Regulatory Peptides最新文献

{"title":"DPP8 and DPP9 expression in cynomolgus monkey and Sprague Dawley rat tissues","authors":"Eric. B. Harstad ,&nbsp;Jonathan S. Rosenblum ,&nbsp;Mark D. Gorrell ,&nbsp;William E. Achanzar ,&nbsp;Lauro Minimo ,&nbsp;Jiangyue Wu ,&nbsp;Laura Rosini-Marthaler ,&nbsp;Russell Gullo ,&nbsp;Nicole D. Ordway ,&nbsp;Mark S. Kirby ,&nbsp;Kristina D. Chadwick ,&nbsp;Gregory N. Cosma ,&nbsp;Carolyn F. Moyer","doi":"10.1016/j.regpep.2013.07.003","DOIUrl":"10.1016/j.regpep.2013.07.003","url":null,"abstract":"<div><p><span>Dipeptidyl peptidases<span> (DPPs) are proteolytic enzymes that regulate many physiological systems by degrading </span></span>signaling peptides<span><span>. DPP8<span><span><span> and DPP9 are distinct from DPP4 in sequence, cellular localization and expression levels, thus implying distinct functions. However, DPP8 and DPP9 expression needs further delineation. We evaluated DPP4, DPP8 and DPP9 expression using three independent methods at the mRNA, protein, and functional levels to better understand the local physiological contribution of each </span>enzyme<span>. Sprague Dawley rats and </span></span>cynomolgus monkeys were selected for DPP4, DPP8 and DPP9 expression profiling to represent animal species commonly utilized for drug preclinical safety evaluation. A novel Xhibit assay of DPP protease activity was applied in addition to newly available antibodies for immunohistochemical localization. This combined approach can facilitate a functional evaluation of protease expression, which is important for understanding physiological relevance. Few inter-species differences were observed. Tissue mRNA and protein levels generally correlated to functional DPP4 and DPP8/9 </span></span>enzymatic activity<span>. All three proteins were seen in epithelial cells, lymphoid cells and some endothelial and vascular smooth muscle cells. Combined DPP8/DPP9 enzymatic activity was uniformly intracellular across tissues at approximately 10-fold lower levels than non-renal DPP4. Consistent levels of each DPP were detected among most non-renal tissues in rats and monkeys. DPP4 was ubiquitous, principally detected on cell membranes of epithelial and endothelial cells and was greatest in the kidney. The expression patterns suggest that DPP8 and DPP9 may act similarly across tissues, and that their actions might in part overlap with DPP4.</span></span></p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.07.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31578091","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification, tissue distribution and regulation of preproghrelin in the brain and gut of Schizothorax prenanti","authors":"RongBin Wei,&nbsp;Tao Liu,&nbsp;ChaoWei Zhou,&nbsp;XingDong Zhang,&nbsp;DengYue Yuan,&nbsp;Tao Wang,&nbsp;FangJun Lin,&nbsp;Hu Chen,&nbsp;HongWei Wu,&nbsp;ZhiQiong Li","doi":"10.1016/j.regpep.2013.07.002","DOIUrl":"10.1016/j.regpep.2013.07.002","url":null,"abstract":"<div><p><span><span>Ghrelin is an important </span>gastrointestinal hormone involved in the regulation of feeding in both mammals and fish. In this study, the preproghrelin cDNA sequence was cloning in the gut of </span><em>Schizothorax prenanti</em> (<em>S. prenanti</em>). The preproghrelin gene, encoding 103-amino acids, was strongly expressed in the gut and brain using real-time quantitative RT-PCR (qPCR). The <em>S. prenanti</em> preproghrelin was detected in embryonic developmental stages. Further, it was detectable in unfertilized eggs, suggesting that ghrelin could be classified as maternal mRNA. An experiment was conducted to determine the expression profile of ghrelin during post-feeding and fasting status of the brain and gut. The results revealed a significant postprandial decrease in ghrelin mRNA expression in the gut 6<!--> <!-->h post-feeding (hpf) and brain (1.5 and 9<!--> <!-->hpf) compared to an unfed control group, indicating that food intake and processing affect the regulation of expression of ghrelin in <em>S. prenanti</em><span>. The constructed recombinant plasmid pMD-19</span> <!