Relevant bibliographies by topics / Thyrotropin releasing hormone – Receptors

Academic literature on the topic 'Thyrotropin releasing hormone – Receptors'

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Published: 4 June 2021
Last updated: 12 February 2022

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

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Thyrotropin releasing hormone – Receptors"

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Sun, Yuh-Man. "Cloning and charaterisation of the Thyrotrophin-releasing hormone receptor and Gonadotrophin-relasing hormone receptor from chicken pituitary gland." Doctoral thesis, University of Cape Town, 1998. http://hdl.handle.net/11427/26973.

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The hypothalamic hormones, thyrotrophin-releasing hormone (TRH) and gonadotrophin-releasing hormone (GnRH), play pivotal roles in the growth and sexual maturation of chickens. In chickens, TRH regulates the release and synthesis of thyrotrophin (TSH) and also acts as a growth hormone-releasing factor. GnRH stimulates the release and synthesis of gonadotrophins (LH and FSH). TRH and GnRH are released and stored in the median eminence, and both hormones are transported into the pituitary gland via the hypophysial portal circulation. TRH and GnRH exert their physiological functions by binding to their specific receptors (TRH receptor and GnRH receptor, respectively) on the surface of cells in the pituitary gland. The activated receptors couple to guanine nucleotide-binding regulatory proteins (G proteins), Gq and/or G11, which in turn triggers the secondary messenger [1,2- diacylglycerol (DAG) and inositoltrisphosphate (IP3)] signalling cascade. The signalling generates the physiological effects of the hormones. The TRH-R and GnRH-R are members of G-protein coupled receptor (GPCR) family. The objective of this thesis was to clone and characterise the chicken TRH and GnRH receptors as useful tools for investigating the regulatory roles of TRH and GnRH receptors in the growth and sexual maturation of chickens. In addition, sequence information of the receptors would potentially assist in elucidating the binding sites and the molecular nature of the processes involved in receptor activation.
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Dromey, Jasmin Rachel. "Elucidating novel aspects of hypothalamic releasing hormone receptor regulation." University of Western Australia. School of Medicine and Pharmacology, 2008. http://theses.library.uwa.edu.au/adt-WU2008.0133.

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[Truncated abstract] G-protein coupled receptors (GPCRs) form one of the largest superfamilies of cell-surface receptors and respond to a vast range of stimuli including light, hormones and neurotransmitters. Although structurally similar, GPCRs are regulated by many diverse proteins, which allow the specific functions of each receptor to be carried out. This thesis focussed on two well-documented GPCRs, the thyrotropin releasing hormone receptor (TRHR) and gonadotrophin-releasing hormone receptor (GnRHR), which control the thyroid and reproductive endocrine pathways respectively. Although each of these anterior pituitary receptors is responsible for distinct physiological responses, both are integral to normal development and homeostasis. This thesis focused on three areas of GPCR regulation: ?-arrestin recruitment, transcription factor regulation and receptor up-regulation. The role of the cytoplasmic protein, ?-arrestin, has perhaps been previously underestimated in GPCR regulation, but it is now increasingly apparent that ?-arrestins not only inhibit further G-protein activation and assist in GPCR internalisation but also act as complex scaffolding platforms to mediate and amplify downstream signalling networks for hours after initial GPCR activation. It is therefore becoming increasingly important to be able to monitor such complexes in live cells over longer time-frames. ... Members of the E2F transcription family have been previously identified by this laboratory as potential GnRHR interacting proteins, via a yeast-2-hybrid screen and BRET. This thesis further investigated the role of E2F family members and demonstrates that a range of GPCRs are able to activate E2F transcriptional activity when stimulated by agonist. However, despite GnRHR displaying robust E2F transcriptional activation upon agonist stimulation, this did not result in any conclusive evidence for functional regulation, although it is possible E2F may modulate and assist in GnRHR trafficking. Furthermore it is apparent that E2F family members are highly redundant, as small effects in GnRHR binding and cell growth were only observed when protein levels of both E2F4 and E2F5 were altered. During the course of the investigation into the effect of E2F transcription on GPCR function, it was evident that long-term agonist stimulation of GnRHR had a profound effect on its expression. As this was explored further, it became clear that this agonist-induced up-regulation was both dose- and time-dependent. Furthermore, altering levels of intracellular calcium and receptor recycling/synthesis could modulate GnRHR up-regulation. In addition, an extremely sensitive CCD camera has been used for the first time to visualise the luciferase activity attributed to GnRHR up-regulation. Overall, this thesis demonstrates the complex nature of GPCR regulation. For the first time, long-term BRET analysis on ?-arrestin interactions with both classes of GPCRs has been examined in a variety of cellular formats. This has given valuable insights into the roles of phosphorylation and internalisation on ?-arrestin interaction. Additionally, this thesis has revealed that prolonged agonist exposure increases receptor expression levels, which has major implications for drug therapy regimes in the treatment of endocrine-related disorders and tumours.
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Kaur, Baljit. "The conformational analysis of thyrotropin releasing hormone and its analogues." Thesis, Manchester Metropolitan University, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.284878.

