DOCSLIB.ORG

Chemical Composition and Mineral Content of Soil, Plant and Animal Tissues in Some Camel Production Areas in the Sudan

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Chemical Composition and Mineral Content of Soil, Plant and Animal Tissues in Some Camel Production Areas in the Sudan In the Name of Allah, the Beneficent, the Merciful. Chemical Composition and Mineral Content of Soil, Plant and Animal Tissues in Some Camel Production Areas in the Sudan BY ALI MAHMOUD AHMED SHAMAT BVSc. (1979) University of Khartoum DTVSc. (1988), Edinburgh University U.K MSc. (1993) University of Reading U.K A thesis submitted in accordance with the requirements of the University of Khartoum for the degree of the Doctor of Philosophy (Ph.D) Supervisor Prof. Amir Mohammed Salih Faculty of animal production,University of Khartoum Department of animal nutrition, Faculty of animal production, University of Khartoum February- 2008 LIST OF CONTENTS Page List of contents…………………………………………………………… i List of tables……………………………………………………………… viii List of figures……………………………………………………………. xii List of appendix………………………………………………………….. xvi Dedication……………………………………………………………….. xvii Acknowledgements………………………………………………………. xviii English abstract…………………………………………………………… xix xxii .…………………………………………………………………… اﻟﺨﻼﺻﻪ Chapter one………………………………………………………………... Introduction……………………………………………………………… 1 Chapter two ………………………………………………………………. Literature Review………………………………………………………… 11 Agro-ecological zones…………………………………………………… 12 2.1.1. Desert…………………………………………………………………….. 12 2.1.2. Semi-desert……………………………………………………………….. 12 2.1.3. Low rainfall savannah……………………………………………………. 14 2.1.4. High rainfall savannah…………………………………………………… 15 2.1.5. Mountains…………………………………………………………………. 15 2.2. Camel owners of the Sudan (Aballa)…………………………………….. 15 2.3. Camel types in the Sudan…………………………………………………. 16 2.4. Interesting characteristics of camels……………………………………… 17 2.4.1. Sight and sense…………………………………………………………… 18 2.4.2. Body structure…………………………………………………………….. 18 2.4.3. Feeding habits……………………………………………………………. 18 2.4.4. Watering…………………………………………………………………. 20 2.4.5. Body temperature…………………………………………………………. 21 2.5. Camel management and husbandry practices……………………………… 21 2.5.1. Camels Migration Patterns…………………………………………………. 22 2.5.1.1. Darfur Region……………………………………………………………… 22 2.5.1.2. Kordofan Region…………………………………………………………… 23 2.5.1.3. Eastern Region…………………………………………………………….. 24 2.5.2. Herd structure……………………………………………………………… 25 2.6. Limitations to camel production in the Sudan……………………………. 27 2.6.1. Socio-economical problems………………………………………………. 27 2.6.2. Nutritional disorders of certain nutrients………………………………….. 29 2.6.2.1. Watering…………………………………………………………………… 30 2.6.2.2. Feeding…………………………………………………………………….. 31 2.6.2.2.1. Energy and Protein………………………………………………………… 31 2.6.2.2.2. Vitamins……………………………………………………………………. 33 2.6.2.3.3. Minerals…………………………………………………………………….. 34 2.7. Factors Influencing Mineral Requirements………………………………… 37 2.7.1. Mineral status of Sudan soil………………………………………………... 37 i 2.7.1.1. Yermosols……………………………………………………………….. 38 2.7.1.2. Arenosols……………………………………………………………….. 38 2.7.1.3. Vertisols………………………………………………………………….. 39 2.7.1.4. Nitosols……………………………………………………………………. 40 2.7.1.5. Fluvisols…………………………………………………………………… 40 2.7.1.6. Hill soils……………………………………………………………………. 40 2.7.1.7. Ferralsols…………………………………………………………............. 40 2.8. Mineral status of plants…………………………………………………… 41 2.9. Mineral Status of Ruminants……………………………………………… 43 2.9.1. Blood……………………………………………………………………… 46 2.9.2. Bone……………………………………………………………………….. 48 2.9.3. Liver……………………………………………………………………….. 48 2.10. Mineral deficiencies, Toxicities and imbalances in the camel…………….. 49 2.10.1. Calcium and Phosphorus………………………………………………….. 49 2.10.2. Magnesium (Mg)…………………………………………………………… 50 2.10.3. Sodium chloride……………………………………………………………. 51 2.10.4. Potassium (K)……………………………………………………………… 53 2.10.5. Copper and Molybdenum…………………………………………............ 