-->T-ghrelin was transformed to <em>Escherichia coli</em><span><span> BL21 and induced with IPTG, and the expressed product was identified by SDS-PAGE. The prokaryotic expression vector for ghrelin was constructed successfully, and </span>fusion protein was expressed in </span><em>E. coli</em> BL21, which laid the foundation for the further study on the function of this protein and its mechanism. Overall, our results provide evidence for a highly conserved structure and biological actions of ghrelin in <em>S. prenanti</em>. Further studies are required to identify the tissue specific functions of ghrelin in <em>S. prenanti</em>.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.07.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31578093","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparison of immunomodulatory functions of three peptides from the chicken bursa of Fabricius","authors":"Xiao-Dong Liu ,&nbsp;Bin Zhou ,&nbsp;Rui-Bing Cao ,&nbsp;Xiu-Li Feng ,&nbsp;Xin-Feng Li ,&nbsp;Pu-Yan Chen","doi":"10.1016/j.regpep.2013.07.007","DOIUrl":"10.1016/j.regpep.2013.07.007","url":null,"abstract":"<div><p><span>The bursa of Fabricius (BF) is the acknowledged central humoral immune organ unique to birds which plays important roles in B cell development and antibody production. Little information on immunomodulatory functions of BF is reported, except for several reported active bursal-derived peptides. Three peptides were identified and characterized from BF through RP-HPLC and MADIL-TOF methods. They are named as bursal peptide (BP)-I, BP-II, BP-III. These peptides promoted </span>CFU<span> pre-B formation and decreased PU.1 expression. The different immunomodulatory activities of these three bursal peptides on antibody and cytokine productions<span> were verified by the immunization comparative experiment. The results showed the three bursal peptides enhanced AIV-specific antibody and cytokine production, T-cell immunophenotyping at reachable concentrations. These results indicate the important orientations for the comprehensive understanding of the humoral central immune system, and provide a novel insight on new experimental reagents for immuno-adjuvant or immunopharmacological.</span></span></p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.07.007","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31612358","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Therapeutic concentrations of valproate but not amitriptyline increase neuropeptide Y (NPY) expression in the human SH-SY5Y neuroblastoma cell line","authors":"Lorna A. Farrelly ,&nbsp;Niall T.P. Savage ,&nbsp;Cristina O'Callaghan ,&nbsp;André Toulouse ,&nbsp;Deniz M. Yilmazer-Hanke","doi":"10.1016/j.regpep.2013.08.005","DOIUrl":"10.1016/j.regpep.2013.08.005","url":null,"abstract":"<div><p>Neuropeptide Y (NPY) is a peptide found in the brain and autonomic nervous system, which is associated with anxiety, depression, epilepsy, learning and memory, sleep, obesity and circadian rhythms. NPY has recently gained much attention as an endogenous antiepileptic and antidepressant agent, as drugs with antiepileptic and/or mood-stabilizing properties may exert their action by increasing NPY concentrations, which in turn can reduce anxiety and depression levels, dampen seizures or increase seizure threshold.</p><p><span>We have used human neuroblastoma<span> SH-SY5Y cells to investigate the effect of valproate (VPA) and amitriptyline (AMI) on NPY expression at therapeutic plasma concentrations of 0.6</span></span> <!-->mM and 630<!--> <span>nM, respectively. In addition, 12-O-tetradecanoylphorbol-13-acetate (TPA) known to differentiate SH-SY5Y cells into a neuronal phenotype and to increase NPY expression through activation of protein kinase C (PKC) was applied as a positive control (16</span> <span><span>nM). Cell viability after drug treatment was tested with a 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. NPY expression was measured using immunofluorescence and quantitative RT-PCR (qRT-PCR). Results from </span>immunocytochemistry have shown NPY levels to be significantly increased following a 72</span> <!