請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/82486
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 魏嘉徵(Chia-Cheng Wei) | |
dc.contributor.author | Chia-Tung Wu | en |
dc.contributor.author | 吳家彤 | zh_TW |
dc.date.accessioned | 2022-11-25T07:45:38Z | - |
dc.date.available | 2023-09-03 | |
dc.date.copyright | 2021-09-29 | |
dc.date.issued | 2021 | |
dc.date.submitted | 2021-09-06 | |
dc.identifier.citation | Alexander, A. G., Marfil, V., Li, C. (2014). Use of Caenorhabditis elegans as a model to study Alzheimer’s disease and other neurodegenerative diseases. Front Genet, 5, 279. doi:10.3389/fgene.2014.00279 Allaman, I., Bélanger, M., Magistretti, P. J. (2015). Methylglyoxal, the dark side of glycolysis. Front Neurosci, 9, 23. doi:10.3389/fnins.2015.00023 Allen, R. E., Lo, T. W., Thornalley, P. J. (1993). Purification and characterisation of glyoxalase II from human red blood cells. Eur J Biochem, 213(3), 1261-1267. doi:10.1111/j.1432-1033.1993.tb17877.x Alzheimer's association. (2021). 2021 Alzheimer's disease facts and figures. Alzheimers Dement, 17(3), 327-406. doi:10.1002/alz.12328 Amicarelli, F., Colafarina, S., Cattani, F., Cimini, A., Di Ilio, C., Ceru, M. P., Miranda, M. (2003). Scavenging system efficiency is crucial for cell resistance to ROS-mediated methylglyoxal injury. Free Radic Biol Med, 35(8), 856-871. doi:10.1016/s0891-5849(03)00438-6 Anderson, G. L., Cole, R. D., Williams, P. L. (2004). Assessing behavioral toxicity with Caenorhabditis elegans. Environ Toxicol Chem, 23(5), 1235-1240. doi:10.1897/03-264 Angstman, N. B., Frank, H. G., Schmitz, C. (2016). Advanced behavioral analyses show that the presence of food causes subtle changes in C. elegans movement. Front Behav Neurosci, 10, 60. doi:10.3389/fnbeh.2016.00060 Ansari, M. A., Scheff, S. W. (2010). Oxidative stress in the progression of Alzheimer disease in the frontal cortex. J Neuropathol Exp Neurol, 69(2), 155-167. doi:10.1097/NEN.0b013e3181cb5af4 Arey, R. N., Murphy, C. T. (2017). Conserved regulators of cognitive aging: from worms to humans. Behav Brain Res, 322(Pt B), 299-310. doi:10.1016/j.bbr.2016.06.035 Armstrong, R. A., Winsper, S. J., Blair, J. A. (1995). Hypothesis: is Alzheimer's disease a metal-induced immune disorder? Neurodegener, 4(1), 107-111. doi:10.1006/neur.1995.0013 Arribas-Lorenzo, G., Morales, F. J. (2010). Analysis, distribution, and dietary exposure of glyoxal and methylglyoxal in cookies and their relationship with other heat-induced contaminants. J Agric Food Chem, 58(5), 2966-2972. doi:10.1021/jf902815p Auten, R. L., Davis, J. M. (2009). Oxygen toxicity and reactive oxygen species: the devil is in the details. Pediatr Res, 66(2), 121-127. doi:10.1203/PDR.0b013e3181a9eafb Ayaz, M., Sadiq, A., Junaid, M., Ullah, F., Ovais, M., Ullah, I., Shahid, M. (2019). Flavonoids as prospective neuroprotectants and their therapeutic propensity in aging associated neurological disorders. Front Aging Neurosci, 11, 155. doi:10.3389/fnagi.2019.00155 Ayoub, F. M., Allen, R. E., Thornalley, P. J. (1993). Inhibition of proliferation of human leukaemia 60 cells by methylglyoxal in vitro. Leuk Res, 17(5), 397-401. doi:10.1016/0145-2126(93)90094-2 Barbosa, M. C., Grosso, R. A., Fader, C. M. (2019). Hallmarks of aging: an autophagic perspective. Front Endocrinol, 9, 790. doi:10.3389/fendo.2018.00790 Beisswenger, B. G., Delucia, E. M., Lapoint, N., Sanford, R. J., Beisswenger, P. J. (2005). Ketosis leads to increased methylglyoxal production on the Atkins diet. Ann N Y Acad Sci, 1043, 201-210. doi:10.1196/annals.1333.025 Bhuiyan, M. N., Mitsuhashi, S., Sigetomi, K., Ubukata, M. (2017). Quercetin inhibits advanced glycation end product formation via chelating metal ions, trapping methylglyoxal, and trapping reactive oxygen species. Biosci Biotechnol Biochem, 81(5), 882-890. doi:10.1080/09168451.2017.1282805 Blackwell, T. K., Steinbaugh, M. J., Hourihan, J. M., Ewald, C. Y., Isik, M. (2015). SKN-1/Nrf, stress responses, and aging in Caenorhabditis elegans. Free Radic Biol Med, 88(Pt B), 290-301. doi:10.1016/j.freeradbiomed.2015.06.008 Braidy, N., Behzad, S., Habtemariam, S., Ahmed, T., Daglia, M., Nabavi, S. M., Nabavi, S. F. (2017). Neuroprotective effects of citrus fruit-derived flavonoids, nobiletin and tangeretin in Alzheimer's and