53 2.10.5.1. Copper in liver…………………………………………………………….. 54 2.10.6. Iron (Fe)…………………………………………………………………… 55 2.10.7. Zinc (Zn)…………………………………………………………………… 56 2.10.8. Manganese (Mn)…………………………………………………………… 57 2.10.9. Cobalt (CO) and Selenium (Se)……………………………………………. 58 2.10.10. Fluorine (Fl)………………………………………………………………. 59 2.10.11. Sulphur (S) and Nitrogen (N)……………………………………............... 59 2.10.12. Iodine (I)…………………………………………………………………… 60 Chapter three……………………………………………………………… Materials and Methods…………………………………………………… 62 3.1. The study area……………………………………………………………… 62 3.1.1. Geographical and Major Topographic Features of the Study Areas……….. 62 3.1.1.1. Western Region……………………………………………………………. 62 3.1.1.2. Eastern Region……………………………………………………………... 63 3.1.1.2.1. Norther Sudan……………………………………………………………… 63 3.1.1.2.2. Central Sudan………………………………………………………………. 63 3.1.1.2.3. Eastern Sudan………………………………………………………………. 63 3.2. Sampling and data collection………………………………………………. 64 3.2.1. Western Region…………………………………………………………….. 65 3.2.1.1. Kordofan camels…………………………………………………................ 65 3.2.1.2. Darfur camels………………………………………………………………. 65 3.2.2. Eastern Sudan camels………………………………………………………. 66 3.3. Camel tissue samples collection……………………………………………. 67 3.3.1. Whole blood samples collection…………………………………………… 67 3.3.2. Liver and bone samples collection…………………………………………. 68 3.4. Plant, soil and water samples collection…………………………………… 69 3.4.1. Plant samples collection……………………………………………………. 69 ii 3.4.2. Soil and water samples collection………………………………………….. 70 3.5. Chemical analysis methods………………………………………………… 70 3.5.1. Plant analysis method……………………………………………………… 70 3.5.1.1. Weende proximate analysis……………………………………………….. 70 3.5.1.2. Plant wet digestion method for mineral content analysis…………………. 71 3.5.2. Soil analysis method………………………………………………………. 71 3.5.3. Water analysis method……………………………………………………... 72 3.5.4. Liver analysis method……………………………………………………… 72 3.5.5. Bone analysis method………………………………………………............. 72 3.5.6. Serum analysis methods……………………………………………............. 72 3.5.6.1. Serum calcium and magnesium determination method……………………. 73 3.5.6.2. Serum inorganic phosphorus determination method………………………. 73 3.5.6.3. Serum copper, zinc, and total iron determination methods………............... 73 3.5.6.4. Serum sodium and potassium determination methods……………………... 73 3.6. Natroun Supplementation Trial……………………………………….......... 73 3.6.1. Ration formulation…………………………………………………............. 76 3.6.2. Experimental animals………………………………………………………. 77 3.6.3. Collection of blood samples………………………………………………... 77 3.6.4. Laboratory Techniques……………………………………………………... 77 3.6.5. Live weight measurement………………………………………………….. 78 3.7. Statistical analysis…………………………………………………….......... 78 Chapter Four Results 79 4.1. Browse and Forages Analysis Results……………………………………... 80 4.1.1. Browse and forage proximate analysis……………………………………. 80 4.1.2. Results of proximate analysis…………………………………………….. 80 4.1.3. Effect of location on browse and forage proximate composition………….. 80 4.1.4. Effect of season on browse and forage proximate composition……………. 81 4.1.5. The interaction effect of location and season on browse and forages……… 81 4.2. Hydrochemical evaluation of groundwater in Western and Eastern Regions Results ……………………………………………………………………. 82 4.3. Soil mineral concentrations………………………………………………. 85 4.3.1. Effect of location on soil mineral concentration…………………………. 85 4.3.2. Effect of season on soil mineral concentration…………………………… 85 4.3.3. The interaction effect of location and season on soil mineral concentration. 86 4.3.3.1. Soil pH, extractable soil sodium and extractable soil potassium………….. 86 4.3.3.2. Extractable soil mineral (Ca, P and Mg)…………………………............... 87 4.3.3.3. Extractable soil minerals (Cu, Zn and Fe)………………………………… 87 4.3.3.4. Extractable soil minerals (Co,Mo and Mn)………………………............... 