Which Is the Task of Neuroglobin in Antarctic Hemoglobin-Less Icefish?
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The Evolution of Hemoglobin. by Ross Hardison
American Scientist March-April 1999 v87 i2 p126(1) Page 1 the evolution of hemoglobin. by Ross Hardison A comparative study of hemoglobin was conducted to explain how an ancestral single-function molecule gave rise to descending molecules with varied functions. Hemoglobin is the molecule in red blood cells responsible for giving blood its color and for carrying oxygen throughout the body. New functions of metallo-porphyrin rings or a kind of molecular cage embedded in proteins were developed with the appearance of atmospheric oxygen. The presence of hemoglobin in both oxygen-needing and non-oxygen needing organisms suggests the same evolutionary roots. © COPYRIGHT 1999 Sigma Xi, The Scientific Research If similar compounds are used in all of these reactions, Society then how do the different functions arise? The answer lies in the specific structure of the organic component, most Studies of a very ancient protein suggest that changes in often a protein, that houses the porphyrin ring. The gene regulation are an important part of the evolutionary configuration of each protein determines what biochemical story service the protein will perform. The appearance of atmospheric oxygen on earth between Because they have such an ancient lineage, the one and two billion years ago was a dramatic and, for the porphyrin-containing molecules provide scientists with a primitive single-celled creatures then living on earth, a rare opportunity to follow the creation of new biological potentially traumatic event. On the one hand, oxygen was compounds from existing ones. That is, how does an toxic. On the other hand, oxygen presented opportunities ancestral molecule with a single function give rise to to improve the process of metabolism, increasing the descendant molecules with varied functions? In my efficiency of life’s energy-generating systems. -
Hemoglobin, Myoglobin and Neuroglobin in Endogenous Thiosulfate Production Processes
International Journal of Molecular Sciences Review The Role of Hemoproteins: Hemoglobin, Myoglobin and Neuroglobin in Endogenous Thiosulfate Production Processes Anna Bilska-Wilkosz *, Małgorzata Iciek, Magdalena Górny and Danuta Kowalczyk-Pachel Chair of Medical Biochemistry, Jagiellonian University Collegium Medicum ,7 Kopernika Street, Kraków 31-034, Poland; [email protected] (M.I.); [email protected] (M.G.); [email protected] (D.K.-P.) * Correspondence: [email protected]; Tel.: +48-12-4227-400; Fax: +48-12-4223-272 Received: 5 May 2017; Accepted: 16 June 2017; Published: 20 June 2017 Abstract: Thiosulfate formation and biodegradation processes link aerobic and anaerobic metabolism of cysteine. In these reactions, sulfite formed from thiosulfate is oxidized to sulfate while hydrogen sulfide is transformed into thiosulfate. These processes occurring mostly in mitochondria are described as a canonical hydrogen sulfide oxidation pathway. In this review, we discuss the current state of knowledge on the interactions between hydrogen sulfide and hemoglobin, myoglobin and neuroglobin and postulate that thiosulfate is a metabolically important product of this processes. Hydrogen sulfide oxidation by ferric hemoglobin, myoglobin and neuroglobin has been defined as a non-canonical hydrogen sulfide oxidation pathway. Until recently, it appeared that the goal of thiosulfate production was to delay irreversible oxidation of hydrogen sulfide to sulfate excreted in urine; while thiosulfate itself was only an intermediate, transient metabolite on the hydrogen sulfide oxidation pathway. In the light of data presented in this paper, it seems that thiosulfate is a molecule that plays a prominent role in the human body. Thus, we hope that all these findings will encourage further studies on the role of hemoproteins in the formation of this undoubtedly fascinating molecule and on the mechanisms responsible for its biological activity in the human body. -
Adult, Embryonic and Fetal Hemoglobin Are Expressed in Human Glioblastoma Cells