Parkinson's disease. CNS Neurol Disord Drug Targets, 16(4), 387-397. doi:10.2174/1871527316666170328113309 Brenner, S. (1974). The genetics of Caenorhabditis elegans. Genetics, 77(1), 71-94. Cai, W., Uribarri, J., Zhu, L., Chen, X., Swamy, S., Zhao, Z., Grosjean, F., Simonaro, C., Kuchel, G. A., Schnaider-Beeri, M., Woodward, M., Striker, G. E., Vlassara, H. (2014). Oral glycotoxins are a modifiable cause of dementia and the metabolic syndrome in mice and humans. Proc Natl Acad Sci U S A, 111(13), 4940-4945. doi: 10.1073/pnas.1316013111. Cai, Z., Hussain, M. D., Yan, L. J. (2014). Microglia, neuroinflammation, and beta-amyloid protein in Alzheimer's disease. Int J Neurosci, 124(5), 307-321. doi:10.3109/00207454.2013.833510 Calabrese, E. J., Baldwin, L. A. (2003). Toxicology rethinks its central belief. Nature, 421(6924), 691-692. doi:10.1038/421691a Caldwell, K. A., Willicott, C. W., Caldwell, G. A. (2020). Modeling neurodegeneration in Caenorhabditis elegans. Dis Model Mech, 13(10). doi:10.1242/dmm.046110 Calixto, A., Jara, J. S., Court, F. A. (2012). Diapause formation and downregulation of insulin-like signaling via DAF-16/FOXO delays axonal degeneration and neuronal loss. PLoS Genet, 8(12), e1003141. doi:10.1371/journal.pgen.1003141 C. elegans Sequencing Consortium. (1998). Genome sequence of the nematode C. elegans: a platform for investigating biology. Science, 282(5396), 2012-2018. doi:10.1126/science.282.5396.2012 Chan, C. M., Huang, D. Y., Huang, Y. P., Hsu, S. H., Kang, L. Y., Shen, C. M., Lin, W. W. (2016). Methylglyoxal induces cell death through endoplasmic reticulum stress-associated ROS production and mitochondrial dysfunction. J Cell Mol Med, 20(9), 1749-1760. doi:10.1111/jcmm.12893 Chang, T., Wang, R., Wu, L. (2005). Methylglyoxal-induced nitric oxide and peroxynitrite production in vascular smooth muscle cells. Free Radic Biol Med, 38(2), 286-293. doi:10.1016/j.freeradbiomed.2004.10.034 Chartier-Harlin, M. C., Crawford, F., Houlden, H., Warren, A., Hughes, D., Fidani, L. (1991). Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene. Nature, 353(6347), 844-846. doi:10.1038/353844a0 Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., Collin, F. (2018). Oxidative stress and the amyloid beta peptide in Alzheimer's disease. Redox Biol, 14, 450-464. doi:10.1016/j.redox.2017.10.014 Choudhary, D., Chandra, D., Kale, R. K. (1997). Influence of methylglyoxal on antioxidant enzymes and oxidative damage. Toxicol Lett, 93(2-3), 141-152. doi:10.1016/s0378-4274(97)00087-8 Christen, Y. (2000). Oxidative stress and Alzheimer disease. Am J Clin Nutr, 71(2), 621S-629S. doi:10.1093/ajcn/71.2.621s Cirmi, S., Ferlazzo, N., Lombardo, G. E., Ventura-Spagnolo, E., Gangemi, S., Calapai, G., Navarra, M. (2016). Neurodegenerative diseases: might citrus flavonoids play a protective role? Molecules, 21(10), 1312. doi:10.3390/molecules21101312 Comber, S. D., Conrad, A. U., Höss, S., Webb, S., Marshall, S. (2006). Chronic toxicity of sediment-associated linear alkylbenzene sulphonates (LAS) to freshwater benthic organisms. Environ Pollut, 144(2), 661-668. doi:10.1016/j.envpol.2005.12.049 Cui, Y., Wu, J., Jung, S. C., Park, D. B., Maeng, Y. H., Hong, J. Y., Eun, S. Y. (2010). Anti-neuroinflammatory activity of nobiletin on suppression of microglial activation. Biol Pharm Bull, 33(11), 1814-1821. doi:10.1248/bpb.33.1814 Culetto, E., Sattelle, D. B. (2000). A role for Caenorhabditis elegans in understanding the function and interactions of human disease genes. Hum Mol Genet, 9(6), 869-877. doi:10.1093/hmg/9.6.869 Currò, M., Risitano, R., Ferlazzo, N., Cirmi, S., Gangemi, C., Caccamo, D., Navarra, M. (2016). Citrus bergamia juice extract attenuates β-amyloid-induced pro-inflammatory activation of THP-1 cells through MAPK and AP-1 pathways. Sci Rep, 6, 20809. doi:10.1038/srep20809 Dafre, A. L., Schmitz, A. E., Maher, P. (2017). Methylglyoxal-induced AMPK activation leads to autophagic degradation of thioredoxin 1 and glyoxalase 2 in HT22 nerve cells. Free Radic Biol Med, 108, 270-279. doi:10.1016/j.freeradbiomed.2017.03.028 Daigle, I., Li, C. (1993). APL-1, a Caenorhabditis elegans gene encoding a protein related to the human beta-amyloid protein precursor. Proc Natl Acad Sci U S A, 90(24), 12045-12049. doi:10.1073/pnas.90.24.12045 Degen, J., Hellwig, M., Henle, T. (2012). 