-->h but not 24<!--> <!-->h VPA treatment. A further increase in expression was observed with simultaneous VPA and TPA treatment, suggesting that the two agents may increase NPY expression through different mechanisms. The increase in NPY mRNA by VPA and TPA was confirmed with qRT-PCR after 72<!--> <!-->h. In contrast, AMI had no effect on NPY expression in SH-SY5Y cells.</p><p>Together, the data point to an elevation of human NPY mRNA and peptide levels by therapeutic concentrations of VPA following chronic treatment. Thus, upregulation of NPY may have an impact in anti-cancer treatment of neuroblastomas with VPA, and antagonizing hypothalamic NPY effects may help to ameliorate VPA-induced weight gain and obesity without interfering with the desired central effects of VPA.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.08.005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31697809","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Gestational hypertension in atrial natriuretic peptide knockout mice and the developmental origins of salt-sensitivity and cardiac hypertrophy","authors":"David W.J. Armstrong ,&nbsp;M. Yat Tse ,&nbsp;Perrie F. O'Tierney-Ginn ,&nbsp;Philip G. Wong ,&nbsp;Nicole M. Ventura ,&nbsp;Judy J. Janzen-Pang ,&nbsp;Murray F. Matangi ,&nbsp;Amer M. Johri ,&nbsp;B. Anne Croy ,&nbsp;Michael A. Adams ,&nbsp;Stephen C. Pang","doi":"10.1016/j.regpep.2013.08.006","DOIUrl":"10.1016/j.regpep.2013.08.006","url":null,"abstract":"<div><h3>Objective</h3><p>To determine the effect of gestational hypertension on the developmental origins of blood pressure (BP), altered kidney gene expression, salt-sensitivity and cardiac hypertrophy (CH) in adult offspring.</p></div><div><h3>Methods</h3><p><span>Female mice lacking atrial natriuretic peptide (ANP</span> <!-->−/−) were used as a model of gestational hypertension. Heterozygous ANP<!--> <!-->+/− offspring was bred from crossing either ANP<!--> <!-->+/+ females with ANP<!--> <!-->−/− males yielding ANP<!--> <!-->+/−^WT offspring, or from ANP<!--> <!-->−/− females with ANP<!--> <!-->+/+ males yielding ANP<!--> <!-->+/−^KO offspring. Maternal BP during pregnancy was measured using radiotelemetry. At 14<!--> <span><span>weeks of age, offspring BP, gene and protein expression were measured in the kidney with real-time quantitative PCR, receptor binding assay and </span>ELISA.</span></p></div><div><h3>Results</h3><p>ANP<!--> <!-->+/−^KO offspring exhibited normal BP at 14<!--> <!-->weeks of age, but displayed significant CH (P<!--> <!-->&lt;<!--> <!-->0.001) as compared to ANP<!--> <!-->+/−^WT offspring. ANP<!--> <!-->+/−^KO offspring exhibited significantly increased gene expression of natriuretic peptide receptor A (NPR-A) (P<!--> <!-->&lt;<!--> <span>0.001) and radioligand binding studies demonstrated significantly reduced NPR-C binding (P</span> <!-->=<!--> <!-->0.01) in the kidney. Treatment with high salt diet increased BP (P<!--> <!-->&lt;<!--> <span>0.01) and caused LV hypertrophy (P</span> <!-->&lt;<!--> <!-->0.001) and interstitial myocardial fibrosis only in ANP<!--> <!-->+/−^WT and not ANP<!--> <!-->+/−^KO offspring, suggesting gestational hypertension programs the offspring to show resistance to salt-induced hypertension and LV remodeling. Our data demonstrate that altered maternal environments can determine the salt-sensitive phenotype of offspring.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.08.006","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31687836","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of angiotensin II on rhythmic per2 expression in the suprachiasmatic nucleus and heart and daily rhythm of activity in Wistar rats","authors":"Iveta Herichová ,&nbsp;Dorota Šoltésová ,&nbsp;Kristína Szántóová ,&nbsp;Boris Mravec ,&nbsp;Denisa Neupauerová ,&nbsp;Anna Veselá ,&nbsp;Michal Zeman","doi":"10.1016/j.regpep.2013.06.016","DOIUrl":"10.1016/j.regpep.2013.06.016","url":null,"abstract":"<div><p>Endogenous daily rhythms are generated by the hierarchically