Changes in Plasma Melanocyte Stimulating Hormone, ACTH
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Leptin Stimulates Pituitary Prolactin Release Through an Extracellular Signal-Regulated Kinase-Dependent Pathway
275 Leptin stimulates pituitary prolactin release through an extracellular signal-regulated kinase-dependent pathway Christian K Tipsmark, Christina N Strom, Sean T Bailey and Russell J Borski Department of Zoology, North Carolina State University, Raleigh, North Carolina 27695-7617, USA (Correspondence should be addressed to C K Tipsmark who is now at Institute of Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark; Email: [email protected]) Abstract Leptin was initially identified as a regulator of appetite and leptin are mediated by the activation of extracellular signal- weight control centers in the hypothalamus, but appears to be regulated kinase (ERK1/2) but nothing is known about the involved in a number of physiological processes. This study cellular mechanisms by which leptin might regulate PRL was carried out to examine the possible role of leptin in secretion in vertebrates. We therefore tested whether regulating prolactin (PRL) release using the teleost pituitary ERK1/2 might be involved in the leptin PRL response and model system. This advantageous system allows isolation of a found that the ERK inhibitor, PD98059, hindered leptin- nearly pure population of lactotropes in their natural, in situ induced PRL release. We further analyzed leptin response by aggregated state. The rostral pars distalis were dissected from quantifying tyrosine and threonine phosphorylation of tilapia pituitaries and exposed to varying concentrations of ERK1/2 using western blots. One hour incubation with leptin (0, 1, 10, 100 nM) for 1 h. Release of PRL was leptin induced a concentration-dependent increase in stimulated by leptin in a potent and concentration-dependent phosphorylated, and thus active, ERK1/2. -
Searching for Novel Peptide Hormones in the Human Genome Olivier Mirabeau
Searching for novel peptide hormones in the human genome Olivier Mirabeau To cite this version: Olivier Mirabeau. Searching for novel peptide hormones in the human genome. Life Sciences [q-bio]. Université Montpellier II - Sciences et Techniques du Languedoc, 2008. English. tel-00340710 HAL Id: tel-00340710 https://tel.archives-ouvertes.fr/tel-00340710 Submitted on 21 Nov 2008 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. UNIVERSITE MONTPELLIER II SCIENCES ET TECHNIQUES DU LANGUEDOC THESE pour obtenir le grade de DOCTEUR DE L'UNIVERSITE MONTPELLIER II Discipline : Biologie Informatique Ecole Doctorale : Sciences chimiques et biologiques pour la santé Formation doctorale : Biologie-Santé Recherche de nouvelles hormones peptidiques codées par le génome humain par Olivier Mirabeau présentée et soutenue publiquement le 30 janvier 2008 JURY M. Hubert Vaudry Rapporteur M. Jean-Philippe Vert Rapporteur Mme Nadia Rosenthal Examinatrice M. Jean Martinez Président M. Olivier Gascuel Directeur M. Cornelius Gross Examinateur Résumé Résumé Cette thèse porte sur la découverte de gènes humains non caractérisés codant pour des précurseurs à hormones peptidiques. Les hormones peptidiques (PH) ont un rôle important dans la plupart des processus physiologiques du corps humain. -
Effects of Β-Lipotropin and Β-Lipotropin-Derived Peptides on Aldosterone Production in the Rat Adrenal Gland
Effects of β-Lipotropin and β-Lipotropin-derived Peptides on Aldosterone Production in the Rat Adrenal Gland Hiroaki Matsuoka, … , Patrick J. Mulrow, Roberto Franco-Saenz J Clin Invest. 