Relevant bibliographies by topics / Ghrelin

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Academic literature on the topic 'Ghrelin'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "Ghrelin"

1

Schwandt, Sara E., Sarath C. Peddu, and Larry G. Riley. "Differential Roles for Octanoylated and Decanoylated Ghrelins in Regulating Appetite and Metabolism." International Journal of Peptides 2010 (March 17, 2010): 1–6. http://dx.doi.org/10.1155/2010/275804.

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Since its identification in 1999, ghrelin has been identified in all vertebrate groups. The “active core” of ghrelin is highly conserved among vertebrates, suggesting its biological activity to be also conserved. In fish, both acylated forms of ghrelin have been identified; however, the ratio of the ghrelin-C8 to ghrelin-C10 is not as great as observed in mammals. In the tilapia (Oreochromis mossambicus), ghrelin-C10 is the major form of ghrelin. Since fish are known to inhabit every ecological niche on earth, studies on fish have provided valuable insight into vertebrate physiology in general; it is likely that understanding the role of both acylated forms of ghrelin, in more detail, in fish will result into novel insights in the biology of ghrelin within vertebrates. In this paper we discuss ghrelin's role in regulating appetite and metabolism in fish, in general, and provide evidence that the two tilapia ghrelins exhibit different biological roles.
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2

De Vriese, Carine, and Christine Delporte. "Autocrine proliferative effect of ghrelin on leukemic HL-60 and THP-1 cells." Journal of Endocrinology 192, no. 1 (January 2007): 199–205. http://dx.doi.org/10.1677/joe.1.06881.

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Ghrelin is a 28 amino acid peptide hormone that is mainly produced by the stomach, but also by several tissues and tumors. Ghrelin is octanoylated on the Ser3, but is also detected as a des-acylated form. Only the acylated ghrelin activates the GH secretagogue receptor (GHS-R) type 1a to stimulate GH release, and regulate food intake and energy metabolism. For the first time, we report that ghrelin and des-acyl ghrelin are present in human promyelocytic HL-60, monocytic THP-1 and lymphoblastic SupT1 cell lines. The human leukemic cell lines did not express the functional GHS-R 1a, whereas they expressed GHS-R 1b, a truncated variant of the receptor. Leukemic cell proliferation was not modified by the addition of octanoylated or des-acyl ghrelins. However, THP-1 and HL-60 cell proliferations were inhibited by SB801, an antibody directed against the N-terminal octanoylated portion of ghrelin, suggesting that octanoylated ghrelin stimulates cell proliferation via an autocrine pathway involving an as yet unidentified ghrelin receptor. Both octanoylated and des-acyl ghrelins did not alter the basal adenylate cyclase activity. Treatments of THP-1 and SupT1 cells by both octanoylated and des-acyl ghrelins did not modify the adenylate cyclase activity in response to vasoactive intestinal peptide, suggesting that ghrelin is unlikely to modulate the anti-inflammatory and differentiating properties of vasoactive intestinal peptide.
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Heppner, Kristy M., and Jenny Tong. "MECHANISMS IN ENDOCRINOLOGY: Regulation of glucose metabolism by the ghrelin system: multiple players and multiple actions." European Journal of Endocrinology 171, no. 1 (July 2014): R21—R32. http://dx.doi.org/10.1530/eje-14-0183.

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Ghrelin is a 28-amino acid peptide secreted mainly from the X/A-like cells of the stomach. Ghrelin is found in circulation in both des-acyl (dAG) and acyl forms (AG). Acylation is catalyzed by the enzyme ghrelinO-acyltransferase (GOAT). AG acts on the GH secretagogue receptor (GHSR) in the CNS to promote feeding and adiposity and also acts on GHSR in the pancreas to inhibit glucose-stimulated insulin secretion. These well-described actions of AG have made it a popular target for obesity and type 2 diabetes mellitus pharmacotherapies. However, despite the lack of a cognate receptor, dAG appears to have gluco-regulatory action, which adds an additional layer of complexity to ghrelin's regulation of glucose metabolism. This review discusses the current literature on the gluco-regulatory action of the ghrelin system (dAG, AG, GHSR, and GOAT) with specific emphasis aimed toward distinguishing AG vs dAG action.
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4

Delporte, Christine. "Structure and Physiological Actions of Ghrelin." Scientifica 2013 (2013): 1–25. http://dx.doi.org/10.1155/2013/518909.

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Ghrelin is a gastric peptide hormone, discovered as being the endogenous ligand of growth hormone secretagogue receptor. Ghrelin is a 28 amino acid peptide presenting a uniquen-octanoylation modification on its serine in position 3, catalyzed by ghrelinO-acyl transferase. Ghrelin is mainly produced by a subset of stomach cells and also by the hypothalamus, the pituitary, and other tissues. Transcriptional, translational, and posttranslational processes generate ghrelin and ghrelin-related peptides. Homo- and heterodimers of growth hormone secretagogue receptor, and as yet unidentified receptors, are assumed to mediate the biological effects of acyl ghrelin and desacyl ghrelin, respectively. Ghrelin exerts wide physiological actions throughout the body, including growth hormone secretion, appetite and food intake, gastric secretion and gastrointestinal motility, glucose homeostasis, cardiovascular functions, anti-inflammatory functions, reproductive functions, and bone formation. This review focuses on presenting the current understanding of ghrelin and growth hormone secretagogue receptor biology, as well as the main physiological effects of ghrelin.
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5

Delporte, Christine. "Recent Advances in Potential Clinical Application of Ghrelin in Obesity." Journal of Obesity 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/535624.