organized circadian system predominantly synchronized by the external light (L): dark (D) cycle. During recent years several humoral signals have been found to influence the generation and manifestation of daily rhythm. Since most studies have been performed under <em>in vitro</em> conditions, the mechanisms employed under <em>in vivo</em><span> conditions need to be investigated. Our study focused on angiotensin II (angII)-mediated regulation of </span><em>Per2</em><span><span> expression in the suprachiasmatic nuclei (SCN) and heart and spontaneous locomotor activity in </span>Wistar rats under synchronized conditions. Angiotensin II was infused (100</span> <!-->ng/kg/min) <em>via</em> subcutaneously implanted osmotic minipumps for 7 or 28<!--> <!-->days. Samples were taken in 4-h intervals during a 24<!--> <!-->h<!--> <span>cycle and after a light pulse applied in the first and second part of the dark phase. Gene expression was measured using real time PCR. Locomotor activity was monitored using an infrared camera with a remote control installed in the animal facility. Seven days of angII infusion caused an increase in blood pressure and heart/body weight index and 28</span> <!-->days of angII infusion also increased water intake in comparison with controls. We observed a distinct daily rhythm in <em>Per2</em> expression in the SCN and heart of control rats and infused rats. Seven days of angII infusion did not influence <em>Per2</em> expression in the heart. 28<!--> <!-->days of angII treatment caused significant phase advance and a decrease in nighttime expression of <em>Per2</em> and influenced expression of clock controlled genes <em>Rev</em>-<em>erb alpha</em> and <em>Dbp</em> in the heart compared to the control. Four weeks of angII infusion decreased the responsiveness of <em>Per2</em> expression in the SCN to a light pulse at the end of the dark phase of the 24<!--> <!-->h<!--> <!-->cycle. Expression of mRNA coding angiotensin-converting enzyme (ACE) and angiotensin-converting enzyme 2 (ACE2) showed a daily rhythm in the heart of control rats. Four weeks of angII infusion caused a decrease in amplitude of rhythmic expression of <em>Ace</em>, the disappearance of rhythm and an increase in <em>Ace2</em> expression. The <em>Ace/Ace2</em> ratio showed a rhythmic pattern in the heart of control rats with peak levels during the dark phase. Angiotensin II infusion decreased the mean <em>Ace/Ace2</em><span> mRNA ratio in the heart. We observed a significant daily rhythm in expression of brain natriuretic peptide (BNP) in the heart of control rats. In hypertensive rats mean value of </span><em>Bnp</em> expression increased. Locomotor activity showed a distinct daily rhythm in both groups. Angiotensin II time dependently decreased ratio of locomotor activity in active <em>versus</em> passive phase of 24<!--> <!-->h<!--> <!-->cycle. To conclude, 28<!--> <!-->days of subcutaneous","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.06.016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31578092","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Anxiolytic action of neuromedin-U and neurotransmitters involved in mice","authors":"G. Telegdy,&nbsp;A. Adamik","doi":"10.1016/j.regpep.2013.07.008","DOIUrl":"10.1016/j.regpep.2013.07.008","url":null,"abstract":"<div><p><span><span>Peptide Neuromedin-U (NmU) is widely distributed in the central nervous system<span> and the peripheral tissues. Its physiological effects include the regulation of blood pressure, heart rate, and body temperature, and the inhibition of gastric acid secretion<span>. The action of NmU in rats is mediated by two G-protein-coupled receptors, NmU-1R and NmU-2R. NmU-2R is present mainly in the brain, and NmU-1R mainly in the periphery. Despite the great variety of the physiological action of NmU, little is known about its possible effects in different forms of behavior<span>, such as anxiety. In the present work, NmU-23 (the rodent form of the peptide) was tested for its effect on anxiety in elevated plus maze<span> test in mice. For detection of