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Characterisation and Partial Purification of a Novel Prohormone Processing Enzyme from Ovine Adrenal Medulla
Volume 246, number 1,2, 44-48 FEB 06940 March 1989 Characterisation and partial purification of a novel prohormone processing enzyme from ovine adrenal medulla N. Tezapsidis and D.C. Parish Biochemistry Group, School of Biological Sciences, University of Sussex, Falmer, Brighton, Sussex, England Received 3 January 1989 An enzymatic activity has been identified which is capable of generating a product chromatographically identical with adrenorphin from the model substrate BAM 12P. This enzyme was purified by gel filtration and ion-exchange chromatog- raphy and characterised as having a molecular mass between 30 and 45 kDa and an acidic pL The enzyme is active at the acid pH expected in the secretory vesicle interior and is inhibited by EDTA, suggesting that it is a metalloprotease. This activity could not be mimicked by incubation with lysosomal fractions and it meets the criteria to be considered as a possible prohormone processing enzyme. Prohormone processing; Adrenorphin; Secretory vesiclepurification 1. INTRODUCTION The purification of an endopeptidase responsi- ble for the generation of adrenorphin was under- Active peptide hormones are released from their taken, using the ovine adrenal medulla as a source. precursors by endoproteolytic cleavage at highly Adrenorphin is known to be located in the adrenal specific sites. The commonest of these is cleavage medulla of all species so far investigated [6]. at pairs of basic residues such as lysine and Secretory vesicles (also known as chromaffin arginine [1,2]. However another common class of granules) were isolated as a preliminary purifica- processing sites are known to be at single arginine tion step, since it is known that prohormone pro- residues, adjacent to a proline [3]. -
Endocrinology
Endocrinology INTRODUCTION Endocrinology 1. Endocrinology is the study of the endocrine system secretions and their role at target cells within the body and nervous system are the major contributors to the flow of information between different cells and tissues. 2. Two systems maintain Homeostasis a. b 3. Maintain a complicated relationship 4. Hormones 1. The endocrine system uses hormones (chemical messengers/neurotransmitters) to convey information between different tissues. 2. Transport via the bloodstream to target cells within the body. It is here they bind to receptors on the cell surface. 3. Non-nutritive Endocrine System- Consists of a variety of glands working together. 1. Paracrine Effect (CHEMICAL) Endocrinology Spring 2013 Page 1 a. Autocrine Effect i. Hormones released by cells that act on the membrane receptor ii. When a hormone is released by a cell and acts on the receptors located WITHIN the same cell. Endocrine Secretions: 1. Secretions secreted Exocrine Secretion: 1. Secretion which come from a gland 2. The secretion will be released into a specific location Nervous System vs tHe Endocrine System 1. Nervous System a. Neurons b. Homeostatic control of the body achieved in conjunction with the endocrine system c. Maintain d. This system will have direct contact with the cells to be affected e. Composed of both the somatic and autonomic systems (sympathetic and parasympathetic) Endocrinology Spring 2013 Page 2 2. Endocrine System a. b. c. 3. Neuroendocrine: a. These are specialized neurons that release chemicals that travel through the vascular system and interact with target tissue. b. Hypothalamus à posterior pituitary gland History of tHe Endocrine System Bertold (1849)-FATHER OF ENDOCRINOLOGY 1. -
Genscript Product Catalog 2013-2014 Genscript Product Catalog
GenScript Product Catalog 2013-2014 GenScript Product Catalog www.genscript.com GenScript USA Inc. 860 Centennial Ave. Piscataway, NJ 08854USA Tel: 1-732-885-9188 / 1-732-885-9688 Toll-Free Tel: 1-877-436-7274 Fax: 1-732-210-0262 / 1-732-885-5878 Email: [email protected] Nucleic Acid Purification and Analysis Business Development Tel: 1-732-317-5088 PCR PCR and Cloning Email: [email protected] Protein Analysis Antibodies 2013-2014 Peptides Welcome to GenScript GenScript USA Incorporation, founded in 2002, is a fast-growing biotechnology company and contract research organization (CRO) specialized in custom services and consumable products for academic and pharmaceutical research. Built on our assembly-line mode, one-stop solutions, continuous improvement, and