Anticholinesterase Pesticides: Metabolism, Neurotoxicity, by Tetsuo Satoh, Ramesh C. Gupta PDF

By Tetsuo Satoh, Ramesh C. Gupta

ISBN-10: 0470410302

ISBN-13: 9780470410301

ISBN-10: 0470640502

ISBN-13: 9780470640500

This publication deals an immense reference resource in regards to the most typical sessions of insecticides for researchers engaged within the sector of neurotoxicology, metabolism, and epidemiology. The ebook offers information about thorough characterization of aim and non-target enzymes and proteins interested in toxicity and metabolism; and epidemiology of poisonings and fatalities in humans from brief- and lengthy- time period exposures to those insecticides in numerous occupational settings on somebody state foundation in addition to on an international foundation. The early part of the ebook offers with metabolism, mechanisms and biomonitoring of anticholinesterase insecticides, whereas the later half bargains with epidemiological experiences, regulatory concerns, and healing intervention.Content:
Chapter 1 Acetylcholinesterase and Acetylcholine Receptors: mind nearby Heterogeneity (pages 1–18): Haruo Kobayashi, Tadahiko Suzuki, Fumiaki Akahori and Tetsuo Satoh
Chapter 2 Genomic Implications of Anticholinesterase Sensitivities (pages 19–24): Jonathan E. Cohen, Alon Friedman, Gabrial Zimmermann and Hermona Soreq
Chapter three Butyrylcholinesterase: assessment, constitution, and serve as (pages 25–41): Oksana Lockridge, Ellen G. Duysen and Patrick Masson
Chapter four Carboxylesterases: assessment, constitution, functionality, and Polymorphism (pages 43–56): Masakiyo Hosokawa and Tetsuo Satoh
Chapter five Carboxylesterases within the Metabolism and Toxicity of insecticides (pages 57–75): Colin J. Jackson, John G. Oakeshott, Juan C. Sanchez?Hernandez and Craig E. Wheelock
Chapter 6 The Metabolic Activation and Detoxication of Anticholinesterase pesticides (pages 77–84): Janice E. Chambers, Edward C. Meek and Matthew Ross
Chapter 7 Paraoxonase 1: constitution, functionality, and Polymorphisms (pages 85–95): Lucio G. Costa and Clement E. Furlong
Chapter eight Long?Term Neurotoxicological results of Anticholinesterases after both Acute or persistent publicity (pages 97–108): Angelo Moretto, Manuela Tiramani and Claudio Colosio
Chapter nine Molecular Toxicology of Neuropathy goal Esterase (pages 109–120): Yi?Jun Wu and Ping?An Chang
Chapter 10 Detoxication of Anticholinesterase insecticides (pages 121–132): Miguel A. Sogorb and Eugenio Vilanova
Chapter eleven Involvement of Oxidative tension in Anticholinesterase Pesticide Toxicity (pages 133–147): Dejan Milatovic, Michael Aschner, Ramesh C. Gupta, Snjezana Zaja?Milatovic and Gregory Barnes
Chapter 12 primary Mechanisms of Seizures and Lethality Following Anticholinesterase Pesticide publicity (pages 149–164): Andrzej Dekundy and Rafal M. Kaminski
Chapter thirteen Apoptosis prompted by means of Anticholinesterase insecticides (pages 165–174): Qing Li
Chapter 14 Gene Expression (pages 175–188): Shirin Pournourmohammadi and Mohammad Abdollahi
Chapter 15 Organophosphates as Endocrine Disruptors (pages 189–202): Shigeyuki Kitamura, Kazumi Sugihara, Nariaki Fujimoto and Takeshi Yamazaki
Chapter sixteen Developmental Neurotoxicity of Anticholinesterase insecticides (pages 203–223): John Flaskos and Magdalini Sachana
Chapter 17 Toxicity of Anticholinesterase insecticides in Neonates and kids (pages 225–236): Diane Rohlman and Linda McCauley
Chapter 18 Neurotoxicity of Organophosphates and Carbamates (pages 237–265): Kiran Dip Gill, Govinder vegetation, Vidhu Pachauri and Swaran J. S. Flora
Chapter 19 Biomonitoring of insecticides: Pharmacokinetics of Organophosphorus and Carbamate pesticides (pages 267–287): Charles Timchalk
Chapter 20 Novel Biomarkers of Organophosphate publicity (pages 289–302): Tetsuo Satoh, Salmaan H. Inayat?Hussain, Michihiro Kamijima and Jun Ueyama
Chapter 21 Biomarkers of Carcinogenesis in terms of Pesticide Poisoning (pages 303–313): Manashi Bagchi, Shirley Zafra?Stone, Francis C. Lau and Debasis Bagchi
Chapter 22 Anticholinesterase insecticides Interactions (pages 315–327): Ramesh C. Gupta and Dejan Milatovic
Chapter 23 interplay of Anticholinesterase insecticides with Metals (pages 329–339): Jitendra ok. Malik, Avinash G. Telang, Ashok Kumar and Ramesh C. Gupta
Chapter 24 Epidemiological experiences of Anticholinesterase Pesticide Poisoning: worldwide influence (pages 341–355): Claudio Colosio, Francesca Vellere and Angelo Moretto
Chapter 25 Epidemiological stories of Anticholinesterase Pesticide Poisoning in Chile (pages 357–363): Floria Pancetti, Muriel Ramirez and Mauricio Castillo
Chapter 26 Epidemiological reports of Anticholinesterase Pesticide Poisoning in China (pages 365–377): Yueming Jiang
Chapter 27 Epidemiological experiences of Anticholinesterase Pesticide Poisoning in Egypt (pages 379–401): Sameeh A. Mansour
Chapter 28 Epidemiological reviews of Anticholinesterase Pesticide Poisoning in Greece (pages 403–416): M. Stefanidou, S. Athanaselis, C. Spiliopoulou and C. Maravelias
Chapter 29 Epidemiological experiences of Anticholinesterase Pesticide Poisoning in India (pages 417–431): P. ok. Gupta
Chapter 30 Poisoning with Anticholinesterase pesticides in Iran (pages 433–446): Mohammad Abdollahi
Chapter 31 Epidemiological experiences of Anticholinesterase Pesticide Poisoning in Israel (pages 447–456): Yoram Finkelstein, Elihu D. Richiter and Michael Aschner
Chapter 32 Epidemiological reports of Anticholinesterase Pesticide Poisoning in Japan (pages 457–462): Takemi Yoshida and Yumiko Kuroki
Chapter 33 Epidemiological stories of Anticholinesterase Pesticide Poisoning in Korea (pages 463–470): Hyung?Keun Roh, Bum Jin Oh, Mi?Jin Lee and Joo?Hyun Suh
Chapter 34 Epidemiological experiences of Anticholinesterase Pesticide Poisoning in Mexico (pages 471–480): Betzabet Quintanilla?Vega, Norma Perez?Herrera and Elizabeth Rojas?Garcia
Chapter 35 Epidemiological experiences of Anticholinesterase Pesticide Poisoning in Serbia (pages 481–494): Milan Jokanovic, Biljana Antonijevic and Slavica Vuccinic
Chapter 36 Epidemiological reports of Anticholinesterase Pesticide Poisoning in Spain (pages 495–508): Antonio F. Hernandez, Tesifon Parron, Jose L. Serrano and Porfirio Marin
Chapter 37 Epidemiological experiences of Anticholinesterase Pesticide Poisoning in Taiwan (pages 509–521): Tzeng Jih Lin, Dong Zong Hung, Jin Lian Tsai, Sheng Chuan Hu and Jou?Fang Deng
Chapter 38 Epidemiological reports of Anticholinesterase Pesticide Poisoning in Thailand (pages 523–532): Winai Wananukul
Chapter 39 Epidemiological experiences of Anticholinesterase Pesticide Poisoning in Turkey (pages 533–540): Ismet Cok
Chapter forty Epidemiology of Anticholinesterase Pesticide Poisoning within the usa (pages 541–566): Anna M. Fan
Chapter forty-one Regulatory elements of Anticholinesterase insecticides (pages 567–579): Kai Savolainen
Chapter forty two scientific remedy of Poisoning with Organophosphates and Carbamates (pages 581–597): Milan Jokanovic

