Оксидантный статус и ростовые процессы в нервной ткани новорожденных крыс после пренатальной свинцовой интоксикации и фармакологическая коррекция возникающих нарушений
Диссертация
Актуальность проблемы. Пагубное воздействие свинца на организм человека в настоящее время является глобальной экологической проблемой, которой уделяется большое внимание, в том числе на государственном уровне. Свинец является тяжёлым металлом и относится к токсикантам I класса опасности. Токсическое действие соединений свинца является причиной развития патологических состояний всех без исключения… Читать ещё >
Список литературы
- Берберова H.T. Из жизни свободных радикалов // Соросовский образовательный журнал. 2007. Т. 6. №. 5. С. 39−44.
- Большаков А.П. Глутаматная нейротоксичность: нарушение ионного гомеостаза, дисфункция митохондрий, изменение активности клеточных систем // Нейрохимия. 2008. Т. 25. № 3. С. 157−169.
- Викторов И.В., Хаспеков Л. Г., Шашкова H.A. Руководство по культивированию нервной ткани: методы, техника, проблемы. М.: Наука. 1986. С. 141−166.
- Владимиров Ю.А. Свободные радикалы в биологических системах // Соросовский образовательный журнал. 2000. Т. 6. № 12. С. 13−19.
- Владимиров Ю.А., Арчаков А. И. Перекисное окисление липидов в биологических мембранах. М.: Наука. 1972. 365 с.
- Габибов М.М., Мусаев Б. С., Мурадова Г. Р. Влияние солей кадмия и свинца на некоторые показатели липидного обмена органов сеголетков карпа (Cyprinus carpio L.) // Известия ВУЗов. Северо-Кавказский регион. Естественные науки. 2007. № 5. С.45−48.
- Гаврилов В.Б., Гаврилова А. Р., Мажуль Л. М. Анализ методов определения продуктов перекисного окисления липидов в сыворотке крови по тесту с тиобарбитуровой кислотой // Вопросы медицинской химии. 1987. № 1. С. 118−122.
- Гаврилова К.И. Биохимические изменения в головном мозгу при экспериментальной свинцовой интоксикации // Автореф. дис. канд. биол. наук. Молотов. 1956. 17 с.
- Гнидой И.М. и Дихлярук И.И. Иммунный статус у детей при действии свинца в низких дозах // Украшский медичний часопис. 2002. № 6. С. 125 127.
- Ю.Зербино Д. Д., Соломенчук Т. Н., Поспишиль Ю. А. Свинец этиологический фактор поражения сосудов: основные доказательства // Архив патологии. 1997. Т. 59. № 1.С. 9−12.
- Зозуля Ю.А., Барабой В. А., Сутковой Д. А. Свободнорадикальное окисление и антиоксидантная защита при патологии головного мозга М.: Знание-М. 2000. 344 с.
- Кения М.В., Лукаш А. И., Гуськов E.H. Роль низкомолекуляных антиоксидантов при окислительном стрессе // Успехи соврем, биологии. — 1993. Т. 113. №.4. С. 456−469.
- Керимов Б.Ф. Глутатион дефицитное состояние нервной ткани голодавших животных интенсифицирует пероксидное окисление липидов и окисление белковых SH-групп // Укр. 6ioxiM. журн. 2004. Т. 76. №. 1. С. 108−113.
- Козлова М.В., Шурыгин, А .Я., Сидоренко И. П., Каленчук В. У. Влияние препарата бализ-2 на рост культуры симпатических ганглиев крыс различных линий // Нейрофизиология. 1988. Т. 20. №. 4. С. 550−557.
- Колесниченко Л.С., Кулинский В. И. Глутатионтрансферазы // Успехи соврем, биологии. 1989. Т. 107. №. 2. С. 179−194.
- Кудряшов Ю.Б., Кучеренко Н. Е., Васильев А. Н. Радиорезистентность и регуляция метаболизма нервной ткани. Киев.: Либщь. 1992. 234 с.
- Кудряшов Ю.Б., Соболев A.C. Об участии системы цАМФ в противолучевом эффекте // Радиобиология. 1977. Т. 17. № 5. 687−699.
- Кулинский В.И., Колесниченко Л. С. Биологическая роль глютатиона // Успехи современной биологии. 1990. Т. 110. Вып. 1. С. 20−33.
- Кулинский В.И., Колесниченко JI.C. Структура, свойства, биологическая роль и регуляция глутатионпероксидазы // Успехи современной биологии. 1993. Т. 113. Вып. 1. С. 107−122.
- Луговской С.П., Легкоступ Л. А. Механизмы биологического действия свинца на пищеварительную систему // Сучасш проблеми токсикологи. 2002. № 2. С. 45−50.
- Макаров В.К., Жданова Т. Г., Исаханова И. И., Голикова Г. С. Распределение свинца в органах и тканях белых крыс при хронической затравке // Гигиена труда и проф. заболевания. 1976. № 4. С. 40−43.
- Матвеев А.Г. Феномен цитотоксичности и механизм повреждения нейронов коры при гипоксии и ишемии // Pacific Medical Journal. 2004. N. 2. P. 18−23.
- Мозг. Теоретические и клинические аспекты. Под ред. Покровского В. И. М.: Медицина 2003. 536 с.
- Моин В.М. Простой и специфический метод определения активности глутатионпероксидазы в эритроцитах // Лабораторное дело. 1986. №. 12. С. 724−729.
- Персиянцева H.A., Бирих K.P., Дворецкова Е. А. и др. Вклад протеинкиназы С в механизм нарушения Са2±гомеостаза в культивируемых нейронах крысы при гиперстимуляции глутаматных рецепторов // Бюлл. эксперим. биол. и мед. 2008. Т. 145. № 5. С. 533−537.
- Петрович Ю.А. и Подорожная Р.П. Селеноэнзимы и другие селенпротеины, их биологическое значение // Успехи современной биологии. 1981. Т. 81. № 1.С. 127−144.
- Пинелис В.Г., Быкова Л. П., Богачёв А. П. и др. Токсическое действие глутамата на культивируемые зернистые клетки мозжечка снижает внутриклеточное содержание АТФ. Роль ионов Са2+ // Бюлл. эксперим. биол. и мед. 1997. Т. 123. № 2. С. 162−164.
- Привалова Л.И., Кузьмин C.B., Малых О. Л. и др. Роль загрязнения среды обитания свинцом в задержке психологического развития детей дошкольного возраста // Вестник РАМН. 2002. № 11. С. 50−53.
- Розанов В.А. Нейротоксичность свинца в детском возрасте: эпидемиологические, клинические и нейрохимические аспекты // Украшский медичний часопис. 2000. № 5(19). С. 9−17.
- Рыжавский Б.Я., Лебедько O.A., Белолюбская Д. С. Влияние препарата «гистохром» на выраженность отдалённых последствий пренатального воздействия нитрата свинца в головном мозге крыс // Бюлл. эксперим. биол. и мед. 2008. Т. 146. № 8. С. 236−240.
- Рыжавский Б.Я., Михайлов В. И., Фельдшеров Ю. И. и др. Влияние введения свинца беременным крысам на головной мозг их потомства (отдалённые последствия) // Бюлл. эксперим. биол. и мед. 2000. Т. 129. № 1. С. 28−30.
- Соколовский В.В., Кузьмина B.C., Москадынова Г. А., Петрова Н. Н. Спектрофотометрическое определение тиолов в сыворотке крови // Клиническая лабораторная диагностика. 1997. № 11. С. 20−21.
- Стародумов В Л. Дефицит нутриентов как возможное условие развития интоксикации, вызванной воздействием малых доз свинца // Гигиена и санитария. 2003. № 3. С. 60−62.
- Фархутдинов P.P. Методы исследования хемилюминесценции биологического материала на хемилюминомере XJI-003 // В кн.: Методы оценки антиоксидантной активности веществ лечебного и профилактического назначения. М.: РУДН. 2005. С. 147−155.
- Филиппович Ю.Б., Егорова Т. А., Севастьянова Г. А. Практикум по общей биохимии // М. 1975. 319 с.
- Чалисова Н.И., Мелькишев В. Ф., Акоев Г. Н. и др. Стимулирующее влияние пролактина на рост нейритов чувствительных нейронов в органотипической культуре // Цитология. 1991. Т. 33. С. 29−31.
- Чухловина M.JI. Свинец и нервная система (обзор) // Гигиена и санитария. 1977. №. 5. С. 39−42.
- Шурыгин А.Я. Препарат бализ. Краснодар. 2002. 416 с.
- Юсупова Л.Б. О повышении точности определения активности глутатионредуктазы эритроцитов // Лабораторное дело. 1989. № 4. С. 19−21.