stringent IP protection, GenScript provides a comprehensive portfolio of products and services at the most competitive prices in the industry to meet your research needs every day. Over the years, GenScript’s scientists have developed many innovative technologies that allow us to maintain our position at the cutting edge of biological and medical research while offering cost-effective solutions for customers to accelerate their research. Our advanced expertise includes proprietary technology for custom gene synthesis, OptimumGeneTM codon optimization technology, CloneEZ® seamless cloning technology, FlexPeptideTM technology for custom peptide synthesis, BacPowerTM technology for protein expression and purification, T-MaxTM adjuvant and advanced nanotechnology for custom antibody production, as well as our ONE-HOUR WesternTM detection system and eStain® protein staining system. GenScript offers a broad range of reagents, optimized kits, and system solutions to help you unravel the mysteries of biology. We also provide a comprehensive portfolio of customized services that include Bio-Reagent, Bio-Assay, Lead Optimization, and Antibody Drug Development which can be effectively integrated into your value chain and your operations. -
Identification of Molecules Relevant for the Invasiveness of Fibrosarcomas and Melanomas
Helsinki University Biomedical Dissertations No. 148 IDENTIFICATION OF MOLECULES RELEVANT FOR THE INVASIVENESS OF FIBROSARCOMAS AND MELANOMAS Pirjo Nummela Department of Pathology Haartman Institute Faculty of Medicine and Division of Biochemistry Department of Biosciences Faculty of Biological and Environmental Sciences University of Helsinki Finland Academic dissertation To be presented for public examination with the permission of the Faculty of Biological and Environmental Sciences of the University of Helsinki in the Lecture Hall 2 of Haartman Institute (Haartmaninkatu 3, Helsinki), on 13.5.2011 at 12 o’clock noon. Helsinki 2011 Supervisor Docent Erkki Hölttä, M.D., Ph.D. Department of Pathology Haartman Institute University of Helsinki Thesis committee Docent Jouko Lohi, M.D., Ph.D. Department of Pathology Haartman Institute University of Helsinki and Pirjo Nikula-Ijäs, Ph.D. Division of Biochemistry Department of Biosciences University of Helsinki Reviewers Professor Veli-Matti Kähäri, M.D., Ph.D. Department of Dermatology University of Turku and Turku University Hospital and Docent Jouko Lohi, M.D., Ph.D. Opponent Professor Jyrki Heino, M.D., Ph.D. Department of Biochemistry and Food Chemistry University of Turku Custos Professor Kari Keinänen, Ph.D. Division of Biochemistry Department of Biosciences University of Helsinki ISBN 978-952-92-8821-2 (paperback) ISBN 978-952-10-6924-6 (PDF) ISSN 1457-8433 http://ethesis.helsinki.fi Helsinki University Print Helsinki 2011 To Juha, Joona, and Joel TABLE OF CONTENTS LIST OF ORIGINAL PUBLICATIONS -
Properties of Chemically Oxidized Kininogens*
Vol. 50 No. 3/2003 753–763 QUARTERLY Properties of chemically oxidized kininogens*. Magdalena Nizio³ek, Marcin Kot, Krzysztof Pyka, Pawe³ Mak and Andrzej Kozik½ Faculty of Biotechnology, Jagiellonian University, Kraków, Poland Received: 30 May, 2003; revised: 01 August, 2003; accepted: 11 August, 2003 Key words: bradykinin, N-chlorosuccinimide, chloramine-T, kallidin, kallikrein, reactive oxygen species Kininogens are multifunctional proteins involved in a variety of regulatory pro- cesses including the kinin-formation cascade, blood coagulation, fibrynolysis, inhibi- tion of cysteine proteinases etc. A working hypothesis of this work was that the prop- erties of kininogens may be altered by oxidation of their methionine residues by reac- tive oxygen species that are released at the inflammatory foci during phagocytosis of pathogen particles by recruited neutrophil cells. Two methionine-specific oxidizing reagents, N-chlorosuccinimide (NCS) and chloramine-T (CT), were used to oxidize the high molecular mass (HK) and low molecular mass (LK) forms of human kininogen. A nearly complete conversion of methionine residues to methionine sulfoxide residues in the modified proteins was determined by amino acid analysis. Production of kinins from oxidized kininogens by plasma and tissue kallikreins was significantly lower (by at least 70%) than that from native kininogens. This quenching effect on kinin release could primarily be assigned to the modification of the critical Met-361 residue adja- cent to the internal kinin sequence in kininogen. However, virtually no kinin could be formed by human plasma kallikrein from NCS-modified HK. This observation sug- gests involvement of other structural effects detrimental for kinin production. In- deed, NCS-oxidized HK was unable to bind (pre)kallikrein, probably due to the modifi- cation of methionine and/or tryptophan residues at the region on the kininogen mole- cule responsible for the (pro)enzyme binding. -
