{"title":"Effects of voluntary running in the female mice lateral septum on BDNF and corticotropin-releasing factor receptor 2.","authors":"Sofia Gustafsson, Wen Liang, Susanne Hilke","doi":"10.1155/2011/932361","DOIUrl":"https://doi.org/10.1155/2011/932361","url":null,"abstract":"<p><p>Voluntary physical activities are known to modulate anxiety and depressive/like behaviors in both animals and humans. Brain derived neurotrophic factor (BDNF), has been reported to be elevated following exercise. BDNF, as well as type 2 corticotrophin releasing factor receptor (CRFR) 2, has been shown to mediate anxiety-like behavior. In the present study we examined the effects of long-term voluntary exercise on the transcripts for BDNF and CRFR2 in the lateral septum (LS) and for CRF in the central amygdala (CeA) in female mice. Thus, increased activity of CRF in the CeA is associated with anxiety-like behavior. Quantitative RT-PCR was employed to measure levels of mRNA in punch biopsies from LS and CeA. In addition, measurements of the concentration of corticosterone and leptin in plasma were employed. In the LS, we found a three-fold increase of BDNF mRNA (P < 0.05) but no significant change in CRFR2 mRNA. No changes in CRF in the amygdala were observed but we found a decrease in the levels of plasma corticosterone. Plasma leptin and the weight of perigonadal fat pads were decreased following exercise. In conclusion, these data show that BDNF gene expression in the LS is influenced by long-term exercise in females but not CRFR2.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2011 ","pages":"932361"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2011/932361","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30188363","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
André Abts, Antonino Mavaro, Jan Stindt, Patrick J Bakkes, Sabine Metzger, Arnold J M Driessen, Sander H J Smits, Lutz Schmitt
{"title":"Easy and rapid purification of highly active nisin.","authors":"André Abts, Antonino Mavaro, Jan Stindt, Patrick J Bakkes, Sabine Metzger, Arnold J M Driessen, Sander H J Smits, Lutz Schmitt","doi":"10.1155/2011/175145","DOIUrl":"https://doi.org/10.1155/2011/175145","url":null,"abstract":"<p><p>Nisin is an antimicrobial peptide produced and secreted by several L. lactis strains and is specifically active against Gram-positive bacteria. In previous studies, nisin was purified via cation exchange chromatography at low pH employing a single-step elution using 1 M NaCl. Here, we describe an optimized purification protocol using a five-step NaCl elution to remove contaminants. The obtained nisin is devoid of impurities and shows high bactericidal activity against the nisin-sensitive L. lactis strain NZ9000. Purified nisin exhibits an IC(50) of ~3 nM, which is a tenfold improvement as compared to nisin obtained via the one-step elution procedure.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2011 ","pages":"175145"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2011/175145","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30160968","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Susana B Bravo, Jorge E Caminos, Carmen R González, María J Vázquez, María F Garcés, Libia A Cepeda, María E R García-Rendueles, Antonio Iglesias-Gamarra, Consuelo Gómez-Díaz, Miguel Lopez, Justo P Castaño, Carlos Diéguez, Rubén Nogueiras
{"title":"Leptin and fasting regulate rat gastric glucose-regulated protein 58.","authors":"Susana B Bravo, Jorge E Caminos, Carmen R González, María J Vázquez, María F Garcés, Libia A Cepeda, María E R García-Rendueles, Antonio Iglesias-Gamarra, Consuelo Gómez-Díaz, Miguel Lopez, Justo P Castaño, Carlos Diéguez, Rubén Nogueiras","doi":"10.1155/2011/969818","DOIUrl":"https://doi.org/10.1155/2011/969818","url":null,"abstract":"<p><p>The stomach secretes a wide range of peptides with essential metabolic functions, and thereby plays an important role in the regulation of energy homeostasis. Disulfide isomerase glucose-regulated protein 58 (GRp58) is a molecular chaperone member of the endoplasmic reticulum (ER) stress signaling pathway, which is a marker for human gastric cancer. Since GRp58 seems to be regulated by a phosphorylation/dephosphorylation pattern shift, we used the 2DE gel methodology and peptide mass fingerprinting-protein identification by means of MALDI-TOF mass spectrometry. We show that gastric mucosa GRp58 is dephosphorylated by fasting, and this effect is blunted when fasted rats are treated with leptin. Furthermore, we assessed the gene expression of GRp58 under different physiological settings known to be associated with energy homeostasis (fasting, leptin treatment and leptin deficiency). We found that intraperitoneal administration of leptin increases whereas leptin deficiency decreases GRp58 mRNA levels. However, GRp58 expression remains unchanged after fasting, indicating that leptin actions on GRp58 are no direct sensitivity to fasting. Dissection of the molecular pathways mediating the interactions between ER stress-related factors and nutrient availability, as well as their target genes, may open a new avenue for the study of obesity and other metabolic disorders.