1981;68(3):752-759. https://doi.org/10.1172/JCI110311. Research Article To investigate the role of non-ACTH pituitary peptides on steroidogenesis, we studied the effects of synthetic β-lipotropin, β-melanotropin, and β-endorphin on aldosterone and corticosterone stimulation using rat adrenal collagenase-dispersed capsular and decapsular cells. β-lipotropin induced a significant aldosterone stimulation in a dose-dependent fashion (10 nM-1 μM). β-endorphin, which is the carboxyterminal fragment of β-lipotropin, did not stimulate aldosterone production at the doses used (3 nM-6 μM). β-melanotropin, which is the middle fragment of β-lipotropin, showed comparable effects on aldosterone stimulation. β-lipotropin and β-melanotropin did not affect corticosterone production in decapsular cells. Although ACTH1-24 caused a significant increase in cyclic AMP production in capsular cells in a dose-dependent fashion (1 nM-1 μM), β-lipotropin and β-melanotropin did not induce an increase in cyclic AMP production at the doses used (1 nM-1 μM). The β-melanotropin analogue (glycine[Gly]10-β-melanotropin) inhibited aldosterone production induced by β- lipotropin or β-melanotropin, but did not inhibit aldosterone production induced by ACTH1-24 or angiotensin II. Corticotropin-inhibiting peptide (ACTH7-38) inhibited not only ACTH1-24 action but also β-lipotropin or β-melanotropin action; however it did not affect angiotensin II-induced aldosterone production. (saralasin [Sar]1; alanine [Ala]8)- Angiotensin II inhibited the actions of β-lipotropin and β-melanotropin as well as angiotensin II. -
Lipotropin, Melanotropin and Endorphin: in Vivo Catabolism and Entry Into Cerebrospinal Fluid
LE JOURNAL CANAD1EN DES SCIENCES NEUROLOGIQUES Lipotropin, Melanotropin and Endorphin: In Vivo Catabolism and Entry into Cerebrospinal Fluid P. D. PEZALLA, M. LIS, N. G. SEIDAH AND M. CHRETIEN SUMMARY: Anesthetized rabbits were INTRODUCTION (Rudman et al., 1974). These findings given intravenous injections of either Beta-lipotropin (beta-LPH) is a suggest, albeit weakly, that the pep beta-lipotropin (beta-LPH), beta- peptide of 91 amino acids that was tide might cross the blood-brain bar melanotropin (beta-MSH) or beta- first isolated from ovine pituitary rier. In the case of beta-endorphin, endorphin. The postinjection concentra glands (Li et al., 1965). Although there are physiological studies both tions of these peptides in plasma and cerebrospinal fluid (CSF) were measured beta-LPH has a number of physiologi supporting and negating the possibil by radioimmunoassay (RIA). The plasma cal actions including the stimulation ity that beta-endorphin crosses the disappearance half-times were 13.7 min of lipolysis and melanophore disper blood-brain barrier. The study of for beta-LPH, 5.1 min for beta-MSH, and sion, it is believed to function princi Tseng et al. (1976) supports this pos 4.8 min for beta-endorphin. Circulating pally as a prohormone for beta- sibility since they observed analgesia beta-LPH is cleaved to peptides tenta melanotropin (beta-MSH) and beta- in mice following intravenous injec tively identified as gamma-LPH and endorphin. Beta-MSH, which com tion of beta-endorphin. However, beta-endorphin. Each of these peptides prises the sequence 41-58 of beta- Pert et al. (1976) were unable to elicit appeared in the CSF within 2 min postin LPH, is considerably more potent central effects in rats by intravenous jection. -
I AMYLIN MEDIATES BRAINSTEM
AMYLIN MEDIATES BRAINSTEM CONTROL OF HEART RATE IN THE DIVING REFLEX A Dissertation Submitted to The Temple University Graduate Board In Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy By Fan Yang May, 2012 Examination committee members: Dr. Nae J Dun (advisor), Dept. of Pharmacology, Temple University Dr. Alan Cowan, Dept. of Pharmacology, Temple University Dr. Lee-Yuan Liu-Chen, Dept. of Pharmacology, Temple University Dr. Gabriela Cristina Brailoiu, Dept. of Pharmacology, Temple University Dr. Parkson Lee-Gau Chong, Dept. of Biochemistry, Temple University Dr. Hreday Sapru (external examiner), Depts. of Neurosciences, Neurosurgery & Pharmacology/Physiology, UMDNJ-NJMS. i © 2012 By Fan Yang All Rights Reserved ii ABSTRACT AMYLIN’S ROLE AS A NEUROPEPTIDE IN THE BRAINSTEM Fan Yang Doctor of Philosophy Temple University, 2012 Doctoral Advisory Committee Chair: Nae J Dun, Ph.D. Amylin, or islet amyloid polypeptide is a 37-amino acid member of the calcitonin peptide family. Amylin role in the brainstem and its function in regulating heart rates is unknown. The diving reflex is a powerful autonomic reflex, however no neuropeptides have been described to modulate its function. In this thesis study, amylin expression in the brainstem involving pathways between the trigeminal ganglion and the nucleus ambiguus was visualized and characterized using immunohistochemistry. Its functional role in slowing heart rate and also its involvement in the diving reflex were elucidated using stereotaxic microinjection, whole-cel patch-clamp, and a rat diving model. Immunohistochemical and tract tracing studies in rats revealed amylin expression in trigeminal ganglion cells, which also contained vesicular glutamate transporter 2 positive. -