88 4.4. Mineral concentrations of browse and forage…………………………….. 88 4.4.1. Effect of location on mineral concentration of browse and forages………. 88 4.4.2. Effect of season on mineral concentration of browse and forages…………. 89 4.4.3. The interaction effect of location and season on mineral oncentration of browse and forages……………………………………………………... 89 4.4.3.1. Calcium (Ca) ………………………………………………………………. 89 iii 4.4.3.2. Phosphorus (P) …………………………………………………………….. 89 4.4.3.3. Potassium (K) ……………………………………………………………… 90 4.4.3.4. Magnesium (Mg) ………………………………………………………….. 90 4.4.3.5. Sodium (Na) ………………………………………………………………. 90 4.4.3.6. Copper (Cu) ……………………………………………………………….. 91 4.4.3.7. Zinc (Zn) …………………………………………………………………... 91 4.4.3.8. Cobalt (Co) ………………………………………………………………… 91 4.4.3.9. Manganese (Mn) …………………………………………………………... 92 4.4.3.10. Iron (Fe) ……………………………………………………………………. 92 4.4.3.11. Molybdenum (Mo) ………………………………………………………… 92 4.5. Mineral concentration of camel tissues……………………………………. 94 4.5.1. Blood serum minerals……………………………………………………… 94 4.5.1.1. Blood serum calcium………………………………………………………. 94 4.5.1.1.1. Effect of season on serum Ca level………………………………………… 94 4.5.1.1.2. Effect of location on serum Ca level……………………………………….. 95 4.5.1.1.3. Interaction effect of sex and location on serum Ca level…………………... 95 4.5.1.1.4. Interaction effect of season and location on serum Ca level……………….. 98 4.5.1.1.5. Interaction effect of sex and season on serum Ca level……………………. 100 4.5.1.1.6. Effect of sex, season and location on prevalence of calcium critical level………………………………………………………………………… 100 4.5.1.1.6. Interaction effect of location, sex and season on serum Ca critical 4. level………………………………………………………………………. 102 4.5.1.2. Blood serum phosphorus………………………………………………….. 105 4.5.1.2.1. Effect of season on serum P level…………………………………………. 105 4.5.1.2.2. Effect of locations on serum P level………………………………………. 106 4.5.1.2.3. Interaction effect of sex and location on serum P level…………………… 106 4.5.1.2.4. Interaction effect of season and location
Load more

Recommended publications
  • From Nutrition to Health: the Role of Natural Products – a Review
    8 From Nutrition to Health: The Role of Natural Products – A Review H.G. Mikail Department of Pharmacology and Toxicology, Faculty of Veterinary Medicine, University of Abuja, Abuja, Nigeria 1. Introduction The word natural literally means something that is present in or produced by nature and not artificial or man-made (Spainhour, 2005). Although, many effective poisons are natural products (Schoental, 1965). When the word natural is used in written or verbiage form, many a times refer to something good or pure (Spainhour, 2005). Today, the term natural products are commonly understood to refer to herbs, herbal concoctions, dietary supplements, traditional medicine including Chinese traditional medicine, or other alternative medicine (Holt, and Chandra, 2002). In general, natural products are either of prebiotic origin or originate from microbes, plants, or animal sources (Nakanishi, 1999a; Nakanishi, 1999b). As chemicals, natural products include such classes of compounds as terpenoids, polyketides, amino acids, peptides, proteins, carbohydrates, lipids, nucleic acid bases, ribonucleic acid (RNA), deoxyribonucleic acid (DNA), and so forth. Natural products are an expression of organism’s increase in life complexity by nature (Jarvis, 2000). It is good to understand what ‘nutrition’ and ‘a nutrition perspective’ mean. It should be understood that food and nutrition are not the same. Nutrition is both the outcome and the process of providing the nutrients needed for health, growth, development and survival. Although food—as the source of these nutrients—is an important part of this process, it is not by itself sufficient. Good health management services, as well as good caring practices are other important and necessary inputs needed in maintaining good health apart from good nutrition (SCN, 2004).
