Application of Complementary and Alternative Medicine on Neurodegenerative Disorders: Current Status and Future Prospects
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Oilseeds As Crop Biofactories for Industrial Raw Materials
AOF Forum, 2004 Grain & chemical industry drivers Oilseeds as crop ! Global competition increasing biofactories for ! Downward pressure on price and market share industrial raw ! Need to diversify away from commodities ! Need to capture maximum value materials Allan Green ! Desirable to replace petroleum with renewable CSIRO Plant Industry sources of industrial raw materials ! Need for increased biodegradability of C O C O C O industrial products C C C C C C O C O C O C Opportunities for industrial use Seed oils are triglycerides ! Current Australian non-food use of vegetable oils ! Seed oils are comprised almost entirely of is about 12,000 tonnes (~3% of total oil usage) triglycerides composed of fatty acids ! Long-term opportunities exist for:- ! Oils are deposited in the seed in oilbodies - direct use in lubricants and inks - bio-diesel fuels (e.g. rapeseed ME) - specialty oleochemicals - pure fatty acids (e.g. oleic acid) - fatty acid derivatives (e.g. erucamide) - alkyl units for polymers (e.g. nylon) - biodegradable plastics - pharmaceutical proteins Fatty acids are like petrochemicals Oil composition can be changed ! Fatty acids are simply hydrocarbon chains ! Seed oils are needed only for energy of various lengths with a carboxyl group storage and release during germination (~COOH) at one end (i.e. no structural role) ! Fatty acids can have bond types or functional groups that allow them to be ! Fatty acid composition can therefore be cleaved or derivatised by chemical dramatically modified, provided that new processing fatty -
Role of Epoxide Hydrolases in Lipid Metabolism
Biochimie 95 (2013) 91e95 Contents lists available at SciVerse ScienceDirect Biochimie journal homepage: www.elsevier.com/locate/biochi Mini-review Role of epoxide hydrolases in lipid metabolism Christophe Morisseau* Department of Entomology and U.C.D. Comprehensive Cancer Center, One Shields Avenue, University of California, Davis, CA 95616, USA article info abstract Article history: Epoxide hydrolases (EH), enzymes present in all living organisms, transform epoxide-containing lipids to Received 29 March 2012 1,2-diols by the addition of a molecule of water. Many of these oxygenated lipid substrates have potent Accepted 8 June 2012 biological activities: host defense, control of development, regulation of blood pressure, inflammation, Available online 18 June 2012 and pain. In general, the bioactivity of these natural epoxides is significantly reduced upon metabolism to diols. Thus, through the regulation of the titer of lipid epoxides, EHs have important and diverse bio- Keywords: logical roles with profound effects on the physiological state of the host organism. This review will Epoxide hydrolase discuss the biological activity of key lipid epoxides in mammals. In addition, the use of EH specific Epoxy-fatty acids Cholesterol epoxide inhibitors will be highlighted as possible therapeutic disease interventions. Ó Juvenile hormone 2012 Elsevier Masson SAS. All rights reserved. 1. Introduction hydrolyzed by a water molecule [8]. Based on this mechanism, transition-state inhibitors of EHs have been designed (Fig. 1B). Epoxides are three atom cyclic ethers formed by the oxidation of These ureas and amides are tight-binding competitive inhibitors olefins. Because of their highly polarized oxygen-carbon bonds and with low nanomolar dissociation constants (KI) [9] [10]. -
Appendix 1 – Protocol for Preventing Or Reversing Chronic Disease The
Appendix 1 – Protocol for Preventing or Reversing Chronic Disease The first author has developed a protocol over the past decade for preventing or reversing chronic disease based on the following systemic medical principle: “at the present time, removal of cause is a necessary, but not necessarily sufficient, condition for restorative treatment to be effective”[1]. The protocol methodology refines the age-old principles of both reducing harm in addition to providing treatment, and allows better identification of factors that contribute to the disease process (so that they may be eliminated if possible). These contributing factors are expansive and may