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Ghrelin is the natural ligand of the growth hormone secretagogue receptor (GHS-R1a). Ghrelin is a 28 amino acid peptide possessing a unique acylation on the serine in position 3 catalyzed by ghrelinO-acyltransferase (GOAT). Ghrelin stimulates growth hormone secretion, but also appetite, food intake, weight gain, and gastric emptying. Ghrelin is involved in weight regulation, obesity, type 2 diabetes, and metabolic syndrome. Furthermore, a better understanding of ghrelin biology led to the identification of molecular targets modulating ghrelin levels and/or its biological effects: GOAT, ghrelin, and GHS-R1a. Furthermore, a recent discovery, showing the involvement of bitter taste receptor T2R in ghrelin secretion and/or synthesis and food intake, suggested that T2R could represent an additional interesting molecular target. Several classes of ghrelin-related pharmacological tools for the treatment of obesity have been or could be developed to modulate the identified molecular targets.
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6

Holliday, Nicholas D., Birgitte Holst, Elena A. Rodionova, Thue W. Schwartz, and Helen M. Cox. "Importance of Constitutive Activity and Arrestin-Independent Mechanisms for Intracellular Trafficking of the Ghrelin Receptor." Molecular Endocrinology 21, no. 12 (December 1, 2007): 3100–3112. http://dx.doi.org/10.1210/me.2007-0254.

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Abstract The ghrelin receptor (GhrelinR) and its related orphan GPR39 each display constitutive signaling, but only GhrelinRs undergo basal internalization. Here we investigate these differences by considering the roles of the C tail receptor domains for constitutive internalization and activity. Furthermore the interaction between phosphorylated receptors and β-arrestin adaptor proteins has been examined. Replacement of the FLAG-tagged GhrelinR C tail with the equivalent GPR39 domain (GhR-39 chimera) preserved Gq signaling. However in contrast to the GhrelinR, GhR-39 receptors exhibited no basal and substantially decreased agonist-induced internalization in transiently transfected HEK293 cells. Internalized GhrelinR and GhR-39 were predominantly localized to recycling compartments, identified with transferrin and the monomeric G proteins Rab5 and Rab11. Both the inverse agonist [d-Arg1, d-Phe5, d-Trp7,9, Leu11] substance P and a naturally occurring mutant GhrelinR (A204E) with eliminated constitutive activity inhibited basal GhrelinR internalization. Surprisingly, we found that noninternalizing GPR39 was highly phosphorylated and that basal and agonist-induced phosphorylation of the GhR-39 chimera was elevated compared with GhrelinRs. Moreover, basal GhrelinR endocytosis occurred without significant phosphorylation, and it was not prevented by cotransfection of a dominant-negative β-arrestin1(319–418) fragment or by expression in β-arrestin1/2 double-knockout mouse embryonic fibroblasts. In contrast, agonist-stimulated GhrelinRs recruited the clathrin adaptor green fluorescent protein-tagged β-arrestin2 to endosomes, coincident with increased receptor phosphorylation. Thus, GhrelinR internalization to recycling compartments depends on C-terminal motifs and constitutive activity, but the high levels of GPR39 phosphorylation, and of the GhR-39 chimera, are not sufficient to drive endocytosis. In addition, basal GhrelinR internalization occurs independently of β-arrestins.
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Gupta, Deepali, Salil Varshney, Kripa Shankar, Sherri Osborne-Lawrence, Nathan P. Metzger, and Jeffrey Marc Zigman. "Role of Growth Hormone in Ghrelin’s Metabolic Actions." Journal of the Endocrine Society 5, Supplement_1 (May 1, 2021): A553. http://dx.doi.org/10.1210/jendso/bvab048.1127.

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Abstract Objective: Ghrelin regulates eating, body weight, and blood glucose. Upon binding to its receptor (growth hormone secretagogue receptor; GHSR), administered ghrelin increases food intake, body weight, and blood glucose. In contrast, blocking ghrelin lowers body weight and food intake. Also, mice that lack ghrelin or GHSR develop life-threatening hypoglycemia when submitted to a prolonged caloric restriction protocol providing only 40% of usual daily calories. Although GHSR was first identified in the pituitary, ghrelin was first defined by its ability to stimulate GH secretion via GHSRs, GH replacement prevents hypoglycemia in ghrelin-KO mice undergoing prolonged caloric restriction, and GH is known to modulate body composition, relatively little attention has been devoted to the role of GH-secreting pituitary somatotrophs (“GH cells”) in ghrelin action. The objective here was to determine the requirement for GHSR-expressing GH cells in mediating ghrelin’s metabolic actions. Methods: Mice with GH cell-selective GHSR deletion were generated by crossing novel GH-IRES-Cre mice to novel floxed-GHSR mice. GH cell-selective GHSR knockout mice and three control littermate groups were studied. Plasma GH, food intake, and blood glucose were measured after ip or sc ghrelin administration. Blood glucose and plasma GH were measured over the course of a 15-d calorie restriction protocol providing only 40% of usual daily calories. Results: In mice with GH cell-selective GHSR deletion, ghrelin-induced GH secretion and food intake were attenuated (by 84.1% at 15 min and by 35.3% at 45 min, respectively) as compared to controls; ghrelin-induced blood glucose elevation was unchanged. Mice with GH cell-selective GHSR deletion exhibited an attenuated GH rise (by 76.8%) over the 15-d calorie restriction period, yet they nonetheless resisted life-threatening hypoglycemia which is observed in similarly-treated ghrelin-KO mice, GHSR-null mice, and mice with hepatocyte-selective GH receptor deletion. Conclusions: These results suggest that GH cell-expressed GHSRs are required for ghrelin’s acute orexigenic and GH secretory actions but are dispensable for ghrelin’s glucoregulatory actions, at least in the settings assessed here. Although GH cell-expressed GHSRs are required for the progressive GH elevations associated with prolonged calorie restriction, they are not required for ghrelin’s overall protective effects to block prolonged calorie restriction-associated hypoglycemia.
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8

Lin, Tsung-Chieh, Yuan-Ming Yeh, Wen-Lang Fan, Yu-Chan Chang, Wei-Ming Lin, Tse-Yen Yang, and Michael Hsiao. "Ghrelin Upregulates Oncogenic Aurora A to Promote Renal Cell Carcinoma Invasion." Cancers 11, no. 3 (March 4, 2019): 303. http://dx.doi.org/10.3390/cancers11030303.