    [Show full text]
  • As an Indicator of Nutritional Status in Marine Bacteria
    The ISME Journal (2012) 6, 524–530 & 2012 International Society for Microbial Ecology All rights reserved 1751-7362/12 www.nature.com/ismej ORIGINAL ARTICLE Mg2 þ as an indicator of nutritional status in marine bacteria Mikal Heldal1, Svein Norland1, Egil Severin Erichsen2, Ruth-Anne Sandaa1, Aud Larsen3, Frede Thingstad1 and Gunnar Bratbak1 1Department of Biology, University of Bergen, Bergen, Norway; 2Laboratory for Electron Microscopy, University of Bergen, Bergen, Norway and 3Uni Environment, Uni Research, Bergen, Norway Cells maintain an osmotic pressure essential for growth and division, using organic compatible solutes and inorganic ions. Mg2 þ , which is the most abundant divalent cation in living cells, has not been considered an osmotically important solute. Here we show that under carbon limitation or dormancy native marine bacterial communities have a high cellular concentration of Mg2 þ (370–940 mM) and a low cellular concentration of Na þ (50–170 mM). With input of organic carbon, the average cellular concentration of Mg2 þ decreased 6–12-fold, whereas that of Na þ increased ca 3–4-fold. The concentration of chlorine, which was in the range of 330–1200 mM, and was the only inorganic counterion of quantitative significance, balanced and followed changes in the concentra- tion of Mg2 þ þ Na þ . In an osmotically stable environment, like seawater, any major shift in bacterial osmolyte composition should be related to shifts in growth conditions, and replacing organic compatible solutes with inorganic solutes is presumably a favorable strategy when growing in carbon-limited condition. A high concentration of Mg2 þ in cells may also serve to protect and stabilize macromolecules during periods of non-growth and dormancy.
    [Show full text]
  • A Short Review of Iron Metabolism and Pathophysiology of Iron Disorders
    medicines Review A Short Review of Iron Metabolism and Pathophysiology of Iron Disorders Andronicos Yiannikourides 1 and Gladys O. Latunde-Dada 2,* 1 Faculty of Life Sciences and Medicine, Henriette Raphael House Guy’s Campus King’s College London, London SE1 1UL, UK 2 Department of Nutritional Sciences, School of Life Course Sciences, King’s College London, Franklin-Wilkins-Building, 150 Stamford Street, London SE1 9NH, UK * Correspondence: [email protected] Received: 30 June 2019; Accepted: 2 August 2019; Published: 5 August 2019 Abstract: Iron is a vital trace element for humans, as it plays a crucial role in oxygen transport, oxidative metabolism, cellular proliferation, and many catalytic reactions. To be beneficial, the amount of iron in the human body needs to be maintained within the ideal range. Iron metabolism is one of the most complex processes involving many organs and tissues, the interaction of which is critical for iron homeostasis. No active mechanism for iron excretion exists. Therefore, the amount of iron absorbed by the intestine is tightly controlled to balance the daily losses. The bone marrow is the prime iron consumer in the body, being the site for erythropoiesis, while the reticuloendothelial system is responsible for iron recycling through erythrocyte phagocytosis. The liver has important synthetic, storing, and regulatory functions in iron homeostasis. Among the numerous proteins involved in iron metabolism, hepcidin is a liver-derived peptide hormone, which is the master regulator of iron metabolism. This hormone acts in many target tissues and regulates systemic iron levels through a negative feedback mechanism. Hepcidin synthesis is controlled by several factors such as iron levels, anaemia, infection, inflammation, and erythropoietic activity.