A 0.70% E 0.80% Is 0.90%
US 20080317666A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2008/0317666 A1 Fattal et al. (43) Pub. Date: Dec. 25, 2008 (54) COLONIC DELIVERY OF ACTIVE AGENTS Publication Classification (51) Int. Cl. (76) Inventors: Elias Fattal, Paris (FR); Antoine A6IR 9/00 (2006.01) Andremont, Malakoff (FR); A61R 49/00 (2006.01) Patrick Couvreur, A6II 5L/12 (2006.01) Villebon-sur-Yvette (FR); Sandrine A6IPI/00 (2006.01) Bourgeois, Lyon (FR) (52) U.S. Cl. .......................... 424/1.11; 424/423; 424/9.1 (57) ABSTRACT Correspondence Address: Drug delivery devices that are orally administered, and that David S. Bradlin release active ingredients in the colon, are disclosed. In one Womble Carlyle Sandridge & Rice embodiment, the active ingredients are those that inactivate P.O.BOX 7037 antibiotics, such as macrollides, quinolones and beta-lactam Atlanta, GA 30359-0037 (US) containing antibiotics. One example of a Suitable active agent is an enzyme Such as beta-lactamases. In another embodi ment, the active agents are those that specifically treat colonic (21) Appl. No.: 11/628,832 disorders, such as Chrohn's Disease, irritable bowel syn drome, ulcerative colitis, colorectal cancer or constipation. (22) PCT Filed: Feb. 9, 2006 The drug delivery devices are in the form of beads of pectin, crosslinked with calcium and reticulated with polyethylene imine. The high crosslink density of the polyethyleneimine is (86). PCT No.: PCT/GBO6/OO448 believed to stabilize the pectin beads for a sufficient amount of time such that a Substantial amount of the active ingredi S371 (c)(1), ents can be administered directly to the colon. -
Evolution of the Neuropeptide Y and Opioid Systems and Their Genomic
It's time to try Defying gravity I think I'll try Defying gravity And you can't pull me down Wicked List of Papers This thesis is based on the following papers, which are referred to in the text by their Roman numerals. I Sundström G, Larsson TA, Brenner S, Venkatesh B, Larham- mar D. (2008) Evolution of the neuropeptide Y family: new genes by chromosome duplications in early vertebrates and in teleost fishes. General and Comparative Endocrinology Feb 1;155(3):705-16. II Sundström G, Larsson TA, Xu B, Heldin J, Lundell I, Lar- hammar D. (2010) Interactions of zebrafish peptide YYb with the neuropeptide Y-family receptors Y4, Y7, Y8a and Y8b. Manuscript III Sundström G, Xu B, Larsson TA, Heldin J, Bergqvist CA, Fredriksson R, Conlon JM, Lundell I, Denver RJ, Larhammar D. (2010) Characterization of the neuropeptide Y system's three peptides and six receptors in the frog Silurana tropicalis. Manu- script IV Dreborg S, Sundström G, Larsson TA, Larhammar D. (2008) Evolution of vertebrate opioid receptors. Proc Natl Acad Sci USA Oct 7;105(40):15487-92. V Sundström G, Dreborg S, Larhammar D. (2010) Concomitant duplications of opioid peptide and receptor genes before the origin of jawed vertebrates. PLoS One May 6;5(5):e10512. VI Sundström G, Larsson TA, Larhammar D. (2008) Phylogenet- ic and chromosomal analyses of multiple gene families syntenic with vertebrate Hox clusters. BMC Evolutionary Biology Sep 19;8:254. VII Widmark J, Sundström G, Ocampo Daza D, Larhammar D. (2010) Differential evolution of voltage-gated sodium channels in tetrapods and teleost fishes. -
Rfamide Peptides: Structure, Function, Mechanisms and Pharmaceutical Potential