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Ghrelin is a peptide hormone, originally identified from the stomach, that functions as an endogenous ligand of the growth hormone secretagogue receptor (GHSR) and promotes growth hormone (GH) release and food intake. Increasing reports point out ghrelin’s role in cancer progression. We previously characterized ghrelin’s prognostic significance in the clear cell subtype of renal cell carcinoma (ccRCC), and its pro-metastatic ability via Snail-dependent cell migration. However, ghrelin’s activity in promoting cell invasion remains obscure. In this study, an Ingenuity Pathway Analysis (IPA)-based investigation of differentially expressed genes in Cancer Cell Line Encyclopedia (CCLE) dataset indicated the potential association of Aurora A with ghrelin in ccRCC metastasis. In addition, a significant correlation between ghrelin and Aurora A expression level in 15 ccRCC cell line was confirmed by variant probes. ccRCC patients with high ghrelin and Aurora A status were clinically associated with poor outcome. We further observed that ghrelin upregulated Aurora A at the protein and RNA levels and that ghrelin-induced ccRCC in vitro invasion and in vivo metastasis occurred in an Aurora A-dependent manner. Furthermore, MMP1, 2, 9 and 10 expressions are associated with poor outcome. In particular, MMP10 is significantly upregulated and required for the ghrelin-Aurora A axis to promote ccRCC invasion. The results of this study indicated a novel signaling mechanism in ccRCC metastasis.
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Wu, Rongqian, Mian Zhou, Padmalaya Das, Weifeng Dong, Youxin Ji, Derek Yang, Michael Miksa, Fangming Zhang, Thanjavur S. Ravikumar, and Ping Wang. "Ghrelin inhibits sympathetic nervous activity in sepsis." American Journal of Physiology-Endocrinology and Metabolism 293, no. 6 (December 2007): E1697—E1702. http://dx.doi.org/10.1152/ajpendo.00098.2007.

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Our previous studies have shown that norepinephrine (NE) upregulates proinflammatory cytokines by activating α2-adrenoceptor. Therefore, modulation of the sympathetic nervous system represents a novel treatment for sepsis. We have also shown that a novel stomach-derived peptide, ghrelin, is downregulated in sepsis and that its intravenous administration decreases proinflammatory cytokines and mitigates organ injury. However, it remains unknown whether ghrelin inhibits sympathetic activity through central ghrelin receptors [i.e., growth hormone secretagogue receptor 1a (GHSR-la)] in sepsis. To study this, sepsis was induced in male rats by cecal ligation and puncture (CLP). Ghrelin was administered through intravenous or intracerebroventricular injection 30 min before CLP. Our results showed that intravenous administration of ghrelin significantly reduced the elevated NE and TNF-α levels at 2 h after CLP. NE administration partially blocked the inhibitory effect of ghrelin on TNF-α in sepsis. GHSR-la inhibition by the administration of a GHSR-la antagonist, [d-Arg1,d-Phe5, d-Trp7,9,Leu11]substance P, significantly increased both NE and TNF-α levels even in normal animals. Markedly elevated circulating levels of NE 2 h after CLP were also significantly decreased by intracerebroventricular administration of ghrelin. Ghrelin's inhibitory effect on NE release was completely blocked by intracerebroventricular injection of the GHSR-1a antagonist or a neuropeptide Y (NPY)/Y1 receptor antagonist. However, ghrelin's downregulatory effect on TNF-α release was only partially diminished by these agents. Thus ghrelin has sympathoinhibitory properties that are mediated by central ghrelin receptors involving a NPY/Y1 receptor-dependent pathway. Ghrelin's inhibitory effect on TNF-α production in sepsis is partially because of its modulation of the overstimulated sympathetic nerve activation.
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Wu, Wei, Lei Zhu, Zhimin Dou, Qiliang Hou, Sen Wang, Ziqian Yuan, and Bin Li. "Ghrelin in Focus: Dissecting Its Critical Roles in Gastrointestinal Pathologies and Therapies." Current Issues in Molecular Biology 46, no. 1 (January 22, 2024): 948–64. http://dx.doi.org/10.3390/cimb46010061.

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This review elucidates the critical role of ghrelin, a peptide hormone mainly synthesized in the stomach in various gastrointestinal (GI) diseases. Ghrelin participates in diverse biological functions ranging from appetite regulation to impacting autophagy and apoptosis. In sepsis, it reduces intestinal barrier damage by inhibiting inflammatory responses, enhancing GI blood flow, and modulating cellular processes like autophagy and apoptosis. Notably, in inflammatory bowel disease (IBD), serum ghrelin levels serve as markers for distinguishing between active and remission phases, underscoring its potential in IBD treatment. In gastric cancer, ghrelin acts as an early risk marker, and due to its significant role in increasing the proliferation and migration of gastric cancer cells, the ghrelin–GHS-R axis is poised to become a target for gastric cancer treatment. The role of ghrelin in colorectal cancer (CRC) remains controversial; however, ghrelin analogs have demonstrated substantial benefits in treating cachexia associated with CRC, highlighting the therapeutic potential of ghrelin. Nonetheless, the complex interplay between ghrelin’s protective and potential tumorigenic effects necessitates a cautious approach to its therapeutic application. In post-GI surgery scenarios, ghrelin and its analogs could be instrumental in enhancing recovery and reducing complications. This article accentuates ghrelin’s multifunctionality, shedding light on its influence on disease mechanisms, including inflammatory responses and cancer progression, and examines its therapeutic potential in GI surgeries and disorders, advocating for continued research in this evolving field.
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Dissertations / Theses on the topic "Ghrelin"

1

Yoshimoto, Akihiro. "Plasma ghrelin and desacyl ghrelin concentrations in renal failure." Kyoto University, 2007. http://hdl.handle.net/2433/135900.