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2011 ","pages":"969818"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2011/969818","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30286165","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Manuela Donati, Antonietta Di Francesco, Maria Di Paolo, Natascia Fiani, Monica Benincasa, Renato Gennaro, Paola Nardini, Claudio Foschi, Roberto Cevenini
{"title":"Activity of Cathelicidin Peptides against Simkania negevensis.","authors":"Manuela Donati, Antonietta Di Francesco, Maria Di Paolo, Natascia Fiani, Monica Benincasa, Renato Gennaro, Paola Nardini, Claudio Foschi, Roberto Cevenini","doi":"10.1155/2011/708710","DOIUrl":"https://doi.org/10.1155/2011/708710","url":null,"abstract":"<p><p>The in vitro activity of six cathelicidin peptides against the reference strain Z of Simkania negevensis was investigated. Five peptides-PG-1, Bac7, SMAP-29, BMAP-27, and BMAP-28-proved to be active at very low concentrations (1 to 0.1 μg/mL), while LL-37 cathelicidin was ineffective even at a concentration of 100 μg/mL. In comparison to chlamydiae, S. negevensis proved to be more susceptible to the antimicrobial peptides tested.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2011 ","pages":"708710"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2011/708710","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30007720","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Ghrelin o-acyl transferase: bridging ghrelin and energy homeostasis.","authors":"Andrew Shlimun, Suraj Unniappan","doi":"10.1155/2011/217957","DOIUrl":"https://doi.org/10.1155/2011/217957","url":null,"abstract":"<p><p>Ghrelin O-acyl transferase (GOAT) is a recently identified enzyme responsible for the unique n-acyl modification of ghrelin, a multifunctional metabolic hormone. GOAT structure and activity appears to be conserved from fish to man. Since the acyl modification is critical for most of the biological actions of ghrelin, especially metabolic functions, GOAT emerged as a very important molecule of interest. The research on GOAT is on the rise, and several important results reiterating its significance have been reported. Notable among these discoveries are the identification of GOAT tissue expression patterns, effects on insulin secretion, blood glucose levels, feeding, body weight, and metabolism. Several attempts have been made to design and test synthetic compounds that can modulate endogenous GOAT, which could turn beneficial in favorably regulating whole body energy homeostasis. This paper will focus to provide an update on recent advances in GOAT research and its broader implications in the regulation of energy balance.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2011 ","pages":"217957"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2011/217957","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"30160969","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Differential roles for octanoylated and decanoylated ghrelins in regulating appetite and metabolism.","authors":"Sara E Schwandt, Sarath C Peddu, Larry G Riley","doi":"10.1155/2010/275804","DOIUrl":"https://doi.org/10.1155/2010/275804","url":null,"abstract":"<p><p>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.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2010 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2010/275804","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29179530","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Effect of ghrelin on glucose-insulin homeostasis: therapeutic implications.","authors":"Susana Sangiao-Alvarellos, Fernando Cordido","doi":"10.1155/2010/234709","DOIUrl":"https://doi.org/10.1155/2010/234709","url":null,"abstract":"<p><p>Ghrelin is a 28-amino-acid peptide that displays a strong growth hormone- (GH-) releasing activity through the activation of the growth hormone secretagogue receptor (GHSR). The first studies about role of ghrelin were focused on its orexigenic ability, but despite indisputable