include a combination of Lifestyle choices (diet, exercise, smoking), iatrogenic and biotoxin exposures, environmental/occupational exposures, and psychosocial stressors. This strategy exploits the existing literature to identify patterns of biologic response using biomarkers from various modalities of diagnostic testing to capture a much broader list of potential contributing factors. Existing inflammatory bowel diseases (IBD) Biomarker Identification to Remove Contributing Factors and Implement Treatment The initial protocol steps are diagnostic. The main output of these diagnostics will be identification of the biomarker levels and symptoms that reflect abnormalities, and the directions of change required to eliminate these abnormalities. In the present study, hundreds of general and specific biomarkers and symptoms were identified from the core IBD literature. The highest frequency (based on numbers of record appearances) biomarkers and symptoms were extracted, and are listed in Table 1 (highest frequency items first, reading down each column before proceeding to the next column). They are not necessarily consensus biomarkers. They are biomarkers whose values were altered by a treatment or contributing factor, and reported in the core IBD literature. -
Review Article New Insight Into Adiponectin Role in Obesity and Obesity-Related Diseases
Hindawi Publishing Corporation BioMed Research International Volume 2014, Article ID 658913, 14 pages http://dx.doi.org/10.1155/2014/658913 Review Article New Insight into Adiponectin Role in Obesity and Obesity-Related Diseases Ersilia Nigro,1 Olga Scudiero,1,2 Maria Ludovica Monaco,1 Alessia Palmieri,1 Gennaro Mazzarella,3 Ciro Costagliola,4 Andrea Bianco,5 and Aurora Daniele1,6 1 CEINGE-Biotecnologie Avanzate Scarl, Via Salvatore 486, 80145 Napoli, Italy 2 Dipartimento di Medicina Molecolare e Biotecnologie Mediche, UniversitadegliStudidiNapoliFedericoII,` Via De Amicis 95, 80131 Napoli, Italy 3 Dipartimento di Scienze Cardio-Toraciche e Respiratorie, Seconda Universita` degli Studi di Napoli, Via Bianchi 1, 80131 Napoli, Italy 4 Cattedra di Malattie dell’Apparato Visivo, Dipartimento di Medicina e Scienze della Salute, UniversitadelMolise,` ViaDeSanctis1,86100Campobasso,Italy 5 Cattedra di Malattie dell’Apparato Respiratorio, Dipartimento di Medicina e Scienze della Salute, UniversitadelMolise,` ViaDeSanctis1,86100Campobasso,Italy 6 Dipartimento di Scienze e Tecnologie Ambientali Biologiche Farmaceutiche, Seconda UniversitadegliStudidiNapoli,` Via Vivaldi 42, 81100 Caserta, Italy Correspondence should be addressed to Aurora Daniele; [email protected] Received 2 April 2014; Accepted 12 June 2014; Published 7 July 2014 Academic Editor: Beverly Muhlhausler Copyright © 2014 Ersilia Nigro et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, -
Potential Herb–Drug Interactions in the Management of Age-Related Cognitive Dysfunction
pharmaceutics Review Potential Herb–Drug Interactions in the Management of Age-Related Cognitive Dysfunction Maria D. Auxtero 1, Susana Chalante 1,Mário R. Abade 1 , Rui Jorge 1,2,3 and Ana I. Fernandes 1,* 1 CiiEM, Interdisciplinary Research Centre Egas Moniz, Instituto Universitário Egas Moniz, Quinta da Granja, Monte de Caparica, 2829-511 Caparica, Portugal; [email protected] (M.D.A.); [email protected] (S.C.); [email protected] (M.R.A.); [email protected] (R.J.) 2 Polytechnic Institute of Santarém, School of Agriculture, Quinta do Galinheiro, 2001-904 Santarém, Portugal 3 CIEQV, Life Quality Research Centre, IPSantarém/IPLeiria, Avenida Dr. Mário Soares, 110, 2040-413 Rio Maior, Portugal * Correspondence: [email protected]; Tel.: +35-12-1294-6823 Abstract: Late-life mild cognitive impairment and dementia represent a significant burden on health- care systems and a unique challenge to medicine due to the currently limited treatment options. Plant phytochemicals have been considered in alternative, or complementary, prevention and treat- ment strategies. Herbals are consumed as such, or as food supplements, whose consumption has recently increased. However, these products are not exempt from adverse effects and pharmaco- logical interactions, presenting a special risk in aged, polymedicated individuals. Understanding pharmacokinetic and pharmacodynamic interactions is warranted to avoid undesirable adverse drug reactions, which may result in unwanted side-effects or therapeutic failure. The present study reviews the potential interactions between selected bioactive compounds (170) used by seniors for cognitive enhancement and representative drugs of 10 pharmacotherapeutic classes commonly prescribed to the middle-aged adults, often multimorbid and polymedicated, to anticipate and prevent risks arising from their co-administration. -
