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Multi-Scale Impact of Chronic Exposure to Environmental Concentrations Of
Multi-scale impact of chronic exposure to environmental concentrations of chlordecone in freshwater cnidarian, Hydra circumcincta Romain Colpaert, Pierre-Henri Villard, Laetitia de Jong, Marina Mambert, Karim Benbrahim, Joelle Abraldes, Claire Cerini, Valérie Pique, Maxime Robin, Xavier Moreau To cite this version: Romain Colpaert, Pierre-Henri Villard, Laetitia de Jong, Marina Mambert, Karim Benbrahim, et al.. Multi-scale impact of chronic exposure to environmental concentrations of chlordecone in freshwater cnidarian, Hydra circumcincta. Environmental Science and Pollution Research, Springer Verlag, 2020, 27 (33), pp.41052-41062. 10.1007/s11356-019-06859-4. hal-02451113 HAL Id: hal-02451113 https://hal-amu.archives-ouvertes.fr/hal-02451113 Submitted on 23 Jan 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Multi-scale impact of chronic exposure to environmental concentrations of chlordecone in freshwater cnidarian, Hydra circumcincta. Romain COLPAERT1, Pierre-Henri VILLARD1, Laetitia DE JONG1, Marina MAMBERT1, Karim BENBRAHIM1, Joelle ABRALDES1, Claire CERINI2, Valérie PIQUE1, Maxime ROBIN1, Xavier MOREAU1 1 : Aix Marseille Univ, Avignon Univ, CNRS, IRD, IMBE, Marseille, France 2 : Aix Marseille Univ, Inserm U1263, C2VN, Marseille, France Corresponding author: email : [email protected] phone : +33-(0)4-91-83-56-38 Abstract Chlordecone (CLD) is an organochlorine pesticide widely used by the past to control pest insects in banana plantations in the French West Indies. -
OECD Environment Health and Safety Publications Series on Testing and Assessment No
OECD Environment Health and Safety Publications Series on Testing and Assessment No. 21 Detailed Review Paper Appraisal of Test Methods for Sex Hormone Disrupting Chemicals Environment Directorate ORGANISATION FOR ECONOMIC CO-OPERATION AND DEVELOPMENT Paris May 2001 1 Also Published in the Series Testing and Assessment: No. 1, Guidance Document for the Development of OECD Guidelines for Testing of Chemicals (1993; reformatted 1995) No. 2, Detailed Review Paper on Biodegradability Testing (1995) No. 3, Guidance Document for Aquatic Effects Assessment (1995) No. 4, Report of the OECD Workshop on Environmental Hazard/Risk Assessment (1995) No. 5, Report of the SETAC/OECD Workshop on Avian Toxicity Testing (1996) No. 6, Report of the Final Ring-test of the Daphnia magna Reproduction Test (1997) No. 7, Guidance Document on Direct Phototransformation of Chemicals in Water (1997) No. 8, Report of the OECD Workshop on Sharing Information about New Industrial Chemicals Assessment (1997) No. 9 Guidance Document for the Conduct of Studies of Occupational Exposure to Pesticides During Agricultural Application (1997) No. 10, Report of the OECD Workshop on Statistical Analysis of Aquatic Toxicity Data (1998) No. 11, Detailed Review Paper on Aquatic Testing Methods for Pesticides and industrial Chemicals (1998) No. 12, Detailed Review Document on Classification Systems for Germ Cell Mutagenicity in OECD Member Countries (1998) No. 13, Detailed Review Document on Classification Systems for Sensitising Substances in OECD Member Countries 1998) No. 14, Detailed Review Document on Classification Systems for Eye Irritation/Corrosion in OECD Member Countries (1998) No. 15, Detailed Review Document on Classification Systems for Reproductive Toxicity in OECD Member Countries (1998) No. -
Generated by SRI International Pathway Tools Version 25.0, Authors S
An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000238675-HmpCyc: Bacillus smithii 7_3_47FAA Cellular Overview Connections between pathways are omitted for legibility. -
Liver Glucose Metabolism in Humans