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2007) Donepezil- or rivastigmineinduced acetylcholinesterase inactivation is not modulated by neramexane in rat brain. Drug Develop Res 68: 253–260. L. (1989) Prevention and antagonism of acute carbofuran intoxication by memantine and atropine. J Toxicol Environm Health 28: 111 –122. L. (1990) Methyl parathion acute toxicity: prophylaxis and therapy with memantine and atropine. Arch Intl Pharmacol Ther 305: 208 –221. L. (1991a) Novel effects of memantine in antagonizing acute aldicarb toxicity: mechanistic and applied considerations.

Toxicol Appl Pharmacol 148: 46– 49. , and Narahashi, T. (1997) Direct actions of anticholinesterases on the neuronal nicotinic acetylcholine receptor channels. Brain Res 769: 211–218. , and Katsura, I. (2000) Identification and characterization of the high-affinity choline transporter. Nat Neurosci 3: 120 –125. , and Ohta, M. (2003) The chemical disaster response system in Japan. Prehosp Disaster Med 18: 189 –192. Padilla, S. (1995) Regulatory and research issues related to cholinesterase inhibition.

1998). Another disadvanatage is that purified acetylcholinesterase sticks to plastic and glass resulting in large losses unless the protein is highly concentrated or albumin is added. Human butyrylcholinesterase fulfills all the criteria for an effective scavenger. 1. , 1993). 2. Outdated human plasma contains soluble butyrylcholinesterase at a concentration of 5 mg/L. 3. The sugarcoated surface of the butyrylcholinesterase tetramer protects it from proteases. , 2006). 4. , 1988; Stovner and Stadskleiv, 1976).

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Anticholinesterase Pesticides: Metabolism, Neurotoxicity, and Epidemiology by Tetsuo Satoh, Ramesh C. Gupta

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