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Ouafik, L'Houcine. "Etude sur la biosynthèse de la Thyrotropin-Releasing Hormone (TRH) pancréatique." Grenoble 2 : ANRT, 1987. http://catalogue.bnf.fr/ark:/12148/cb37608585w.

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Ouafik, L'Houcine. "Etude sur la biosynthèse de la thyrotropin-releasing hormone (TRH) pancréatique." Aix-Marseille 2, 1987. http://www.theses.fr/1987AIX22004.

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Xiang, Shi Zhan. "Central control of the rat thyroid axis." Thesis, Brunel University, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.320216.

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Chen, Junling. "Ligand-independent activation of steroid hormone receptors by gonadotropin-releasing hormone." Thesis, University of British Columbia, 2010. http://hdl.handle.net/2429/34980.

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Nuclear receptors including estrogen receptors (ERs) and progesterone receptors (PRs) are activated by their ligands as well as by signaling pathways in response to peptide hormones and growth factors. In gonadotrophs, gonadotropin releasing hormones (GnRHs) act via the GnRH receptor (GnRHR). Both GnRH-I and GnRH-II activate an estrogen response element (ERE)-driven luciferase reporter gene in LβT2 mouse pituitary cells, and GnRH-I is more potent in this regard. The ERα is phosphorylated at Ser¹¹⁸ in the nucleus and at Ser¹⁶⁷ in both nucleus and cytoplasm after GnRI-I treatments, and this coincides with increased ERct binding to its co-activator, the P300/CBP-associated factor (PCAF). Most importantly, both GnRH subtypes robustly up-regulate expression of the immediate early response gene, Fosb, while co-treatment with ERα siRNA or PCAF siRNA attenuates this effect. This appears to occur at the transcriptional level because co-recruitment of ERα and PCAF to an ERE within the endogenous Fosb promoter is increased by GnRH treatments, as shown by chromatin immunoprecipitation assays. Furthermore, cross-talk between GnRH-I and PR accentuates gonadotropin production. GnRH-I activates a progesterone response element (PRE)-driven luciferase reporter gene and gonadotropin a subunit (Gsua) gene expression in two mouse gonadotroph cell lines, αT3-1 and LβT2. Up-regulation of the PRE-luciferase reporter gene by GnRH-I is attenuated by pre-treatment with protein kinase A (H89) and protein kinase C (GF109203X) inhibitors, while only GF109203X inhibits GnRH-1-induced Gsua mRNA levels. In both cell lines within the same time-frame, knockdown of PR levels by siRNA reduces GnRH-I activation of Gsua mRNA levels by approximately 40%. Both GnRH-I and GnRH-II also increase mouse Gnrhr-luciferase promoter activity and this is significantly reduced by knockdown of PR in LβT2 cells. We conclude that the effects of GnRH-I on Fosb and Gsua expression, as well as mouse Gnrhr promoter activity in mouse gonadotrophs are mediated by ligand-independent activation of ERα and PR. These ligand-independent effects of GnRHs on steroid hormone receptor function may influence the magnitude of changes in the expression of specific genes in the pituitary during the mouse estrous cycle, which in this context may serve as a model in the human menstrual cycle.
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Ebiou, Jean-Claude. "Le rôle biologique de la thyrotropin-releasing hormone (TRH) dans le pancréas endocrine." Paris 7, 1992. http://www.theses.fr/1992PA077056.