    [Show full text]
  • General Aspects of Metal Ions As Signaling Agents in Health and Disease
    biomolecules Review General Aspects of Metal Ions as Signaling Agents in Health and Disease Karolina Krzywoszy ´nska 1,*, Danuta Witkowska 1,* , Jolanta Swi´ ˛atek-Kozłowska 1, Agnieszka Szebesczyk 1 and Henryk Kozłowski 1,2 1 Institute of Health Sciences, University of Opole, 68 Katowicka St., 45-060 Opole, Poland; [email protected] (J.S.-K.);´ [email protected] (A.S.); [email protected] (H.K.) 2 Faculty of Chemistry, University of Wrocław, 14 F. Joliot-Curie St., 50-383 Wrocław, Poland * Correspondence: [email protected] (K.K.); [email protected] (D.W.); Tel.: +48-77-44-23-549 (K.K); +48-77-44-23-548 (D.W.) Received: 25 August 2020; Accepted: 2 October 2020; Published: 7 October 2020 Abstract: This review focuses on the current knowledge on the involvement of metal ions in signaling processes within the cell, in both physiological and pathological conditions. The first section is devoted to the recent discoveries on magnesium and calcium-dependent signal transduction—the most recognized signaling agents among metals. The following sections then describe signaling pathways where zinc, copper, and iron play a key role. There are many systems in which changes in intra- and extra-cellular zinc and copper concentrations have been linked to important downstream events, especially in nervous signal transduction. Iron signaling is mostly related with its homeostasis. However, it is also involved in a recently discovered type of programmed cell death, ferroptosis. The important differences in metal ion signaling, and its disease-leading alterations, are also discussed.
    [Show full text]
  • Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation?
    Int. J. Mol. Sci. 2015, 16, 16728-16739; doi:10.3390/ijms160816728 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 www.mdpi.com/journal/ijms Article Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation? Helena Öhrvik 1 and Pernilla Wittung-Stafshede 2,* 1 Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala 751 23, Sweden; E-Mail: [email protected] 2 Department of Chemistry, Umeå University, Umeå 901 87, Sweden * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +46-90-786-5347. Academic Editor: Masatoshi Maki Received: 4 June 2015 / Accepted: 20 July 2015 / Published: 23 July 2015 Abstract: The human copper (Cu) chaperone Atox1 delivers Cu to P1B type ATPases in the Golgi network, for incorporation into essential Cu-dependent enzymes. Atox1 homologs are found in most organisms; it is a 68-residue ferredoxin-fold protein that binds Cu in a conserved surface-exposed Cys-X-X-Cys (CXXC) motif. In addition to its well-documented cytoplasmic chaperone function, in 2008 Atox1 was suggested to have functionality in the nucleus. To identify new interactions partners of Atox1, we performed a yeast two-hybrid screen with a large human placenta library of cDNA fragments using Atox1 as bait. Among 98 million fragments investigated, 25 proteins were found to be confident interaction partners. Nine of these were uncharacterized proteins, and the remaining 16 proteins were analyzed by bioinformatics with respect to cell localization, tissue distribution, function, sequence motifs, three-dimensional structures and interaction networks.
