TRH-Like Peptides
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A Comparative Survey of the RF-Amide Peptide Superfamily
EDITORIAL published: 10 August 2015 doi: 10.3389/fendo.2015.00120 Editorial: A comparative survey of the RF-amide peptide superfamily Karine Rousseau 1*, Sylvie Dufour 1 and Hubert Vaudry 2 1 Laboratory of Biology of Aquatic Organisms and Ecosystems (BOREA), Muséum National d’Histoire Naturelle, CNRS 7208, IRD 207, Université Pierre and Marie Curie, UCBN, Paris, France, 2 Laboratory of Neuronal and Neuroendocrine Differentiation and Communication, INSERM U982, International Associated Laboratory Samuel de Champlain, Institute for Research and Innovation in Biomedicine (IRIB), University of Rouen, Mont-Saint-Aignan, France Keywords: RF-amide peptides, receptors, evolution, functions, deuterostomes, protostomes The first member of the RF-amide peptide superfamily to be characterized, in 1977, was the cardioexcitatory peptide, FMRFamide, isolated from the ganglia of the clam Macrocallista nimbosa (1). Since then, a large number of such peptides, designated after their C-terminal arginine (R) and amidated phenylalanine (F) residues, have been identified in representative species of all major phyla. The discovery, 12 years ago, that the RF-amide peptide kisspeptin, acting via GPR54, was essential for the onset of puberty and reproduction, has been a major breakthrough in reproductive physiology (2–4). It has also put in front of the spotlights RF-amide peptides and has invigo- rated research on this superfamily of regulatory neuropeptides. The present Research Topic aims at illustrating major advances achieved, through comparative studies in (mammalian and non- mammalian) vertebrates and invertebrates, in the knowledge of RF-amide peptides in terms of evolutionary history and physiological significance. Since 2006, by means of phylogenetic analyses, the superfamily of RFamide peptides has been divided into five families/groups in vertebrates (5, 6): kisspeptin, 26RFa/QRFP, GnIH (including LPXRFa and RFRP), NPFF, and PrRP. -
Plant Protease Inhibitors: a Defense Strategy in Plants
Biotechnology and Molecular Biology Review Vol. 2 (3), pp. 068-085, August 2007 Available online at http://www.academicjournals.org/BMBR ISSN 1538-2273 © 2007 Academic Journals Standard Review Plant protease inhibitors: a defense strategy in plants Huma Habib and Khalid Majid Fazili* Department of Biotechnology, The University of Kashmir, P/O Naseembagh, Hazratbal, Srinagar -190006, Jammu and Kashmir, India. Accepted 7 July, 2007 Proteases, though essentially indispensable to the maintenance and survival of their host organisms, can be potentially damaging when overexpressed or present in higher concentrations, and their activities need to be correctly regulated. An important means of regulation involves modulation of their activities through interaction with substances, mostly proteins, called protease inhibitors. Some insects and many of the phytopathogenic microorganisms secrete extracellular enzymes and, in particular, enzymes causing proteolytic digestion of proteins, which play important roles in pathogenesis. Plants, however, have also developed mechanisms to fight these pathogenic organisms. One important line of defense that plants have to fight these pathogens is through various inhibitors that act against these proteolytic enzymes. These inhibitors are thus active in endogenous as well as exogenous defense systems. Protease inhibitors active against different mechanistic classes of proteases have been classified into different families on the basis of significant sequence similarities and structural relationships. Specific protease inhibitors are currently being overexpressed in certain transgenic plants to protect them against invaders. The current knowledge about plant protease inhibitors, their structure and their role in plant defense is briefly reviewed. Key words: Proteases, enzymes, protease inhibitors, serpins, cystatins, pathogens, defense. Table of content 1. -