Pharmaceuticals 2011, 4, 1248-1280; doi:10.3390/ph4091248 OPEN ACCESS Pharmaceuticals ISSN 1424-8247 www.mdpi.com/journal/pharmaceuticals Review RFamide Peptides: Structure, Function, Mechanisms and Pharmaceutical Potential Maria Findeisen †, Daniel Rathmann † and Annette G. Beck-Sickinger * Institute of Biochemistry, Leipzig University, Brüderstraße 34, 04103 Leipzig, Germany; E-Mails: [email protected] (M.F.); [email protected] (D.R.) † These authors contributed equally to this work. * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +49-341-9736900; Fax: +49-341-9736909. Received: 29 August 2011; in revised form: 9 September 2011 / Accepted: 15 September 2011 / Published: 21 September 2011 Abstract: Different neuropeptides, all containing a common carboxy-terminal RFamide sequence, have been characterized as ligands of the RFamide peptide receptor family. Currently, five subgroups have been characterized with respect to their N-terminal sequence and hence cover a wide pattern of biological functions, like important neuroendocrine, behavioral, sensory and automatic functions. The RFamide peptide receptor family represents a multiligand/multireceptor system, as many ligands are recognized by several GPCR subtypes within one family. Multireceptor systems are often susceptible to cross-reactions, as their numerous ligands are frequently closely related. In this review we focus on recent results in the field of structure-activity studies as well as mutational exploration of crucial positions within this GPCR system. The review summarizes the reported peptide analogs and recently developed small molecule ligands (agonists and antagonists) to highlight the current understanding of the pharmacophoric elements, required for affinity and activity at the receptor family. -
Co-Regulation of Hormone Receptors, Neuropeptides, and Steroidogenic Enzymes 2 Across the Vertebrate Social Behavior Network 3 4 Brent M
bioRxiv preprint doi: https://doi.org/10.1101/435024; this version posted October 4, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. 1 Co-regulation of hormone receptors, neuropeptides, and steroidogenic enzymes 2 across the vertebrate social behavior network 3 4 Brent M. Horton1, T. Brandt Ryder2, Ignacio T. Moore3, Christopher N. 5 Balakrishnan4,* 6 1Millersville University, Department of Biology 7 2Smithsonian Conservation Biology Institute, Migratory Bird Center 8 3Virginia Tech, Department of Biological Sciences 9 4East Carolina University, Department of Biology 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 1 bioRxiv preprint doi: https://doi.org/10.1101/435024; this version posted October 4, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. 1 Running Title: Gene expression in the social behavior network 2 Keywords: dominance, systems biology, songbird, territoriality, genome 3 Corresponding Author: 4 Christopher Balakrishnan 5 East Carolina University 6 Department of Biology 7 Howell Science Complex 8 Greenville, NC, USA 27858 9 [email protected] 10 2 bioRxiv preprint doi: https://doi.org/10.1101/435024; this version posted October 4, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. -
Five Decades of Research on Opioid Peptides: Current Knowledge and Unanswered Questions
Molecular Pharmacology Fast Forward. Published on June 2, 2020 as DOI: 10.1124/mol.120.119388 This article has not been copyedited and formatted. The final version may differ from this version. File name: Opioid peptides v45 Date: 5/28/20 Review for Mol Pharm Special Issue celebrating 50 years of INRC Five decades of research on opioid peptides: Current knowledge and unanswered questions Lloyd D. Fricker1, Elyssa B. Margolis2, Ivone Gomes3, Lakshmi A. Devi3 1Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA; E-mail: [email protected] 2Department of Neurology, UCSF Weill Institute for Neurosciences, 675 Nelson Rising Lane, San Francisco, CA 94143, USA; E-mail: [email protected] 3Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, Annenberg Downloaded from Building, One Gustave L. Levy Place, New York, NY 10029, USA; E-mail: [email protected] Running Title: Opioid peptides molpharm.aspetjournals.org Contact info for corresponding author(s): Lloyd Fricker, Ph.D. Department of Molecular Pharmacology Albert Einstein College of Medicine 1300 Morris Park Ave Bronx, NY 10461 Office: 718-430-4225 FAX: 718-430-8922 at ASPET Journals on October 1, 2021 Email: [email protected] Footnotes: The writing of the manuscript was funded in part by NIH grants DA008863 and NS026880 (to LAD) and AA026609 (to EBM). List of nonstandard abbreviations: ACTH Adrenocorticotrophic hormone AgRP Agouti-related peptide (AgRP) α-MSH Alpha-melanocyte stimulating hormone CART Cocaine- and amphetamine-regulated transcript CLIP Corticotropin-like intermediate lobe peptide DAMGO D-Ala2, N-MePhe4, Gly-ol]-enkephalin DOR Delta opioid receptor DPDPE [D-Pen2,D- Pen5]-enkephalin KOR Kappa opioid receptor MOR Mu opioid receptor PDYN Prodynorphin PENK Proenkephalin PET Positron-emission tomography PNOC Pronociceptin POMC Proopiomelanocortin 1 Molecular Pharmacology Fast Forward. -