1,2-Dicarbonyl compounds in commonly consumed foods. J Agric Food Chem, 60(28), 7071-7079. doi: 10.1021/jf301306g Delle Monache, S., Sanità, P., Trapasso, E., Ursino, M. R., Dugo, P., Russo, M., Navarra, M. (2013). Mechanisms underlying the anti-tumoral effects of citrus bergamia juice. PLoS One, 8(4), e61484. doi:10.1371/journal.pone.0061484 Deng, Y., Yu, P. H. (1999). Simultaneous determination of formaldehyde and methylglyoxal in urine: involvement of semicarbazide-sensitive amine oxidase-mediated deamination in diabetic complications. J Chromatogr Sci, 37(9), 317-322. doi:10.1093/chromsci/37.9.317 Desai, K. M., Chang, T., Wang, H., Banigesh, A., Dhar, A., Liu, J., Untereiner, A., Wu, L. (2010). Oxidative stress and aging: is methylglyoxal the hidden enemy? Can J Physiol Pharmacol, 88(3), 273-284. doi:10.1139/y10-001 Di Loreto, S., Caracciolo, V., Colafarina, S., Sebastiani, P., Gasbarri, A., Amicarelli, F. (2004). Methylglyoxal induces oxidative stress-dependent cell injury and up-regulation of interleukin-1beta and nerve growth factor in cultured hippocampal neuronal cells. Brain Res, 1006(2), 157-167. doi:10.1016/j.brainres.2004.01.066 Di Penta, A., Moreno, B., Reix, S., Fernandez-Diez, B., Villanueva, M., Errea, O., Villoslada, P. (2013). Oxidative stress and proinflammatory cytokines contribute to demyelination and axonal damage in a cerebellar culture model of neuroinflammation. PLoS One, 8(2), e54722. doi:10.1371/journal.pone.0054722 Distler, M. G., Plant, L. D., Sokoloff, G., Hawk, A. J., Aneas, I., Wuenschell, G. E., Palmer, A. A. (2012). Glyoxalase 1 increases anxiety by reducing GABAA receptor agonist methylglyoxal. J Clin Invest, 122(6), 2306-2315. doi:10.1172/jci61319 Dostal, V., Link, C. D. (2010). Assaying β-amyloid toxicity using a transgenic C. elegans model. J Vis Exp, (44), 2252. doi:10.3791/2252 Drake, J., Link, C. D., Butterfield, D. A. (2003). Oxidative stress precedes fibrillar deposition of Alzheimer's disease amyloid beta-peptide (1-42) in a transgenic Caenorhabditis elegans model. Neurobiol Aging, 24(3), 415-420. doi:10.1016/s0197-4580(02)00225-7 Ejaz, S., Ejaz, A., Matsuda, K., Lim, C. W. (2006). Limonoids as cancer chemopreventive agents. J Chin Chem Soc, 86(3), 339-345. doi:10.1002/jsfa.2396 Fang, C., Gu, L., Smerin, D., Mao, S., Xiong, X. (2017). The interrelation between reactive oxygen species and autophagy in neurological disorders. Oxid Med Cell Longev, 2017, 8495160. doi:10.1155/2017/8495160. Fica-Contreras, S. M., Shuster, S. O., Durfee, N. D., Bowe, G. J. K., Henning, N. J., Hill, S. A., Choi, S. (2017). Glycation of Lys-16 and Arg-5 in amyloid-β and the presence of Cu2+ play a major role in the oxidative stress mechanism of Alzheimer's disease. J Biol Inorg Chem, 22(8), 1211-1222. doi:10.1007/s00775-017-1497-5 Fiory, F., Lombardi, A., Miele, C., Giudicelli, J., Beguinot, F., Van Obberghen, E. (2011). Methylglyoxal impairs insulin signalling and insulin action on glucose-induced insulin secretion in the pancreatic beta cell line INS-1E. Diabetologia, 54(11), 2941-2952. doi:10.1007/s00125-011-2280-8 Florez-McClure, M. L., Hohsfield, L. A., Fonte, G., Bealor, M. T., Link, C. D. (2007). Decreased insulin-receptor signaling promotes the autophagic degradation of beta-amyloid peptide in C. elegans. Autophagy, 3(6), 569-580. doi:10.4161/auto.4776 Gomez-Isla, T., West, H. L., Rebeck, G. W., Harr, S. D., Growdon, J. H., Locascio, J. J., Hyman, B. T. (1996). Clinical and pathological correlates of apolipoprotein E epsilon 4 in Alzheimer's disease. Ann Neurol, 39(1), 62-70. doi:10.1002/ana.410390110 Gonzalez, F. J. (1988). The molecular biology of cytochrome P450s. Pharmacol Rev, 40(4), 243-288. Gruber, J., Schaffer, S., Halliwell, B. (2008). The mitochondrial free radical theory of ageing--where do we stand? Front Biosci, 13, 6554-6579. doi:10.2741/3174 Guntern, R., Bouras, C., Hof, P. R., Vallet, P. G. (1992). An improved thioflavine S method for staining neurofibrillary tangles and senile plaques in Alzheimer’s disease. Experientia, 48, 8-10. doi:10.1007/BF01923594. Gutierrez-Zepeda, A., Santell, R., Wu, Z., Brown, M., Wu, Y. J., Khan, I., Luo, Y. (2005). Soy isoflavone glycitein protects against beta amyloid-induced toxicity and oxidative stress in