiazepoxide, an inverse agonist, had no effect. TRH up-regulation was mimicked by phorbol ester and blocked by the protein kinase C inhibitor GF109203X in combination with thapsigargin, which prevents a calcium response. TRH and phorbol ester increased the density of immunoreactive receptors localized at the cell surface and [3H]MeTRH (where MeTRH stands for [N3-methyl-His]TRH) binding. TRH also increased the concentration of a truncated, internalization-defective receptor. Analysis of cell lines stably expressing TRH receptors fused to the green fluorescent protein on a fluorescence-activated cell sorter showed that TRH and phorbol ester caused 2.7- and 6.8-fold increases in fusion protein expression respectively. TRH receptor up-regulation was only partially accounted for by changes in receptor mRNA, which increased 1.7-fold. TRH caused a small increase in receptor concentration in the presence of cycloheximide, actinomycin D or MG132. In contrast with the results obtained with the TRH receptor, agonist decreased the concentration of stably expressed β2-adrenergic receptors. These results show that TRH increases receptor concentration by a complex mechanism that requires signal transduction but not receptor endocytosis.

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44

Theodoropoulou, M., T. Arzberger, Y. Gruebler, Z. Korali, P. Mortini, W. Joba, AE Heufelder, GK Stalla, and L. Schaaf. "Thyrotrophin receptor protein expression in normal and adenomatous human pituitary." Journal of Endocrinology 167, no. 1 (October 1, 2000): 7–13. http://dx.doi.org/10.1677/joe.0.1670007.

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Thyrotrophin (TSH) synthesis and secretion is under the positive control of thyrotrophin releasing hormone and under the negative control of the thyroid hormones. However, it is hypothesised that TSH has a direct effect on the regulation of its own synthesis through an intrapituitary loop mediated by pituitary TSH receptors (TSH-R). The aim of this investigation was to study the expression of TSH-R in normal human pituitary at mRNA and protein levels, and to compare the pattern of protein expression between different pituitary adenomas. Using RT-PCR we were able to detect TSH-R mRNA in the normal pituitary, and immunohistochemical studies showed TSH-R protein expression in distinct areas of the anterior pituitary. Double immunostaining with antibodies against each of the intrapituitary hormones and S100 revealed that TSH-R protein is present in thyrotrophs and folliculostellate cells. Examination of 58 pituitary adenomas, including two clinically active and two clinically inactive thyrotroph adenomas, revealed TSH-R immunopositivity in only the two clinically inactive thyrotroph adenomas. This study shows, for the first time, the presence of TSH-R protein in the normal anterior pituitary and in a subset of thyrotroph adenomas. The expression of TSH-R in the thyrotroph and folliculostellate cell subpopulations provides preliminary evidence of a role for TSH in autocrine and paracrine regulatory pathways within the anterior pituitary gland.

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45

Volpi, R., P. Chiodera, L. Cerri, G. Roberti, G. Salati, P. Ferrari, R. Delsignore, G. Pedretti, L. d'Amato, and V. Coiro. "Cholinergic mediation of growth hormone secretion induced by thyrotropin-releasing hormone in cirrhotic patients." Acta Endocrinologica 114, no. 4 (April 1987): 603–8. http://dx.doi.org/10.1530/acta.0.1140603.

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Abstract. In order to evaluate the possible involvement of muscarinic cholinergic receptors in the GH response to TRH in patients with liver cirrhosis, 8 males with post-hepatitic cirrhosis and 11 males with postalcoholic cirrhosis were primed with the anticholinergic agent pirenzepine and tested with TRH. In addition, 10 male patients affected by piecemeal necrosis were tested in a similar manner. High basal concentrations of GH were found in all groups. None of the patients with piecemeal necrosis responded to TRH, whereas in patients with post-hepatitic and in post-alcoholic cirrhosis, TRH induced a significant rise in GH levels. The priming with pirenzepine (40 mg given iv 10 min before TRH) completely blocked the TRH-induced GH increase, but did not affect the TRH-induced TSH release. These data suggest that a muscarinic cholinergic pathway is involved in the anomalous response of GH to TRH in patients with liver cirrhosis. The lack of effect of pirenzepine on the TRH-stimulated TSH release suggests that the muscarinic cholinergic mediation is peculiar for the effect of TRH on GH secretion.

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46

Brady, K. D., and A. H. Tashjian. "Synthesis and characterization of a high-affinity photoactivatable analogue of thyrotropin-releasing hormone." Biochemical Journal 281, no. 1 (January 1, 1992): 179–84. http://dx.doi.org/10.1042/bj2810179.

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An analogue of thyrotropin-releasing hormone (TRH, pGlu-His-ProNH2), i.e. pGlu-His-ProNH-(CH2)6-(4-azidosalicylamide) (TRH-ASA), has been synthesized and, in a radioiodinated form (TRH-IASA), characterized and used as a photoaffinity reagent to label the TRH receptor on rat pituitary GH4C1 cells. TRH-IASA bound to GH4C1 cells with high affinity (Kd = 8 nM), comparable with that of TRH binding. The binding of TRH-IASA was competitive with binding of TRH, two TRH analogues and a TRH receptor antagonist, chlordiazepoxide. TRH-IASA did not bind to or label GH12C1 cells, which lack functional TRH receptors. Labelling of GH4C1 cells with TRH-IASA followed by SDS/PAGE and autoradiography of membrane proteins demonstrated labelling of a single polypeptide which ran as a diffuse band between 71 and 91 kDa, centred at 76 kDa. No change in this labelling pattern was observed as a function of the length of time (between 5 min and 2 h) that GH4C1 cells were incubated with 3 nM-TRH-IASA. Using either a very short (5 s) photolysis interval or low TRH-IASA concentrations, only the 76 kDa band was labelled. Minor bands appeared only after extended photolysis and use of high TRH-IASA concentrations. We conclude that the TRH receptor from rat pituitary GH4C1 cells is a single peptide with an apparent molecular mass of 76 kDa. Details of the chemical synthesis of TRH-ASA are given in Supplementary Publication SUP 50167 (5 pages), which has been deposited at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1992) 281, 5.

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47

Yoshida, Shigeru. "Gonadotropin-releasing hormone (GnRH) and thyrotropin-releasing hormone (TRH) receptors expressed in Xenopus oocytes by injection of mammalian anterior pituitary mRNA." Neuroscience Research Supplements 16 (January 1991): 164. http://dx.doi.org/10.1016/0921-8696(91)91128-f.

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48

Ladram, A., M. Bulant, and P. Nicolas. "Characterization of receptors for thyrotropin-releasing hormone-potentiating peptide on rat anterior pituitary membranes." Journal of Biological Chemistry 267, no. 36 (December 1992): 25697–702. http://dx.doi.org/10.1016/s0021-9258(18)35663-1.

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49

Manaker, S., S. B. Caine, and A. Winokur. "Alterations in receptors for thyrotropin-releasing hormone, serotonin, and acetylcholine in amyotrophic lateral sclerosis." Neurology 38, no. 9 (September 1, 1988): 1464. http://dx.doi.org/10.1212/wnl.38.9.1464.

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50

Shen, Der C., Mao T. Lin, and Lee R. Shian. "Thyrotropin-Releasing Hormone-Induced Hyperglycemia: Possible Involvement of Cholinergic Receptors in the Lateral Hypothalamus." Neuroendocrinology 41, no. 6 (1985): 499–503. http://dx.doi.org/10.1159/000124226.

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