Anorexia Nervosa: a Unified Neurological Perspective Tasneem Fatema Hasan, Hunaid Hasan
Int. J. Med. Sci. 2011, 8 679 Ivyspring International Publisher International Journal of Medical Sciences 2011; 8(8):679-703 Review Anorexia Nervosa: A Unified Neurological Perspective Tasneem Fatema Hasan, Hunaid Hasan Mahatma Gandhi Mission’s Medical College, Aurangabad, Maharashtra, India Corresponding author: [email protected] or [email protected]. 1345 Daniel Creek Road, Mississau- ga, Ontario, L5V1V3, Canada. © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/ licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited. Received: 2011.05.03; Accepted: 2011.09.19; Published: 2011.10.22 Abstract The roles of corticotrophin-releasing factor (CRF), opioid peptides, leptin and ghrelin in anorexia nervosa (AN) were discussed in this paper. CRF is the key mediator of the hypo- thalamo-pituitary-adrenal (HPA) axis and also acts at various other parts of the brain, such as the limbic system and the peripheral nervous system. CRF action is mediated through the CRF1 and CRF2 receptors, with both HPA axis-dependent and HPA axis-independent ac- tions, where the latter shows nil involvement of the autonomic nervous system. CRF1 re- ceptors mediate both the HPA axis-dependent and independent pathways through CRF, while the CRF2 receptors exclusively mediate the HPA axis-independent pathways through uro- cortin. Opioid peptides are involved in the adaptation and regulation of energy intake and utilization through reward-related behavior. Opioids play a role in the addictive component of AN, as described by the “auto-addiction opioids theory”. -
Lactation and Appetite-Regulating Hormones: Increased Maternal Plasma Peptide YY Concentrations 3–6 Months Postpartum
Downloaded from British Journal of Nutrition (2015), 114, 1203–1208 doi:10.1017/S0007114515002536 © The Authors 2015 https://www.cambridge.org/core Lactation and appetite-regulating hormones: increased maternal plasma peptide YY concentrations 3–6 months postpartum Greisa Vila1,*, Judith Hopfgartner1, Gabriele Grimm2, Sabina M. Baumgartner-Parzer1, . IP address: Alexandra Kautzky-Willer1, Martin Clodi1 and Anton Luger1 1Department of Internal Medicine III, Division of Endocrinology and Metabolism, Medical University of Vienna, 170.106.34.90 Vienna 1090, Austria 2Department of Medical and Chemical Laboratory Diagnostics, Medical University of Vienna, Vienna 1090, Austria – – – (Submitted 12 October 2014 Final revision received 27 May 2015 Accepted 11 June 2015 First published online 24 August 2015) , on 28 Sep 2021 at 07:22:14 Abstract Breast-feeding is associated with maternal hormonal and metabolic changes ensuring adequate milk production. In this study, we investigate the impact of breast-feeding on the profile of changes in maternal appetite-regulating hormones 3–6 months postpartum. Study participants were age- and BMI-matched lactating mothers (n 10), non-lactating mothers (n 9) and women without any history of pregnancy or breast-feeding in the previous 12 months (control group, n 10). During study sessions, young mothers breast-fed or bottle-fed their babies, and maternal blood , subject to the Cambridge Core terms of use, available at samples were collected at five time points during 90 min: before, during and after feeding the babies. Outcome parameters were plasma concentrations of ghrelin, peptide YY (PYY), leptin, adiponectin, prolactin, cortisol, insulin, glucose and lipid values. At baseline, circulating PYY concentrations were significantly increased in lactating mothers (100·3(SE 6·7) pg/ml) v.