Natural Product Standards (1)
Natural Product Standards (1) Group Name Product Name CAS No Purity Storage Cat. No. PKG Size List Price ($) Soy Bean Daidzein 486-66-8 98% (HPLC) R NH010102 10 mg 58.00 NH010103 100 mg 344.00 Glycitein 40957-83-3 98% (HPLC) R NH010202 10 mg 156.00 NH010203 100 mg 1,130.00 Genistein 446-72-0 98% (HPLC) R NH010302 10 mg 58.00 NH010303 100 mg 219.00 Daidzin 552-66-9 98% (HPLC) R NH012102 10 mg 138.00 NH012103 100 mg 1,130.00 Glycitin 40246-10-4 98% (HPLC) R NH012202 10 mg 156.00 NH012203 100 mg 1,130.00 Genistin 529-59-9 98% (HPLC) R NH012302 10 mg 156.00 NH012303 100 mg 1,130.00 6" -O-Acetyldaidzin 71385-83-6 98% (HPLC) F NH013101 1 mg 173.00 6" -O-Acetylglycitin 134859-96-4 98% (HPLC) F NH013201 1 mg 173.00 6" -O-Acetylgenistin 73566-30-0 98% (HPLC) F NH013301 1 mg 173.00 6" -O-Malonyldaidzin 124590-31-4 98% (HPLC) F NH014101 1 mg 173.00 6" -O-Malonylglycitin 137705-39-6 98% (HPLC) F NH014201 1 mg 173.00 6" -O-Malonylgenistin 51011-05-3 98% (HPLC) F NH014301 1 mg 173.00 Isoflavone Aglycon Mixture B Total 95% (HPLC) RT NH015204 1 g 344.00 Isoflavone Glucoside Mixture A Total 95% (HPLC) RT NH016104 1 g 346.00 8-Hydroxydaidzein 75187-63-2 98% (HPLC) R NH017102 5 mg 415.00 8-Hydroxyglycitein 113762-90-6 98% (HPLC) R NH017202 5 mg 415.00 8-Hydroxygenistein 13539-27-0 98% (HPLC) R NH017302 5 mg 415.00 Green Tea (-) -Epicatechin 〔(-) -EC 〕 490-46-0 99% (HPLC) R NH020102 10 mg 92.00 NH020103 100 mg 507.00 (-) -Epigallocatechin 〔(-) -EGC 〕 970-74-1 99% (HPLC) R NH020202 10 mg 138.00 NH020203 100 mg 761.00 (-) -Epicatechin gallate 〔(-) -ECg 〕 1257-08-5 -
Metabolic Enzyme/Protease
Inhibitors, Agonists, Screening Libraries www.MedChemExpress.com Metabolic Enzyme/Protease Metabolic pathways are enzyme-mediated biochemical reactions that lead to biosynthesis (anabolism) or breakdown (catabolism) of natural product small molecules within a cell or tissue. In each pathway, enzymes catalyze the conversion of substrates into structurally similar products. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation. Metabolism maintains the living state of the cells and the organism. Proteases are used throughout an organism for various metabolic processes. Proteases control a great variety of physiological processes that are critical for life, including the immune response, cell cycle, cell death, wound healing, food digestion, and protein and organelle recycling. On the basis of the type of the key amino acid in the active site of the protease and the mechanism of peptide bond cleavage, proteases can be classified into six groups: cysteine, serine, threonine, glutamic acid, aspartate proteases, as well as matrix metalloproteases. Proteases can not only activate proteins such as cytokines, or inactivate them such as numerous repair proteins during apoptosis, but also expose cryptic sites, such as occurs with β-secretase during amyloid precursor protein processing, shed various transmembrane proteins such as occurs with metalloproteases and cysteine proteases, or convert receptor agonists into antagonists and vice versa such as chemokine conversions carried out by metalloproteases, dipeptidyl peptidase IV and some cathepsins. In addition to the catalytic domains, a great number of proteases contain numerous additional domains or modules that substantially increase the complexity of their functions. -
Download Product Insert (PDF)