514 INTERNATIONAL JOURNAL OF ONCOLOGY 44: 514-520, 2014 Adult, embryonic and fetal hemoglobin are expressed in human glioblastoma cells MARWAN EMARA1,2, A. ROBERT TURNER1 and JOAN ALLALUNIS-TURNER1 1Department of Oncology, University of Alberta and Alberta Health Services, Cross Cancer Institute, Edmonton, AB T6G 1Z2, Canada; 2Center for Aging and Associated Diseases, Zewail City of Science and Technology, Cairo, Egypt Received September 7, 2013; Accepted October 7, 2013 DOI: 10.3892/ijo.2013.2186 Abstract. Hemoglobin is a hemoprotein, produced mainly in Introduction erythrocytes circulating in the blood. However, non-erythroid hemoglobins have been previously reported in other cell Globins are hemo-containing proteins, have the ability to types including human and rodent neurons of embryonic bind gaseous ligands [oxygen (O2), nitric oxide (NO) and and adult brain, but not astrocytes and oligodendrocytes. carbon monoxide (CO)] reversibly. They have been described Human glioblastoma multiforme (GBM) is the most aggres- in prokaryotes, fungi, plants and animals with an enormous sive tumor among gliomas. However, despite extensive basic diversity of structure and function (1). To date, hemoglobin, and clinical research studies on GBM cells, little is known myoglobin, neuroglobin (Ngb) and cytoglobin (Cygb) repre- about glial defence mechanisms that allow these cells to sent the vertebrate globin family with distinct function and survive and resist various types of treatment. We have tissue distributions (2). During ontogeny, developing erythro- shown previously that the newest members of vertebrate blasts sequentially express embryonic {[Gower 1 (ζ2ε2), globin family, neuroglobin (Ngb) and cytoglobin (Cygb), are Gower 2 (α2ε2), and Portland 1 (ζ2γ2)] to fetal [Hb F(α2γ2)] expressed in human GBM cells. -
The Effects of Temperature on Hemoglobin in Capitella Teleta
THE EFFECTS OF TEMPERATURE ON HEMOGLOBIN IN CAPITELLA TELETA by Alexander M. Barclay A thesis submitted to the Faculty of the University of Delaware in partial fulfillment of the requirements for the degree of Master of Science in Marine Studies Summer 2013 c 2013 Alexander M. Barclay All Rights Reserved THE EFFECTS OF TEMPERATURE ON HEMOGLOBIN IN CAPITELLA TELETA by Alexander M. Barclay Approved: Adam G. Marsh, Ph.D. Professor in charge of thesis on behalf of the Advisory Committee Approved: Mark A. Moline, Ph.D. Director of the School of Marine Science and Policy Approved: Nancy M. Targett, Ph.D. Dean of the College of Earth, Ocean, and Environment Approved: James G. Richards, Ph.D. Vice Provost for Graduate and Professional Education ACKNOWLEDGMENTS I extend my sincere gratitude to the individuals that either contributed to the execution of my thesis project or to my experience here at the University of Delaware. I would like to give special thanks to my adviser, Adam Marsh, who afforded me an opportunity that exceeded all of my prior expectations. Adam will say that I worked very independently and did not require much guidance, but he served as an inspiration and a role model for me during my studies. Adam sincerely cares for each of his students and takes the time and thought to tailor his research program to fit each person's interests. The reason that I initially chose to work in Adam's lab was that he expressed a genuine excitement for science and for his lifes work. His enthusiasm resonated with me and helped me to find my own exciting path in science. -
Hemoprotein Dalam Tubuh Manusia Tinjauan Pustaka
http://jurnal.fk.unand.ac.id 22 Tinjauan Pustaka Hemoprotein dalam Tubuh Manusia Husnil Kadri Abstrak Hemoprotein adalah protein dengan kandungan hem yang terdapat hampir dalam semua sel manusia, hewan, dan pigmen fotosintesis tumbuhan. Ada berbagai macam hemoprotein yang tersebar luas dalam tubuh manusia, seperti hemoglobin, myoglobin, citoglobin, neuroglobin, dan lain-lain. Semua hemoprotein tersebut memiliki fungsi beragam yang penting untuk berlangsungnya proses metabolisme dalam tubuh. Struktur hem pada pigmen fotosintesis (klorofil) tumbuhan sama dengan hemoglobin pada manusia, tetapi ion logam pada klorofil adalah magnesium (Mg) sedangkan pada hemoglobin adalah besi (Fe). Perbedaan inilah yang kurang diketahui oleh sebagian masyarakat sehingga ada yang mengira mengkonsumsi klorofil tumbuhan dapat meningkatkan kadar hemoglobin darah. Oleh karena itu, artikel ini bertujuan untuk mengetahui perbedaan antara hemoprotein manusia dengan klorofil dan fungsi hemoprotein dalam tubuh manusia. Berdasarkan bentuk ion Fe pada gugus hemnya, maka hemoprotein dapat dibagi atas: (1) Hemoprotein yang memiliki ion Fe2+ sehingga mampu mengikat oksigen yaitu; hemoglobin, myoglobin, neuroglobin, dan cytoglobin. (2) Hemoprotein yang memiliki ion Fe3+ sehingga berperan sebagai enzim oksidoreduktase yaitu; Sitokrom P450, Sitokrom yang terlibat dalam fosforilasi oksidatif, katalase, triptopan pirolase, dan NO sintase. Kata kunci: hemoprotein, ion Fe2+, ion Fe3+ Abstract Hemoproteins are proteins containing heme that widely distributed in humans, animals, and photosynthetic pigment of plants. There are many kind of hemoproteins in human body, such as hemoglobin, myoglobin, cytoglobin, neuroglobin, etc. Hemoproteins have the varied functions to keep normal metabolism in the body. Photosynthetic pigment of plants (chlorophyll) and human’s hemoglobin have the same structure but the metal ions are different. Chlorophyll has magnesium and human’s hemoglobin has iron (Fe). -