Targeting the Phosphatidylinositide-3 Kinase Pathway and the Mitogen
Targeting the Phosphatidylinositide-3 Kinase Pathway and the Mitogen-Activated-Protein Kinase Pathway through Thymosin-β4, Exercise, and Negative Regulators to Promote Retinal Ganglion Cell Survival or Regeneration by Mark Magharious A thesis submitted in conformity with the requirements for the degree of Master of Science Rehabilitation Sciences Institute University of Toronto © Copyright by Mark Magharious 2015 Targeting the Phosphatidylinositide-3 Kinase Pathway and the Mitogen-Activated-Protein Kinase Pathway through Thymosin-β4, Exercise, and Negative Regulators to Promote Retinal Ganglion Cell Survival or Regeneration Mark Magharious Master of Science Rehabilitation Sciences Institute University of Toronto 2015 Abstract The phosphatidylinositide-3 kinase (PI3K) and mitogen-activated-protein kinase (MAPK) pathways mediate cellular survival in the presence of apoptotic stimuli. These pathways are known to promote the survival of injured retinal ganglion cells (RGCs), central nervous system neurons that project visual information from the retina to the brain. Injury to the optic nerve triggers apoptosis of RGCs. This work demonstrates that Thymosin-β4, a peptide involved in actin sequestration, both enhances RGC survival after injury and increases axonal regeneration. Moreover, Thymosin-β4 modulates the PI3K and MAPK pathways. In addition, this study demonstrates that exercise reduces apoptosis of injured RGCs, and explores the function of the PI3K and MAPK pathways in this process. Finally, small peptides are used to interfere with the functions of PTEN, a negative regulator of the PI3K pathway, as well as Erbin and BCR, negative regulators in the MAPK pathway. These peptides enhance RGC survival and axonal regeneration after injury. ii Acknowledgments I would like to take this opportunity to recognize all those who helped me through the process of researching and writing this thesis. -
And VLDV-Neurophysins (Evolution/Gene Duplication/Polypeptide Processing/Neuropeptides/Neurosecretion) M
Proc. Nati Acad. Sci. USA Vol. 80, pp. 2839-2843, May 1983 Biochemistry Identification of human neurophysins: Complete amino acid sequences of MSEL- and VLDV-neurophysins (evolution/gene duplication/polypeptide processing/neuropeptides/neurosecretion) M. T. CHAUVET, D. HURPET, J. CHAUVET, AND R. ACHER Laboratory of Biological Chemistry, University of Paris VI, 96, Bd Raspail, 75006, Paris, France Communicated by Choh Hao Li, January 27, 1983 ABSTRACT Twohuman neurophysins have been purified from Preliminary results on the NH2-terminal amino acid se- acetone-desiccated posterior pituitaries by acidic extraction, mo- quences of human neurophysin I or VLDV-neurophysin (5, 6, lecular sieving, and ion-exchange chromatography. The complete 10) and neurophysin II or MSEL-neurophysin (8, 10) have been amino acid sequence of each protein has been determined by us- published. These results are in agreement with the presence ing a sequencer and characterizing two sets of overlapping en- of only two types of neurophysins in the gland and with the zymic peptides. The two neurophysins belong to two structural hypothesis that the two hormones oxytocin and [8-arginine]va- families previously defined as MSEL- and VLDV-neurophysins sopressin and the two neurophysins are cleavage products of according to the nature of the residues in positions 2, 3, 6, and 7. common with (MSEL-neurophysins contain methionine-2, serine-3, glutamic acid- precursors (11, 12). The present work deals the 6, and leucine-7; VLDV-neurophysins contain valine-2, leucine-3, isolation of the two human neurophysins and the determination aspartic acid-6, and valine-7.) Human MSEL-neurophysin has only of the complete amino acid sequences of MSEL- and VLDV- 93 residues instead of 95 usually found in MSEL-neurophysins neurophysins. -
Design, Synthesis, Kinetic Analysis, Molecular Modeling, and Pharmacological Evaluation of Novel Inhibitors of Peptide Amidation