PRODUCT INFORMATION (±)12(13)-EpOME Item No. 52450 Formal Name: (±)12(13)epoxy-9Z-octadecenoic acid Synonyms: (±)2,13-EODE, Isoleukotoxin, COOH (±)-Vernolic Acid MF: C18H32O3 FW: 296.5 Chemical Purity: ≥98% O Supplied as: A solution in methyl acetate NOTE: Relative stereochemistry shown in chemical structure Storage: -20°C Stability: ≥1 year Information represents the product specifications. Batch specific analytical results are provided on each certificate of analysis. Laboratory Procedures (±)12(13)-EpOME is supplied as a solution in methyl acetate. To change the solvent, simply evaporate the methyl acetate under a gentle stream of nitrogen and immediately add the solvent of choice. Solvents such as ethanol, DMSO, and dimethyl formamide purged with an inert gas can be used. The solubility of (±)12(13)-EpOME in these solvents is approximately 50 mg/ml. Further dilutions of the stock solution into aqueous buffers or isotonic saline should be made prior to performing biological experiments. Ensure that the residual amount of organic solvent is insignificant, since organic solvents may have physiological effects at low concentrations. If an organic solvent-free solution of (±)12(13)-EpOME is needed, it can be prepared by evaporating the methyl acetate and directly dissolving the neat oil in aqueous buffers. The solubility of (±)12(13)-EpOME in PBS (pH 7.2) is approximately 1 mg/ml. We do not recommend storing the aqueous solution for more than one day. Description (±)12(13)-EpOME is the 12,13-cis epoxide form of linoleic acid (Item Nos. 90150 | 90150.1 | 21909).1,2 It is formed primarily via linoleic acid metabolism by the cytochrome P450 (CYP) isoforms CYP2J2, CYP2C8, and CYP2C9, however, CYP1A1 can contribute to (±)12(13)-EpOME production when pharmacologically induced.2 (±)12(13)-EpOME (500 µM) induces mitochondrial dysfunction and cell death in renal proximal tubule epithelial cells. -
Epomes Act As Immune Suppressors in a Lepidopteran Insect
www.nature.com/scientificreports OPEN EpOMEs act as immune suppressors in a lepidopteran insect, Spodoptera exigua Mohammad Vatanparast1, Shabbir Ahmed1, Dong‑Hee Lee2, Sung Hee Hwang3, Bruce Hammock3 & Yonggyun Kim1* Epoxyoctadecamonoenoic acids (EpOMEs) are epoxide derivatives of linoleic acid (9,12‑octadecadienoic acid) and include 9,10‑EpOME and 12,13‑EpOME. They are synthesized by cytochrome P450 monooxygenases (CYPs) and degraded by soluble epoxide hydrolase (sEH). Although EpOMEs are well known to play crucial roles in mediating various physiological processes in mammals, their role is not well understood in insects. This study chemically identifed their presence in insect tissues: 941.8 pg/g of 9,10‑EpOME and 2,198.3 pg/g of 12,13‑EpOME in fat body of a lepidopteran insect, Spodoptera exigua. Injection of 9,10‑EpOME or 12,13‑EpOME into larvae suppressed the cellular immune responses induced by bacterial challenge. EpOME treatment also suppressed the expression of antimicrobial peptide (AMP) genes. Among 139 S. exigua CYPs, an ortholog (SE51385) to human EpOME synthase was predicted and its expression was highly inducible upon bacterial challenge. RNA interference (RNAi) of SE51385 prevented down‑regulation of immune responses at a late stage (> 24 h) following bacterial challenge. A soluble epoxide hydrolase (Se-sEH) of S. exigua was predicted and showed specifc expression in all development stages and in diferent larval tissues. Furthermore, its expression levels were highly enhanced by bacterial challenge in diferent tissues. RNAi reduction of Se‑sEH interfered with hemocyte‑spreading behavior, nodule formation, and AMP expression. To support the immune association of EpOMEs, urea‑based sEH inhibitors were screened to assess their inhibitory activities against cellular and humoral immune responses of S. -
RECENT ADVANCES in BIOTECHNOLOGY & NANOBIOTECHNOLOGY (Int-BIONANO-2016) February 10-12, 2016
INTERNATIONAL CONFERENCE ON RECENT ADVANCES IN BIOTECHNOLOGY & NANOBIOTECHNOLOGY (Int-BIONANO-2016) February 10-12, 2016 CONFERENCE PROCEEDINGS (ISSN: 0975-6299) AMITY INSTITUTE OF BIOTECHNOLOGY AMITY UNIVERSITY MADHYA PRADESH, GWALIOR 1 International Journal of Pharma & Bio Sciences Spl Ed. (Int-BIONANO-2016) ORGANISING COMMITTEE CHIEF PATRON Dr. Aseem Chauhan Additional President, RBEF (An Umbrella foundation of all Amity Institutes) Chancellor, Amity University Rajasthan, Jaipur PATRON Prof.(Dr.) Sunil Saran Chancellor, Amity University Madhya Pradesh Gwalior CHAIRPERSON Lt. Gen. V. K. Sharma AVSM (Retd.), Vice Chancellor, Amity University Madhya Pradesh, Gwalior ORGANISING SECRETARY Prof.