    [Show full text]
  • Iron Metabolism and Iron Disorders Revisited in the Hepcidin
    CENTENARY REVIEW ARTICLE Iron metabolism and iron disorders revisited Ferrata Storti Foundation in the hepcidin era Clara Camaschella,1 Antonella Nai1,2 and Laura Silvestri1,2 1Regulation of Iron Metabolism Unit, Division of Genetics and Cell Biology, San Raffaele Scientific Institute, Milan and 2Vita Salute San Raffaele University, Milan, Italy ABSTRACT Haematologica 2020 Volume 105(2):260-272 ron is biologically essential, but also potentially toxic; as such it is tightly controlled at cell and systemic levels to prevent both deficien- Icy and overload. Iron regulatory proteins post-transcriptionally con- trol genes encoding proteins that modulate iron uptake, recycling and storage and are themselves regulated by iron. The master regulator of systemic iron homeostasis is the liver peptide hepcidin, which controls serum iron through degradation of ferroportin in iron-absorptive entero- cytes and iron-recycling macrophages. This review emphasizes the most recent findings in iron biology, deregulation of the hepcidin-ferroportin axis in iron disorders and how research results have an impact on clinical disorders. Insufficient hepcidin production is central to iron overload while hepcidin excess leads to iron restriction. Mutations of hemochro- matosis genes result in iron excess by downregulating the liver BMP- SMAD signaling pathway or by causing hepcidin-resistance. In iron- loading anemias, such as β-thalassemia, enhanced albeit ineffective ery- thropoiesis releases erythroferrone, which sequesters BMP receptor lig- ands, thereby inhibiting hepcidin. In iron-refractory, iron-deficiency ane- mia mutations of the hepcidin inhibitor TMPRSS6 upregulate the BMP- Correspondence: SMAD pathway. Interleukin-6 in acute and chronic inflammation increases hepcidin levels, causing iron-restricted erythropoiesis and ane- CLARA CAMASCHELLA [email protected] mia of inflammation in the presence of iron-replete macrophages.
    [Show full text]
  • Identification, Sequencing, and Cellular Localization of Hepcidin in Guinea
    389 Identification, sequencing, and cellular localization of hepcidin in guinea pig (Cavia porcellus) Peggy Schwarz, Pavel Strnad, Nadine Singer, Franz Oswald, Robert Ehehalt1, Guido Adler and Hasan Kulaksiz Division of Gastroenterology, Department of Internal Medicine, University Hospital Ulm, Albert-Einstein-Allee 23, D-89081 Ulm, Germany 1Division of Gastroenterology, Department of Internal Medicine, University Hospital Heidelberg, Im Neuenheimer Feld 410, D-69120 Heidelberg, Germany (Correspondence should be addressed to H Kulaksiz; Email: [email protected]) Abstract Hepcidin, a cysteine-rich peptide hormone with anti- system. Western blot analyses showed a distinct immuno- microbial and iron-regulatory activity, plays a central role in reactive band of w8 kDa, consistent with the predicted regulating iron metabolism during inflammation, hypoxia, size of prohepcidin, and revealed that guinea pig hepcidin iron deficiency, and iron overload. The aim of this study protein is synthesized predominantly in the liver, and with was to isolate and sequence the guinea pig hepcidin gene and lower expression in kidney, heart, and pancreas. Immuno- show peptide’s tissue distribution to identify the guinea pig histochemical studies showed hepcidin predominantly at the as good animal model to study the regulation and function basolateral membrane domain of hepatocytes in periportal of hepcidin. The guinea pig hepcidin cDNA contains a regions. In pancreas, hepcidin immunoreactivity was con- 252 bp open reading frame encoding for an 83 amino acid fined to endocrine islets of Langerhans, while hepcidin was protein with eight highly conserved cysteine residues. seen in tubules, but not in the glomeruli in the kidney. Phylogenetic analyses showed that guinea pig hepcidin was Our data identify guinea pig as a convenient model more related to human and chimpanzee than to rodents like organism to study the role of hepcidin, given the remarkable mouse or rat.