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2

Seim, Inge. "A re-examination of the Ghrelin and Ghrelin receptor genes." Thesis, Queensland University of Technology, 2009. https://eprints.qut.edu.au/29171/1/Inge_Seim_Citation.pdf.

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The last few years have seen dramatic advances in genomics, including the discovery of a large number of non-coding and antisense transcripts. This has revolutionised our understanding of multifaceted transcript structures found within gene loci and their roles in the regulation of development, neurogenesis and other complex processes. The recent and continuing surge of knowledge has prompted researchers to reassess and further dissect gene loci. The ghrelin gene (GHRL) gives rise to preproghrelin, which in turn produces ghrelin, a 28 amino acid peptide hormone that acts via the ghrelin receptor (growth hormone secretagogue receptor/GHSR 1a). Ghrelin has many important physiological and pathophysiological roles, including the stimulation of growth hormone (GH) release, appetite regulation, and cancer development. A truncated receptor splice variant, GHSR 1b, does not bind ghrelin, but dimerises with GHSR 1a, and may act as a dominant negative receptor. The gene products of ghrelin and its receptor are frequently overexpressed in human cancer While it is well known that the ghrelin axis (ghrelin and its receptor) plays a range of important functional roles, little is known about the molecular structure and regulation of the ghrelin gene (GHRL) and ghrelin receptor gene (GHSR). This thesis reports the re-annotation of the ghrelin gene, discovery of alternative 5’ exons and transcription start sites, as well as the description of a number of novel splice variants, including isoforms with a putative signal peptide. We also describe the discovery and characterisation of a ghrelin antisense gene (GHRLOS), and the discovery and expression of a ghrelin receptor (growth hormone secretagogue receptor/GHSR) antisense gene (GHSR-OS). We have identified numerous ghrelin-derived transcripts, including variants with extended 5' untranslated regions and putative secreted obestatin and C-ghrelin transcripts. These transcripts initiate from novel first exons, exon -1, exon 0 and a 5' extended 1, with multiple transcription start sites. We used comparative genomics to identify, and RT-PCR to experimentally verify, that the proximal exon 0 and 5' extended exon 1 are transcribed in the mouse ghrelin gene, which suggests the mouse and human proximal first exon architecture is conserved. We have identified numerous novel antisense transcripts in the ghrelin locus. A candidate non-coding endogenous natural antisense gene (GHRLOS) was cloned and demonstrates very low expression levels in the stomach and high levels in the thymus, testis and brain - all major tissues of non-coding RNA expression. Next, we examined if transcription occurs in the antisense orientation to the ghrelin receptor gene, GHSR. A novel gene (GHSR-OS) on the opposite strand of intron 1 of the GHSR gene was identified and characterised using strand-specific RT-PCR and rapid amplification of cDNA ends (RACE). GHSR-OS is differentially expressed and a candidate non-coding RNA gene. In summary, this study has characterised the ghrelin and ghrelin receptor loci and demonstrated natural antisense transcripts to ghrelin and its receptor. Our preliminary work shows that the ghrelin axis generates a broad and complex transcriptional repertoire. This study provides the basis for detailed functional studies of the the ghrelin and GHSR loci and future studies will be needed to further unravel the function, diagnostic and therapeutic potential of the ghrelin axis.
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3

Seim, Inge. "A re-examination of the Ghrelin and Ghrelin receptor genes." Queensland University of Technology, 2009. http://eprints.qut.edu.au/29171/.

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The last few years have seen dramatic advances in genomics, including the discovery of a large number of non-coding and antisense transcripts. This has revolutionised our understanding of multifaceted transcript structures found within gene loci and their roles in the regulation of development, neurogenesis and other complex processes. The recent and continuing surge of knowledge has prompted researchers to reassess and further dissect gene loci. The ghrelin gene (GHRL) gives rise to preproghrelin, which in turn produces ghrelin, a 28 amino acid peptide hormone that acts via the ghrelin receptor (growth hormone secretagogue receptor/GHSR 1a). Ghrelin has many important physiological and pathophysiological roles, including the stimulation of growth hormone (GH) release, appetite regulation, and cancer development. A truncated receptor splice variant, GHSR 1b, does not bind ghrelin, but dimerises with GHSR 1a, and may act as a dominant negative receptor. The gene products of ghrelin and its receptor are frequently overexpressed in human cancer While it is well known that the ghrelin axis (ghrelin and its receptor) plays a range of important functional roles, little is known about the molecular structure and regulation of the ghrelin gene (GHRL) and ghrelin receptor gene (GHSR). This thesis reports the re-annotation of the ghrelin gene, discovery of alternative 5’ exons and transcription start sites, as well as the description of a number of novel splice variants, including isoforms with a putative signal peptide. We also describe the discovery and characterisation of a ghrelin antisense gene (GHRLOS), and the discovery and expression of a ghrelin receptor (growth hormone secretagogue receptor/GHSR) antisense gene (GHSR-OS). We have identified numerous ghrelin-derived transcripts, including variants with extended 5' untranslated regions and putative secreted obestatin and C-ghrelin transcripts. These transcripts initiate from novel first exons, exon -1, exon 0 and a 5' extended 1, with multiple transcription start sites. We used comparative genomics to identify, and RT-PCR to experimentally verify, that the proximal exon 0 and 5' extended exon 1 are transcribed in the mouse ghrelin gene, which suggests the mouse and human proximal first exon architecture is conserved. We have identified numerous novel antisense transcripts in the ghrelin locus. A candidate non-coding endogenous natural antisense gene (GHRLOS) was cloned and demonstrates very low expression levels in the stomach and high levels in the thymus, testis and brain - all major tissues of non-coding RNA expression. Next, we examined if transcription occurs in the antisense orientation to the ghrelin receptor gene, GHSR. A novel gene (GHSR-OS) on the opposite strand of intron 1 of the GHSR gene was identified and characterised using strand-specific RT-PCR and rapid amplification of cDNA ends (RACE). GHSR-OS is differentially expressed and a candidate non-coding RNA gene. In summary, this study has characterised the ghrelin and ghrelin receptor loci and demonstrated natural antisense transcripts to ghrelin and its receptor. Our preliminary work shows that the ghrelin axis generates a broad and complex transcriptional repertoire. This study provides the basis for detailed functional studies of the the ghrelin and GHSR loci and future studies will be needed to further unravel the function, diagnostic and therapeutic potential of the ghrelin axis.
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4