(Dr.) Rajesh Singh Tomar Director, Amity Institute of Biotechnology Dean (Academics), Amity University Madhya Pradesh, Gwalior JOINT SECRETARIES Dr. Raghvendra Kumar Mishra Coordinator & Assistant Professor-AIB Amity University Madhya Pradesh, Gwalior Dr. Vikas Shrivastava Assistant Professor-AIB Amity University Madhya Pradesh, Gwalior Dr. Shuchi Kaushik Assistant Professor-AIB Amity University Madhya Pradesh, Gwalior Dr. Anurag Jyoti Assistant Professor-AIB Amity University Madhya Pradesh, Gwalior 2 International Journal of Pharma & Bio Sciences Spl Ed. (Int-BIONANO-2016) INTERNATIONAL ADVISORY COMMITTEE Prof.(Dr.) Sushil Kumar INSA, Honorary Scientist, India Dr. W. Selvamurthy Director General - Amity Directorate of Science & Innovation, Amity University, NOIDA, India Prof.(Dr.)P.B.S. Bhadoria Agricultural & Food Engineering Chairman, Commercial Establishment and Licensing Committee IIT Kharagpur, India Prof.(Dr.) Anastasia Kanellou Technical Educational Institute, Athens, Greece Dr. Wolfgang Fritzsche Head, Department of Nanobiophotonics Leibniz Institute of Photonic Technology, Jena, Germany Dr. Gitanjali Yadav Scientist, NIPGR, New Delhi 3 International Journal of Pharma & Bio Sciences Spl Ed. (Int-BIONANO-2016) Editorial Board of Proceedings of Int-BIONANO-2016 Editor-in-Chief Prof. -
Increasing Renewable Oil Content and Utility
University of Kentucky UKnowledge Theses and Dissertations--Plant and Soil Sciences Plant and Soil Sciences 2017 INCREASING RENEWABLE OIL CONTENT AND UTILITY William Richard Serson University of Kentucky, [email protected] Digital Object Identifier: https://doi.org/10.13023/ETD.2017.243 Right click to open a feedback form in a new tab to let us know how this document benefits ou.y Recommended Citation Serson, William Richard, "INCREASING RENEWABLE OIL CONTENT AND UTILITY" (2017). Theses and Dissertations--Plant and Soil Sciences. 89. https://uknowledge.uky.edu/pss_etds/89 This Doctoral Dissertation is brought to you for free and open access by the Plant and Soil Sciences at UKnowledge. It has been accepted for inclusion in Theses and Dissertations--Plant and Soil Sciences by an authorized administrator of UKnowledge. For more information, please contact [email protected]. STUDENT AGREEMENT: I represent that my thesis or dissertation and abstract are my original work. Proper attribution has been given to all outside sources. I understand that I am solely responsible for obtaining any needed copyright permissions. I have obtained needed written permission statement(s) from the owner(s) of each third-party copyrighted matter to be included in my work, allowing electronic distribution (if such use is not permitted by the fair use doctrine) which will be submitted to UKnowledge as Additional File. I hereby grant to The University of Kentucky and its agents the irrevocable, non-exclusive, and royalty-free license to archive and make accessible my work in whole or in part in all forms of media, now or hereafter known. -
Download Product Insert (PDF)
PRODUCT INFORMATION (±)12(13)-EpOME-d4 Item No. 10009996 Formal Name: (±)12(13)epoxy-9Z-octadecenoic-9,10,12,13-d4 acid Synonyms: (±)12,13-EODE-d4, Isoleukotoxin-d4, (±)-Vernolic Acid-d4 D D MF: C18H28D4O3 COOH FW: 300.5 Chemical Purity: ≥98% Deuterium DDO Incorporation: ≥99% deuterated forms (d1-d4); ≤1% d0 Supplied as: A solution in methyl acetate NOTE: Relative stereochemistry shown in chemical structure Storage: -20°C Stability: ≥1 year Information represents the product specifications. Batch specific analytical results are provided on each certificate of analysis. Laboratory Procedures (±)12(13)-EpOME-d4 contains four deuterium atoms at the 9, 10, 12, and 13 positions. It is intended for use as an internal standard for the quantification of (±)12(13)-EpOME (Item No. 52450) by GC- or LC-MS. The accuracy of the sample weight in this vial is between 5% over and 2% under the amount shown on the vial. If better precision is required, the deuterated standard should be quantitated against a more precisely weighed unlabeled standard by constructing a standard curve of peak intensity ratios (deuterated versus unlabeled). (±)12(13)-EpOME-d4 is supplied as a solution in methyl acetate. To change the solvent, simply evaporate the methyl acetate under a gentle stream of nitrogen and immediately add the solvent of choice. Solvents such as ethanol, DMSO, and dimethyl formamide purged with an inert gas can be used. The solubility of (±)12(13)-EpOME-d4 in is these solvents is approximately 50 mg/ml. Description (±)12(13)-EpOME-d4 is intended for use as an internal standard for the quantification of 12(13)- EpOME by GC- or LC-MS.