Evidence for Two Different Modes of Tripeptide Disappearance in Human Intestine. Uptake by Peptide Carrier Systems and Hydrolysis by Peptide Hydrolases
Evidence for two different modes of tripeptide disappearance in human intestine. Uptake by peptide carrier systems and hydrolysis by peptide hydrolases. S A Adibi, … , S S Masilamani, P M Amin J Clin Invest. 1975;56(6):1355-1363. https://doi.org/10.1172/JCI108215. Research Article The intestinal fate of two tripeptides (triglycine and trileucine), which differ markedly in solubility and molecular weight, have been investigated by jejunal perfusion in healthy human volunteers. Rates of glycine or leucine uptake from test solutions containing triglycine or trileucine were greater than from test solutions containing corresponding amounts of free glycine or free leucine, respectively. The rate of glycine uptake from a 100 mM triglycine solution was greater than that from a 150 mM diglycine solution. At each infused load of triglycine (e.g., 1,000 mumol/min) the rates (micromoles/minutes per 30 cm) of either triglycine disappearance (810 +/- 40) or glycine absorption (2,208 +/- 122) were markedly greater than the luminal accumulation rates of either diglycine (56 +/- 10) or free glycine (110 +/- 18). The luminal accumulation rate of free leucine during infusion of a 5 mM trileucine solution was over threefold greater than that of free glycine during the infusion of a 5 mM triglycine solution. Luminal fluid exhibited no hydrolytic activity against triglycine, but contained some activity against trileucine. Saturation of free amino acid carrier system with a large load of leucine did not affect glycine absorption rate from a triglycine test solution, but isoleucine markedly inhibited the uptake from a trileucine solution. When the carrier system for dipeptides was saturated with a large amount of glycylleucine, […] Find the latest version: https://jci.me/108215/pdf Evidence for Two Different Modes of Tripeptide Disappearance in Human Intestine UPTAKE BY PEPTIDE CARRIER SYSTEMS AND HYDROLYSIS BY PEPTIDE HYDROLASES SIAMAK A. -
Safety Assessment of Tripeptide-1, Hexapeptide-12, and Related Amides As Used in Cosmetics
Safety Assessment of Tripeptide-1, Hexapeptide-12, and Related Amides as Used in Cosmetics Status: Draft Report for Panel Review Release Date: February 21, 2014 Panel Meeting Date: March 17-18, 2014 The 2014 Cosmetic Ingredient Review Expert Panel members are: Chair, Wilma F. Bergfeld, M.D., F.A.C.P.; Donald V. Belsito, M.D.; Curtis D. Klaassen, Ph.D.; Daniel C. Liebler, Ph.D.; Ronald A Hill, Ph.D. James G. Marks, Jr., M.D.; Ronald C. Shank, Ph.D.; Thomas J. Slaga, Ph.D.; and Paul W. Snyder, D.V.M., Ph.D. The CIR Director is Lillian J. Gill, D.P.A. This report was prepared by Wilbur Johnson, Jr., M.S., Senior Scientific Analyst and Bart Heldreth, Ph.D., Chemist. © Cosmetic Ingredient Review 1620 L STREET, N.W., SUITE 1200 ◊ WASHINGTON, DC 20036-4702 ◊ PH 202.331.0651 ◊ FAX 202.331.0088 ◊ [email protected] Commitment & Credibility since 1976 Memorandum To: CIR Expert Panel Members and Liaisons From: Wilbur Johnson, Jr. Senior Scientific Analyst Date: February 21, 2014 Subject: Draft Report on Tripeptide-1, Hexapeptide-12, and Related Amides The draft report on palmitoyl oligopeptides was tabled at the March 18-19, 2013 CIR Expert Panel meeting, pending reorganization of the safety assessment. During the meeting, the Panel was provided with a letter from the CIR Science and Support Committee, recommending the creation of a new ingredient group consisting of ingredients for which the peptide sequence is known, namely, tripeptide -1, hexapeptide-12 and specific related amides. This has been done. Additionally, at the March meeting, further information was sought to better understand the extent and manner in which solid-phase peptide synthesis is used to create the peptide portion of ingredients included in the safety assessment. -