the possible involvement of neurotransmitters<span>, the mice were pretreated with receptor blockers: haloperidol (a D2, dopamine receptor antagonist), </span></span></span></span></span></span>propranolol<span> (a β-adrenergic receptor antagonist), atropine (a nonselective muscarinic acetylcholine receptor antagonist), phenoxybenzamine (a nonselective α-adrenergic receptor antagonist) or nitro-</span></span><span>l</span><span>-arginine (a nitric oxide synthase inhibitor). The peptide and nitro-</span><span>l</span><span>-arginine were administered into the lateral brain ventricle, while the receptor blockers were applied intraperitoneally.</span></p><p>An NmU-23 dose 0.5<!--> <!-->μg elicited anxiolytic action, whereas this action is faded away when the dose was increased. For further testing therefore 0.5<!--> <!-->μg i.c.v. was used. Propranolol and atropine fully blocked the NmU-induced anxiolytic action, while haloperidol, phenoxybenzamine and nitro-<span>l</span>-arginine were ineffective.</p><p>The results suggest that β-adrenergic and cholinergic mechanisms are involved in the anxiolytic action of NmU.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.07.008","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31612357","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of pericardial and plasma ghrelin levels in patients with ischemic and non-ischemic heart disease","authors":"Balazs Sax ,&nbsp;Béla Merkely ,&nbsp;Katalin Túri ,&nbsp;Andrea Nagy ,&nbsp;Abdelkrim Ahres ,&nbsp;István Hartyánszky ,&nbsp;Tivadar Hüttl ,&nbsp;Zoltán Szabolcs ,&nbsp;Károly Cseh ,&nbsp;Violetta Kékesi","doi":"10.1016/j.regpep.2013.08.003","DOIUrl":"10.1016/j.regpep.2013.08.003","url":null,"abstract":"<div><p><span>Ghrelin is an endocrine regulatory peptide with multiple functions including cardioprotective effects. It is produced in various tissues among others in the myocardium. Pericardial fluid has been proven to be a biologically active compartment of the heart that communicates with the myocardial interstitium. Thus, pericardial level of certain agents may reflect their concentration in the myocardium well. In our study we measured acylated (active) and total (acylated and non-acylated) pericardial and plasma ghrelin levels of patients with ischemic and non-ischemic heart disease. Pericardial fluid and plasma samples were obtained from patients with coronary artery disease (ISCH, n</span> <!-->=<!--> <span>54) or valvular heart disease (VHD, n</span> <!-->=<!--> <span>41) undergoing cardiac surgery. Acylated pericardial ghrelin concentrations were found to be significantly higher in patients with ischemic heart disease (ISCH vs. VHD, 32</span> <!-->±<!--> <!-->3 vs. 16<!--> <!-->±<!--> <!-->2<!--> <!-->pg/ml, p<!--> <!-->&lt;<!--> <span>0.01), whereas plasma levels of the peptide showed no difference between patient groups. Pericardial-to-plasma ratio, an index abolishing systemic effects on local ghrelin level was also significantly higher in ISCH group for both acylated and total ghrelin. Plasma total ghrelin showed negative correlation to BMI, plasma insulin and insulin resistance index HOMA-A. Pericardial acylated and total ghrelin concentrations were negatively correlated with posterior wall thickness (R</span> <!-->=<!--> <!-->−<!--> <!-->0.31, p<!--> <!-->&lt;<!--> <!-->0.05 and R<!--> <!-->=<!--> <!-->−<!--> <!-->0.35, p<!--> <!-->&lt;<!--> <span>0.01, respectively). Plasma insulin concentration and HOMA-A showed significant negative correlation with pericardial ghrelin levels. In conclusion, increased pericardial active ghrelin content and higher pericardial-to-plasma ghrelin ratio were found in ischemic heart disease as compared to non-ischemic patients suggesting an increased ghrelin production of the chronically ischemic myocardium. According to our results, pericardial ghrelin content is negatively influenced by left ventricular hypertrophy and insulin resistance.</span></p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.08.