Fitting Together the Evolutionary Puzzle Pieces of the Immunoglobulin T Gene from Antarctic Fishes
Preprints (www.preprints.org) | NOT PEER-REVIEWED | Posted: 27 November 2020 doi:10.20944/preprints202011.0685.v1 Article Fitting together the evolutionary puzzle pieces of the Immunoglobulin T gene from Antarctic fishes Alessia Ametrano1,2 Marco Gerdol3, Maria Vitale1,4, Samuele Greco3, Umberto Oreste1, Maria Rosaria Coscia1,* 1 Institute of Biochemistry and Cell Biology - National Research Council of Italy, 80131 Naples, Italy; [email protected] (A.A.); [email protected] (U.O.); [email protected] (M.R.C.) 2 Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, University of Campania Luigi Vanvitelli, 81100 Caserta, Italy; [email protected] (A.A.) 3 Department of Life Sciences, University of Trieste, 34127 Trieste, Italy; [email protected] (M.G.); [email protected] (S.G.) 1,4 Department of Molecular Medicine and Medical biotechnology, University of Naples Federico II, 80131 Naples, Italy (Present address); [email protected] (M.V.) * Correspondence: [email protected]; Tel.: +0039 081 6132556 (M.R.C.) Abstract: Cryonotothenioidea is the main group of fishes that thrive in the extremely cold Antarctic environment, thanks to the acquisition of peculiar morphological, physiological and molecular adaptations. We have previously disclosed that IgM, the main immunoglobulin isotype in teleosts, display typical cold-adapted features. Recently, we have analyzed the gene encoding the heavy chain constant region (CH) of the IgT isotype from the Antarctic teleost Trematomus bernacchii (family Nototheniidae), characterized by the near-complete deletion of the CH2 domain. Here, we aimed to track the loss of the CH2 domain along notothenioid phylogeny and to identify its ancestral origins. -
Ancient Climate Change, Antifreeze, and the Evolutionary Diversification of Antarctic Fishes
Ancient climate change, antifreeze, and the evolutionary diversification of Antarctic fishes Thomas J. Neara,b,1, Alex Dornburgb, Kristen L. Kuhnb, Joseph T. Eastmanc, Jillian N. Penningtonb,d, Tomaso Patarnelloe, Lorenzo Zanef, Daniel A. Fernándezg, and Christopher D. Jonesh aPeabody Museum of Natural History and bDepartment of Ecology and Evolutionary Biology, Yale University, New Haven, CT 06520 cDepartment of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, OH 45701; dEzra Stiles College, Yale University, New Haven, CT 06520 eDepartment of Public Health, Comparative Pathology and Veterinary Hygiene, Università di Padova, 35020 Legnaro, Italy; fDepartment of Biology, Università di Padova, 35131 Padua, Italy; gCentro Austral de Investigaciones Científicas, 9410 Ushuaia, Argentina; and hAntarctic Ecosystem Research Division, Southwest Fisheries Science Center, National Oceanic and Atmospheric Administration National Marine Fisheries Service, La Jolla, CA 92037 Edited by David M. Hillis, University of Texas, Austin, TX, and approved January 25, 2012 (received for review September 15, 2011) The Southern Ocean around Antarctica is among the most rapidly they are more species-rich than their non-Antarctic sister line- warming regions on Earth, but has experienced episodic climate age (approximately 100 vs. one species) (9). Molecular di- change during the past 40 million years. It remains unclear how vergence time analyses have attempted to correlate the origin of ancient periods of climate change have shaped Antarctic bio- the AFGP-bearing Antarctic notothenioids with a period of diversity. The origin of antifreeze glycoproteins (AFGPs) in Ant- global cooling and widespread glaciation of Antarctica that be- arctic notothenioid fishes has become a classic example of how the gan at the onset of the Eocene–Oligocene boundary (14, 15), evolution of a key innovation in response to climate change can approximately 35 Ma (16, 17), leading to the conclusion that the drive adaptive radiation. -
The Hemoglobins of Sub-Antarctic Fishes of the Suborder Notothenioidei