Peptide Handbook a Guide to Peptide Design and Applications in Biomedical Research
Peptide Handbook A Guide to Peptide Design and Applications in Biomedical Research First Edition www.GenScript.com GenScript USA Inc. 860 Centennial Ave. Piscataway, NJ 08854 USA Phone: 1-732-885-9188 Toll-Free: 1-877-436-7274 Fax: 1-732-885-5878 Table of Contents The Universe of Peptides Reliable Synthesis of High-Quality Peptides Molecular structure 3 by GenScript Characteristics 5 Categories and biological functions 8 Analytical methods 10 Application of Peptides Research in structural biology 12 Research in disease pathogenesis 12 Generating antibodies 13 FlexPeptideTM Peptide Synthesis Platform which takes advantage of the latest Vaccine development 14 peptide synthesis technologies generates a large capacity for the quick Drug discovery and development 15 synthesis of high-quality peptides in a variety of lengths, quantities, purities Immunotherapy 17 and modifications. Cell penetration-based applications 18 Anti-microorganisms applications 19 Total Quality Management System based on multiple rounds of MS and HPLC Tissue engineering and regenerative medicine 20 analyses during and after peptide synthesis ensures the synthesis of Cosmetics 21 high-quality peptides free of contaminants, and provides reports on peptide Food industry 21 solubility, quality and content. Synthesis of Peptides Diverse Delivery Options help customers plan their peptide-based research Chemical synthesis 23 according to their time schedule and with peace of mind. Microwave-assisted technology 24 ArgonShield™ Packing eliminates the experimental variation caused by Ligation technology 26 oxidization and deliquescence of custom peptides through an innovative Recombinant technology 28 Modifications packing and delivery technology. 28 Purification 30 Expert Support offered by Ph.D.-level scientists guides customers from Product identity and quality control 31 peptide design and synthesis to reconstitution and application. -
Effect of the Natural Sweetener Xylitol on Gut Hormone Secretion and Gastric Emptying in Humans: a Pilot Dose-Ranging Study
nutrients Article Effect of the Natural Sweetener Xylitol on Gut Hormone Secretion and Gastric Emptying in Humans: A Pilot Dose-Ranging Study Anne Christin Meyer-Gerspach 1,2,* , Jürgen Drewe 3, Wout Verbeure 4 , Carel W. le Roux 5, Ludmilla Dellatorre-Teixeira 5, Jens F. Rehfeld 6, Jens J. Holst 7 , Bolette Hartmann 7, Jan Tack 4, Ralph Peterli 8, Christoph Beglinger 1,2 and Bettina K. Wölnerhanssen 1,2,* 1 St. Clara Research Ltd. at St. Claraspital, 4002 Basel, Switzerland; [email protected] 2 Faculty of Medicine, University of Basel, 4001 Basel, Switzerland 3 Department of Clinical Pharmacology and Toxicology, University Hospital of Basel, 4001 Basel, Switzerland; [email protected] 4 Translational Research Center for Gastrointestinal Disorders, Catholic University of Leuven, 3000 Leuven, Belgium; [email protected] (W.V.); [email protected] (J.T.) 5 Diabetes Complications Research Centre, Conway Institute University College Dublin, 3444 Dublin, Ireland; [email protected] (C.W.l.R.); [email protected] (L.D.-T.) 6 Department of Clinical Biochemistry, Rigshospitalet, University of Copenhagen, 2100 Copenhagen, Denmark; [email protected] 7 Department of Biomedical Sciences and Novo Nordisk Foundation Center for Basic Metabolic Research, Faculty of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark; [email protected] (J.J.H.); [email protected] (B.H.) 8 Department of Surgery, Clarunis, St. Claraspital, 4002 Basel, Switzerland; [email protected] * Correspondence: [email protected] (A.C.M.-G.); [email protected] (B.K.W.); Tel.: +41-61-685-85-85 (A.C.M.-G. -