transgenic Caenorhabditis elegans. BMC Neurosci, 6(1), 54. doi:10.1186/1471-2202-6-54 Hansen, F., Pandolfo, P., Galland, F., Torres, F. V., Dutra, M. F., Batassini, C., Guerra, M. C., Leite, M. C., Gonçalves, C. A. (2016). Methylglyoxal can mediate behavioral and neurochemical alterations in rat brain. Physiol Behav, 164(Pt A), 93-101. doi: 10.1016/j.physbeh.2016.05.046 Heimfarth, L., Loureiro, S. O., Pierozan, P., de Lima, B. O., Reis, K. P., Torres, E. B., Pessoa-Pureur, R. (2013). Methylglyoxal-induced cytotoxicity in neonatal rat brain: a role for oxidative stress and MAP kinases. Metab Brain Dis, 28(3), 429-438. doi:10.1007/s11011-013-9379-1 Herrup, K. (2010). Reimagining Alzheimer's disease--an age-based hypothesis. J Neurosci, 30(50), 16755-16762. doi:10.1523/jneurosci.4521-10.2010 Hoogewijs, D., Houthoofd, K., Matthijssens, F., Vandesompele, J., Vanfleteren, J. R. (2008). Selection and validation of a set of reliable reference genes for quantitative sod gene expression analysis in C. elegans. BMC Mol Biol, 9(1), 1-8. doi:10.1186/1471-2199-9-9 Hopper, D. J., Cooper, R. A. (1971). The regulation of Escherichia coli methylglyoxal synthase: a new control site in glycolysis? FEBS Lett, 13(4), 213-216. doi:10.1016/0014-5793(71)80538-0 Hoque, T. S., Uraji, M., Hoque, M. A., Nakamura, Y., Murata, Y. (2017). Methylglyoxal induces inhibition of growth, accumulation of anthocyanin, and activation of glyoxalase I and II in Arabidopsis thaliana. J Biochem Mol Toxicol, 31(7), e21901. doi:10.1002/jbt.21901 Horvitz, H. R., Chalfie, M., Trent, C., Sulston, J. E., Evans, P. D. (1982). Serotonin and octopamine in the nematode Caenorhabditis elegans. Science, 216(4549), 1012-1014. doi:10.1126/science.6805073 Huang, C. W., Li, S. W., Liao, V. H C. (2017). Chronic ZnO-NPs exposure at environmentally relevant concentrations results in metabolic and locomotive toxicities in Caenorhabditis elegans. Environ Pollut, 220(Pt B), 1456-1464. doi:10.1016/j.envpol.2016.10.086 Huang, X., Wang, F., Chen, W., Chen, Y., Wang, N., von Maltzan, K. (2012). Possible link between the cognitive dysfunction associated with diabetes mellitus and the neurotoxicity of methylglyoxal. Brain Res, 1469, 82-91. doi:10.1016/j.brainres.2012.06.011 International Agency for Research on Cancer. (1991). Coffee, tea, mate, methylxanthines and methylglyoxal. IARC working group on the evaluation of carcinogenic risks to humans, Lyon, 27 February to 6 March 1990. IARC Monogr Eval Carcinog Risks Hum, 51, 1-513. Iqbal, K., Liu, F., Gong, C. X., Grundke-Iqbal, I. (2010). Tau in Alzheimer disease and related tauopathies. Curr Alzheimer Res, 7(8), 656-664. doi:10.2174/156720510793611592 Kaletta, T., Hengartner, M. O. (2006). Finding function in novel targets: C. elegans as a model organism. Nat Rev Drug Discov, 5(5), 387-398. doi:10.1038/nrd2031 Kanda, K., Nishi, K., Kadota, A., Nishimoto, S., Liu, M. C., Sugahara, T. (2012). Nobiletin suppresses adipocyte differentiation of 3T3-L1 cells by an insulin and IBMX mixture induction. Biochim Biophys Acta, 1820(4), 461-468. doi:10.1016/j.bbagen.2011.11.015 Kang, J. H. (2003). Oxidative damage of DNA by the reaction of amino acid with methylglyoxal in the presence of Fe(III). Int J Biol Macromol, 33(1), 43-48. doi:10.1016/S0141-8130(03)00064-3 Kang, J., Lemaire, H. G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K. H., Müller-Hill, B. (1987). The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature, 325(6106), 733-736. doi:10.1038/325733a0 Kaur, S., DasGupta, G., Singh, S. (2019). Altered neurochemistry in Alzheimer’s disease: targeting neurotransmitter receptor mechanisms and therapeutic strategy. Neurophysiology, 51(4), 293-309. doi:10.1007/s11062-019-09823-7 Kay, A. J., Hunter, C. P. (2001). CDC-42 regulates PAR protein localization and function to control cellular and embryonic polarity in C. elegans. Curr Biol, 11(7), 474-481. doi:10.1016/S0960-9822(01)00141-5 Kikuchi, S., Shinpo, K., Moriwaka, F., Makita, Z., Miyata, T., Tashiro, K. (1999). Neurotoxicity of methylglyoxal and 3-deoxyglucosone on cultured cortical neurons: synergism between glycation and oxidative stress, possibly involved in neurodegenerative diseases. J Neurosci Res, 57(2), 280-289. doi:10.1002/(sici)1097-4547(19990715)57:2<280::Aid-jnr14>3.0.Co;2-u