Biosci. Rep. (2016) / 36 / art:e00416 / doi 10.1042/BSR20160385 Liver glucose metabolism in humans Mar´ıa M. Adeva-Andany*1, Noemi Perez-Felpete*,´ Carlos Fernandez-Fern´ andez*,´ Cristobal´ Donapetry-Garc´ıa* and Cristina Pazos-Garc´ıa* *Nephrology Division, Hospital General Juan Cardona, c/ Pardo Bazan´ s/n, 15406 Ferrol, Spain Synopsis Information about normal hepatic glucose metabolism may help to understand pathogenic mechanisms underlying obesity and diabetes mellitus. In addition, liver glucose metabolism is involved in glycosylation reactions and con- nected with fatty acid metabolism. The liver receives dietary carbohydrates directly from the intestine via the portal vein. Glucokinase phosphorylates glucose to glucose 6-phosphate inside the hepatocyte, ensuring that an adequate flow of glucose enters the cell to be metabolized. Glucose 6-phosphate may proceed to several metabolic path- ways. During the post-prandial period, most glucose 6-phosphate is used to synthesize glycogen via the formation of glucose 1-phosphate and UDP–glucose. Minor amounts of UDP–glucose are used to form UDP–glucuronate and UDP– galactose, which are donors of monosaccharide units used in glycosylation. A second pathway of glucose 6-phosphate metabolism is the formation of fructose 6-phosphate, which may either start the hexosamine pathway to produce UDP-N-acetylglucosamine or follow the glycolytic pathway to generate pyruvate and then acetyl-CoA. Acetyl-CoA may enter the tricarboxylic acid (TCA) cycle to be oxidized or may be exported to the cytosol to synthesize fatty acids, when excess glucose is present within the hepatocyte. Finally, glucose 6-phosphate may produce NADPH and ribose 5-phosphate through the pentose phosphate pathway. -
Datasheet: VMA00346 Product Details
Datasheet: VMA00346 Description: MOUSE ANTI AKR1C2 Specificity: AKR1C2 Format: Purified Product Type: PrecisionAb™ Monoclonal Isotype: IgG2a Quantity: 100 µl Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution Western Blotting 1/1000 PrecisionAb antibodies have been extensively validated for the western blot application. The antibody has been validated at the suggested dilution. Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Further optimization may be required dependant on sample type. Target Species Human Product Form Purified IgG - liquid Preparation Mouse monoclonal antibody prepared by affinity chromatography on Protein G Buffer Solution Phosphate buffered saline Preservative 0.09% Sodium Azide (NaN3) Stabilisers Immunogen Recombinant human AKR1C2 External Database Links UniProt: P52895 Related reagents Entrez Gene: 1646 AKR1C2 Related reagents Synonyms DDH2 Specificity Mouse anti Human AKR1C2 antibody recognizes the aldo-keto reductase family 1 member C2, also known as 3-alpha-HSD3, DD-2, DD/BABP, aldo-keto reductase family 1 member C2, Page 1 of 2 chlordecone reductase homolog HAKRD, dihydrodiol dehydrogenase 2, bile acid binding protein, 3-alpha hydroxysteroid dehydrogenase, type III, pseudo-chlordecone reductase, testicular 17,20-desmolase deficiency, trans-1,2-dihydrobenzene-1,2-diol dehydrogenase and type II dihydrodiol dehydrogenase. Encoded by the AKR1C2 gene, aldo-keto reductase family 1 member C2 is a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. -
(A) Sources, Including As Appropriate (Provide Summary Information
UNEP/POPS/POPRC.1/4 Format for submitting pursuant to Article 8 of the Stockholm Convention the information specified in Annex E of the Convention Introductory information Name of the submitting Party/observer NGO Observer: Pesticide Action Network on behalf of the International POPs Elimination Network (IPEN) Contact details Clare Butler Ellis PhD, M.Inst.P, C.Env. Pesticide Action Network UK [email protected] Joseph DiGangi, PhD Environmental Health Fund +001-312-566-0985 [email protected] Chemical name Chlordecone Chemical name: 1,1a,3,3a,4,5,5,5a,5b,6-decachloro-octahydro-1,3,4-metheno-2H- cyclobuta[cd]pentalen-2-one CAS=143-50-0 Common trade names: GC 1189, Kepone, Merex Synonyms: Chlordecone, Chlordecone Kepone, Decachloroketone, Decachlorooctahydro-1,3,4-metheno-2H-cyclobuta(cd)pentalen-2-one, Decachloropentacyclo(5.3.0.0.0.0 2,6,4,10,5,9)decane-3-one, Decachlorotetracyclodecanone