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L'objectif de ce travail est la recherche du rôle biologique de la TRH pancréatique. La TRH a été initialement isolée de l'hypothalamus et caractérisée comme pGlu-His-ProNH₂. Elle a ensuite été détectée dans le pancréas endocrine désigne comme deuxième site de synthèse du peptide. La TRH est synthétisée à partir d'un précurseur de haut poids moléculaire. La maturation complète de celui-ci génèrerait 5 molécules de TRH, et 7 peptides de connexion. Nous avons montré que la TRH secrétée par le pancréas a les mêmes caractéristiques chromatographiques que le peptide synthétique. La sécrétion de la TRH pendant le développement est stimulé par le glucose et l'arginine, tandis que ces mêmes secretagogues inhibent la sécrétion chez l'adulte. Fait intéressant, la sécrétion de la TRH augmente avec l’âge, en dépit de la chute des contenus pancréatiques. Nous avons caractérise deux peptides de connexion de la prepro-TRH: prepro-TRH160-169 et prepro-TRH178-199, dans des ilots de Langerhans, et le prepro-TRH178-199 dans le milieu de sécrétion. Concernant le rôle biologique de la TRH pancréatique, nous avons montré que: la TRH exogène stimule la sécrétion basale du glucagon; l'immunoneutralisation de la TRH endogène secrétée par l'anticorps anti-TRH inhibe significativement la sécrétion du glucagon induite par l'arginine, la sécrétion de somatostatine est légèrement inhibée. Sur une fistule pancréatique, la TRH inhibe la sécrétion exocrine des protéines, bicarbonates, et du sodium. Les résultats préliminaires sur les cellules acinaires indiquent une absence d'effet TRH. L'effet TRH, observe in vivo, serait medié par le système nerveux central. Au cours du développement, la TRH n'a pas d'effet sur les secrétions d'insuline et glucagon. Nous pensons qu'elle agirait sur le processus de prolifération des cellules insulaires. La TRH stimule la sécrétion du glucagon des cellules alpha. Il serait intéressant de rechercher l'action biologique des deux peptides de connexion. La détermination du mécanisme d'action de la TRH pancréatique implique la caractérisation des sites de liaison spécifiques. Ce travail a été publié dans: Endocrinology 1992, 130(3):1371-1379; Endocrinology 1992, 131(2) (à paraitre en aout); prostate tumeurs 1991, (7):9-10 et 1992(9):6-7.
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Ma, Chi-him Eddie. "Molecular studies of gonadotropin releasing hormone receptors and estrogen receptors in goldfish (Carassius auratus)." Click to view the E-thesis via HKUTO, 2000. http://sunzi.lib.hku.hk/hkuto/record/B4257531X.

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馬智謙 and Chi-him Eddie Ma. "Molecular studies of gonadotropin releasing hormone receptors and estrogen receptors in goldfish (Carassius auratus)." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2000. http://hub.hku.hk/bib/B4257531X.

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Books on the topic "Thyrotropin releasing hormone – Receptors"

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Deshpande, Shripad B. Thyrotropin releasing hormone on spinal reflexes. Varanasi: Ganga Kaveri Pub. House, 1997.

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Papadopoulou, Nikoletta. Localisation of corticotropin releasing hormone and its receptors in human endometrium and rat reproductive tissues. [s.l.]: typescript, 1998.

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Gillespie, Julia M. A. Melatonin mediated regulation of gonadotropin-releasing hormone (GnRH): Role of melatonin receptors and circadian rhythms. Ottawa: National Library of Canada, 2002.

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Gore, Andrea C. GnRH, the master molecule of reproduction. Boston: Kluwer Academic Publishers, 2002.