Kim, J., Kim, N. H., Sohn, E., Kim, C. S., Kim, J. S. (2010). Methylglyoxal induces cellular damage by increasing argpyrimidine accumulation and oxidative DNA damage in human lens epithelial cells. Biochem Biophys Res Commun, 391(1), 346-351. doi:10.1016/j.bbrc.2009.11.061 Koop, D. R., Casazza, J. P. (1985). Identification of ethanol-inducible P-450 isozyme 3a as the acetone and acetol monooxygenase of rabbit microsomes. J Biol Chem, 260(25), 13607-13612. Kuhla, B., Boeck, K., Schmidt, A., Ogunlade, V., Arendt, T., Münch, G., Lüth, H. J. (2007). Age- and stage-dependent glyoxalase I expression and its activity in normal and Alzheimer's disease brains. Neurobiol Aging, 28(1), 29-41. doi:10.1016/j.neurobiolaging.2005.11.007 Kumar, S., Pandey, A. K. (2013). Chemistry and biological activities of flavonoids: an overview. Sci World J, 2013, 162750. doi:10.1155/2013/162750 Lai, M. K., Tsang, S. W., Alder, J. T., Keene, J., Hope, T., Esiri, M. M., Chen, C. P. (2005). Loss of serotonin 5-HT2A receptors in the postmortem temporal cortex correlates with rate of cognitive decline in Alzheimer’s disease. Psychopharmacol, 179(3), 673-677. doi:10.1007/s00213-004-2077-2 Lee, Y. C., Cheng, T. H., Lee, J. S., Chen, J. H., Liao, Y. C., Fong, Y., Shih, Y. W. (2011). Nobiletin, a citrus flavonoid, suppresses invasion and migration involving FAK/PI3K/Akt and small GTPase signals in human gastric adenocarcinoma AGS cells. Mol Cell Biochem, 347(1-2), 103-115. doi:10.1007/s11010-010-0618-z Lee, Y. S., Cha, B. Y., Saito, K., Yamakawa, H., Choi, S. S., Yamaguchi, K., Woo, J. T. (2010). Nobiletin improves hyperglycemia and insulin resistance in obese diabetic ob/ob mice. Biochem Pharmacol, 79(11), 1674-1683. doi:10.1016/j.bcp.2010.01.034 Levitan, D., Greenwald, I. (1995). Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature, 377(6547), 351-354. doi:10.1038/377351a0 Li, G., Zheng, L., Chen, C., Liu, X., Zhang, W. (2019). Brain senescence caused by elevated levels of reactive metabolite methylglyoxal on D-galactose-induced aging mice. Front Neurosci, 13, 1004. doi:10.3389/fnins.2019.01004 Lim, J., Luderer, U. (2011). Oxidative damage increases and antioxidant gene expression decreases with aging in the mouse ovary. Biol Reprod, 84(4), 775-782. doi:10.1095/biolreprod.110.088583 Li, X., Greenwald, I. (1997). HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling. Proc Natl Acad Sci U S A, 94(22), 12204-12209. doi:10.1073/pnas.94.22.12204 Li, X. H., Du, L. L., Cheng, X. S., Jiang, X., Zhang, Y., Lv, B. L., Zhou, X. W. (2013). Glycation exacerbates the neuronal toxicity of β-amyloid. Cell Death Dis, 4(6), e673-e673. doi:10.1038/cddis.2013.180 Libina, N., Berman, J. R., Kenyon, C. (2003). Tissue-specific activities of C. elegans DAF-16 in the regulation of lifespan. Cell, 115(4), 489-502. doi:10.1016/s0092-8674(03)00889-4 Liguori, I., Russo, G., Curcio, F., Bulli, G., Aran, L., Della-Morte, D., Abete, P. (2018). Oxidative stress, aging, and diseases. Clin Interv Aging, 13, 757-772. doi:10.2147/CIA.S158513 Link, C. D. (1995). Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans. Proc Natl Acad Sci U S A, 92(20), 9368-9372. doi:10.1073/pnas.92.20.9368 Link, C. D. (2006). C. elegans models of age-associated neurodegenerative diseases: lessons from transgenic worm models of Alzheimer's disease. Exp Gerontol, 41(10), 1007-1013. doi:10.1016/j.exger.2006.06.059 Link, C. D., Taft, A., Kapulkin, V., Duke, K., Kim, S., Fei, Q., Sahagan, B. G. (2003). Gene expression analysis in a transgenic Caenorhabditis elegans Alzheimer's disease model. Neurobiol Aging, 24(3), 397-413. doi:10.1016/s0197-4580(02)00224-5 Lo, C. Y., Hsiao, W. T., Chen, X. Y. (2011). Efficiency of trapping methylglyoxal by phenols and phenolic acids. J Food Sci, 76(3), H90-96. doi:10.1111/j.1750-3841.2011.02067.x Lubitz, I., Ricny, J., Atrakchi-Baranes, D., Shemesh, C., Kravitz, E., Liraz-Zaltsman, S., Maksin-Matveev, A., Cooper, I., Leibowitz, A., Uribarri, J., Schmeidler, J., Cai, W., Kristofikova, Z., Ripova, D., LeRoith, D., Schnaider-Beeri, M. (2016). High dietary advanced glycation end products are associated with poorer spatial learning and accelerated Aβ deposition in an Alzheimer mouse model. Aging cell, 15(2), 309-316. doi: 10.1111/acel.12436 Lushchak, V. I. (2014). Free