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31697776","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ghrelin stimulates synaptic formation in cultured cortical networks in a dose-dependent manner","authors":"Irina I. Stoyanova,&nbsp;Joost le Feber,&nbsp;Wim L.C. Rutten","doi":"10.1016/j.regpep.2013.07.004","DOIUrl":"10.1016/j.regpep.2013.07.004","url":null,"abstract":"<div><p><span><span><span>Ghrelin was initially related to appetite stimulation and </span>growth hormone<span> secretion. However, it also has a neuroprotective<span> effect in neurodegenerative diseases and regulates cognitive function. The cellular basis of these processes is related to </span></span></span>synaptic efficacy<span> and plasticity. Previous studies indicated that ghrelin has an excitatory effect on neuronal activity<span>, and stimulates synaptic plasticity </span></span></span><em>in vivo</em>. Plasticity in the adult brain occurs in many different ways, including changes in synapse morphology and number. Therefore, we used <em>in vitro</em><span> neuronal cultures<span> to investigate how ghrelin affects synaptogenesis<span>. We used dissociated cortical cultures of newborn rats, chronically treated with different doses of ghrelin (0.5, 1, 1.5 and 2</span></span></span> <span><span>μM). After one-, two-, three- or four weeks cultures were immunostained for the presynaptic marker synaptophysin. In parallel, additional groups of non-treated cultures were immunostained for detection of </span>ghrelin receptor (GHSR1). During development, GHSR1was increasingly expressed in all type of neurons, as well as the synaptophysin. Synaptic density depended on ghrelin concentration, and was much higher than in controls in all age groups. In conclusion, ghrelin leads to earlier network formation in dissociated cortical networks and an increase in number of synapses. The effect is probably mediated by GHSR1. These findings suggest that ghrelin may provide a novel therapeutic strategy for the treatment of disorders related to synaptic impairment.</span></p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.07.004","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31612359","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ectopic expression of ghrelin affects gastric H+–K+-ATPase activity and expression of GHR/IGF-1 system in weaned mice","authors":"G.M. Du ,&nbsp;M.J. Liu ,&nbsp;N. Parvizi ,&nbsp;R.Q. Zhao","doi":"10.1016/j.regpep.2013.06.002","DOIUrl":"10.1016/j.regpep.2013.06.002","url":null,"abstract":"<div><h3>Objectives</h3><p><span>Ghrelin<span><span> has been implicated in the regulation of gastric growth and functional development, but it is yet to be determined whether and how ghrelin over-expression may modify gastric growth, gastric acid secretion and mRNA expression of other gastric endocrine hormones. 25-day-old mice were injected intramuscularly with vacant plasmid (VP) or </span>recombinant plasmid expressing secretory ghrelin at the doses of 50</span></span> <!-->μg (LG) and 100<!--> <!-->μg (HG).</p></div><div><h3>Results</h3><p>Expression of ghrelin mRNA was detected in muscles 15<!--> <!-->days post-injection, being most abundant in HG mice. In accordance with the ghrelin expression, gastric weight increased (<em>P</em> <!-->&lt;<!--> <span>0.05) in HG mice, compared with VP control group. Significant increase of gastric mucosa H</span>⁺–K⁺-ATPase mRNA expression was detected in HG mice compared to VP control group (<em>P</em> <!-->&lt;<!--> <span>0.05). Compared with VP mice, gastric somatostatin (SS) mRNA expression decreased in LG and HG mice (</span><em>P</em> <!-->&lt;<!--> <span>0.05), while gastric gastrin expression had no significant difference.</span></p></div><div><h3>Conclusions</h3><p>I.M. injection of plasmid encoding ghrelin improved gastric growth and gastric acid secretion with decreased SS mRNA in weaned mice.</p></div>","PeriodicalId":20853,"journal":{"name":"Regulatory Peptides","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.regpep.2013.06.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31551221","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}