    [Show full text]
  • A Systems Biology Approach to Iron Metabolism Reinhard C
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by OpenCommons at University of Connecticut University of Connecticut OpenCommons@UConn UCHC Articles - Research University of Connecticut Health Center Research 1-2014 A Systems Biology Approach to Iron Metabolism Reinhard C. Laubenbacher University of Connecticut School of Medicine and Dentistry Suzy V. Torti University of Connecticut School of Medicine and Dentistry Follow this and additional works at: https://opencommons.uconn.edu/uchcres_articles Part of the Life Sciences Commons, and the Medicine and Health Sciences Commons Recommended Citation Laubenbacher, Reinhard C. and Torti, Suzy V., "A Systems Biology Approach to Iron Metabolism" (2014). UCHC Articles - Research. 270. https://opencommons.uconn.edu/uchcres_articles/270 HHS Public Access Author manuscript Author Manuscript Author ManuscriptAdv Exp Author Manuscript Med Biol. Author Author Manuscript manuscript; available in PMC 2015 June 13. Published in final edited form as: Adv Exp Med Biol. 2014 ; 844: 201–225. doi:10.1007/978-1-4939-2095-2_10. A Systems Biology Approach to Iron Metabolism J. Chifman1, R. Laubenbacher2, and S.V. Torti3,* 1Department of Cancer Biology, Wake Forest School of Medicine, Winston Salem NC 27157 USA 2Center for Quantitative Medicine, University of Connecticut Health Center, Farmington CT 06030 USA 3Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington CT 06030 USA Abstract Iron is critical to the survival of almost all living organisms. However, inappropriately low or high levels of iron are detrimental and contribute to a wide range of diseases. Recent advances in the study of iron metabolism have revealed multiple intricate pathways that are essential to the maintenance of iron homeostasis.
    [Show full text]
  • A Study of Biosensors: Novel Application and Novel Electrode
    A STUDY OF BIOSENSORS: NOVEL APPLICATION AND NOVEL ELECTRODE by PO-YUAN (PAUL) LIN Submitted in partial fulfillment of the requirements For the degree of Doctor of Philosophy Dissertation Advisor: Dr. Chung-Chiun Liu Academic Advisor: Dr. James D. McGuffin-Cawley Department of Materials Science and Engineering CASE WESTERN RESERVE UNIVERSITY May, 2013 0 CASE WESTERN RESERVE UNIVERSITY SCHOOL OF GRADUATE STUDIES We hereby approve the thesis/dissertation of Po-Yuan (Paul) Lin Candidate for the Doctor of Philosophy degree*. (signed) Prof. James D. McGuffin-Cawley (chair of the committee) Prof. Chung-Chiun Liu Prof. Mark R. DeGuire Prof. Pirouz Pirouz (date) March 7, 2013 *We also certify that written approval has been obtained for any proprietary material contained therein. i Table of Content Table of Content ....................................................................................................................... ii List of Tables ............................................................................................................................ iv List of Figures ............................................................................................................................ v Abstract ................................................................................................................................... viii Part I: Background and Introduction ............................................................................... 1 Prostate Cancer ................................................................................................................................