radicals, reactive oxygen species, oxidative stress and its classification. Chem Biol Interact, 224, 164-175. doi:10.1016/j.cbi.2014.10.016 Lüth, H. J., Ogunlade, V., Kuhla, B., Kientsch-Engel, R., Stahl, P., Webster, J., Münch, G. (2005). Age- and stage-dependent accumulation of advanced glycation end products in intracellular deposits in normal and Alzheimer's disease brains. Cereb Cortex, 15(2), 211-220. doi:10.1093/cercor/bhh123 Maher, P. (2012). Methylglyoxal, advanced glycation end products and autism: is there a connection? Med Hypotheses, 78(4), 548-552. doi:10.1016/j.mehy.2012.01.032 Manach, C., Scalbert, A., Morand, C., Rémésy, C., Jiménez, L. (2004). Polyphenols: food sources and bioavailability. Am J Clin Nutr, 79(5), 727-747. doi: 10.1093/ajcn/79.5.727 Manoharan, S., Guillemin, G. J., Abiramasundari, R. S., Essa, M. M., Akbar, M., Akbar, M. D. (2016). The role of reactive oxygen species in the pathogenesis of Alzheimer's disease, Parkinson's disease, and Huntington's disease: a mini review. Oxid Med Cell Longev, 2016, 8590578. doi:10.1155/2016/8590578 Markesbery, W. R. (1997). Oxidative stress hypothesis in Alzheimer's disease. Free Radic Biol Med, 23(1), 134-147. doi:10.1016/s0891-5849(96)00629-6 Markesbery, W. R. (1999). The role of oxidative stress in Alzheimer disease. Arch Neurol, 56(12), 1449-1452. doi:10.1001/archneur.56.12.1449 Matsuzaki, K., Yamakuni, T., Hashimoto, M., Haque, A. M., Shido, O., Mimaki, Y., Ohizumi, Y. (2006). Nobiletin restoring beta-amyloid-impaired CREB phosphorylation rescues memory deterioration in Alzheimer's disease model rats. Neurosci Lett, 400(3), 230-234. doi:10.1016/j.neulet.2006.02.077 McColl, G., Rogers, A. N., Alavez, S., Hubbard, A. E., Melov, S., Link, C. D., Lithgow, G. J. (2010). Insulin-like signaling determines survival during stress via posttranscriptional mechanisms in C. elegans. Cell Metab, 12(3), 260-272. doi:10.1016/j.cmet.2010.08.004 Medeiros, M. L., de Oliveira, M. G., Tavares, E. G., Mello, G. C., Anhê, G. F., Mónica, F. Z., Antunes, E. (2020). Long-term methylglyoxal intake aggravates murine Th2-mediated airway eosinophil infiltration. Int Immunopharmacol, 81, 106254. doi:10.1016/j.intimp.2020.106254 Melendez, A., Levined, B. (2009). Autophagy in C. elegans. WormBook: the online review of C. elegans biology, 1-26. doi:10.1895/wormbook.1.147.1 Middleton Jr, E., Kandaswami, C., Theoharides, T. C. (2000). The effects of plant flavonoids on mammalian cells: implications for inflammation, heart disease, and cancer. Pharmacol Rev, 52(4), 673-751. Moore, B. T., Jordan, J. M., Baugh, L. R. (2013). WormSizer: high-throughput analysis of nematode size and shape. PLoS One, 8(2), e57142. doi:10.1371/journal.pone.0057142 Nakajima, A., Aoyama, Y., Shin, E. J., Nam, Y., Kim, H. C., Nagai, T., Yamada, K. (2015). Nobiletin, a citrus flavonoid, improves cognitive impairment and reduces soluble Aβ levels in a triple transgenic mouse model of Alzheimer's disease (3XTg-AD). Behav Brain Res, 289, 69-77. doi:10.1016/j.bbr.2015.04.028 Nakajima, A., Ohizumi, Y. (2019). Potential benefits of nobiletin, A citrus flavonoid, against Alzheimer's disease and Parkinson's disease. Int J Mol Sci, 20(14). doi:10.3390/ijms20143380 Nemet, I., Varga-Defterdarović, L., Turk, Z. (2006). Methylglyoxal in food and living organisms. Mol Nutr Food Res, 50(12), 1105-1117. doi:10.1002/mnfr.200600065 Nigro, C., Leone, A., Fiory, F., Prevenzano, I., Nicolò, A., Mirra, P., Miele, C. (2019). Dicarbonyl stress at the crossroads of healthy and unhealthy aging. Cells, 8(7), 749. doi:10.3390/cells8070749 NIH, National Library of Medicine, National Center for Biotechnology Information. (2021). PubChem compound summary for CID 880, methylglyoxal. Data acquired: 6/5/2021. Retrieved from https://pubchem.ncbi.nlm.nih.gov/compound/Methylglyoxal Nowotny, K., Jung, T., Höhn, A., Weber, D., Grune, T. (2015). Advanced glycation end products and oxidative stress in type 2 diabetes mellitus. Biomolecules, 5(1), 194-222. doi:10.3390/biom5010194 Oliveira, M. G. de., Medeiros, M. L. de., Tavares, E. B. G., Mónica, F. Z., Antunes, E. (2020). Methylglyoxal, a reactive glucose metabolite, induces bladder overactivity in addition to inflammation in mice. Front Physiol, 11, 290. doi:10.3389/fphys.2020.00290 