- Abdulla Е.М. and Campbell I.C. L-BMAA and kainate-induced modulation of neurofilament concentrations as a measure of neurite outgrowth: implications for an in vitro test of neurotoxicity // Toxicology In Vitro. 1993. Vol. 7. P. 341−344.
- Abdulla E.M., Calaminici M. and Campbell I.C. Comparison of neurite outgrowth with neurofilament protein subunit levels in neuroblastoma cells following mercuric oxide exposure // Clin. Exp. Pharmacol. Physiol. 1995. Vol. 22. P. 362 363.
- Adams J.P. and Sweatt J.D. Molecular psychology: roles for the ERK MAP kinase cascade in memory // Annu. Rev. Pharmacol. Toxicol. 2002. Vol. 42. P. 135−163.
- Adonaylo V.N. and Oteiza P.I. Lead intoxication: antioxidant defenses and oxidative damage in rat brain // Toxicology. 1999b. Vol. 135. P. 77−85.
- Adonaylo V.N. and Oteiza P.I. Pb promotes lipid oxidation and alterations in membrane physical properties // Toxicology. 1999a. Vol. 132. P. 19−32.
- Alano C.C., Beutner G., Dirksen R.T. et al. Mitochondrial permeability transition and calcium dynamics in striatal neurons upon intense NMDA receptor activation // J. Neurochem. 2002. Vol. 80. N. 3. P. 531−538.
- Annau Z. and Cuomo V. Mechanisms of neurotoxicity and their relationship to behavioral changes //Toxicology. 1988. Vol. 49. P. 219−225.
- Ariza M.E., Bijur G.N. and Williams M.V. Lead and mercury mutagenesis: role of H202, superoxide dismutase, and xanthine oxidase // Environ. Mol. Mutagen. 1998. Vol. 31. N. 4. P. 352−61.
- Aruoma O.I., Halliwell B., Laughton M.J. et al. The mechanism of initiation of lipid peroxidation. Evidence against a requirement for an iron (II)-iron (III) complex // Biochem J. 1989. Vol. 258. N. 2. 617−620.
- Audesirk T., Audesirk G., Ferguson C. and Shugarts D. Effects of inorganic lead on the differentiation and growth of cultured hippocampal and neuroblastoma cells //Neurotoxicology. 1991. Vol. 12. N. 3. P. 529−538.
- Audesirk T., Shugarts D., Cabell-Kluch L. and Wardle K. The effects of triethyl lead on the development of hippocampal neurons in culture // Cell. Biol. Toxicol. 1995. Vol. 11. N. l.P. 1−10.
- Babu M.S., Gopal N.V., Reddy K.P. Post natal antioxidant enzyme activity of rat brain regions during developmental lead exposure // J. Environ. Biol. 2007. Vol. 28. N. l.P. 21−27.
- Ballatori N. Glutathione mercaptides as transport forms of metals // Adv. Pharmacol. 1994. Vol. 27. P. 271−298.
- Barbour B., Brew H., Attwell D. Electrogenic glutamate uptake in glial cells is activated by intracellular potassium // Nature. 1988. Vol. 335. N. 6189. P. 433 435.
- Bass N.M. Glutathione S-transferases: of rats and man // Hepatology. 1986. Vol. 6. N. 4. P. 754−763.
- Beal M.F. Mechanisms of excitotoxicity in neurologic diseases // FASEB J. 1992. Vol. 6. P. 3338−3344.
- Bechara E.J. Oxidative stress in acute intermittent porphyria and lead poisoning may be triggered by 5-aminolevulinic acid // Braz. J. Med. Biol. Res. 1996. Vol. 29. N. 7. P. 841−851.
- Begum A.N., Jones M.R., Lim G.P. et al. Curcumin structure-function, bioavailability, and efficacy in models of neuroinflammation and Alzheimer’s disease // J. Pharm. and Exp. Therap. 2008. Vol. 326. P. 196−208.
- Bellinger D.C. Lead // Pediatrics. 2004. Vol. 113. P. 1016−1022.
- Bellinger D.C. Lead and neuropsychological function in children: progress and problems in establishing brain-behavior relationships // Adv. Child. Neuropsychol. 1995. Vol. 3. P. 12−45.
- Bellinger D.C. Very low lead exposures and children’s neurodevelopment // Current Opinion in Pediatrics. 2008. Vol. 20. P. 172−177.
- Bennet C., Bettaiya R., Rajanna S. et al. Region specific increase in the antioxidant enzymes and lipid peroxidation products in the brain of rats exposed to lead // Free Radic. Res. 2007. Vol. 41. N. 3. P. 267−273.
- Benowitz L.I. and Routtenberg A. GAP-43: an intrinsic determinant of neuronal development and plasticity // Trends Neurosci. 1997. Vol. 20. N. 2. P. 84−91.
- Bernal J., Lee J.-H., Cribbs L.L. and Perez-Reyes E. Full Reversal of Pb2+ Block of L-Type Ca2+ Channels Requires Treatment with Heavy Metal Antidotes // J. PHARM. AND EXP. THERAP. 1997. Vol. 282. N. 1. P. 172−180.
- Bernard A. and Lauwerys R. Metal-induced alterations of delta-aminolevulinic acid dehydratase // Ann. N. Y. Acad. Sci. 1987.Vol. 514. P. 41−47.
- Bernhardt R., Huber G., Matus A. Differences in the Developmental Patterns of Three Microtubule-associated Proteins in the Rat Cerebellum // The Journal of Neuroscience. 1985. Vol. 5. N. 4. P. 977−991.
- Beyersman D. Interactions in metal carcinogenicity // Toxicol. Lett. 1994. Vol. 72. P. 333−338.
- Bigbee, J.W., Sharma, K.V., Gupta, J.J., and Dupree, J.L. Morphogenic role for acetylcholinesterase in axonal outgrowth during neural development // Environ. Health Perspect. 1999. Vol. 107. Suppl. 1. P. 81−87.
- Bokara K.K., Brown E., McCormick R. et al. Lead-induced increase in antioxidant enzymes and lipid peroxidation products in developing rat brain // Biometals. 2008. Vol. 21. P. 9−16.
- Bondy S.C. and LeBel C.P. The Relationship Between Excitotoxicity and Oxidative Stress in the Central Nervous System // Free Radical Biology & Medicine. 1993. Vol. 14. P. 633−642.
- Bosley T.M., Woodhams P.L., Gordon R.D., and Balazs R. Effects of anoxia on the stimulated release of amino acid neurotransmitters in the cerebellum in vitro // J. Neurochem. 1983. Vol. 40. N.l. P. 189−201.
- Braga M.F.M., Pereira E.F.R., Albuquerque E.X. Nanomolar concentrations of lead inhibit glutamatergic and GABAergic transmission in hippocampal neurons // Brain Research. 1999b. Vol. 826. P. 22−34.
- Braga M.F.M., Pereira E.F.R., Marchioro M., Albuquerque E.X. Lead increases tetrodotoxin-insensitive spontaneous release of glutamate and GABA from hippocampal neurons // Brain Research. 1999a. Vol. 826. P. 10−21.
- Braga M.F.M., Pereira E.F.R., Mike A., Albuquerque E.X. Pb2+ via Protein Kinase C Inhibits Nicotinic Cholinergic Modulation of Synaptic Transmission in124the Hippocampus // J. PHARM. AND EXP. THERAP. 2004. Vol. 311. N. 2. P. 700−710.
- Bressler J., and Goldstein G.W. Mechanisms of lead neurotoxicity // Biochem. Pharmacol. 1991. Vol. 41. N. 4. 479−484.
- Bressler J., Forman S. and Goldstein G.W. Phospholipid metabolism in neural microvascular endothelial cells after exposure to lead in vitro // Toxicol. Appl. Pharmacol. 1994. Vol. 126. N. 2. 352−360.
- Bressler J., Kim K.-ah, Chakraborti T., Goldstein G. Molecular mechanisms of lead neurotoxicity //Neurochemical Research. 1999. Vol. 24. N. 4. P. 595−600.
- Bragg B. and Matus A. PC 12 Cells Express Juvenile Microtubule-associated Proteins during Nerve Growth Factor-induced Neurite Outgrowth // The Journal of Cell Biology. 1988. Vol. 107. P. 643−650.
- Budd S.L., Castilho R.F. and Nicholls D.G. Mitochondrial membrane potential and hydroethidine-monitored superoxide generation in cultured cerebellar granule cells // FEBS Letters. 1997. Vol. 415. N. 1. P. 21−24.
- Burk R.F., Nishiki K., Lawrence R.A. and Chance B. Peroxide removal by selenium-dependent and selenium-independent glutathione peroxidases in hemoglobin-free perfused rat liver // The Journal of Biological Chemistry. 1978. Vol. 253. N. l.P. 43−46.