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Available online at www.sciencedirect.com Polar Science 4 (2010) 295e308 http://ees.elsevier.com/polar/ The hemoglobins of sub-Antarctic fishes of the suborder Notothenioidei Daniela Coppola a, Daniela Giordano a, Alessandro Vergara b, Lelio Mazzarella b, Guido di Prisco a, Cinzia Verde a, Roberta Russo a,* a Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy b Department of Chemistry, University of Naples ‘Federico II’, Complesso Universitario Monte S. Angelo, Via Cinthia, I-80126 Naples, Italy Received 16 December 2009; revised 19 April 2010; accepted 19 April 2010 Available online 12 May 2010 Abstract Fishes of the perciform suborder Notothenioidei provide an excellent opportunity for studying the evolution and functional importance of evolutionary adaptations to temperature. To understand the unique biochemical features of high-Antarctic noto- thenioids, it is important to improve our knowledge of these highly cold-adapted stenotherms with new information on their sub- Antarctic relatives. This paper focuses on the oxygen-transport system of two non-Antarctic species, Eleginops maclovinus and Bovichtus diac- anthus. Unlike most Antarctic notothenioids, the blood of E. maclovinus and B. diacanthus displays high hemoglobin (Hb) multiplicity. E. maclovinus, the sister group of Antarctic notothenioids, has one cathodal (Hb C) and two anodal components (Hb 1, Hb 2). B. diacanthus, one of the most northern notothenioids, has three major Hbs. The multiple Hbs may have been maintained as a response to temperature differences and fluctuations of temperate waters, much larger than in the Antarctic. -
Optimization of Multiparameters for Increased Yields of Cytochrome B5 in Bioreactors
molecules Article Optimization of Multiparameters for Increased Yields of Cytochrome B5 in Bioreactors Ricardo F. S. Pereira 1,2 and Carla C. C. R. de Carvalho 1,2,* 1 Department of Bioengineering, iBB—Institute for Bioengineering and Biosciences, Instituto Superior Técnico, Universidade de Lisboa, Av. Rovisco Pais, 1049-001 Lisboa, Portugal; [email protected] 2 Associate Laboratory i4HB—Institute for Health and Bioeconomy, Instituto Superior Técnico, Universidade de Lisboa, Av. Rovisco Pais, 1049-001 Lisboa, Portugal * Correspondence: [email protected]; Tel.: +351-21-841-9594 Abstract: The production of recombinant proteins is gaining increasing importance as the market requests high quality proteins for several applications. However, several process parameters affect both the growth of cells and product yields. This study uses high throughput systems and statistical methods to assess the influence of fermentation conditions in lab-scale bioreactors. Using this methodology, it was possible to find the best conditions to produce cytochrome b5 with recombinant cells of Escherichia coli. Using partial least squares, the height-to-diameter ratio of the bioreactor, aeration rate, and PID controller parameters were found to contribute significantly to the final biomass and cytochrome concentrations. Hence, we could use this information to fine-tune the process parameters, which increased cytochrome production and yield several-fold. Using aeration of 1 vvm, a bioreactor with a height-to-ratio of 2.4 and tuned PID parameters, a production of 72.72 mg/L of cytochrome b5 in the culture media, and a maximum of product to biomass yield of 24.97 mg/g could be achieved. -
Exploiting and Engineering Hemoproteins for Abiological
Available online at www.sciencedirect.com ScienceDirect Exploiting and engineering hemoproteins for abiological carbene and nitrene transfer reactions 1 2 1 Oliver F Brandenberg , Rudi Fasan and Frances H Arnold The surge in reports of heme-dependent proteins as catalysts However, a significant hurdle is presented by the fact for abiotic, synthetically valuable carbene and nitrene transfer that a number of valuable chemical transformations, reactions dramatically illustrates the evolvability of the protein including many catalyzed by synthetic catalysts, do not world and our nascent ability to exploit that for new enzyme have biocatalytic counterparts. The necessary enzymes chemistry. We highlight the latest additions to the hemoprotein- simply do not exist. One effective approach to creating catalyzed reaction repertoire (including carbene Si–H and C–H new enzymes has been to engineer existing proteins to insertions, Doyle–Kirmse reactions, aldehyde olefinations, exhibit new, synthetically useful reactivity, mainly by azide-to-aldehyde conversions, and intermolecular nitrene exploiting their metallo-cofactors and other cofactors for C–H insertion) and show how different hemoprotein scaffolds new