Onozuka, H., Nakajima, A., Matsuzaki, K., Shin, R. W., Ogino, K., Saigusa, D., Ohizumi, Y. (2008). Nobiletin, a citrus flavonoid, improves memory impairment and Abeta pathology in a transgenic mouse model of Alzheimer's disease. J Pharmacol Exp Ther, 326(3), 739-744. doi:10.1124/jpet.108.140293 Pacher, P., Beckman, J. S., Liaudet, L. (2007). Nitric oxide and peroxynitrite in health and disease. Physiol Rev, 87(1), 315-424. doi:10.1152/physrev.00029.2006 Palmisano, N. J., Meléndez, A. (2019). Autophagy in C. elegans development. Dev Biol, 447(1), 103-125. doi:10.1016/j.ydbio.2018.04.009 Panza, F., Lozupone, M., Logroscino, G., Imbimbo, B. P. (2019). A critical appraisal of amyloid-β-targeting therapies for Alzheimer disease. Nat Rev Neurol, 15(2), 73-88. doi:10.1038/s41582-018-0116-6 Pickford, F., Masliah, E., Britschgi, M., Lucin, K., Narasimhan, R., Jaeger, P. A., Wyss-Coray, T. (2008). The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice. J Clin Invest, 118(6), 2190-2199. doi:10.1172/jci33585 Pietrzak, R. H., Lim, Y. Y., Neumeister, A., Ames, D., Ellis, K. A., Harrington, K. (2015). Amyloid-β, anxiety, and cognitive decline in preclinical Alzheimer disease: a multicenter, prospective cohort study. JAMA Psychiatry, 72(3), 284-291. doi:10.1001/jamapsychiatry.2014.2476 Porta-de-la-Riva, M., Fontrodona, L., Villanueva, A., Cerón, J. (2012). Basic Caenorhabditis elegans methods: synchronization and observation. J Vis Exp, (64), e4019. doi:10.3791/4019 Rabie, E., Serem, J. C., Oberholzer, H. M., Gaspar, A. R. M., Bester, M. J. (2016). How methylglyoxal kills bacteria: an ultrastructural study. Ultrastruct Pathol, 40(2), 107-11. doi:10.3109/01913123.2016.1154914. Rahman, M. A., Rahman, M. H., Biswas, P., Hossain, M. S., Islam, R., Hannan, M. A., Rhim, H. (2020). Potential therapeutic role of phytochemicals to mitigate mitochondrial dysfunctions in Alzheimer's disease. Antioxidants, 10(1). doi:10.3390/antiox10010023 Ravichandran, M., Priebe, S., Grigolon, G., Rozanov, L., Groth, M., Laube, B., Ristow, M. (2018). Impairing L-threonine catabolism promotes healthspan through methylglyoxal-mediated proteohormesis. Cell Metab, 27(4), 914-925. doi:10.1016/j.cmet.2018.02.004 Regitz, C., Dußling, L. M., Wenzel, U. (2014). Amyloid-beta (Aβ₁₋₄₂)-induced paralysis in Caenorhabditis elegans is inhibited by the polyphenol quercetin through activation of protein degradation pathways. Mol Nutr Food Res, 58(10), 1931-1940. doi:10.1002/mnfr.201400014 Riboulet-Chavey, A., Pierron, A., Durand, I., Murdaca, J., Giudicelli, J., Van Obberghen, E. (2006). Methylglyoxal impairs the insulin signaling pathways independently of the formation of intracellular reactive oxygen species. Diabetes, 55(5), 1289-1299. doi:10.2337/db05-0857 Richard, J. P. (1993). Mechanism for the formation of methylglyoxal from triosephosphates. Biochem Soc Trans, 21(2), 549-553. doi:10.1042/bst0210549 Ross, C. A., Poirier, M. A. (2004). Protein aggregation and neurodegenerative disease. Nat. Med, 10(7), S10-S17. doi:10.1038/nm1066 Sanz, N., Díez-Fernández, C., Andrés, D., Cascales, M. (2002). Hepatotoxicity and aging: endogenous antioxidant systems in hepatocytes from 2-, 6-, 12-, 18- and 30-month-old rats following a necrogenic dose of thioacetamide. Biochim Biophys Acta, 1587(1), 12-20. doi:10.1016/s0925-4439(02)00048-0 Sato, J., Wang, Y. M., van Eys, J. (1980). Methylglyoxal formation in rat liver cells. J Biol Chem, 255(5), 2046-2050. Saul, N., Baberschke, N., Chakrabarti, S., Stürzenbaum, S. R., Lieke, T., Menzel, R., Steinberg, C. E. (2014). Two organobromines trigger lifespan, growth, reproductive and transcriptional changes in Caenorhabditis elegans. Environ Sci Pollut Res Int, 21(17), 10419-10431. doi:10.1007/s11356-014-2932-6 Sawin, E. R., Ranganathan, R., Horvitz, H. R. (2000). C. elegans locomotory rate is modulated by the environment through a dopaminergic pathway and by experience through a serotonergic pathway. Neuron, 26(3), 619-631. doi:10.1016/s0896-6273(00)81199-x Seo, H. W., Cheon, S. M., Lee, M. H., Kim, H. J., Jeon, H., Cha, D. S. (2015). Catalpol modulates lifespan via DAF-16/FOXO and SKN-1/Nrf2 activation in Caenorhabditis elegans. Evid Based Complement Alternat Med, 2015, 524878. doi:10.1155/2015/524878 Shao, X., Chen, H., Zhu, Y., Sedighi, R., Ho, C. T., Sang, S. (2014). Essential