Wisser, Anna-Sophia [Verfasser]. "Untersuchung zur zentralen Appetitregulation durch die Neuropeptide Ghrelin, desacyl-Ghrelin und Obestatin / Anna-Sophia Wisser." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2010. http://d-nb.info/1024335119/34.

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de, Amorim Laura Miranda. "The roles of the preproghrelin-derived peptides - ghrelin, desacyl ghrelin and obestatin - in prostate cancer." Thesis, Queensland University of Technology, 2012. https://eprints.qut.edu.au/53260/1/Laura_de_Amorim_thesis.pdf.

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Prostate cancer is the second most common cause of cancer related deaths in Western men. Despite the significant improvements in current treatment techniques, there is no cure for advanced metastatic, castrate-resistant disease. Early detection and prevention of progression to a castrate-resistant state may provide new strategies to improve survival. A number of growth factors have been shown to act in an autocrine/paracrine manner to modulate prostate cancer tumour growth. Our laboratory has previously shown that ghrelin and its receptors (the functional GHS-R1a and the non-functional GHS-R1b) are expressed in prostate cancer specimens and cell lines. We have shown that ghrelin increases cell proliferation in the PC3 and LNCaP prostate cancer cell lines through activation of ERK1/2, suggesting that ghrelin could regulate prostate cancer cell growth and play a role in the progression of the disease. Ghrelin is a 28 amino-acid peptide hormone, identified to be the natural ligand of the growth hormone secretagogue receptor (GHS-R1a). It is well characterised as a growth hormone releasing and as an orexigenic peptide that stimulates appetite and feeding and regulates energy expenditure and bodyweight. In addition to its orexigenic properties, ghrelin has been shown to play a regulatory role in a number of systems, including the reproductive, immune and cardiovascular systems and may play a role in a number of pathological conditions such as chronic heart failure, anorexia, cachexia, obesity, diabetes and cancer. In cancer, ghrelin and its receptor are expressed in a range of tumours and cancer cell lines and ghrelin has been demonstrated to modulate cell proliferation, apoptosis, migration and invasion in some cell types. The ghrelin gene (GHRL) encodes preproghrelin peptide, which is processed to produce three currently known functional peptides - ghrelin, desacyl ghrelin and obestatin. Prohormone convertases (PCs) have been shown to cleave the preproghrelin peptide into two primary products - the 28 amino acid peptide, ghrelin, and the remaining 117 amino acid C-terminal peptide, C-ghrelin. C-ghrelin can then be further processed to produce the 23 amino acid peptide, obestatin. Ghrelin circulates in two different forms - an octanoylated form (known as ghrelin) and a non-octanoylated form, desacyl ghrelin. The unique post-translational addition of octanoic acid to the serine 3 residue of the propeptide chain to form acylated ghrelin is catalysed by ghrelin O-acyltransferase (GOAT). This modification is necessary for binding of ghrelin to its only known functional receptor, the GHS-R1a. As desacyl ghrelin cannot bind and activate the GHS-R1a, it was initially thought to be an inactive peptide, despite the fact that it circulates at much higher levels than ghrelin. Further research has demonstrated that desacyl ghrelin is biologically active and shares some of the actions of ghrelin, as well as having some opposing and distinct roles. Interestingly, both ghrelin and desacyl ghrelin have been shown to modulate apoptosis, cell differentiation and proliferation in some cell types, and to stimulate cell proliferation through activation of ERK1/2 and PI3K/Akt pathways. The third known peptide product of the ghrelin preprohormone, obestatin, was initially thought to oppose the actions of ghrelin in appetite regulation and food intake and to mediate its effects through the G protein-coupled receptor 39 (GPR39). Subsequent research failed to reproduce the initial findings, however, and the possible anorexigenic effects of obestatin, as well as the identity of its receptor, remain unclear. Obestatin plays some important physiological roles, including roles in improving memory, the inhibition of thirst and anxiety, increased secretion of pancreatic juice, and regulation of cell proliferation, survival, apoptosis and differentiation. Preliminary studies have also shown that obestatin stimulates cell proliferation in some cell types through activation of ERK1/2, Akt and PKC pathways. Overall, however, at the commencement of this PhD project, relatively little was known regarding the functions and mechanisms of action of the preproghrelin-derived functional peptides in modulating prostate cancer cell proliferation. The roles of obestatin, and desacyl ghrelin as potential growth factors had not previously been investigated, and the potential expression and regulation of the preproghrelin processing enzymes, GOAT and prohormone convertases was unknown in prostate cancer cell lines. Therefore, the overall objectives of this study were to: 1. investigate the effects of obestatin on cell proliferation and signaling in prostate cancer cell lines 2. compare the effects of desacyl ghrelin and ghrelin on cell proliferation and signaling in prostate cancer cell lines 3. investigate whether prostate cancer cell lines possess the necessary enzymatic machinery to produce ghrelin and desacyl ghrelin and if these peptides can regulate GOAT expression Our laboratory has previously shown that ghrelin stimulates cell proliferation in the PC3 and LNCaP prostate cancer cell line through activation of the ERK1/2 pathway. In this study it has been demonstrated that treatments with either ghrelin, desacyl ghrelin or obestatin over 72 hours significantly increased cell proliferation in the PC3 prostate cancer cell line but had no significant effect in the RWPE-1 transformed normal prostate cell line. Ghrelin (1000nM) stimulated