DESIGN, SYNTHESIS, KINETIC ANALYSIS, MOLECULAR MODELING, AND PHARMACOLOGICAL EVALUATION OF NOVEL INHIBITORS OF PEPTIDE AMIDATION A Thesis Presented to the Academic Faculty by Michael Scott Foster In Partial Fulfillment Of the Requirements for the Degree Doctor of Philosophy in Chemistry Georgia Institute of Technology December 2008 DESIGN, SYNTHESIS, KINETIC ANALYSIS, MOLECULAR MODELING, AND PHARMACOLOGICAL EVALUATION OF NOVEL INHIBITORS OF PEPTIDE AMIDATION Approved by: Dr. Sheldon W. May Dr. Stanley H. Pollock School of Chemistry and Biochemistry Pharmaceutical Sciences Georgia Institute of Technology Mercer University Dr. James C. Powers Dr. Niren Murthy School of Chemistry and Biochemistry School of Biomedical Engineering Georgia Institute of Technology Georgia Institute of Technology Dr. Nicholas V. Hud Date Approved: August 12, 2008 School of Chemistry and Biochemistry Georgia Institute of Technology For Dr. Sheldon W. May, without whose indefatigable kindness, patience, good humor, and positive attitude, I surely would never have completed this work. For Amanda, whose loyalty, love, and trust throughout these many years have ever been a blessing to me. For Dave, the best brother a person could ask for. And for my mother, who gave me everything. I am sorry you could not be here to share in my success. ACKNOWLEDGEMENTS I give, again, my deepest thanks to Dr. Sheldon May for the opportunity to work alongside him and with his group for these wonderful years. Also, many thanks to Dr. Charlie Oldham for listening to me gripe about ill-conceived software default settings and shoddy instrument engineering without every becoming more than mildly irritated with me. His encyclopedic knowledge of many different scientific and technical fields has been a wonderful benefit to my graduate career. -
Evolution of Neuropeptide Signalling Systems (Doi:10.1242/Jeb.151092) Maurice R
© 2018. Published by The Company of Biologists Ltd | Journal of Experimental Biology (2018) 221, jeb193342. doi:10.1242/jeb.193342 CORRECTION Correction: Evolution of neuropeptide signalling systems (doi:10.1242/jeb.151092) Maurice R. Elphick, Olivier Mirabeau and Dan Larhammar There was an error published in J. Exp. Biol. (2018) 221, jeb151092 (doi:10.1242/jeb.151092). In Fig. 2, panels B and C are identical. The correct figure is below. The authors apologise for any inconvenience this may have caused. Journal of Experimental Biology 1 © 2018. Published by The Company of Biologists Ltd | Journal of Experimental Biology (2018) 221, jeb151092. doi:10.1242/jeb.151092 REVIEW Evolution of neuropeptide signalling systems Maurice R. Elphick1,*,‡, Olivier Mirabeau2,* and Dan Larhammar3,* ABSTRACT molecular to the behavioural level (Burbach, 2011; Schoofs et al., Neuropeptides are a diverse class of neuronal signalling molecules 2017; Taghert and Nitabach, 2012; van den Pol, 2012). that regulate physiological processes and behaviour in animals. Among the first neuropeptides to be chemically identified in However, determining the relationships and evolutionary origins of mammals were the hypothalamic neuropeptides vasopressin and the heterogeneous assemblage of neuropeptides identified in a range oxytocin, which act systemically as hormones (e.g. regulating of phyla has presented a huge challenge for comparative physiologists. diuresis and lactation) and act within the brain to influence social Here, we review revolutionary insights into the evolution of behaviour (Donaldson and Young, 2008; Young et al., 2011). neuropeptide signalling that have been obtained recently through Evidence of the evolutionary antiquity of neuropeptide signalling comparative analysis of genome/transcriptome sequence data and by emerged with the molecular identification of neuropeptides in – ‘deorphanisation’ of neuropeptide receptors. -
G Protein‐Coupled Receptors
S.P.H. Alexander et al. The Concise Guide to PHARMACOLOGY 2019/20: G protein-coupled receptors. British Journal of Pharmacology (2019) 176, S21–S141 THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: G protein-coupled receptors Stephen PH Alexander1 , Arthur Christopoulos2 , Anthony P Davenport3 , Eamonn Kelly4, Alistair Mathie5 , John A Peters6 , Emma L Veale5 ,JaneFArmstrong7 , Elena Faccenda7 ,SimonDHarding7 ,AdamJPawson7 , Joanna L Sharman7 , Christopher Southan7 , Jamie A Davies7 and CGTP Collaborators 1School of Life Sciences, University of Nottingham Medical School, Nottingham, NG7 2UH, UK 2Monash Institute of Pharmaceutical Sciences and Department of