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Gore, Andrea C. GnRH, the master molecule of reproduction. Boston: Kluwer Academic Publishers, 2002.

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Gore, Andrea C. GnRH, the master molecule of reproduction. Boston: Kluwer Academic Publishers, 2002.

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Karteris, Emmanouil. Expression and signal transduction characteristics of the corticotropin-releasing hormone (CRH) receptors in human placenta and fetal membranes. [s.l.]: typescript, 2000.

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Geoffrey, Metcalf, Jackson Ivor M. D, and New York Academy of Sciences., eds. Thyrotropin-releasing hormone: Biomedical significance. New York, N.Y: New York Academy of Sciences, 1989.

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1958-, Parhar Ishwar S., ed. Gonadotropin-releasing hormone: Molecules and receptors. Amsterdam: Elsevier, 2002.

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Metcalf, Geoffrey. Thyrotropin-Releasing Hormone: Biomedical Significance (Annals of the New York Academy of Sciences). New York Academy of Sciences, 1989.

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Book chapters on the topic "Thyrotropin releasing hormone – Receptors"

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Prasad, Chandan. "Thyrotropin-Releasing Hormone." In Neurochemical Systems, 175–200. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7018-5_8.

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Goodman, R. H., and G. Mandel. "Biosynthesis of Thyrotropin releasing hormone." In Thyrotropin, edited by G. Leb, A. Passath, O. Eber, and H. Höfler, 3–6. Berlin, Boston: De Gruyter, 1987. http://dx.doi.org/10.1515/9783110867398-002.

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Kannan, C. R. "Thyrotropin and Thyrotropin-Releasing Hormone." In The Pituitary Gland, 145–69. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1849-1_5.

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Bauer, Karl, Lutz Schomburg, Heike Heuer, and Martin K. H. Schäfer. "Thyrotropin Releasing Hormone (TRH), the TRH-Receptor and the TRH-Degrading Ectoenzyme; Three Elements of a Peptidergic Signalling System." In Results and Problems in Cell Differentiation, 13–42. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-540-49421-8_2.

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Garbutt, James C., Susan G. Silva, and George A. Mason. "Thyrotropin-Releasing Hormone (TRH)." In Alcohol and Hormones, 127–45. Totowa, NJ: Humana Press, 1995. http://dx.doi.org/10.1007/978-1-4612-0243-1_6.

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Colao, Annamaria, and Claudia Pivonello. "Thyrotropin Releasing Hormone (TRH)." In Encyclopedia of Pathology, 1. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-319-28845-1_5122-1.

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Sherman, Jack E., and Ned H. Kalin. "Corticotrophin-Releasing Hormone." In Neural and Endocrine Peptides and Receptors, 195–204. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5152-8_15.

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Bambini, Giovanni, Enio Martino, Sebastiano Grasso, Giuseppe Pardo, and Fabrizio Aghini-Lombardi. "Ontogeny of Human Pancreatic Thyrotropin-Releasing Hormone." In Frontiers in Thyroidology, 299–301. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5260-0_50.

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Baumann, G. "Growth Hormone-Releasing Hormone Receptors and Pituitary Development." In Hypothalamic-Pituitary Development, 48–60. Basel: KARGER, 2001. http://dx.doi.org/10.1159/000060862.

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Mancini, Antonio, Domenico Valle, Gianluigi Conte, Michele Perrelli, Edoardo Menini, Vittorio Mignani, Paolo Carducci, Francesco Della Corte, and Laura De Marinis. "Growth Hormone (GH) Releasing Hormone- and Thyrotropin Releasing Hormone-Induced GH Release in the Acute Phase of Trauma." In Growth Hormone Secretagogues, 335–45. New York, NY: Springer New York, 1996. http://dx.doi.org/10.1007/978-1-4612-2396-2_21.

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Conference papers on the topic "Thyrotropin releasing hormone – Receptors"

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Fekete, Csaba, and Ronald M. Lechan. "Regulation of hypophysiotropic thyrotropin- and corticotrophin-releasing hormone neurons by feeding-related signals." In Xth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2007. http://dx.doi.org/10.1135/css200709043.

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