cell proliferation in the PC3 prostate cancer cell line by 31.66 6.68% (p<0.01) with the WST-1 method, and 13.55 5.68% (p<0.05) with the CyQUANT assay. Desacyl ghrelin (1000nM) increased cell proliferation in PC3 cells by 21.73 2.62% (p<0.01) (WST-1), and 15.46 7.05% (p<0.05) (CyQUANT) above untreated control. Obestatin (1000nM) induced a 28.37 7.47% (p<0.01) (WST-1) and 12.14 7.47% (p<0.05) (CyQUANT) significant increase in cell proliferation in the PC3 prostate cancer cell line. Ghrelin and desacyl ghrelin treatments stimulated Akt and ERK phosphorylation across a range of concentrations (p<0.01). Obestatin treatment significantly stimulated Akt, ERK and PKC phosphorylation (p<0.05). Through the use of specific inhibitors, the MAPK inhibitor U0126 and the Akt1/2 kinase inhibitor, it was demonstrated that ghrelin- and obestatin-induced cell proliferation in the PC3 prostate cancer cell line is mediated through activation of ERK1/2 and Akt pathways. Although desacyl ghrelin significantly stimulated Akt and ERK phosphorylation, U0126 failed to prevent desacyl ghrelin-induced cell proliferation suggesting ghrelin and desacyl ghrelin might act through different mechanisms to increase cell proliferation. Ghrelin and desacyl ghrelin have shown a proliferative effect in osteoblasts, pancreatic -cells and cardiomyocytes through activation of ERK1/2 and PI3K/Akt pathways. Here it has been shown that ghrelin and its non-acylated form exert the same function and stimulate cell proliferation in the PC3 prostate cancer cell line through activation of the Akt pathway. Ghrelin-induced proliferation was also mediated through activation of the ERK1/2 pathway, however, desacyl ghrelin seems to stimulate cell proliferation in an ERK1/2-independent manner. As desacyl ghrelin does not bind and activate GHSR1a, the only known functional ghrelin receptor, the finding that both ghrelin and desacyl ghrelin stimulate cell proliferation in the PC3 cell line suggests that these peptides could be acting through the yet unidentified alternative ghrelin receptor in this cell type. Obestatin treatment also stimulated PKC phosphorylation, however, a direct role for this pathway in stimulating cell proliferation could not be proven using available PKC pathway inhibitors, as they caused significant cell death over the extended timeframe of the cell proliferation assays. Obestatin has been shown to stimulate cell proliferation through activation of PKC isoforms in human retinal epithelial cells and in the human gastric cancer cell line KATO-III. We have demonstrated that all of the prostate-derived cell lines examined (PC3, LNCaP, DU145, 22Rv1, RWPE-1 and RWPE-2) expressed GOAT and at least one of the prohormone convertases, which are known to cleave the proghrelin peptide, PC1/3, PC2 and furin, at the mRNA level. These cells, therefore, are likely to possess the necessary machinery to cleave the preproghrelin protein and to produce the mature ghrelin and desacyl ghrelin peptides. In addition to prohormone convertases, the presence of octanoic acid is essential for acylated ghrelin production. In this study octanoic acid supplementation significantly increased cell proliferation in the PC3 prostate cancer cell line by over 20% compared to untreated controls (p<0.01), but surprisingly, not in the DU145, LNCaP or 22Rv1 prostate cancer cell lines or in the RWPE-1 and RWPE-2 prostate-derived cell lines. In addition, we demonstrated that exogenous ghrelin induced a statistically significant two-fold decrease in GOAT mRNA expression in the PC3 cell line (p<0.05), suggesting that ghrelin could pontentially downregulate its own acylation and, therefore, regulate the balance between ghrelin and desacyl ghrelin. This was not observed, however, in the DU145 and LNCaP prostate cancer cell lines. The GOAT-ghrelin system represents a direct link between ingested nutrients and regulation of ghrelin production and the ghrelin/desacyl ghrelin ratio. Regulation of ghrelin acylation is a potentially attractive and desirable tool for the development of better therapies for a number of pathological conditions where ghrelin has been shown to play a key role. The finding that desacyl ghrelin stimulates cell proliferation in the PC3 prostate cancer cell line, and responds to ghrelin in the same way, suggests that this cell line expresses an alternative ghrelin receptor. Although all the cell lines examined expressed both GHS-R1a and GHS-R1b mRNA, it remains uncertain whether these cell lines express the unidentified alternative ghrelin receptor. It is possible that the varied responses seen could be due to the expression of different ghrelin receptors in different cell lines. In addition to GOAT, prohormone convertases and octanoic acid availability may regulate the production of different peptides from the ghrelin preprohormone. The studies presented in this thesis provide significant new information regarding the roles and mechanisms of action of the preproghrelin-derived peptides, ghrelin, desacyl ghrelin and obestatin, in modulating prostate cancer cell line proliferation. A number of key questions remain to be resolved, however, including the identification of the alternative ghrelin/desacyl ghrelin receptor, the identification of the obestatin receptor, a clarification of the signaling mechanisms which mediate cell proliferation in response to obestatin treatment and a better understanding of the regulation at both the gene and post-translational levels of functional peptide generation. Further studies investigating the role of the ghrelin axis using in vivo prostate cancer models may be warranted. Until these issues are determined, the potential for the ghrelin axis, to be recognised as a novel useful target for therapy for cancer or other pathologies will be uncertain.
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Pöttinger, Thomas. "Die Modulation von Ghrelin, einem kardiovaskulären Hormon und des Ghrelin-Rezeptors in Myokard chronisch herzinsuffizienter Patienten." Diss., lmu, 2012. http://nbn-resolving.de/urn:nbn:de:bvb:19-146674.