Ultraviolet Irradiation on a Pyrite Surface Improves Triglycine Adsorption
life Article Ultraviolet Irradiation on a Pyrite Surface Improves Triglycine Adsorption Santos Galvez-Martinez and Eva Mateo-Marti * Centro de Astrobiología (CSIC-INTA), Ctra. Ajalvir, Km. 4, 28850 Torrejón de Ardoz, Spain; [email protected] * Correspondence: [email protected]; Tel.: + 34-915-872-973 Received: 27 July 2018; Accepted: 9 October 2018; Published: 25 October 2018 Abstract: We characterized the adsorption of triglycine molecules on a pyrite surface under several simulated environmental conditions by X-ray photoemission spectroscopy. The triglycine molecular adsorption on a pyrite surface under vacuum conditions (absence of oxygen) shows the presence of + two different states for the amine functional group (NH2 and NH3 ), therefore two chemical species (anionic and zwitterionic). On the other hand, molecular adsorption from a solution discriminates the NH2 as a unique molecular adsorption form, however, the amount adsorbed in this case is higher than under vacuum conditions. Furthermore, molecular adsorption on the mineral surface is even favored if the pyrite surface has been irradiated before the molecular adsorption occurs. Pyrite surface chemistry is highly sensitive to the chemical changes induced by UV irradiation, as XPS analysis shows the presence of Fe2O3 and Fe2SO4—like environments on the surface. Surface chemical changes induced by UV help to increase the probability of adsorption of molecular species and their subsequent concentration on the pyrite surface. Keywords: pyrite; triglycine; XPS; peptide; sulfide mineral; UV; surface; adsorption; prebiotic chemistry 1. Introduction Minerals can be very promising surfaces for studying biomolecule surface processes, which are of principal relevance in the origin of life and a source of chemical complexity [1,2]. -
Safety Assessment of Tripeptide-1, Hexapeptide-12, Their Metal Salts and Fatty Acyl Derivatives, and Palmitoyl Tetrapeptide-7 As Used in Cosmetics
Safety Assessment of Tripeptide-1, Hexapeptide-12, their Metal Salts and Fatty Acyl Derivatives, and Palmitoyl Tetrapeptide-7 as Used in Cosmetics Status: Draft Final Report for Panel Review Release Date: May 16, 2014 Panel Meeting Date: June 9-10, 2014 The 2014 Cosmetic Ingredient Review Expert Panel members are: Chair, Wilma F. Bergfeld, M.D., F.A.C.P.; Donald V. Belsito, M.D.; Curtis D. Klaassen, Ph.D.; Daniel C. Liebler, Ph.D.; Ronald A Hill, Ph.D.; James G. Marks, Jr., M.D.; Ronald C. Shank, Ph.D.; Thomas J. Slaga, Ph.D.; and Paul W. Snyder, D.V.M., Ph.D. The CIR Director is Lillian J. Gill, D.P.A. This report was prepared by Wilbur Johnson, Jr., M.S., Senior Scientific Analyst and Bart Heldreth, Ph.D., Chemist. © Cosmetic Ingredient Review 1620 L STREET, N.W., SUITE 1200 ◊ WASHINGTON, DC 20036-4702 ◊ PH 202.331.0651 ◊ FAX 202.331.0088 ◊ [email protected] Commitment & Credibility since 1976 Memorandum To: CIR Expert Panel Members and Liaisons From: Wilbur Johnson, Jr. Senior Scientific Analyst Date: May 16, 2014 Subject: Draft Final Report on Tripeptide-1, Hexapeptide-12, their Metal Salts and Fatty Acyl Derivatives, and Palmitoyl Tetrapeptide-7 At the March 17-18, 2014 Expert Panel meeting, the Panel concluded that tripeptide-1, hexapeptide-12, their metal salts and fatty acyl derivatives, and palmitoyl tetrapeptide-7 are safe in the present practices of use and concentration and issued a tentative report. Comments and use concentration data received from the Council have been addressed/ incorporated. Included in this package for your review is the draft final report, the CIR report history, Literature search strategy, Ingredient Data profile, 2014 FDA VCRP data, Minutes from the March 2014 Panel Meeting, and comments (pcpc1pdf file) and use concentration data (data 1 file) received from the Council. -
What Is Pancreatic Polypeptide and What Does It Do?