Pharmacology, Monash University, Parkville, Victoria 3052, Australia 3Clinical Pharmacology Unit, University of Cambridge, Cambridge, CB2 0QQ, UK 4School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, BS8 1TD, UK 5Medway School of Pharmacy, The Universities of Greenwich and Kent at Medway, Anson Building, Central Avenue, Chatham Maritime, Chatham, Kent, ME4 4TB, UK 6Neuroscience Division, Medical Education Institute, Ninewells Hospital and Medical School, University of Dundee, Dundee, DD1 9SY, UK 7Centre for Discovery Brain Sciences, University of Edinburgh, Edinburgh, EH8 9XD, UK Abstract The Concise Guide to PHARMACOLOGY 2019/20 is the fourth in this series of biennial publications. The Concise Guide provides concise overviews of the key properties of nearly 1800 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. -
United States Patent (19) 11 Patent Number: 5,039,660 Leonard Et Al
United States Patent (19) 11 Patent Number: 5,039,660 Leonard et al. (45. Date of Patent: Aug. 13, 1991 54 PARTIALLY FUSED PEPTIDE PELLET 4,667,014 5/1987 Nestor, Jr. et al. ................. 514/800 4,801,577 / 1989 Nestor, Jr. et al. ................. 54/800 75 Inventors: Robert J. Leonard, Lynnfield, Mass.; S. Mitchell Harman, Ellicott City, Primary Examiner-Lester L. Lee Md. Attorney, Agent, or Firm-Wolf, Greenfield & Sacks 73 Assignee: Endocon, Inc., South Walpole, Mass. (57) ABSTRACT 21 Appl. No.: 163,328 A bioerodible pellet capable of administering an even 22 Filed: Mar. 2, 1988 and continuous dose of a peptide over a period of up to a year, when subcutaneously implanted, is provided. (51) Int. Cl’.............................................. C07K 17/08 (52 U.S.C. .......................................... 514/8; 514/12; The bioerodible implant is a partially-fused pellet, 514/14: 514/15; 514/16; 514/17; 514/18; which pellet has a peptide drug homogeneously-bound 514/19; 514/800 in a matrix of a melted and recrystallized, nonpolymer Field of Search ................... 514/8, 12, 14, 15, 16, carrier. Preferably, the nonpolymer carrier is a steroid (58) and in particular is cholesterol or a cholesterol deriva 514/17, 18, 19, 800 tive. In one embodiment, the peptide drug is growth (56) References Cited hormone-releasing hormone. A method for making the U.S. PATENT DOCUMENTS bioerodible pellet also is provided. 4,164,560 8/1979 Folkman et al. .................... 424/427 '4,591,496 5/1986 Cohen et al. .......................... 424/78 13 Claims, 4 Drawing Sheets U.S. Patent Aug. -
Deer Thymosin Beta 10 Functions As a Novel Factor for Angiogenesis And
Zhang et al. Stem Cell Research & Therapy (2018) 9:166 https://doi.org/10.1186/s13287-018-0917-y RESEARCH Open Access Deer thymosin beta 10 functions as a novel factor for angiogenesis and chondrogenesis during antler growth and regeneration Wei Zhang1,2†, Wenhui Chu1,2†, Qingxiu Liu1,2†, Dawn Coates3, Yudong Shang1,2 and Chunyi Li1,2* Abstract Background: Deer antlers are the only known mammalian organ with vascularized cartilage that can completely regenerate. Antlers are of real significance as a model of mammalian stem cell-based regeneration with particular relevance to the fields of chondrogenesis, angiogenesis, and regenerative medicine. Recent research found that thymosin beta 10 (TMSB10) is highly expressed in the growth centers of growing antlers. The present study reports here the expression, functions, and molecular interactions of deer TMSB10. Methods: The TMSB10 expression level in both tissue and cells in the antler growth center was measured. The effects of both exogenous (synthetic protein) and endogenous deer TMSB10 (lentivirus-based overexpression) on antlerogenic periosteal cells (APCs; nonactivated antler stem cells with no basal expression of TMSB10) and human umbilical vein endothelial cells (HUVECs; endothelial cells with no basal expression of TMSB10) were evaluated to determine whether TMSB10 functions on chondrogenesis and angiogenesis. Differences in deer and human TMSB10 in angiogenesis and molecular structure were determined using animal models and molecular dynamics simulation, respectively. The molecular mechanisms underlying deer TMSB10 in promoting angiogenesis were also explored. Results: Deer TMSB10 was identified as a novel proangiogenic factor both in vitro and in vivo. Immunohistochemistry revealed that TMSB10 was widely expressed in the antler growth center in situ, with the highest expression in the reserve mesenchyme, precartilage, and transitional zones.