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Gauna, Carlotta. "Metabolic aspects of the ghrelin system." [S.l.] : Rotterdam : [The Author] ; Erasmus University [Host], 2007. http://hdl.handle.net/1765/10528.

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Samsuddin, Salma. "Effects of Ghrelin in the Heart." Thesis, Queen Mary, University of London, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.515731.

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Sung, E. Z. H. "Ghrelin, motilin in health and disease." Thesis, University of Warwick, 2012. http://wrap.warwick.ac.uk/51542/.

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Ghrelin is a 28 amino-acid peptide produced predominantly by the stomach. Two main isoforms of ghrelin are currently known (octanoyl- and desoctanoyl ghrelin). It functions as a circulating orexigenic hormone In addition, it has an effect on the nervous, cardiovascular and immune system. Current data suggest that ghrelin may have beneficial anti-inflammatory effects. Chapter 3 in this thesis primarily examines the relationship between ghrelin and inflammation in Crohn’s disease (CD). Modulation of inflammation with infliximab, a powerful anti-TNFα antibody therapy, can increase total ghrelin concentration by 25%. In addition, a normal physiological post-prandial decrease in ghrelin following a meal is restored when infused with infliximab, suggesting a dysregulation of ghrelin in CD patients with active inflammation. At cellular level, there is evidence that ghrelin may have an immunosuppressive effect on activated T-lymphocytes. Chapter 4 of this thesis examines the effect of ghrelin, a manufactured agonist and des-octanoyl ghrelin on NFκB activation on a human Blymphocyte cell line. This study demonstrated that exposure to octanoyl ghrelin confers an initial increase of NFκB activation in inactivated cells of up to 50% which suggests a pro-inflammatory effect. However, NFκB activation appears to decrease at much higher concentrations of octanoyl ghrelin, which may indicate toxicity at supra-physiological levels. Ghrelin is also involved in the regulation of gastric motility and has structural similarities to motilin. Symptoms of delayed gastric emptying can occur long after cancer chemotherapy has ended. Chapter 5 of this thesis compares the contractility and pro-motility neurotransmitter expression in chemotherapy and non-chemotherapy exposed stomach tissues obtained from patients undergoing surgery for oesophagogastric cancers. Chemotherapy exposed tissues have reduced contractility to carbachol and apparent destruction of the cholinergic activity. The tendency for ghrelin receptors to increase suggests an attempt to upregulate compensating systems. In conclusion, ghrelin can be altered by inflammation and may have beneficial effects on gastric motility.
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Hataya, Yuji. "Studies on clinical significance of ghrelin." Kyoto University, 2005. http://hdl.handle.net/2433/145298.

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Books on the topic "Ghrelin"

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Ghigo, Ezio, Andrea Benso, and Fabio Broglio, eds. Ghrelin. Boston, MA: Springer US, 2004. http://dx.doi.org/10.1007/b111715.

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E, Ghigo, Benso Andrea, and Broglio Fabio, eds. Ghrelin. Boston: Kluwer Academic, 2004.

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Smith, Roy G. Ghrelin in Health and Disease. Totowa, NJ: Humana Press, 2012.

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Smith, Roy G., and Michael O. Thorner, eds. Ghrelin in Health and Disease. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-903-7.

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Portelli, Jeanelle, and Ilse Smolders, eds. Central Functions of the Ghrelin Receptor. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0823-3.

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Yamada, Hiromasa, and Kintaro Takahashi. Ghrelin: Production, action mechanisms and physiological effects. New York: Nova Biomedical, Nova Science Publishers, Inc., 2012.

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The belly fat fix: Taming ghrelin, your hunger hormone, for quick, healthy weight loss. Emmaus, Pennsylvania: Rodale, 2013.

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Giannitsopoulou, Kalliopi. The effect of subcutaneous Ghrelin administration on appetite of malnourished renal patients. Roehampton: University of Surrey Roehampton, 2004.

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Muircheartaigh, Aogán Ó. Oíche ghréine. Baile Átha Cliath: Coiscéim, 1987.

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Seán, Ó Cadhain, and Wood Tim, eds. An tSean-Ghréig. Baile Átha Cliath: An Gúm, 1996.

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Book chapters on the topic "Ghrelin"

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Gauna, Carlotta, and Aart Jan van der Lely. "Metabolic Actions of Ghrelin." In Ghrelin, 165–78. Boston, MA: Springer US, 2004. http://dx.doi.org/10.1007/1-4020-7971-0_11.

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Takimoto, Yoshiyuki. "Ghrelin." In Encyclopedia of Behavioral Medicine, 957. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-39903-0_1233.

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Galik, Elizabeth, Shin Fukudo, Yukari Tanaka, Yori Gidron, Tavis S. Campbell, Jillian A. Johnson, Kristin A. Zernicke, et al. "Ghrelin." In Encyclopedia of Behavioral Medicine, 866–67. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-1005-9_1233.