    [Show full text]
  • Supplementary Information
    Supplementary Information Table S1. Confident hits from a cDNA yeast two-hybrid screen using Atox1 as bait and a human placenta RP6 fragment library as prey. Detected interactions with highest predicted biological scores (PBS) are listed below divided in categories from A (highest confidence rank) to F. No C or E scores were found. Functional annotation extracted from Geneontology. (Nine additional hits were detected that corresponded to Genbank IDs of unknown functions, not listed.) PBS Target Function (Direct Annotation) Cell migration; transmembrane receptor protein tyrosine phosphatase A PTPRF activity; integral component of plasma membrane; cell adhesion; negative regulation of receptor binding; peptidyl-tyrosine dephosphorylation snRNA transcription from RNA pol III promoter; positive regulation of protein A ICE1 complex assembly; transcriptionally active chromatin; positive regulation of intracellular protein transport; transcription elongation factor complex A ATP7B Known Atox1 partner (positive control), Cu binding B ATP7A Known Atox1 partner (positive control), Cu binding DNA methylation on cytosine; DNA-methyltransferase activity; B DNMT1 regulation of gene expression, epigenetic zinc binding B CRELD2 Cysteine-rich with EGF-like domain protein 2; protein binding; calcium binding B ZFHX3 Protein binding; sequence-specific DNA binding transcription factor activity zinc binding Cytoplasmic polyadenylation element-binding protein 4 D CPEB4 nucleotide binding; nucleic acid binding; RNA binding D LMCD1 Negative regulation of transcription;
    [Show full text]
  • The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution
    antioxidants Review The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution Yuta Hatori 1 and Svetlana Lutsenko 2,* 1 Faculty of Pharmacy, Yasuda Women’s University, Hiroshima 731-0153, Japan; [email protected] 2 Department of Physiology, Johns Hopkins University School of Medicine, 725 N. Wolfe street, Baltimore, MD 21205, USA * Correspondance: [email protected]; Tel.: +1-410-614-4661 Academic Editors: Ananda S. Prasad and Bin Bao Received: 24 May 2016; Accepted: 22 July 2016; Published: 27 July 2016 Abstract: Human antioxidant protein 1 (Atox1) is a small cytosolic protein with an essential role in copper homeostasis. Atox1 functions as a copper carrier facilitating copper transfer to the secretory pathway. This process is required for activation of copper dependent enzymes involved in neurotransmitter biosynthesis, iron efflux, neovascularization, wound healing, and regulation of blood pressure. Recently, new cellular roles for Atox1 have emerged. Changing levels of Atox1 were shown to modulate response to cancer therapies, contribute to inflammatory response, and protect cells against various oxidative stresses. It has also become apparent that the activity of Atox1 is tightly linked to the cellular redox status. In this review, we summarize biochemical information related to a dual role of Atox1 as a copper chaperone and an antioxidant. We discuss how these two activities could be linked and contribute to establishing the intracellular copper balance and functional identity of cells during differentiation. Keywords: copper; heavy metal; glutathione; Atox1; copper chaperone 1. Introduction Copper is the major redox-active element in most biological systems. As a redox catalyst, copper is utilized in many essential cellular processes including energy production by the respiratory chain, biosynthesis and degradation of neurotransmitters, formation of collagen matrix, redox signaling in angiogenesis, and removal of superoxide.
    [Show full text]
  • Structure and Mechanism of a Primate Ferroportin
    bioRxiv preprint doi: https://doi.org/10.1101/2020.03.04.975748; this version posted March 5, 2020. 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 Structure and mechanism of a primate ferroportin 2 3 Zhenning Ren1,*, Shuai Gao2,*, Jiemin Shen1,*, Lie Wang1, Zhichun Xu1, Ye Yu1, Preetham 4 Bachina1, Hanzhi Zhang1, Arthur Laganowsky3, Nieng Yan2, Ming Zhou1, #, Yaping Pan1,*,# 5 1Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College 6 of Medicine, Houston, TX 77030, USA 7 2Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA 8 3Department of Chemistry, Texas A & M University, College Station, TX 77843, USA 9 10 * These authors contributed equally to the work. 11 # Correspondence to M. Zhou ([email protected]) and Y. Pan ([email protected]) 12 13 bioRxiv preprint doi: https://doi.org/10.1101/2020.03.04.975748; this version posted March 5, 2020. 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. 14 Abstract 15 Ferroportin is the only cellular iron exporter in human and essential for iron homoeostasis. 16 Mutations in ferroportin are associated with hemochromatosis or ferroportin diseases 17 characterized by a paradoxical combination of anemia and abnormal accumulation of iron in 18 cells.
    [Show full text]