What is Pancreatic Polypeptide and what does it do? This document aims to evaluate current understanding of pancreatic polypeptide (PP), a gut hormone with several functions contributing towards the maintenance of energy balance. Successful regulation of energy homeostasis requires sophisticated bidirectional communication between the gastrointestinal tract and central nervous system (CNS; Williams et al. 2000). The coordinated release of numerous gastrointestinal hormones promotes optimal digestion and nutrient absorption (Chaudhri et al., 2008) whilst modulating appetite, meal termination, energy expenditure and metabolism (Suzuki, Jayasena & Bloom, 2011). The Discovery of a Peptide Kimmel et al. (1968) discovered PP whilst purifying insulin from chicken pancreas (Adrian et al., 1976). Subsequent to extraction of avian pancreatic polypeptide (aPP), mammalian homologues bovine (bPP), porcine (pPP), ovine (oPP) and human (hPP), were isolated by Lin and Chance (Kimmel, Hayden & Pollock, 1975). Following extensive observation, various features of this novel peptide witnessed its eventual classification as a hormone (Schwartz, 1983). Molecular Structure PP is a member of the NPY family including neuropeptide Y (NPY) and peptide YY (PYY; Holzer, Reichmann & Farzi, 2012). These biologically active peptides are characterized by a single chain of 36-amino acids and exhibit the same ‘PP-fold’ structure; a hair-pin U-shaped molecule (Suzuki et al., 2011). PP has a molecular weight of 4,240 Da and an isoelectric point between pH6 and 7 (Kimmel et al., 1975), thus carries no electrical charge at neutral pH. Synthesis Like many peptide hormones, PP is derived from a larger precursor of 10,432 Da (Leiter, Keutmann & Goodman, 1984). Isolation of a cDNA construct, synthesized from hPP mRNA, proposed that this precursor, pre-propancreatic polypeptide, comprised 95 residues (Boel et al., 1984) and is processed to produce three products (Leiter et al., 1985); PP, an icosapeptide containing 20-amino acids and a signal peptide (Boel et al., 1984). -
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. -
Peptides and How They Work with Kristina Kannada, Hydropeptide Fine Lines and Wrinkles Are the #1 Concern for Skin Care Consumers Chronological Vs
Peptides And How They Work with Kristina Kannada, Hydropeptide Fine lines and wrinkles are the #1 concern for skin care consumers Chronological vs. Photoaging Factors Involved in Skin Aging Proteolic activity: Increase in degradation of proteins by cellular enzymes Free radical damage: Increase in unpaired electrons that accelerate aging Growth factors: Decrease in signaling molecules and cellular processes DEJ: Decrease in skin cohesion What happens with aging? 1: Thinning of the skin 2: Collagen fragmentation 3: Dermal epidermal junction (DEJ) flattening 4: Wrinkle formation Collagen and Aging Collagen gives skin structural support. It is the most abundant form of protein in the ECM, and its decrease is a major factor in wrinkle formation. 29 types of collagen have been identified. They are divided into five families according to type of structure: Fibrillar (Type I, II, III, V, XI), Facit (Type IX, XII, XIV), Short Chain (Type VIII, X), Basement Member (Type IV), and Other (Type VI, VII, XIII). Important types of collagen in terms of skin aging: • I: Most abundant form. Gives strength to the dermis. • III: Second most abundant form. Gives elasticity to the dermis. • IV: Major component of basement membrane. Forms a "chicken-wire" mesh with laminins and proteoglycans that influence cell adhesion, migration and differentiation. • V: Regulates the diameter of Collagen I and III fibers. • VI: A major component of microfibrils. Increases cell strength. • VII: Provides stability and anchors the dermis to the DEJ. • XVII: A transmembrane protein that is a structural component of hemidesmosomes, improving adhesion of the keratinocytes to the underlying membrane. A good skin care regimen must support multiple skin proteins for the best results. -
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.