decachlorooctahydro- , Date of submission 27 January 2006 (a) Sources, including as appropriate (provide summary information and relevant references) (i) Production data: Quantity 1 “Chlordecone is no longer produced commercially in the United States. Between 1951 and 1975, approximately 3.6 million pounds (1.6 million kg) of chlordecone were produced in the United States (Epstein 1978). During this period, Allied Chemical Annex E information on chlordecone 1 UNEP/POPS/POPRC.1/4 Company produced approximately 1.8 million pounds (816,500 kg) of chlordecone at plants in Claymont, Delaware; Marcus Hook, Pennsylvania and Hopewell, Virginia. In 1974, because of increasing demand for chlordecone and a need to use their facility in Hopewell, Virginia, for other purposes, Allied Chemical transferred its chlordecone manufacturing to Life Sciences Products Company (EPA 1978b). -
Research Article Effect of Chlordecone on The
NorCal Open Access Publications Journal of Aquatic Research and NORCAL Marine Sciences OPEN ACCESS PUBLICATION Volume 2; Issue 2 Asifa KP and Chitra KC Research Article ISSN 2639-4618 Effect of Chlordecone on the Reproductive Potential of the Cichlid Fish, Pseudetroplus Maculatus (Bloch, 1795) Asifa KP, Chitra KC* Endocrinology and Toxicology Laboratory, Department of Zoology, University of Calicut, Kerala, India. *Corresponding author: Chitra KC, Endocrinology and Toxicology Laboratory, Department of Zoology, University of Calicut, Kerala, India. Email: [email protected] Received Date: 16 March, 2019; Accepted Date: 03 May, 2019; Published Date: 17 May, 2019 Abstract Introduction The present study was undertaken to evaluate that chlordecone, During the past few decades, large number of environmental an organochlorine pesticide, possessing estrogenic properties contaminants such as, pesticides, pharmaceutical drugs, plas- are known to influence the reproductive potential of the cich- tic products, natural phytochemicals etc. has been continu- lid fish, Pseudetroplus maculatus. Chlordecone at two sublethal ously released into various compartments of both terrestrial concentrations, 3.5 and 7µg/L, were exposed to fish for 4, 7, 15 and aquatic ecosystems, which are known to disrupt the en- and 30 days in order to evaluate the level of vitellogenin, main- docrine system of animals, including humans. Such chemicals taining the control groups. Vitellogenin concentrations were are called endocrine-disrupting chemicals (EDCs), which can measured in both male and female fishes by using indirect end- interfere with biosynthesis, transport, action, metabolism and points, such as alkali-labile phosphoprotein (ALP), total pro- removal of various hormones in the body resulting in varia- tein and calcium concentrations in the blood plasma. -
In Silico Pharmacodynamics, Toxicity Profile and Biological Activities of the Saharan Medicinal Plant Limoniastrum Feei
Brazilian Journal of Pharmaceutical Sciences Article http://dx.doi.org/10.1590/s2175-97902017000300061 In silico pharmacodynamics, toxicity profile and biological activities of the Saharan medicinal plant Limoniastrum feei Ouahab Ammar* Department of Pharmacy, Faculty of Medical Sciences, University of Batna 2, Algeria In-silico study was performed to find the pharmacodynamics, toxicity profiles and biological activities of three phytochemicals isolated from Limoniastrum feei (Plumbagenaceae). Online pharmacokinetic tools were used to estimate the potential of Quercetin, kaempferol-3-O-β-D-glucopyranoside (astragalin) and quercitin-7-O-β-D-glucopyranoside as specific drugs. Then the prediction of potential targets of these compounds were investigated using PharmMapper. Auto-Dock 4.0 software was used to investigate the different interactions of these compounds with the targets predicted earlier. The permeability of quercetin s rule of five. Hematopoietic prostaglandin (PG) D׳ was found within the range stated by Lipinski synthase (HPGDS), farnesyl diphosphate synthetase (FPPS) and the deoxycytidine kinase (DCK) were