pharmacological data, the evidence for a physiological role for ghrelin in the control of appetite is much less clear. Mice with targeted deletion of either ghrelin or the GHSR exhibit an essentially normal metabolic phenotype when fed a regular chow diet, suggesting that ghrelin may have a redundant role in the regulation of food intake. RNAs for ghrelin as well as GHSR are expressed in the pancreas of rats and humans and several studies propose that ghrelin could have an important function in glucose homeostasis and insulin release, independent of GH secretion. Low plasma ghrelin levels are associated with elevated fasting insulin levels and insulin resistance, suggesting both physiological and pathophysiological roles for ghrelin. For this reason, at least theoretically, ghrelin and/or its signalling manipulation could be useful for the treatment or prevention of diseases of glucose homeostasis such as type 2 diabetes.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2010 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2010/234709","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29179533","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Ghrelin, des-acyl ghrelin, and obestatin: regulatory roles on the gastrointestinal motility.","authors":"Mineko Fujimiya, Akihiro Asakawa, Koji Ataka, Chih-Yen Chen, Ikuo Kato, Akio Inui","doi":"10.1155/2010/305192","DOIUrl":"https://doi.org/10.1155/2010/305192","url":null,"abstract":"<p><p>Ghrelin, des-acyl ghrelin, and obestatin are derived from a common prohormone, preproghrelin by posttranslational processing, originating from endocrine cells in the stomach. To examine the regulatory roles of these peptides, we applied the manometric measurement of gastrointestinal motility in freely moving conscious rat or mouse model. Ghrelin exerts stimulatory effects on the motility of antrum and duodenum in both fed and fasted state of animals. Des-acyl ghrelin exerts inhibitory effects on the motility of antrum but not on the motility of duodenum in the fasted state of animals. Obestatin exerts inhibitory effects on the motility of antrum and duodenum in the fed state but not in the fasted state of animals. NPY Y2 and Y4 receptors in the brain may mediate the action of ghrelin, CRF type 2 receptor in the brain may mediate the action of des-acyl ghrelin, whereas CRF type 1 and type 2 receptors in the brain may mediate the action of obestatin. Vagal afferent pathways might be involved in the action of ghrelin, but not involved in the action of des-acyl ghrelin, whereas vagal afferent pathways might be partially involved in the action of obestatin.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2010 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2915652/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29200117","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A Laviano, Z Krznaric, K Sanchez-Lara, I Preziosa, A Cascino, F Rossi Fanelli
{"title":"Chronic renal failure, cachexia, and ghrelin.","authors":"A Laviano, Z Krznaric, K Sanchez-Lara, I Preziosa, A Cascino, F Rossi Fanelli","doi":"10.1155/2010/648045","DOIUrl":"https://doi.org/10.1155/2010/648045","url":null,"abstract":"<p><p>Protein energy wasting is frequently observed in patients with advanced chronic renal failure and end-stage renal disease. Anorexia and reduced food intake are critical contributing factors and negatively impact on patients' survival. Ghrelin is a prophagic peptide produced by the stomach and acting at the hypothalamic level to increase the activity of orexigenic neurons. In patients with chronic renal disease, plasma levels are increased as a likely effect of reduced renal clearance. Nevertheless, patients' food intake is significantly reduced, suggesting inflammation-mediated resistance of hypothalamic nuclei to peripheral signals. A number of forms of evidence show that ghrelin resistance could be overcome by the administration of exogenous ghrelin. Therefore, ghrelin has been proposed as a potential strategy to improve food intake in chronic renal failure patients with protein energy wasting. Preliminary data are encouraging although larger prospective clinical trials are needed to confirm the results and to identify those patients who are likely to benefit most from the administration of exogenous ghrelin.</p>","PeriodicalId":14239,"journal":{"name":"International Journal of Peptides","volume":"2010 ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1155/2010/648045","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"29268497","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}