- Canfield R.L., Henderson C.R. Jr., Cory-Slechta D.A. et al. Intellectual impairment in children with blood lead concentrations below 10 microg per deciliter//N. Engl. J. Med. -2003. Vol. 348. — 1517−1526.
- Chen A., Cai B., Kim N. et al. Lead exposure, IQ, and behavior in urban 5- to 7-year-olds: does lead affect behavior only by lowering IQ? // Pediatrics. 2007. Vol. 119. N. 3.P. 650−658.
- Chetty Ch.S., Vemuri M.C., Campbell Kh. and Suresh Ch. Lead-induced cell death of human neuroblastoma cells involves GSH deprivation // Cellular & Molecular Biology Letters. 2005. Vol. 10. P. 413−423.
- Chougule P., Patil B., Kanase A. Lead nitrate induced unallied expression of liver and kidney functions in male albino rats // J. Environ. Biol. 2005. Vol. 26. N. 2. P. 421−424.
- Christie N.T. and Costa M. In Vitro Assessment of the Toxicity of Metal Compounds. IV. Disposition of Metals in Cells: Interactions with Membranes, Glutathione, Metallothionein, and DNA // Biological Trace Element Research. 1984. Vol. 6. P. 139−158.
- Clark G.D. and Rothman S.M. Blockade of excitatory amino acid receptors protects anoxic hippocampal slices // Neuroscience. 1987. Vol. 21. N. 3. P. 665 671.
- Cline H.T., Witret S., Jones K.W. Low lead levels stunt neuronal growth in a reversible manner // Proc. Natl. Acad. Sci. USA. 1996. Vol. 93. P. 9915−9920.
- Cohen G. Catalase, glutathione peroxidase, superoxid dismutase, and cytochrom P-450 // Enzymes in the nervous system. New York: Oxford Reven Press. 1983. N. 4. P. 315−330.
- Connor J.A. Digital imaging of free calcium changes and of spatial gradients in growing processes in single, mammalian central nervous system cells // Proc. Nati. Acad. Sci. USA. 1986. Vol. 83. P. 6179−6183.
- Conway Y.G., Kauffman R.C., Tsukada T., Thurman R.G. Glucuronidation of 1-hydroxycoumarin in periportal and pericentral regions of the liver lobuli // Mol. Pharmacol. 1984. Vol. 25. P. 487−493.
- Corona J.C., Tovar-y-Romo L.B., Tapia R. Glutamate excitotoxicity and therapeutic targets for amyotrophic lateral sclerosis // Expert. Opin. Ther. Targets. 2007. Vol. 11. N. 11. P. 1415−1428.
- Costello B., Meymandi A. and Freeman J.A. Factors Influencing GAP-43 Gene Expression in PC 12 Pheochromocytoma Ceils // The Journal of Neuroscience. 1990. Vol. 10. N. 4. P. 1396−1406.
- Coyle J.T. and Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders // Science. 1993. Vol. 262. N. 5136. P. 689−695.
- Crumpton T., Atkins D.S., Zawia N.H. and Barone S. Lead exposure in pheochromocytoma (PC 12) cells alters neural differentiation and Spl DNA-binding // Neurotoxicology. 2001. Vol. 22. N. 1. P. 49−62.
- Dairam A., Limson J.L., Watkins G.M. et al. Curcuminoids, curcumin, and demethoxycurcumin reduce lead-induced memory deficits in male Wistar rats // J. Agric. Food Chem. 2007. Vol. 55. N. 3. P.1039−1044.
- Davies H.A., Lewis M.J., Rhodes J. and Henderson A.H. Trial of nifedipine for prevention of oesophageal spasm // Digestion. 1987. Vol. 36. N. 2. P. 81−83.
- DeLeve L.D. and Kaplowitz N. Glutathione metabolism and its role in hepatotoxicity // Pharmacol. Ther. 1991. Vol. 52. N. 3. P. 287−305.
- Dingledine R., Borges K., Bowie D., Traynelis S.F. The Glutamate Receptor Ion Channels // Pharm. Rev. 1999. Vol. 51. N. 1. P. 7−61.
- Dresel E.I.E. and Falk J.E. Studies on the biosynthesis of blood pigment. Haem synthesis in hemolysed erythrocytes of chicken blood // Biochem. J. 1954. Vol. 56. P. 156−163.
- Dringen R., Pfeiffer B. and Hamprecht B. Synthesis of the Antioxidant Glutathione in Neurons: Supply by Astrocytes of CysGly as Precursor for Neuronal Glutathione // The Journal of Neuroscience. 1999. Vol. 19. N. l.P. 562 569.
- Dubinsky J.M., Kristal B.S. and Elizondo-Fournier M. An obligate role for oxygen in the early stages of glutamate-induced, delayed neuronal death // The Journal ofNeuroscience. 1995. Vol. 15. N. 11. P. 7071−7078.
- Dupree J.L. and Bigbee J.W. Retardation of neuritic outgrowth and cytoskeletal changes accompany acetylcholinesterase inhibitor treatment in cultured rat dorsal root ganglion neurons // J. Neurosci. Res. 1994. Vol. 39. N. 5. P. 567−575.
- Edgar D.H. and Thoenen H. Selective enzyme induction in a nerve growth factor- responsive pheochromocytoma cell line (PC 12) // Brain Res. 1978. Vol. 154. P. 186−190.
- El-Ashmawy I.M., Ashry K.M., El-Nahas A.F. and Salama O.M. Protection by turmeric and myrrh against liver oxidative damage and genotoxicity induced by lead acetate in mice // Basic Clin. Pharmacol. Toxicol. 2006. Vol. 98. N. 1. 32−37.
- El-Missiry M.A. Prophylactic effect of melatonin on lead-induced inhibition of heme biosynthesis and deterioration of antioxidant systems in male rats // J Biochem Mol Toxicol. 2000. Vol. 14. N. 1. P. 57−62.
- Fahey R.C., Sundquist A.R. Evolution of glutathione metabolism // Adv. Enzymol. Relat. Areas Mol. Biol. 1991. Vol. 64. P. 1−53.
- Fan G., Feng Ch., Li Y. et al. Selection of nutrients for prevention or amelioration of lead-induced learning and memory impairment in rats // Ann. Hyg. 2009. Vol. 53. P. 341−351.
- Favaron M., Manev R.M., Rimland J.M., et al. NMDA-stimulated expression of BDNF mRNA in cultured cerebellar granule neurons //Neuroreport. 1993. Vol. 4. N. 10.P. 1171−1174.
- Finkelstein Y., Koffler B., Rabey J.M. and Gilad G.M. Dynamics of cholinergic synaptic mechanisms in rat hippocampus after stress // Brain. Res. 1985. Vol. 343. N. 2. P. 314−319.
- Finkelstein Y., Markowitz M.E. and Rosen J.F. Low-level lead-induced neurotoxicity in children: an update on central nervous system effects // Brain Research Reviews. 1998. Vol. 27. P. 168−176.128
- Flora S.J.S., Pande M., Bhadauria S. and Kannan G.M. Combined administration of taurine and meso 2,3-dimercaptosuccinic acid in the treatment of chronic lead intoxication in rats // Hum. Exp. Toxicol. 2004. Vol. 23. P. 157−166.
- Flora S.J.S., Saxena G. and Mehta A. Reversal of lead-induced neuronal apoptosis by chelation treatment in rats: role of reactive oxygen species and intracellular Ca2+ // J. PHARM. AND EXP. THERAP. 2007. Vol. 322. N. 1. P. 108−116.
- Fujii T. Structure and function of mammalian brain microtubule-associated proteins // Yakugaku Zasshi. 1994. Vol. 114. N. 7. P. 435−447.
- Functions of glutathione: biochemical, physiological, toxicological and clinical / Ed. by Larsson. New York: Raven press. 1983. 403 p.
- Gallegos M.E.H., Zannatha Ma.M.I., Osornio E.G. et al. Immediate and Delayed Effects of Lead on AChE, GSH-T and Thiols in the Substantia Nigra, Neostriatum and Cortex of the Rat Brain // J. Appl. Toxicol. 2001. Vol. 21. P. 397−401.
- Gilbert H.F. Biological Disulfides: The Third Messenger? Modulation of Phosphofructokinase Activity by Thiol/Disulfide Exchange // The Journal of Biological Chemistry. 1982. Vol. 257. N. 20. P. 12 086−12 091.
- Gilbert M.E., Kelly M.E., Samsam T.E. and Goodman J.H. Chronic developmental lead exposure reduces neurogenesis in adult rat hippocampus but does not impair spatial learning // Toxicological Sciences. 2005. Vol. 86. N. 2. P. 365−374.