potential targets for quercetin, astragalin and quercetin 7, respectively. Quercetin showed antiallergic and anti-inflammatory activity, while astragalin and quercetin 7 were predicted to have anticancer activities. The activity of Astragalin appeared to be mediated by FPPS inhibition. The inhibition of DCK was predicted as the anticancer mechanisms of quercetin 7. The compounds showed interesting interactions and satisfactory binding energies when docked into their targets. These compounds are proposed to have activities against a variety of human aliments such as allergy, tumors, muscular dystrophy, and diabetic cataracts. Keywords: Limoniastrum feei/pharmacokinetics. Limoniastrum feei/biological activity. Quercetin. Astragalin. Quercetin 7. Medicinal plants. Molecular docking. -
Open Matthew R Moreau Ph.D. Dissertation Finalfinal.Pdf
The Pennsylvania State University The Graduate School Department of Veterinary and Biomedical Sciences Pathobiology Program PATHOGENOMICS AND SOURCE DYNAMICS OF SALMONELLA ENTERICA SEROVAR ENTERITIDIS A Dissertation in Pathobiology by Matthew Raymond Moreau 2015 Matthew R. Moreau Submitted in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy May 2015 The Dissertation of Matthew R. Moreau was reviewed and approved* by the following: Subhashinie Kariyawasam Associate Professor, Veterinary and Biomedical Sciences Dissertation Adviser Co-Chair of Committee Bhushan M. Jayarao Professor, Veterinary and Biomedical Sciences Dissertation Adviser Co-Chair of Committee Mary J. Kennett Professor, Veterinary and Biomedical Sciences Vijay Kumar Assistant Professor, Department of Nutritional Sciences Anthony Schmitt Associate Professor, Veterinary and Biomedical Sciences Head of the Pathobiology Graduate Program *Signatures are on file in the Graduate School iii ABSTRACT Salmonella enterica serovar Enteritidis (SE) is one of the most frequent common causes of morbidity and mortality in humans due to consumption of contaminated eggs and egg products. The association between egg contamination and foodborne outbreaks of SE suggests egg derived SE might be more adept to cause human illness than SE from other sources. Therefore, there is a need to understand the molecular mechanisms underlying the ability of egg- derived SE to colonize the chicken intestinal and reproductive tracts and cause disease in the human host. To this end, the present study was carried out in three objectives. The first objective was to sequence two egg-derived SE isolates belonging to the PFGE type JEGX01.0004 to identify the genes that might be involved in SE colonization and/or pathogenesis. -
Transcriptomic and Proteomic Profiling Provides Insight Into
BASIC RESEARCH www.jasn.org Transcriptomic and Proteomic Profiling Provides Insight into Mesangial Cell Function in IgA Nephropathy † † ‡ Peidi Liu,* Emelie Lassén,* Viji Nair, Celine C. Berthier, Miyuki Suguro, Carina Sihlbom,§ † | † Matthias Kretzler, Christer Betsholtz, ¶ Börje Haraldsson,* Wenjun Ju, Kerstin Ebefors,* and Jenny Nyström* *Department of Physiology, Institute of Neuroscience and Physiology, §Proteomics Core Facility at University of Gothenburg, University of Gothenburg, Gothenburg, Sweden; †Division of Nephrology, Department of Internal Medicine and Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan; ‡Division of Molecular Medicine, Aichi Cancer Center Research Institute, Nagoya, Japan; |Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden; and ¶Integrated Cardio Metabolic Centre, Karolinska Institutet Novum, Huddinge, Sweden ABSTRACT IgA nephropathy (IgAN), the most common GN worldwide, is characterized by circulating galactose-deficient IgA (gd-IgA) that forms immune complexes. The immune complexes are deposited in the glomerular mesangium, leading to inflammation and loss of renal function, but the complete pathophysiology of the disease is not understood. Using an integrated global transcriptomic and proteomic profiling approach, we investigated the role of the mesangium in the onset