chemistry and improving those activities by directed offer varied reactivity and selectivity. Preparative-scale evolution [3–5]. The resulting fully genetically encoded syntheses of pharmaceutically relevant compounds catalysts could, at least in principle, be incorporated into accomplished with these new catalysts are beginning to in vivo biosynthetic pathways to access new products or demonstrate their biotechnological relevance. Insights into the provide alternative routes to existing products. Repurpos- determinants of enzyme lifetime and product yield are ing existing proteins for new chemistry, a trick used by providing generalizable cues for engineering heme-dependent evolution for eons, has proven particularly fruitful with proteins to further broaden the scope and utility of these heme-dependent proteins. -
Cold-Adapted Antarctic Fish
Gene 433 (2009) 100–101 Contents lists available at ScienceDirect Gene journal homepage: www.elsevier.com/locate/gene Letter to the Editor Cold-adapted Antarctic fish: The discovery of neuroglobin in the dominant suborder Notothenioidei C.-H. Christina Cheng a, Guido di Prisco b, Cinzia Verde b,⁎ a Department of Animal Biology, University of Illinois, Urbana, IL 61801, USA b Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy article info abstract Article history: Novel globins, such as neuroglobin (Ngb) and cytoglobin, have recently been discovered in many Received 31 October 2008 vertebrates. Ngb is mainly expressed in neurons and plays a neuroprotective role during hypoxic stress. Received in revised form 25 November 2008 Neuronal hypoxia and cerebral ischemia induce Ngb expression; knocking down Ngb expression increases Accepted 1 December 2008 hypoxic neuronal injury in vitro and ischemic cerebral injury in vivo. Although Ngb was originally identified Available online 16 December 2008 in mammals, it is also present in fish, including the zebrafish Danio rerio. We have discovered the Ngb gene to be present in red-blooded notothenioid fish species, and in at least 13 of the 16 species of the white- Keywords: fi Neuroglobin blooded ice sh family Channichthyidae. The deduced amino-acid sequences are well conserved. The Notothenioid retention of the Ngb gene by channichthyids, despite the loss of hemoglobin and myoglobin, appears very Icefish intriguing. Red-blooded fish © 2008 Elsevier B.V. All rights reserved. The variety of adaptations underlying the ability of modern high- myoglobin (Mb) in Channichthyidae, reflect the specialisation of Antarctic notothenioid fish to survive at freezing temperatures Antarctic organisms to a narrow range of low temperatures. -
New Insights Into the Organization and Evolution of Vertebrate IRBP Genes
Molecular Phylogenetics and Evolution 48 (2008) 258–269 Contents lists available at ScienceDirect Molecular Phylogenetics and Evolution journal homepage: www.elsevier.com/locate/ympev New insights into the organization and evolution of vertebrate IRBP genes and utility of IRBP gene sequences for the phylogenetic study of the Acanthomorpha (Actinopterygii: Teleostei) Agnès Dettaï *, Guillaume Lecointre UMR 7138 ‘‘Systématique, Adaptation, Evolution”, Département Systématique et Evolution, CP26, Muséum National d’Histoire Naturelle, 57 rue Cuvier, Case Postale 26, 75231 Paris Cedex 05, France article info abstract Article history: The interphotoreceptor retinoid-binding protein (IRBP) coding gene has been used with success for the Received 20 November 2007 large-scale phylogeny of mammals. However, its phylogenetic worth had not been explored in Actinop- Revised 1 April 2008 terygians. We explored the evolution of the structure of the gene and compared the structure predicted Accepted 1 April 2008 from known sequences with that of a basal vertebrate lineage, the sea lamprey Petromyzon marinus. This Available online 11 April 2008 sequence is described here for the first time. The structure made up of four tandem repeats (or modules) arranged in a single gene, as present in Chondrichthyes (sharks and rays) and tetrapods, is also present in Keywords: sea lamprey. In teleosts, one to two paralogous copies of IRBP gene have been identified depending on the Molecular phylogeny genomes. When the sequences from all modules for a wide sampling of vertebrates are compared and Teleostei Acanthomorpha analyzed, all sequences previously assigned to a particular module appear to be clustered together, sug- IRBP gesting that the divergence among modules is older than the split between lampreys and other verte- Interphotoreceptor retinoid-binding protein brates.