- Gill R., Foster A.C., and Woodruff G.N. Systemic administration of MK-801 protects against ischemia-induced hippocampal neurodegeneration in the gerbil // J. Neurosci. 1987. Vol. 7. N. 10. P. 3343−3349.
- Goff D.C. and Wine L. Glutamate in schizophrenia: clinical and research implications // Schizophr. Res. 1997. Vol. 27 N. 2−3. P. 157−168.
- Goldstein G.W. Evidence that lead acts as a calcium substitute in second messenger metabolism //Neurotox. 1993. Vol. 14. N. 2−3. P. 97−101.
- Goslin K. and Banker G. Experimental observations on the development of polarity by hippocampal neurons in culture // The Journal of Cell Biology. 1989. Vol. 108. P. 1507−1516.
- Goswami K., Gachhui R., Bandopadhyay A. Hepatorenal dysfunctions in lead pollution // J. Environ. Sci. Eng. 2005. Vol. 47. N. 1. P. 75−80.
- Greene L. A. and Rukenstein A. Regulation of acetylcholinesterase activity by nerve growth factor. Role of transcription and dissociation from effects on proliferation and neurite outgrowth // J. Biol. Chem. 1981. Vol. 256. P. 63 636 367.
- Guilarte T.R., Toscano C.D., McGlothan J.L. and Weaver S.A. Environmental enrichment reverses cognitive and molecular deficits induced by developmental lead exposure // Ann. Neurol. 2003. Vol. 53. N. 1. P. 50−56.
- Gurer H. and Ercal N. Can antioxidants be beneficial in the treatment of lead poisoning? // Free Radical Biology & Medicine. 2000. Vol. 29. N. 10. P. 927−945.
- Hack N. and Bala’zs R. Selective stimulation of excitatory amino acid receptor subtypes and the survival of granule cells in culture: effect of quisqualate and AMP A //Neurochem. Int. 1994. Vol. 25. N. 3. P. 235−241.
- Hagberg H., Lehmann A., Sandberg M. et al. Ischemia-induced shift of inhibitory and excitatory amino acids from intra- to extracellular compartments // J. Cereb. Blood. Flow. Metab. 1985. Vol. 5 N. 3. P. 413−419.
- Halliwell B. and Chirico S. Lipid peroxidation: its mechanism, measurement and significance//Am. J. Clin. Nutr. 1993. Vol. 57(suppl). P. 715S-725S.
- Hanas J.S., Rodgers J.S., Bantle J.A., Cheng Y.-G. Lead Inhibition of DNA-Binding Mechanism of Cys2His2 Zinc Finger Proteins // Molecular Pharmacology. 1999. Vol. 56. P. 982−988.
- Harris J.W. and Patt H.M. Nbn-protein silfgudryl content and cell cycle dynamic of Ehrlich ascites tumor // Exp. Cell Res. 1969. Vol. 56. N. 1. P. 134 141.
- Hatanaka H. Nerve growth factor-mediated stimulation of tyrosine hydroxylase activity in a clonal rat pheochromocytoma cell line // Brain Res. 1981. Vol. 222. N. 2. P. 225−233.
- Hawkins R.L. and Seeds N.W. Effect of proteases and their inhibitors on neurite outgrowth from neonatal mouse sensory ganglia in culture // Brain Research. 1986. Vol. 398. P. 63−70.
- Hayakawa F., Kimura T., Maeda T. et al. DNA cleavage reaction and linoleic acid peroxidation induced by tea catechins in the presence of cupric ion // Biochim. Biophys. Acta. 1997. Vol. 1336. P. 123−131.
- Heales S.J.R., Lam A.A.J., Duncan A.J. and Land J.M. Neurodegeneration or neuroprotection: the pivotal role of astrocytes // Neurochemical Research. 2004. Vol. 29.N.3. P. 513−519.
- Hinchman C.A. and Ballatori N. Glutathione conjugation and conversion to mercapturic acids can occur as an intrahepatic process // J. Toxicol. Environ. Health. 1994. Vol. 41. N. 4. P. 387−409.
- Hinchman C.A., Matsumotos H., Simmons Th.W. and Ballatorill N. Intrahepatic conversion of a glutathione conjugate to it’s mercapturic acid // The Journal of Biologiccal Cemistry. 1991. Vol. 266. N. 33. P. 22 179−22 185.
- Hjelle O.P., Chaudhry F.A. and Ottersen O.P. Antisera to glutathione: characterization and immunocytochemical application to the rat cerebellum // Eur. J. Neurosci. 1994. Vol. 6. N. 5. P. 793−804.
- Hoffman T.J., Corlija M., Chaplin S.B. et al. Retention of 99mTc.-d, l-HM-PAO in rat brain: an autoradiographic study //J. Cereb. Blood. Flow. Metab. 1988. Vol. 8. N. 6. P. 38−43.
- Hu J.F., Li G.Z. and Li M.J. Protective effect of Gastrodia elata and E-gelatin on lead-induced damage to the structure and function of rat hippocampus // Zhonghua Lao Dong Wei Sheng Zhi Ye Bing Za Zhi. 2003. Vol. 21. N. 2. P. 124 127.
- Huang J. and Philbert M.A. Distribution of glutathione and glutathione-related enzyme systems in mitochondria and cytosol of cultured cerebellar astrocytes and granule cells // Brain Research. 1995. Vol. 680. P. 16−22.
- Huber G. and Matus A. Differences in the cellular distributions of two microtubule-associated proteins, MAPI and MAP2, in rat brain // The Journal of Neuroscience. 1984. Vol. 4. N. 1. P. 151−160.
- Ikeda K., Kinoshta M., Iwasaki G. et al. Neurotrophic effect of angiotensin II, vasopressin and oxytocin on the ventral cord of rat embryo // Intern. J. Neurosci. 1989. V. 48. P.
- Ikonomidou Chr., Bosch F., Miksa M. et al. Blockade of NMDA receptors and apoptotic neurodegeneration in the developing brain // Science. 1999. Vol. 283. N. 5398. P. 70−74.
- In Vitro Neurotoxicology. Principles and Challenges. Methods in Pharmacology and Toxicology. Series Humana Press. Totowa. New Jersey. 2003. 336 p.
- Isaacs J.T. and Binkley F. Cyclic AMP-dependent control of the rat hepatic glutathione disulfide-silfgudryl ratio // Boichem. et Biophys. Acta. 1977. — Vol. 498.-N.1.-P. 29−38.
- Jap Tjoen S.E., Schmidt-Michels M., Oestreicher A.B. et al. Dexamethasone-induced effects on B-50/GAP-43 expression and neurite outgrowth in PC 12 cells // J. Mol. Neurosci. 1992. Vol. 3. N. 4. P. 189−195.
- Jap Tjoen S.E., Schmidt-Michels M.H., Spruijt B.M. et al. Quantitation of the growth-associated protein B-50/GAP-43 and neurite outgrowth in PC 12 cells // J. Neurosci. Res. 1991. Vol. 29. P. 149−154.
- Johnston M.V., Trescher W.H., Ishida A., Nakajima W. Neurobiology of hypoxic-ischemic injury in the developing brain // Pediatric Res. 2001. Vol. 49. N. 6. P. 735−741.
- Kern M. and Audesirk G. Inorganic lead may inhibit neurite development in cultured rat hippocampal neurons through hyperphosphorylation // Tox. and App. Pharm. 1995. Vol. 134. P. 111−123.
- Kern M., Audesirk T. and Audesirk G. Effects of inorganic lead on the differentiation and growth of cortical neurons in culture // Neurotoxicology. 1993. Vol. 14. P. 319−328.
- Kerper L.E. and Hinkle P.M. Cellular uptake of lead is activated by depletion of intracellular calcium stores // The Journal of Biological Chemistry. 1997. Vol. 272. N. 13. P. 8346−8352.
- Khodorov B. Glutamate-induced deregulation of calcium homeostasis and mitochondrial dysfunction in mammalian central neurons // Prog. Biophys. Mol. Biol. 2004. Vol. 86. N. 2. P. 279−351.
- Khodorov B., Pinelis V., Golovina V. et al. On the origin of a sustainedn iincrease in cytosolic Ca concentration after a toxic glutamate treatment of the nerve cell culture // FEBS Letters. 1993. Vol. 324. N. 3. P. 271−273.
- Kiss T. and Osipenko O.N. Toxic effects of heavy metals on ionic channels // Pharmacological Reviews. 1994. Vol. 46. N. 3. P. 245−267.
- Kochhar A., Zivin J.A., Lyden P.D., Mazzarella V. Glutamate antagonist therapy reduces neurologic deficits produced by focal central nervous system ischemia // Arch. Neurol. 1988. Vol. 45. N.2. P. 148−153.
- Korashy H.M. and El-Kadi S.A.O. Regulatory mechanisms modulating the expression of cytochrome P450 1A1 gene by heavy metals // Toxicological Sciences. 2005. Vol. 88(1). P. 39−51.
- Korashy H.M. and El-Kadi S.A.O. Transcriptional regulation of the NAD (P)H:quinone oxidoreductase 1 and glutathione S-transferase Ya genes by mercury, lead, and copper // Drug Metabolism and Disposition. 2006. Vol. 34. No. l.P. 152−165.
- Korsrud G.O. and Meldrum J.B. Effect of diet on the response in rats to lead acetate given orally or in the drinking water // Biol. Trace Elem. Res. 1988. Vol. 17. P. 167−173.
- Kosower N.S. and Kosower E.M. The glutathione status of cells // Int. Rev. Cytol. 1978. Vol. 54. P. 109−160.
- Kowaltowski A.J., Castilho R.F. and Vercesi A.E. Ca (2+)-induced mitochondrial membrane permeabilization: role of coenzyme Q redox state // Am. J. Physiol. Cell Physiol. 1995. Vol. 269. Issue. 1. C141-C147.
- Lachant N.A., Tomoda A. and Tanaka K.R. Inhibition of the pentose phosphate shunt by lead: a potential mechanism for hemolysis in lead poisoning // Blood. 1984. Vol. 63. N. 3. P. 518−524.
- Lafon-Cazal M., Culcasi M., Gaven F. et al. Nitric oxide, superoxide and peroxynitrite: putative mediators of NMDA-induced cell death in cerebellar granule cells //Neuropharmacology. 1993a. Vol. 32. N. l 1. P. 1259−1266.
- Lafon-Cazal M., Pietri S., Culcasi M. and Bockaert J. NMDA-dependent superoxide production and neurotoxicity // Nature. 1993b. Vol. 364. N. 6437. P. 535−537.
- Lanphear B.P., Succop P., Roda S. and Henningsen G. The effect of soil abatement on blood lead levels in children living near a former smelting and milling operation // Public Health Rep. 2003. Vol. 118. N. 2. P. 83−91.
- Lasley S.M. and Gilbert M.E. Rat hippocampal glutamate and GABA relase exhibit biphasic effect as a function of chronic lead exposure level // Toxicology Science. 2002. Vol. 66. P. 139−147.
- Lasley S.M. Regulation of dopaminergic activity, but not tyrosine hydroxylase, is diminished after chronic inorganic lead exposure // Neurotoxicology. 1992. Vol. 13. N. 3. P. 625−635.
- Latta K. and Augustein R.C. The purification and properties of human lens glutathione reductase // Exp. Eur. Res. 1984. Vol. 39. N. 3. P. 343−354.
- LeMoal M. and Simon H. Mesocorticolimbic dopaminergic network: functional and regulatory roles // Physiol. Rev. 1991. Vol. 17. P. 155−234.
- Lenz G.R. and Martell A.E. Metal chelates of some sulfur-containing amino acids //Biochemistry. 1964. Vol. 3. P. 745−750.
- Li P. and Rossman T.G. Genes upregulated in lead-resistant glioma cells reveal possible targets for lead-induced developmental neurotoxicity // Toxicological Sciences. 2001. Vol. 64. P. 90−99.
- Lim D.K. and Ho I.K. Responses to N-methyl-D-aspartate and kainic acid in cerebellar granule cells of lead-exposed rat pups // Neurotoxicology. 1998 Vol. 19. N. LP. 49−55.
- Lindahl L.S., Bird L., Legare M.E. et al. Differential ability of astroglia and neuronal cells to accumulate lead: dependent on cell type and degree of differentiation//Tox. Sci. 1999. Vol. 50. P. 236−243.
- Lipton P. Ischemic Cell Death in Brain Neurons // Physiol. Rev. 1999. Vol. 79. P. 1431−1568.
- Litman P., Barg J., Rindzoonski L. and Ginzburg I. Subcellular localization of tau mRNA in differentiating neuronal cell culture: implications for neuronal polarity//Neuron. 1993. Vol. 10. N. 4. 627−638.
- Liu Q., Chen R., Qin R. Effect of sub-acute low level exposure to lead on cellular immune function in rats // Wei Sheng Yan Jiu. 2000. Vol. 29. 6. P. 354 356.
- Loikkanen J., Naarala J., Savolainen K.M. Modification of glutamate-induced oxidative stress by lead: the role of extracellular calcium // Free Radical Biology & Medicine. 1998. Vol. 24. N. 2. P. 377−384.
- Loikkanen J., Naarala J., Vahakangas K.H., Savolainen K.M. Glutamate increases toxicity of inorganic lead in GT1−7 neurons: partial protection induced by flunarizine//Arch. Toxicol. 2003. Vol. 77. P. 663−671.
- Long G.J., Rosen J. F and Schannet F.A.X. Lead Activation of Protein Kinase C from Rat Brain // J. Biol. Chem. 1994. Vol. 269. N. 2. P. 834−837.
- Longo F.M. and Massa S.M. Neuroprotective Strategies in Alzheimer’s Disease // J. Am. Soc. Exp. NeuroTher. 2004. Vol. 1. P. 117−127.92.
- Lowndes H.E., Philbert M.A., Beiswanger C.M. et al. Xenobiotic metabolism in the brain as mechanistic bases for neurotoxicity // In Handbook of neurotoxicology (Eds by Chang L.W. and Dyer R.S.). 1995. New York. P. 1−27.
- Lucas C.A., Czlonkowska A. and Kreutzberg G.W. Regulation of acetylcholinesterase by nerve growth factor in the pheochromocytoma PC 12 cell line //Neurosci. Lett. 1980. Vol. 18. P. 333−337.
- Lunterbung B.H., Smith C.V., Hughes H., Mitchell J.R. Biliary excretion of glutathione and glutathione disulfide in rat // J. Clin. Invest. 1984. Vol. 73. N. 1. P. 124−133.
- Madeja M., Binding N., MuBhoff U. et al. Effects of lead on cloned voltage-operated neuronal potassium channels // Naunyn-Schmiedeberg's Arch. Pharmacol. 1995. Vol. 351. P. 320−327.
- Madeja M., MuBhoff U., Binding N. et al. Effects of Pb2+ on delayed-rectifier potassium channels in acutely isolated hippocampal neurons // J. Neurophysiol. 1997. Vol. 78. P. 2649−2654.
- Mareck A., Fellous A., Francon J. and Nunez J. Changes in composition and activity of microtubule-associated proteins during brain development // Nature. 1980. Vol. 284. N. 5754. P. 353−355.
- Mark L.P., Prost R.W., Ulmer J.L. et al. Pictorial review of glutamate excitotoxicity: fundamental concepts for neuroimaging // Am. J. Neuroradiol. 2001. Vol. 22. P. 1813−1824.
- Markovac J. and Goldstein G.W. Picomolar concentrations of lead stimulate brain protein kinase C //Nature. 1988. Vol. 334. N.6177. P. 71−73.
- Mattson M.P. and Kater S.B. Calcium regulation of neurite elongation and growth cone motility // The Journal of Neuroscience. 1987. Vol. 7. N. 12. P. 40 344 043.
- Mattson M.P., Dou P. and Kater S.B. Outgrowth-regulating pyramidal neurons //The Journal of Neuroscience. 1988b. Vol. 8. N. 6. P. 2087−2100.
- Mattson M.P., Guthrie P.B. and Kater S.B. A role for Na±dependent Ca2+ extrusion in protection against neuronal excitotoxicity // FASEB J. 1989. Vol. 3. P. 2519−2526.
- Mattson M.P., Taylor-Hunter A. and Kater S.B. Neurite outgrowth in individual neurons of a neuronal population is differentially regulated by calcium and cyclic AMP // The Journal of Neuroscience. 1988a. Vol. 8. N.5. P. 1704−1711.
- Mazzolini M. Multiple pathways of Pb permeation in rat cerebellar granule neurons // J. Neurochem. 2001 Vol. 79. P. 407−416.
- McFeeters R.L. and Oswald R.E. Emerging structural explanations of ionotropic glutamate receptor function // FASEB J. 2004. Vol. 18. P. 428−438.
- Meiri K.F., Willard M. and Johnson M.I. Distribution and phosphorylation of the growth-associated protein GAP-43 in regenerating sympathetic neurons in culture // The Journal of Neuroscience. 1988. Vol. 8. N. 7. P. 2571−2581.
- Meister A. and Anderson M.E. Glutathione // Annu. Rev. Biochem. 1983. Vol. 52. P. 711−760.
- Meister A. and Tate S.S. Glutathione and related y-glutamyl compounds: biosynthesis and utilization // Annu. Rev. Biochem. 1976. Vol. 45. P. 559−604.
- Meister A. Glutathione metabolism and it’s selective modification // The Journal of Biological Chemistry. 1988. Vol. 263. N. 33. P. 17 205−17 208.
- Meister A. Glutathione-ascorbic acid antioxidant system in animals // The Journal of Biological Chemistry. 1994. Vol. 269. N. 13. P. 9397−9400.
- Meldrum B.S. Glutamate as a Neurotransmitter in the brain: review of physiology and pathology // J. Nutr. 2000. Vol. 130. P. 1007S-1015S.138
- Meldrum B.S. Protection against ischaemic neuronal damage by drugs acting on excitatory neurotransmission // Cerebrovasc. Brain. Metab. Rev. 1990. Vol. 2 N. l.P. 27−57.
- Mendelsohn A.L., Dreyer B.P., Fierman A.H. et al. Low-Level Lead Exposure and Behavior in Early Childhood // Pediatrics. 1998. Vol. 101. N. 3. P. el0.
- Metzger F., Wiese S. and Sendtner M. Effect of glutamate on dendritic growth in embryonic rat motoneurons // The Journal of Neuroscience. 1998. Vol. 18. N. 5. P.1735−1742.
- Mishra R., Gupta S.K., Meiri K.F. et al. GAP-43 is key to mitotic spindle control and centrosome-based polarization in neurons // Cell Cycle. 2008. Vol. 7. N. 3. P. 348−357.
- Miwa N., Yamazaki H., Nagaoka Y et al. Altered production of the active oxygen species is involved in enhanced cytotoxic action of acylated derivatives of ascorbate to tumor cells // Biochim. and Biophys. Acta. 1989. Vol. 26. N. 2. P. 144−151.
- Monks T.J., Ghersi-Egea J.-F., Philbert M. et al. Symposium overview: The role of glutathione in neuroprotection and neurotoixcity // Tox. Sci. 1999. Vol. 51. P. 161−177.
- Monteiro H.P., Abdalla D.S., Augusto O. and Bechara E.J. Free radical generation during delta-aminolevulinic acid autoxidation: induction by hemoglobin and connections with porphyrinpathies // Arch. Biochem. Biophys. 1989. Vol. 271. N. l.P. 206−216.
- Monteiro H.P., Abdalla D.S., Faljoni-Alario A. and Bechara E.J. Generation of active oxygen species during coupled autoxidation of oxyhemoglobin and delta-aminolevulinic acid//Biochim. Biophys. Acta. 1986. Vol. 881. N. 1. P. 100−106.
- Monteiro H.P., Bechara E.J. and Abdalla D.S. Free radicals involvement in neurological porphyrias and lead poisoning // Mol. Cell. Biochem. 1991. Vol. 103. N. l.P. 73−83.
- Moreira E.G., Jordao de Magalhaes Rosa G., Barros S.B.M. et al. Antioxidant defense in rat brain regions after developmental lead exposure // Toxicology.2001. Vol. 169. P. 145−151.
- Naarala J., Loikkanen J.J., Ruotsalainen M.H., Savolainen K.M. Lead amplifies glutamate-induced oxidative stress // Free Radic. Biol. Med. 1995. Vol. 19. P. 689−693.
- Nicholls D. and Attwell D. The release and uptake of excitatory amino acids // Trends Pharmacol. Sci. 1990. Vol. 11. N. 11. P. 462−468.
- Nicholls D.G. and Budd S.L. Mitochondria and neuronal survival // Physiological Rev. 2000. Vol. 80. N. 1. P. 315−360.
- Nishizawa Y. Glutamate release and neuronal damage in ischemia // Life Sciences. 2001. Vol. 69. P. 369−381.
- Nissim I. Newer aspects of glutamine/glutamate metabolism: the role of acute pH changes // Am. J. Physiol. Renal. Physiol. 1999. Vol. 277. P. 493−497.
- Oh S.M. and Betz A.L. Interaction between free radicals and excitatory amino acids in the formation of ischemic brain edema in rats // Stroke. 1991. Vol. 22. N. 7. P. 915−921.
- Omelchenko I.A., Nelson C.S. and Allen Ch.N. Lead inhibition of N-methyl-D-aspartate receptors containing NR2A, NR2C and NR2D subunits // J. PHARM. AND EXP. THERAP. 1997. Vol. 282. P. 1458−1464.
- Othman A. L and El-Missiry M.A. Role of selenium against lead toxicity in male rats // J. Biochem. Mol. Toxicol. 1998. Vol. 12. P. 345−349.
- Paglini G., Peris LMascotti F. et al. Tau protein function in axonal formation //Neurochem Res. 2000. Vol. 25. N. 1. P. 37−42.
- Pande M. and Flora S J.S. Lead induced oxidative damage and its response to combined administration of a-lipoic acid and succimers in rats // Toxicology.2002. Vol. 177. P. 187−196.
- Pande M. and Flora S.J.S. Lead induced oxidative damage and its response to combined administration of a-lipoic acid and succimers in rats // Toxicology. 2002. Vol. 177. P. 187−196.
- Patrick L. Lead toxicity part II: the role of free radical damage and the use of antioxidants in the pathology and treatment of lead toxicity // Altern. Med. Rev. 2006. Vol. 11.N.2.P. 114−127.
- Pellmar T.C., Roney D. and Lepinski D.L. Role of glutathione in repair of free radical damage in hippocampus in vitro // Brain Res. 1992. Vol. 583. N. 1−2. P. 194−200.
- Peng Sh., Hajela R.K., Atchison W.D. Characteristics of block by Pb2+ of function of human neuronal L-, N-, and R-type Ca2+ channels transiently expressed in human embryonic kidney 293 cells // Molecular Pharmacology. 2002 Vol. 62. N. 6. P. 1418−1430.
- PeiTone-Bizzozero N.I., Finklestein S.P. and Benowitz L.I. Synthesis of a growth-associated cerebrocortical neurons in vitro // The Journal of Neuroscience. 1986. Vol. 6. N.12. P. 3721−3730.
- Petit T.L., LeBoutillier J.C. and Brooks W.J. Altered sensitivity to NMDA following developmental lead exposure in rats // Physiol. Behav. 1992. Vol. 52. N. 4. P. 687−693.
- Phillis J.W., Song D., O’Regan M.H. Inhibition by anion channel blockers of ischemia-evoked release of excitotoxic and other amino acids from rat cerebral cortex//Brain. Res. 1997. Vol. 758. N. 1−2. P. 9−16.
- Ponnusamy K., Mohan M., Nagaraja H.S. Protective antioxidant effect of Centella asiatica bioflavonoids on lead acetate induced neurotoxicity // Med. J. Malaysia. 2008. Vol. 63. Suppl. A: 102.141
- Power J.H.T., Shannon J.M., Blumbergs P.C. and Gai W.-P. Nonselenium glutathione peroxidase in human brain, elevated levels in Parkinson’s disease and dementia with Lewy bodies // American Journal of Pathology. 2002. Vol. 161. N. 3. P. 885−894.
- Prehn J.H. Mitochondrial transmembrane potential and free radical production in excitotoxic neurodegeneration // Naunyn Schmiedebergs Arch. Pharmacol. 1998. Vol. 357. N. 3. P. 316−322.
- Przyborski S.A. and Cambray-Deakin M.A. Developmental changes in GAP-43 expression in primary cultures of rat cerebellar granule cells // Mol. Brain Res. 1994. Vol. 25. P. 273−285.
- Przyborski S.A. and Cambray-Deakin M.A. Developmental regulation of MAP2 variants during neuronal differentiation in vitro // Brain research. Developmental brain research. 1995. Vol. 89. N. 2. P. 187−201.
- Qian Y., Mikeska G., Harris E.D. et al. Effect of lead exposure and accumulation on copper homeostasis in cultured C6 rat glioma cells // Toxicology and Applied Pharmacology. 1999. Vol. 158. P. 41−49.
- Ralston D.M. and O’Halloran T.V. Ultrasensitivity and heavy-metal selectivity of the allosterically modulated MerR transcription complex // Proc. Natl. Acad. Sci. USA. 1990. Vol. 87. P. 3846−3850.
- Reynolds I J. and Hastings T.G. Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation // The Journal ofNeuroscience. 1995. Vol. 15. N. 5. P. 3318−3327.
- Richman P.G. and Meister A. Regulation of y-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione // The Journal of Biological Chemistry. 1975. Vol. 250. N. 4. P. 1422−1426.
- Riederer B. and A. Matus Differential expression of distinct microtubule-ssociated proteins during brain development // PNAS. 1985. Vol. 82. P. 60 066 009.
- Rogan W.J. Safety and efficacy of succimer in toddlers with blood lead levels of 20−44 mg/dL // Pediatric Res. 2000. Vol. 48. N. 5. P. 593−599.142
- Rossi D.J., Oshima T. and Attwell D. Glutamate release in severe brain ischaemia is mainly by reversed uptake //Nature. 2000. Vol. 403. N. 6767. P. 316 321.
- Rossi R., Dalle-Donne I., Milzani A., Giustarini D. Oxidized forms of glutathione in peripheral blood as biomarkers of oxidative stress // Clinical Chemistry. 2006. Vol. 52. N. 7. P. 1406−1414.
- Roth C.A., Hoffman T.J., Corlija M. et al. The effect of ligand structure on glutathione-mediated decomposition of propylene amine oxime derivatives // Int. J. Rad. Appl. Instrum. B. 1992. Vol. 19. N. 7. P. 783−790.
- Rothman S. Synaptic release of excitatory amino acid neurotransmitter mediates anoxic neuronal death // J. Neurosci. 1984. Vol. 4. No. 7. P. 1884−1891.
- Sandhir R. and Gill. K.D. Alterations in calcium homeostasis on lead exposure in rat synaptosomes //Mol. Cell. Biochem. 1994d. Vol. 131. P. 25−33.
- Sandhir R. and Gill. K.D. Calmodulin and cAMP dependent synaptic vesicle protein phosphorylation in rat cortex following lead exposure // Inr. J. Eiochm. 1994c. Vol. 26. N. 12. P. 1383−1389.
- Sandhir R. and Gill. K.D. Effect of lead on lipid peroxidation in liver of rats // Biol. Trace Elem. Res. 1995. Vol. 48. N. 1. 91−97.
- Sandhir R. and Gill. K.D. Effect of lead on the biological acclivity of the calmodulin in rat brain // Exp. Mol. Pathol. 1994b. Vol. 61. P. 69−75.
- Sandhir R. and Gill. K.D. Lead perturbs calmodulin dependent cyclic AMP metabolism in rat central nervous system // Biochem. Mol. Biol. 1994a. Vol. 33. N. 4. P. 729−742.
- Sandhir R., Julka D. and Gill. K.D. Lipoperoxidative damage on lead exposure in rat brain and its implications on membrane bound enzymes // Pharmacol. Toxicol. 1994. Vol. 74. N. 2. P. 66−71.
- Sasaki T. and Senda N. Evaluation of glutathione localization in brain using 99mTc meso-HMPAO // J. Nucl. Med. 1999. Vol. 40. P. 1056−1060.
- Savolainen K.M., Loikkanen J., Eerikainen S., Naarala J. Glutamate-stimulated ROS production in neuronal cultures: interactions with lead and the cholinergic system //Neurotoxicology. 1998b. Vol. 19. N. 4−5. P. 669−674.
- Savolainena K.M., Loikkanena J., Eerikainena S., Naaralaa J. Interactions of excitatory neurotransmitters and xenobiotics in excitotoxicity and oxidative stress: glutamate and lead // Toxicology Letters. 1998a. Vol. 102−103. P. 363−367.
- Savolainena K.M., Loikkanena J., Naaralaa J. Amplification of glutamate-induced oxidative stress II Toxicology Letters. 1995. Vol. 82−83. P. 399−405.
- Saxena G. and Flora S.J.S. Lead-induced oxidative stress and hematological alterations and their response to combined administration of calcium disodium EDTA with a thiol chelator in rats // J. Biochem. Mol. Toxicol. 2004. Vol. 18. N. 4. P. 221−233.
- Schmitt B.M., Berger U.V., Douglas R.M. et al. Na/HC03 Cotransporters in rat brain: expression in glia, neurons and choroid plexus // The Journal of Neuroscience. 2000. Vol. 20. N. 18. P. 6839−6848.
- Schmitt T.J., Zawia N. and Harry G.J. GAP-43 mRNA expression in the developing rat brain: alterations following lead-acetate exposure // Neurotoxicology. 1996. Vol. 17. N. 2. P. 407−414.
- Schneider J.S., Huang F.N., Vemuri M.C. Effects of low-level lead exposure on cell survival and neurite length in primary mesencephalic cultures // Neurotoxicology and Teratology. 2003. Vol. 25. P. 555−559.
- Schneider J.S., Lee M.H., Anderson D.W. et al. Enriched environment during development is protective against lead-induced neurotoxicity // Brain Res. 2001. Vol. 896. N. 1−2. P. 48−55.
- Schrauzer G.N. Effects of selenium antagonists on cancer susceptibility: new aspects of chronic heavy metal toxicity // Sangyo Ika Daigaku Zasshi. 1987. V. 9(Suppl.). P. 208−215.
- Scortegagna M., Chikhale E. andHanbauer I. Effect of lead on cytoskeletal proteins expressed in E 14 mesencephalic primary cultures // Neurochem. Int. 1998. Vol. 32. P. 353−359.
- Selevan Sh.G., Rice D.C., Hogan K.A. Blood lead concentration and delayed puberty in girls //N. Engl. J. Med. 2003. Vol. 348. P. 1527−1536.
- Shafiq-ur-Rehman S. Lead-induced regional lipid peroxidation in brain // Toxicol. Lett. 1984. Vol. 21. P. 333−337.
- Shaw P.J. and Ince P.G. Glutamate, excitotoxicity and amyotrophic lateral sclerosis // J. Neurol. 1997. Vol. 244. P. 3−14.
- Shen S.R., Yang X.Q., Zhao B.L. Prooxidant effect of tea polyphenols in vitro //J. Tea Science. 1992. Vol. 12. P.145−150.
- Shukla P.K., Khanna V.K., Khan M.Y. and Srimal R.C. Protective effect of curcumin against lead neurotoxicity in rat // Human & Experimental Toxicology. 2003. Vol. 22. P. 653−658.
- Sierra E.M. and Tiffany-Castiglioni E. Reduction of glutamine synthetase activity in astroglia exposed in culture to low levels of inorganic lead // Toxicology. 1991. Vol. 65. N. 3. P. 295−304.
- Sierra E.M., Rowles T.K., Martin J. et al. Low level lead neurotoxicity in a pregnant guinea pigs model: neuroglial enzyme activities and brain trace metal concentrations//Toxicology. 1989. Vol. 59. N. 1 P. 81−96.
- Sies H., Brigelius R., Akerboom T.P.M. Intrahepatic glutathione status // in Functions of glutathione: biochemical, physiological, toxicological, and clinical aspects, eds Larsson A., Holmgren A., Orrenius S., Mannervik B. New York. 1983. P. 51−64.
- Simons T.J.B. Cellular interactions between lead and calcium // British Medical Bulletin. 1986. Vol. 42. N. 4. P. 431−434.145
- Simons T.J.B. Lead-calcium interactions in cellular lead toxicity // Neurotoxicology. 1993. Vol. 14. N. 2−3. P. 77−85.
- Slivka A., Spina M.B. and Cohen G. Reduced and oxidized glutathione in human and monkey brain // Neurosci. Lett. 1987. Vol. 74. N. 1. P. 112−118.
- Smith C.J., Anderton B.H., Davis D.R. and Gallo J.M. Tau isoform expression and phosphorylation state during differentiation of cultured neuronal cells // FEB S Letters. 1995. Vol. 375. N.3. P. 243−248.
- Sonnewald U., Qu H., Asvhner M. Pharmacology and toxicology of astrocyte-neuron glutamate transport and cycling // J. PHARM. AND EXP. THERAP. 2002. Vol. 301. P. 1−6.
- Strittmatter S.M., Igarashi M. and Fishman M.C. GAP-43 amino terminal peptides modulate growth cone morphology and neurite outgrowth // The Journal of Neuroscience. 1994. Vol. 14. N. 9. P. 5503−5513.
- Struzynska L. A glutamatergic component of lead toxicity in adult brain: The role of astrocytic glutamate transporters // Neurochemistry International. 2009. Vol. 55. P. 151−156.
- Struzynska L. and Sulkowski G. Relationships between glutamine, glutamate, and GABA in nerve endings under Pb-toxicity conditions // Journal of Inorganic Biochemistry. 2004. Vol. 98. P. 951−958.
- Struzynska L., Chalimoniuk M., Sulkowski G. Changes in expression of neuronal and glial glutamate transporters in lead-exposed adult rat brain // Neurochemistry International. 2005b. Vol. 47. P. 326−333.
- Struzynska L., Chalimoniuk M., Sulkowski G. The role of astroglia in Pb-exposed adult rat brain with respect to glutamate toxicity // Toxicology. 2005a. Vol 212. P. 185−194.
- Struzynska L., Dabrowska-Bouta B., Koza K. and Sulkowski Grz. Inflammation-like glial response in lead-exposed immature rat brain // Tox. Sci. 2007. Vol. 95. N. 1. P. 156−162.
- Sugawara T., Fujimura M., Noshita N. et al. Neuronal death/survival signaling pathways in cerebral ischemia // The Journal of the American Society for Experimental NeuroTherapeutics. 2004. Vol. 1. N. 1. P. 17−25.
- Sun D.A., Sombati S., DeLorenzo R.J. Glutamate injury-induced epileptogenesis in hippocampal neurons. An in vitro model of stroke-induced «epilepsy» // Stroke. 2001. Vol. 32. P. 2344−2350.
- Suresh Ch., Dennis A.O., Heinz J. et al. Melatonin protection against lead-induced changes in human neuroblastoma cell cultures // International Journal of Toxicology. 2006. Vol. 25. P. 459−464.
- Takahashi K., Avissar N., Whitin J., Coher H. Purification and characterization of human plasma glutathione peroxidase // Arch. Biochem. Biophys. 1987. Vol. 256. N. 2. P. 677−686.
- Takizawa T., Huang I-Y., Ikita T. and Yoshida A. Human glucose-6-phosphate dehydrogenase: Primary structure and cDNA cloning // Proc. Nati. Acad. Sci. USA. 1986. Vol. 83. P. 4157−4161.
- Taylor C.P., Burke S.P., Weber M.L. Hippocampal slices: glutamate overflow and cellular damage from ischemia are reduced by sodium-channel blockade // J. Neurosc. i Methods. 1995. Vol. 59. N. 1. P. 121−128.
- Taylor S.S., Yang J., Wu J. et al. PKA: a portrait of protein kinase dynamics // Biochim. Biophys. Acta. 2004. Vol. 1697. N. 1−2. P. 259−269.
- Teitelbaum J.S., Zatorre R.J., Carpenter S. et al. Neurologic sequelae of domoic acid intoxication due to the ingestion of contaminated mussels // The New England Journal of Medicine Vol. 322. N. 25. P. 1781−1787.
- Thannhauser T.W., Konishi Ya., Scheraga H.A. Sensitive quantitative analysis of disulfide bonds in polypeptides and proteins // Analytical Biochemistry. 1984. Vol. 138. P. 181−188.
- Tomsig J.L. and Suszkiw J.B. Intracellular mechanism of Pb (2+)-induced norepinephrine release from bovine chromaffin cells // Am. J. Physiol. Cell. Physiol. 1993. Vol. 265. Issue 6. C1630-C1636.
- Toscano C.D. and Guilarte T.R. Lead neurotoxicity: From exposure to molecular effects // Brain Research Reviews. 2005. Vol. 49. P. 529−554.
- Turley K.R., Toledo-Pereyra L.H., Kothari R.U. Molecular mechanisms in the pathogenesis and treatment of acute ischemic stroke // Journal of Investigative Surgery. 2005. Vol. 18. P. 207−218.
- Tymianski M., Charlton M.P., Carlen P.L. and Tator Ch.H. Source specificity of early calcium neurotoxicity in cultured embryonic spinal neurons // The Journal ofNeuroscience. 1993. Vol. 13. N. 5. P. 2085−2104.
- Upasani C.D. and Balaraman R. Protective Effect of spirulina on lead induced deleterious changes in the lipid peroxidation and endogenous antioxidants in rats // Phytother. Res. 2003. Vol. 17. P. 330−334.
- Vallee B.L., Ulmer D.D. Biochemical effects of mercury, cadmium and lead // Annu. Rev. Biochem. 1972. Vol. 41. P. 91−128.
- Valverde M., Fortoul T.I., Diaz-Barriga et al. Genotoxicity induced in CD-I mice by inhaled lead: differential organ response // Mutagenesis. 2002. Vol. 17. N. l.P. 55−61.
- Vergun O., Keelan J., Khodorov B.I. and Duchen M.R. Glutamate-induced mitochondrial depolarisation and perturbation of calcium homeostasis in cultured rat hippocampal neurons // J. Physiol. 1999. Vol. 519. P. 451−466.
- Verina T., Rohde C. A. and Guilarte T. R. Environmental lead exposure during early life alters granule cell neurogenesis and morphology in the hippocampus of young adult rats //Neuroscience. 2007. Vol. 145. P. 1037−1047.
- Vesce S., Jekabsons M.B., Johnson-Cadwell L.I. and Nicholls D.G. Acute glutathione depletion restricts mitochondrial ATP export in cerebellar granule neurons // The Journal of Biological Chemistry. 2005. Vol. 280. N. 46. P. 3 872 038 728.
- Villeda-Hernandez J., Barroso-Moguel R., Mendez-Armenta M. et al. Enhanced brain regional lipid peroxidation in developing rats exposed to low level lead acetate // Brain Research Bulletin. 2001. Vol. 55. N. 2. P. 247−251.
- Volterra A., Trotti D., Tromba C. et al. Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes // The Journal of Neuroscience. 1994. Vol. 14. N. 5. P. 2924−2932.
- Wang Ch., Liang J., Zhang Ch. et al. Effect of ascorbic acid and thiamine supplementation at different concentrations on lead toxicity in liver // Ann. Occup. Hyg. 2007. Vol. 51. N. 6. P. 563−569.
- Wang J., Wu. J. and Zhang Zh. Oxidative Stress in Mouse Brain Exposed to Lead // Ann. Occup. Hyg. 2006. Vol. 50. N. 4. P. 405−409.
- Wang W. and Ballatory N. Endogenous glutathione conjugates: occurrence and biological functions // Pharmacological Reviews. 1998. Vol. 50. N. 3. P. 335−355.
- Wei L., Yu Sh.P., Gottron F. et al. Potassium channel blockers attenuate hypoxia- and ischemia-induced neuronal death in vitro and in vivo // Stroke 2003. Vol. 34. P. 1281−1286.
- White B.C., Sullivan J.M., DeGracia D.J. et al. Brain ischemia and reperfusion: molecular mechanisms of neuronal injury // Journal of the Neurological Sciences. 2000. Vol. 179. P. 1−33.
- White L.D., Cory-Slechta D.A., Gilbert M.E. New and evolving concepts in the neurotoxicology of lead // Toxicology and Applied Pharmacology. 2007. Vol. 225. P. 1−27.
- White W.L., Pond R.S., Buckpitt A.R. Glutathione and glutathione S-trasferases in the urinary bladder of defferent species // Biochem. Pharmacol. 1984. Vol. 33. N. 11. P. 1813−1816.
- Williams T.M., Ndifor A.M., Near J.T. and Reams-Brown R.R. Lead enhances NGF-induced neurite outgrowth in PC 12 cells by potentiating ERK/MAPK activation//Neurotoxicology. 2000. Vol. 21. N.6. P. 1081−1089.
- Xu J., Yan Ch.-H., Wu Sh.-H. et al. Developmental lead exposure alters gene expression of metabotropic glutamate receptors in rat hippocampal neurons// Neuroscience Letters. 2007. Vol. 413. P. 222−226.
- Xu Ya., Li G., Han Ch. et al. Protective effects of Hippophae rhamnoides L. juice on lead-induced neurotoxicity in mice // Biol. Pharm. Bull. 2005. Vol. 28. N. 3. P. 490−494.
- Yagminas A.P., Little P.B., C.G. Rousseaux et al. Neuropathologic findings in young male rats in a subchronic oral toxicity study using triethyl lead // Fundamental and Applied Toxicology. 1992. Vol. 19. P. 380−387.
- Yano S., Tokumitsu H. and Soderling T.R. Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway // Nature. 1998. Vol. 396. N. 6711. P. 584−587.
- Yi E.Y. and Lim D.K. Effects of chronic lead exposure on glutamate release and uptake in cerebellar cells of rat pups // Arch. Pharm. Res. 1998. Vol. 21. N.2. P. 113−119.
- Yiin S.J., Lin T.H. Lead-catalyzed peroxidation of essential unsaturated fatty acid // Biol. Trace Elem. Res. -1994. Vol. 50. — P. 167−172.
- Yin Sh.-T., Tang M.-L., Su L. et al. Effects of Epigallocatechin-3-gallate on lead-induced oxidative damage // Toxicology. 2008. Vol. 249. P. 45−54.
- Zawia N.H. and Harry G.J. Developmental exposure to lead interferes with glial and neuronal differential gene expression in the rat cerebellum // Toxicol. Appl. Pharmacol. 1996. Vol. 138. P. 43−47.
- Zurich M.-G., Eskes C., Honegger P. et al. Maturation-dependent neurotoxicity of lead acetate in vitro: implication of glial reactions // Journal of Neuroscience Research. 2002. Vol. 70. P. 108−116.