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Colao, Annamaria, Claudia Pivonello, and Giovanna Muscogiuri. "Ghrelin." In Encyclopedia of Pathology, 1–6. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-319-28845-1_5108-1.

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Hubl, W. "Ghrelin." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_1252-1.

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Hubl, W. "Ghrelin." In Springer Reference Medizin, 971–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_1252.

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Colao, Annamaria, Claudia Pivonello, and Giovanna Muscogiuri. "Ghrelin." In Endocrine Pathology, 313–18. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-62345-6_5108.

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Peter, Helga, and Thomas Penzel. "Ghrelin." In Springer Reference Medizin, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-642-54672-3_522-1.

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Papotti, Mauro, Eleonora Duregon, and Marco Volante. "Ghrelin and Tumors." In The Ghrelin System, 122–34. Basel: S. KARGER AG, 2013. http://dx.doi.org/10.1159/000346061.

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Gueorguiev, Maria, and Márta Korbonits. "Genetics of the Ghrelin System." In The Ghrelin System, 25–40. Basel: S. KARGER AG, 2013. http://dx.doi.org/10.1159/000348665.

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Conference papers on the topic "Ghrelin"

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Kizilirmak, Deniz, and Bülent Bozkurt. "Relation of ghrelin, obestatin levels and ghrelin/obestatin ratio with asthma." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa1095.

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Kizilirmak, Deniz, and Bülent Bozkurt. "Relation of ghrelin, obestatin levels and ghrelin/obestatin ratio with sleep quality." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa2331.

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Kotanidou, A. N., J. Nikitopoulou, E. Kampisiouli, E. Jahaj, M. Tzanela, I. Dimopoulou, Z. Mastora, C. Routsi, and S. Orfanos. "Ghrelin Alterations During Mouse Endotoxemia." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a5278.

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Lund, Lars, and Robert van den Heuvel. "Ghrelin improves cardiac output in HFrEF." In Heart Failure 2022, edited by Lars Lund and Marc Bonaca. Baarn, the Netherlands: Medicom Medical Publishers, 2022. http://dx.doi.org/10.55788/6e8de9aa.

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Sakamoto, Akihiro, Yasuji Arimura, Shigehisa Yanagi, Nobuhiro Matsumoto, Jun-ichi Ashitani, and Masamitsu Nakazato. "Clinical Significance Of Ghrelin In Advanced Lung Cancer." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a3488.

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Blazhenko, Alexandra A., Platon P. Khokhlov, Andrew A. Lebedev, Evgeny R. Bychkov, Sergey V. Kazakov, Vladenka A. Golts, and Peter D. Shabanov. "Study of brain ghrelin systems in Danio rerio." In II Международная конференция, посвящеенная 100- летию И.А. Држевецкой. СКФУ, 2022. http://dx.doi.org/10.38006/9612-62-6.2022.82.85.

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Stoyanova, Irina I., Remy F. Wiertz, and Wim L. C. Rutten. "Ghrelin expression in dissociated cultures of the rat neocortex." In 2009 4th International IEEE/EMBS Conference on Neural Engineering (NER). IEEE, 2009. http://dx.doi.org/10.1109/ner.2009.5109259.

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Kyomoto, Yohkoh, Takashi Nojiri, Takeshi Tokudome, Motofumi Kumazoe, Koichi Miura, Hiroshi Hosoda, Jun Hino, et al. "Ghrelin protects against bleomycin-induced pulmonary fibrosis in mice." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa918.

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Sağsöz, Hakan. "Expressions of Ghrelin and Obestatin in the Sheep Tongue." In 15th International Congress of Histochemistry and Cytochemistry. Istanbul: LookUs Scientific, 2017. http://dx.doi.org/10.5505/2017ichc.pp-85.

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Nikitopoulou, Ioanna, Anastasia Kotanidou, Alice Vassiliou, Edison Jahaj, and Stylianos Orfanos. "The role of ghrelin in critically-ill patients with sepsis." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa2120.

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Reports on the topic "Ghrelin"

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Glavaski-Joksimovic, Aleksandra, Ksenija Jeftinija, Colin G. Scanes, Lloyd L. Anderson, and Srdija Jeftinija. Ghrelin Stimulates Porcine Somatotropes. Ames (Iowa): Iowa State University, January 2004. http://dx.doi.org/10.31274/ans_air-180814-55.

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Wu, Rongqian. Treatment of TBI and Concomitant Hemorrhage with Ghrelin. Fort Belvoir, VA: Defense Technical Information Center, July 2010. http://dx.doi.org/10.21236/ada542121.

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Bohan, Michelle, Monica Foote, Brian Nonnecke, and Donald C. Beitz. Plane of Nutrition Affects Plasma Ghrelin Concentrations in Neonatal Calves. Ames (Iowa): Iowa State University, January 2007. http://dx.doi.org/10.31274/ans_air-180814-961.

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Wertz, Aimee, Travis Knight, Amanda Kreuder, Michelle Bohan, Don Beitz, and Allen H. Trenkle. Effect of Feed Intake on Plasma Ghrelin Concentration in Beef Cattle. Ames (Iowa): Iowa State University, January 2004. http://dx.doi.org/10.31274/ans_air-180814-564.

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Bohan, Michelle, Lloyd L. Anderson, Allen H. Trenkle, and Donald C. Beitz. Nutrient Regulation of Plasma Ghrelin Concentration in Lean and Overweight Female Humans. Ames (Iowa): Iowa State University, January 2007. http://dx.doi.org/10.31274/ans_air-180814-600.

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Mitoiu, Brindusa Ilinca, Roxana Nartea, and Steliana Roxana Miclaus. Impact of resistance and endurance training on ghrelin and plasma leptin levels in overweight and obese subjects. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, May 2024. http://dx.doi.org/10.37766/inplasy2024.5.0115.

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