and progression of IgAN. Global gene expression was investigated by microarray analysis of the glomerular compartment of renal biopsy specimens from patients with IgAN (n=19) and controls (n=22). Using curated glomerular cell type–specific genes from the published literature, we found differential expression of a much higher percentage of mesangial cell–positive standard genes than podocyte-positive standard genes in IgAN. Principal coordinate analysis of expression data revealed clear separation of patient and control samples on the basis of mesangial but not podocyte cell–positive standard genes. -
Download in English
UNITED NATIONS BC UNEP/CHW.12/5/Add.9 Distr.: General 10 July 2015 Original: English Conference of the Parties to the Basel Convention on the Control of Transboundary Movements of Hazardous Wastes and Their Disposal Twelfth meeting Geneva, 4–15 May 2015 Agenda item 4 (b) (i) Matters related to the implementation of the Convention: scientific and technical matters: technical guidelines Technical guidelines Technical guidelines on the environmentally sound management of wastes consisting of, containing or contaminated with the pesticides aldrin, alpha hexachlorocyclohexane, beta hexachlorocyclohexane, chlordane, chlordecone, dieldrin, endrin, heptachlor, hexachlorobenzene, lindane, mirex, pentachlorobenzene, perfluorooctane sulfonic acid, technical endosulfan and its related isomers or toxaphene or with hexachlorobenzene as an industrial chemical Note by the Secretariat At its twelfth meeting, the Conference of the Parties to the Basel Convention on the Control of Transboundary Movements of Hazardous Wastes and Their Disposal adopted, in decision BC-12/3 on technical guidelines on the environmentally sound management of wastes consisting of, containing or contaminated with persistent organic pollutants, the technical guidelines on the environmentally sound management of wastes consisting of, containing or contaminated with the pesticides aldrin, alpha hexachlorocyclohexane, beta hexachlorocyclohexane, chlordane, chlordecone, dieldrin, endrin, heptachlor, hexachlorobenzene, lindane, mirex, pentachlorobenzene, perfluorooctane sulfonic acid, technical endosulfan and its related isomers or toxaphene or with hexachlorobenzene as an industrial chemical, on the basis of the draft technical guidelines contained in document UNEP/CHW.12/INF/15. The technical guidelines referred to above were prepared by the Food and Agriculture Organization of the United Nations as lead organization for this work taking into account comments received from members of the small intersesssional working group on persistent organic pollutants wastes by 27 March 2015. -
Datasheet: VMA00334 Product Details
Datasheet: VMA00334 Description: MOUSE ANTI AKR1C1 Specificity: AKR1C1 Format: Purified Product Type: PrecisionAb™ Monoclonal Isotype: IgG1 Quantity: 100 µl Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution Western Blotting 1/1000 PrecisionAb antibodies have been extensively validated for the western blot application. The antibody has been validated at the suggested dilution. Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Further optimization may be required dependant on sample type. Target Species Human Product Form Purified IgG - liquid Preparation Mouse monoclonal antibody prepared by affinity chromatography on Protein G Buffer Solution Phosphate buffered saline Preservative 0.09% Sodium Azide (NaN3) Stabilisers Immunogen Recombinant human AKR1C1 External Database Links UniProt: Q04828 Related reagents Entrez Gene: 1645 AKR1C1 Related reagents Synonyms DDH, DDH1 Specificity Mouse anti Human AKR1C1 antibody detects the aldo-keto reductase family 1 member C1, also known as 20-alpha-hydroxysteroid dehydrogenase (20-alpha-HSD), chlordecone reductase Page 1 of 2 homolog HAKRC and high-affinity hepatic bile acid-binding protein (HBAB). Encoded by the AKR1C1 gene, aldo-keto reductase family 1 member C1 is a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors.