<<
>>

Заключение

Трансгенные линии Drosophila воспроизводят многие ключевые признаки НДЗ. В то же время, не следует ожидать, что на этих моделях будут полностью повторены все особенности болезней человека.

Пожалуй, моделирование НДЗ на Drosophila должны рассматриваться как создание чувствительной генетической системы, которая предоставляет возможность быстро и сравнительно недорого выявлять клеточные процессы, вовлеченные в патогенез заболеваний, генетические модификаторы этих процессов, а также тестировать потенциальные терапевтические агенты на многоклеточном организме. Конечно, обязательным условием является проверка открытых на Drosophila новых механизмов и молекул на моделях млекопитающих. Открытие генетических модификаторов в Drosophila поможет выявить соответствующие гены у человека и, следовательно, новые терапевтические мишени.

Литература

Большакова О.И., Жук А.А., Родин Д.И. и др. Влияние гиперэкспрессии гена АРР человека на холинергические и дофаминергические нейроны Drosophila melanogaster // Экологическая генетика. 2013. Т XI. № 1. С.23-31.

Иллариошкин С.Н. Конформационные болезни мозга. М.: Янус-К, 2003. 246 с.

Adams M.D., Sekelsky J.J. From sequence to phenotype: reverse genetics in Drosophila melanogaster // Nat. Rev. Genet. 2002. Vol. 3. P 189-198.

Aguzzi A., Baumann F., Bremer J. The Prion’s Elusive Reason for Being // Annu. Rev. Neurosci. 2008. Vol. 31. P. 439-477.

Andersson K., Pokrzywa M., Dacklin I., Lundgren E. Inhibition of TTR aggregation-induced cell death--a new role for serum amyloid P component // PLoS One. 2013. Vol. 8. P. e55766.

Ashley J., Packard M. Ataman B., Budnik V. Fasciclin II signals new synapse formation through amyloid precursor protein and the scaffolding protein dX11/Mint // J. Neurosci. 2005. Vol. 25. P. 5943-5955.

Baki L., Shioi J., Wen P. et al. PS1 activates PI3K thus inhibiting GSK-3 activity and tau overphosphorylation: effects of FAD mutations // EMBO J.

2004. Vol. 23. P 2586-2596.

Bellen H.J., Levis R.W., Liao G. et al. The BDGP gene disruption project: single transposon insertions associated with 40% of Drosophila genes // Genetics. 2004. Vol. 167. P 761-781.

Bentahir M., Nyabi O.,Verhamme J. et al. Presenilin clinical mutations can affect c-secretase activity by different mechanisms // J. Neurochem. 2006. Vol. 96. P. 732-742.

Berg I., Thor S., Hammarstrom P. Modeling familial amyloidotic polyneuropathy (Transthyretin V30M) in Drosophila melanogaster // Neurodegener. Dis. 2009. Vol.6. P 127-38.

Bier E. Drosophila, the golden bug, emerges as a tool for human genetics // Nat. Rev. Genet. 2005. Vol. 6. P. 9-23.

Bilen J., Bonini N.M. Drosophila as a model for human neurodegenerative disease // Annu. Rev. Genet. 2005. Vol.39. P 153-171.

Brand A.H., Perrimon N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes // Development. 1993. Vol. 118. P. 401-415.

Brown P., Gibbs C.J., Rodgers-Johnson P. et al. Human spongiform encephalopathy: the National Institutes of Health series of 300 cases of experimentally transmitted disease // Ann. Neurol. 1994. Vol. 35. P 513-529.

Buxbaum J.N., Ye Z., Reixach N. et al. Transthyretin protects Alzheimer’s mice from the behavioral and biochemical effects of Abeta toxicity // Proc. Natl. Acad. Sci. USA. 2008. Vol. 105. P. 2681-2686.

Cao W., Song H.J., Gangi T. et al. Identification of novel genes that modify phenotypes induced by Alzheimer’s beta-amyloid overexpression in Drosophila // Genetics. 2008. Vol. 178. P. 1457-1457.

Carmine-Simmen K., Proctor T., Tschape J. et al. Neurotoxic effects induced by the Drosophila amyloid-beta peptide suggest a conserved toxic function // Neurobiol. Dis. 2009. Vol. 33. P. 274-281.

Chakraborty R., Vepuri V., MhatreS.D. et al. Characterization of a Drosophila Alzheimer’s disease model: pharmacological rescue of cognitive defects // PLoS One. 2011. Vol. 6. P. e20799.

Chiang H.C., Iijima K., Hakker I., Zhong Y.

Distinctive roles of different beta-amyloid 42 aggregates in modulation of synaptic functions // FASEB J. 2009. Vol. 23. P. 969-1977.

Chiang H.C., Wang L., Xie Z. et al. PI3 kinase signaling is involved in Abeta-induced memory loss in Drosophila // Proc. Natl. Acad. Sci. USA. 2010. Vol. 107. P. 7060-7065.

Choi S.H., Leight S.N., Lee V.M. et al. Accelerated Abeta deposition in APPswe/PS1deltaE9 mice with hemi- zygous deletions of TTR (transthyretin) // J. Neurosci. 2007. Vol. 27. P. 7006-7010.

Connors L.H., Lim A., Prokaeva T. et al. Tabulation of human transthyretin (TTR) variants // Amyloid. 2003. Vol. 10. P. 160-184.

Crowther D.C., Kinghorn K.J., Miranda E. et al. Intraneuronal Abeta, nonamyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer’s disease // Neuroscience. 2005. Vol. 132. P. 123-135.

Deleault N.R., Dolph P.J., Feany M.B. et al. Post-transcriptional suppression of pathogenic prion protein expression in Drosophila neurons // J. Neurochem. 2003. Vol. 85. P. 1614-1623.

De Strooper B., Annaert W. Proteolytic processing and cell biological functions of the amyloid precursor protein // J. Cell Sci. 2000. Vol. 113. P. 1857-1870.

De Strooper B.D., Annaert W. Presenilins and the intramembrane proteolysis of proteins: facts and fiction // Nat. Cell. Biol. 2001. Vol. 3. P. 221-25.

ElliottD., BrandH. The GAL4 System. A versatile system for the expression of genes. Methods in molecular Biology: Drosophila: Methods and Protocols. Ed. C. Dahmann. Humana. Totowa, NY: Press Inc., 2008. P. 79-85.

Enerly E., Larsson J., Lambertsson A. Reverse genetics in Drosophila: from sequence to phenotype using UAS-RNAi transgenic flies // Genesis. 2002. Vol. 34. P. 152-155.

Fernandez-Funez P., Casas-Tinto S., Zhang Y. et al. In vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoforms // PLoS Genet. 2009. Vol. 5. P. e1000507.

Finelli A., Kelkar A., Song H.-J. et al. A model for studying Alzheimer’s AB42-induced toxicity in Drosophila melanogaster // Mol.

Cell. Neurosci. 2004. Vol. 26. P. 365-375.

Fortini M.E., SkupskiM.P., BoguskiM.S., Hariharan I.K. A survey of human disease gene counterparts in the Drosophila genome // J. Cell. Biol. 2000. Vol. 150. P. 23-30.

Gavin B.A., Dolph M.J., Deleault N.R. et al. Accelerated accumulation of misfolded prion protein and spongiform degeneration in a Drosophila model of Gerstmann- Straussler-Scheinker syndrome // J. Neurosci. 2006. Vol. 26. P. 12408-12414.

Giacomotto J., Segalat L. High-throughput screening and small animal models, where are we? // Br. J. Pharmacol. 2010. Vol. 160. P. 204-216.

Goodman D. Retinoids and retinol-binding proteins // Harvey Lect. 1987. Vol. 81. P. 111-132.

Greeve I., Kretzschmar D., Tschape J.A. et al. Age-dependent neurodegeneration and Alzheimer-amyloid plaque formation in transgenic Drosophila // J. Neurosci. 2004. Vol. 24. P. 3899-3906.

Gunawardena S., Goldstein L.S. Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila // Neuron. 2001. Vol. 32. P. 389-401.

Haass C., Selkoe D.J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide // Nat. Rev. Mol. Cell. Biol. 2007. Vol. 8. P. 101-112.

Han D.D., Stein D., Stevens L.M. Investigating the function of follicular subpopulations during Drosophila oogenesis through hormone-dependent enhancer-targeted cell ablation // Development. 2002. Vol. 127. P. 573-583.

Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics // Science. 2002. Vol. 297. P. 353-356.

Hirai K., Aliev G., Nunomura A. et al. Mitochondrial abnormalities in Alzheimer’s disease // J. Neurosci. 2001. Vol. 21. P. 3017-3023.

Hirth F. Drosophila melanogaster in the study of human neurodegeneration // CNS Neurol. Disord. Drug. Targets. 2010. Vol. 9. P. 504-23.

Huet F., Lu J.T., Myrick K.V et al. A deletion-generator compound element allows deletion saturation analysis for genomewide phenotypic annotation // Proc.

Natl. Acad. Sci. USA. 2002. Vol. 99. P. 9948-9953.

Iijima K., Liu H.-P., ChiangA.-S. et al. Dissecting the pathological effects of human Ap40 and Ap42 in Drosophila: A potential model for Alzheimer’s disease // PNAS. 2004. Vol. 101. P. 6623-6628.

Iijima K., Chiang H.C., Hearn S. A. et. al. Abeta42 mutants with different aggregation profiles induce distinct pathologies in Drosophila // PLoS One. 2008. Vol. 1-9. P. е1703.

Iijima-Ando K., Iijima K. Transgenic Drosophila models of Alzheimer’s disease and tauopathies // Brain. Struct. Funct. 2010. Vol. 214. P 245-262.

Iijima-Ando K., Hearn S.A., Shenton C. et al. Mitochondrial Mislocalization Underlies Ab42-Induced Neuronal Dysfunction in a Drosophila Model of Alzheimer’s Disease // PLoS One. 2009. Vol. 4. P. e8310.

Iwata N., Tsubuki S., Takaki Y. et al. Metabolic regulation of brain Ah by neprilysin // Science. 2001. Vol. 292. P 1550-1552.

Iwata N., Higuchi M., Saido T. Metabolism of amyloid-P peptide and Alzheimer’s disease // Pharmacology & Therapeutics. 2005. Vol. 108. P 129-148.

Jang H., Arce F.T., Ramachandran S. et al. Truncated beta-amyloid peptide channels provide an alternative mechanism for Alzheimer’s Disease and Down syndrome // Proc. Natl. Acad. Sci. USA. 2010. Vol. 107. P. 6538-6543.

Kazazian H.H. Mobile elements: drivers of genome evolution // Science. 2004. Vol. 303. P 1626-1632.

Krasemann S., Zerr I., Weber T. et al. Prior disease associated with a bovel nine octapeptide repeat insertion in the PRNP gene // Brain Res. Vol. Brain Res. 1995. Vol. 34. P. 173-176.

Liu L., Murphy R.M. Kinetics of inhibition of beta-amyloid aggregation by transthyretin // Biochemistry. 2006. Vol. 45. P 15702-15709.

Liz M.A., Fleming C.E., Nunes A.F. et al. Substrate specificity of transthyretin: identification of natural substrates in the nervous system // Biochem. J. 2009. Vol. 419. P. 467-474.

Lu B., VogelH. Drosophila models of neurodegenerative diseases // Annu. Rev. Pathol.

2009. Vol. 4. P 315342.

Luo L.Q., Martin-Morris L.E., White K. Identification, secretion, and neural expression of APPL, a Drosophila protein similar to human amyloid protein precursor // J. Neurosci. 1990. Vol. 10. P 3849-3861.

Luo L., Tully T., White K. Human amyloid precursor protein ameliorates behavioral deficit of flies deleted for Appl gene // Neuron. 1992. Vol. 9. P. 59-605.

Marsh J.L., Thompson LM. Drosophila in the study of neurodegenerative disease // Neuron. 2006. Vol. 52. P 169-78.

Matsumoto K., Toh-eA., Oshima,Y. Genetic control of galactokinase synthesis in Saccharomyces cerevisiae: evidence for constitutive expression of the positive regulatory gene gal4 // J. Bacteriol. 1978. Vol. 134. P. 446-457.

McGuire S.E., Le P. T., Osborn A.J. et al. Spatiotemporal rescue of memory dysfunction in Drosophila // Science. 2003. Vol. 302. P 1765-1768.

MeadS. Prion disease genetics // Eur. J. Hum. Genet. 2006. Vol. 14. P. 273-281.

Metaxakis A., Oehler S., Klinakis A., Savakis C. Minos as a genetic and genomic tool in Drosophila melano- gaster // Genetics. 2005. Vol. 171. P 571-581.

Moloney A., Sattelle D.B., Lomas D.A., Crowther D.C. Alzheimer’s disease: insights from Drosophila mela- nogaster models // Trends Biochem. Sci. 2010. Vol. 35. P. 228-235.

Mullane K., Williams M. Alzheimer’s therapeutics: continued clinical failures question the validity of the amyloid hypothesis-but what lies beyond? // Biochem. Pharmacol. 2013. Vol. 85. P. 289-305.

Myrick K.V., HuetF., Mohr S.E. et al. Large-scale functional annotation and expanded implementations of the P{wHy} hybrid transposon in the Drosophila melanogaster genome // Genetics. 2009. Vol. 182. P. 653-660.

Nagai Y., Fujikake N., Ohno K. et al. Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila // Hum. Mol. Genet. 2003. Vol. 12. P. 1253-1259.

Nicholson L., Singh G.K., Osterwalder T. et al. Spatial and temporal control of gene expression in Drosophila using the inducible GeneSwitch GAL4 system. I. Screen for larval nervous system drivers // Genetics. 2008. Vol. 178. P 215-234.

Olofsson A., Ippel H.J., Baranov V et al. Capture of a dimeric intermediate during transthyretin amyloid formation // J. Biol. Chem. 2001. Vol. 276. P 39592-39599.

Osterwalder T., Yoon K.S., White B.H. Keshishian H. A conditional tissue-specific transgene expression system using inducible GAL4 // Proc. Natl. Acad. Sci. USA. 2001. Vol. 98. P 596-612.

Pandey U.B., Nichols C.D. Human disease models in Drosophila melanogaster and the role of the fly in therapeutic drug discovery // Pharmacol. Rev. 2011. Vol. 63. P. 411-436.

Pokrzywa M., Dacklin I., Hultmark D., Lundgren E. Misfolded transthyretin causes behavioral changes in a Drosophila model for transthyretin-associated amyloidosis // Eur. J. Neurosci, 2007. Vol. 26. P. 913-924.

Pokrzywa M., Dacklin I., VestlingM. et al. Uptake of aggregating transthyretin by fat body in a drosophila model for TTR-associated amyloidosis // PLoS One. 2010. Vol. 5. Р. e14343.

PrusinerS.B. Prions // PNAS. 1998a. Vol. 95. P. 13363-13383.

PrusinerS.B. The prion diseases // Brain Pathol. 1998b. Vol. 8. P. 499-513.

Prusiner S.B., Hsiao K.K. Human prion diseases // Ann. Neurol. 1994. Vol. 35. P. 385-395.

Raeber A.J., Muramoto T., Kornberg T.B., Prusiner S.B. Expression and targeting of Syrian hamster prion protein induced by heat shock in transgenic Drosophila melanogaster // Mech. Dev. 1995. P. 317-327.

Reiter L.T., Potocki L., Chien S. et al. A systematic analysis of human disease-associated gene sequences in Drosophila melanogaster // Genome Res. 2001. Vol. 11. P. 1114-1125.

Rodnguez-Martinez A.B., Garrido J.M., Zarranz J.J. et al. A novel form of human disease with a protease- sensitive prion protein and heterozygosity methionine/valine at codon 129: Case report // BMC Neurol. 2010. Vol. 10. doi: 10.1186/1471-2377-10-99.

Roman G., Endo K., ZongL., DavisR.L. P[Switch], a system for spatial and temporal control of gene expression in Drosophila melanogaster // Proc. Natl. Acad. Sci. USA. 2001. Vol. 98. P. 602-607.

R0rth P. A modular misexpression screen in Drosophila detecting tissue-specific phenotypes // Proc. Natl. Acad. Sci. USA. 1996. Vol. 93. P. 12418-12422.

Rosen D.R., Martin-Morris L., Luo L., White K.A. Drosophila gene encoding a protein resembling the human b-amyloid protein precursor // Proc. Natl. Acad. Sci. USA. 1989. Vol. 86. P. 2478-2482.

SangT.K., Jackson G.R. Drosophila models ofneurodegenerative disease // NeuroRx. 2005. Vol. 2. P. 438-446. Sarantseva S., Timoshenko S., Bolshakova O. et al. Apolipoprotein E-mimetics inhibit neurodegeneration and restore cognitive functions in a transgenic Drosophila model of Alzheimer’s disease // PLoS One. 2009a. Vol. 4. № 12. P. e8191.

Sarantseva S., Bolshakova O., Timoshenko S. et al. Overexpression of human amyloid precursor protein causes neurodegeneration and loss of synaptic proteins in transgenic Drosophila // New Trends in Alzheimer and Parkinson Disorders: ADPD. Eds. Hanin I., Fisher A. Prague: Czech Republic: Medimont, 2009b. P. 245-248.

Saura C., Choi S.-Y., Beglopoulos V et al. Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration // Neuron. 2004. Vol. 42. P. 23-36.

Schwarzman A.L., Gregori L., Vitek M.P. et al. Transthyretin sequesters amyloid beta protein and prevents amyloid formation // Proc. Natl. Acad. Sci. USA. 1994. Vol. 91. P. 8368-8372.

Schwarzman A.L., Singh N., Tsiper M. et al. Endogenous presenilin 1 redistributes to the lamellipodia upon adhesion of Jurkat cells to a collagen matrix // Proc. Natl. Acad. Sci. USA. 1999. Vol. 96. P. 7932-7937.

Selkoe D.J. The cell biology of P-amyloid precursor protein and presenilin in Alzheimer’s disease // Trends Cell. Biol. 1998. Vol. 8. P. 447-453.

Selkoe D.J. Translating cell biology into therapeutic advances in Alzheimer’s disease // Nature. 1999. Vol. 399. P. 23-31.

Singh N., Tsiper M., Romanov V et al. The role of Alzheimer’s disease-related presenilin 1 in intercellular adhesion // Exp. Cell. Res. 2001. Vol. 263. P. 1-13.

Smith D., Wohlgemuth J., Calvi B.R. et al. Hobo enhancer trapping mutagenesis in Drosophila reveals an insertion specificity different from P elements // Genetics. 1993. Vol. 135. P. 1063-1076.

Staudt N., Molitor A., Somogyi K. et al. Gain-of-function screen for genes that affect Drosophila muscle pattern formation // PLoS Genet. 2005. Vol. 1. P. e55.

Tateishi J., Kitamoto T. Inherited prion diseases and transmission to rodents // Brain. Pathol. 1995. Vol. 5. P. 53-59.

Torroja L., Chu H., KotovskyI., White K. Neuronal overexpression of APPL, the Drosophila homologue of the amyloid precursor protein (APP), disrupts axonal transport // Curr. Biol. 1999a. Vol. 9. P. 489-492.

Torroja L., Packard M., Gorczyca M. et al. The Drosophila beta-amyloid precursor protein homolog promotes synapse differentiation at the neuromuscular junction // J Neurosci. 1999b. Vol. 19. P. 7793-7803.

Van de Hoef D.L., Hughes J., Livne-Bar I. et al. Identifying genes that interact with Drosophila presenilin and amyloid precursor protein // Genesis. 2009. Vol. 47. P. 246-260.

Walsh D.M., Selkoe D.J. Deciphering the molecular basis of memory failure in Alzheimer’s disease // Neuron. 2004. Vol. 44. P. 181-193.

WestermarkP., Sletten K., Johansson B., Cornwell G.G. 3rd. Fibril in senile systemic amyloidosis is derived from normal transthyretin // Proc. Natl. Acad. Sci. USA. 1990. Vol. 87. P. 2843-2845.

Woeber K.A., Ingbar S.H. The contribution of thyroxinebinding prealbumin to the binding of thyroxine in human serum, as assessed by immunoadsorption // J. Clin. Invest. 1968. Vol. 47. P. 1710-1721.

Yagi Y., Tomita S., Nakamura M., Suzuki T. Overexpression of human amyloid precursor protein in Drosophila // Mol. Cell. Biol. Res. Commun. 2000. Vol. 4. P. 43-49.

Ye Y., FortiniM.E. Characterization of Drosophila presenilin and its colocalization with Notch during development // Mech. Dev. 1998. Vol. 79. P. 199-211.

Zhao X.L., Wang W.A., Tan J.X. et al. Expression of beta-amyloid induced age-dependent presynaptic and axonal changes in Drosophila // J. Neurosci. 2010. Vol. 20. P. 1512-1522.

Zou W.Q., Puoti G., Xiao X. et al. Variably protease-sensitive prionopathy: a new sporadic disease of the prion protein // Ann. Neurol. 2010. Vol. 68. P. 162-172.

<< | >>
Источник: М.В. Угрюмова. НЕЙРОДЕГЕНЕРАТИВНЫЕ ЗАБОЛЕВАНИЯ: от генома до целостного организма. В 2-х томах. Том 2 / Под ред. М.В. Угрюмова. - М.: Научный мир,2014. - 848 с.. 2014

Еще по теме Заключение:

  1. Заключение
  2. Заключение
  3. Заключение
  4. Заключение
  5. Заключение
  6. Заключение
  7. Заключение
  8. Заключение
  9. 2.5. Рациональное трудоустройство больных по заключению КЭК
  10. Патоморфологическое заключение
  11. Вместо заключения
  12. Параграф пятый. Об общих заключениях по действиям мозга
  13. Механизмы заключения договоров
  14. Заключение: от понимания к действию
- Акушерство и гинекология - Анатомия - Андрология - Биология - Болезни уха, горла и носа - Валеология - Ветеринария - Внутренние болезни - Военно-полевая медицина - Восстановительная медицина - Гастроэнтерология и гепатология - Гематология - Геронтология, гериатрия - Гигиена и санэпидконтроль - Дерматология - Диетология - Здравоохранение - Иммунология и аллергология - Интенсивная терапия, анестезиология и реанимация - Инфекционные заболевания - Информационные технологии в медицине - История медицины - Кардиология - Клинические методы диагностики - Кожные и венерические болезни - Комплементарная медицина - Лучевая диагностика, лучевая терапия - Маммология - Медицина катастроф - Медицинская паразитология - Медицинская этика - Медицинские приборы - Медицинское право - Наследственные болезни - Неврология и нейрохирургия - Нефрология - Онкология - Организация системы здравоохранения - Оториноларингология - Офтальмология - Патофизиология - Педиатрия - Приборы медицинского назначения - Психиатрия - Психология - Пульмонология - Стоматология - Судебная медицина - Токсикология - Травматология - Фармакология и фармацевтика - Физиология - Фтизиатрия - Хирургия - Эмбриология и гистология - Эпидемиология -