structural requirements and additive effects for flavonoids to scavenge methylglyoxal. J Agric Food Chem, 62(14), 3202-3210. doi:10.1021/jf500204s Skovronsky, D. M., Lee, V. M. Y., Trojanowski, J. Q. (2006). Neurodegenerative diseases: new concepts of pathogenesis and their therapeutic implications. Annu Rev Pathol, 1(1), 151-170. doi:10.1146/annurev.pathol.1.110304.100113 Smith, M. A., Taneda, S., Richey, P. L., Miyata, S., Yan, S. D., Stern, D., Perry, G. (1994). Advanced Maillard reaction end products are associated with Alzheimer disease pathology. Proc Natl Acad Sci U S A, 91(12), 5710-5714. doi:10.1073/pnas.91.12.5710 Song, S., Zhang, X., Wu, H., Han, Y., Zhang, J., Ma, E., Guo, Y. (2014). Molecular basis for antioxidant enzymes in mediating copper detoxification in the nematode Caenorhabditis elegans. PLoS One, 9(9), e107685. doi:10.1371/journal.pone.0107685 Sulston, J. E., Horvitz, H. R. (1977). Post-embryonic cell lineages of the nematode, Caenorhabditis elegans. Dev Biol, 56(1), 110-156. doi:10.1016/0012-1606(77)90158-0 Sun, X., Chen, W. D., Wang, Y. D. (2017). DAF-16/FOXO transcription factor in aging and longevity. Front Pharmacol, 8, 548. doi:10.3389/fphar.2017.00548 Szczepanik, J. C., de Almeida, G. R. L., Cunha, M. P., Dafre, A. L. (2020). Repeated methylglyoxal treatment depletes dopamine in the prefrontal cortex, and causes memory impairment and depressive-like behavior in mice. Neurochem Res, 45(2), 354-370. doi:10.1007/s11064-019-02921-2 Tajes, M., Eraso-Pichot, A., Rubio-Moscardó, F., Guivernau, B., Ramos-Fernández, E., Bosch-Morató, M., Muñoz, F. J. (2014). Methylglyoxal produced by amyloid-β peptide-induced nitrotyrosination of trio……… | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/82486 | - |
dc.description.abstract | "甲基乙二醛 (methylglyoxal, MG) 是一種具有高度活性的α-雙羰基化合物 (α-dicarbonyl compound),隨著其逐漸累積,會產生糖化終產物 (advanced glycation end products, AGEs),進而改變生物體內蛋白質之正常結構及功能。阿茲海默症是一種常見的神經退化性疾病,其症狀包含記憶力喪失、認知障礙及行為脫序等。過去MG之相關研究主要針對生物體的老化及糖尿病為主題作探討,而在生物體內對阿茲海默症病徵及相關機制之研究則相對較少。故本篇研究將利用秀麗隱桿線蟲 (Caenorhabditis elegans) 作為評估阿茲海默症之模式生物,並探討暴露MG後對阿茲海默症毒性效應之影響,及進而造成的生物體損傷。 研究結果發現,暴露於0.05、0.1、0.5及1 mM MG並不會影響C. elegans之體長,而其中0.1、0.5及1 mM MG卻能顯著影響C. elegans之運動行為表現,顯示在上述濃度下MG具有神經毒性。而在轉基因種C. elegans CL4176以及C. elegans CL2006的癱瘓試驗中,無論暴露於0.1或0.5 mM MG與控制組相比,皆能顯著加速C. elegans的癱瘓速率。同時實驗發現C. elegans CL2006體內不正常類澱粉蛋白 (amyloid-β peptide1-42, Aβ1-42) 在0.5 mM MG誘導下,能顯著增加其數量和聚集程度;同樣也觀察到其體內活性氧物質 (reactive oxygen species, ROS) 顯著增加。另外,轉基因種C. elegans CL2355可透過溫度上調使其神經細胞大量表達Aβ1-42,於血清素敏感試驗中暴露0.5 mM MG亦能觀察到其運動行為受損,顯示暴露上述濃度下,不僅提升Aβ1-42蛋白累積、ROS及降低活動能力,也會造成神經毒性效應。進而深入探討暴露0.5 mM MG對於生物體內抗氧化及自噬作用相關基因mRNA表達之影響,發現C. elegans wild-type N2暴露MG至成蟲第2天時,其體內抗氧化skn-1及gst-4基因和自噬作用bec-1基因表達量皆顯著上升;至成蟲第8天,與抗氧化相關sod-3、gst-4及hsp-16.2或與自噬作用相關lgg-1基因表達量皆顯著降低;而轉基因種C. elegans CL2006在暴露MG至成蟲第2天時,其體內自噬作用vps-34基因表達量顯著下降;至成蟲第8天時,自噬作用相關lgg-1及bec-1基因表達量皆顯著高於控制組。另外,若同時介入化合物川陳皮素 (nobiletin, NOB),則能顯著延緩C. elegans因MG誘導所增加的癱瘓速率。 綜合本研究之實驗結果,發現長期暴露於MG會促進C. elegans阿茲海默症相關病徵,並影響與抗氧化及自噬作用相關基因之表達,加速神經毒性效應,而介入NOB可減緩MG所誘導的阿茲海默症毒性效應。" | zh_TW |
dc.description.provenance | Made available in DSpace on 2022-11-25T07:45:38Z (GMT). No. of bitstreams: 1 U0001-0309202114333000.pdf: 2667243 bytes, checksum: f158d15d545b59a7084077d2e89ea27f (MD5) Previous issue date: 2021 | en |
dc.description.tableofcontents | "碩士學位論文口試委員會審定書 i 誌謝 ii 摘要 iii Abstract v Graphic abstract vii Highlights viii 目錄 ix 圖次 xii 表次 xiii 1. 研究動機 1 2. 文獻回顧 3 2.1 甲基乙二醛 (methylglyoxal, MG) 3 2.1.1 MG物化性質 3 2.1.2 內生性與外源性來源 4 2.1.3 生物體代謝 5 2.1.4 對於生物體之毒性 6 2.2 神經退化性疾病 7 2.2.1 失智症與阿茲海默症 (Alzheimer’s disease, AD) 之進程 7 2.2.2 AD之成因與危險因子 8 2.2.3 類澱粉蛋白斑塊累積與氧化壓力 8 2.3 柑橘類水果之機能性成分 9 2.3.1 多甲氧基類黃酮-川陳皮素 (nobiletin, NOB) 9 2.4 秀麗隱桿線蟲 (Caenorhabditis elegans) 10 2.4.1 C. elegans 10 2.4.2 以C. elegans探討AD 11 2.4.3 C. elegans抗氧化與自噬作用分子調控機制 12 2.5 研究目的 13 3. 材料方法 15 3.1 實驗架構 15 3.2 實驗材料 16 3.2.1 藥品試劑 16 3.2.2 C. elegans品系與培養條件 16 3.3 實驗方法 17 3.3.1 MG對C. elegans生長發育毒性測試 17 3.3.2 MG對C. elegans運動行為毒性測試 17 3.3.3 MG對C. elegans癱瘓試驗 17 3.3.4 Aβ1-42蛋白螢光染色與定量 18 3.3.5 MG對C. elegans體內活性氧物質 (ROS) 定量試驗 19 3.3.6 MG對C. elegans血清素敏感試驗 19 3.3.7 定量即時聚合酶鏈鎖反應 (qRT-PCR) 分析試驗 20 3.3.8 NOB減緩C. elegans癱瘓試驗 20 3.3.9 統計分析 21 4. 結果與討論 22 4.1 暴露MG對C. elegans生長發育之影響 22 4.2 暴露MG對C. elegans運動行為之影響 24 4.3 暴露MG對C. elegans癱瘓行為之影響 27 4.4 暴露MG對C. elegans體內Aβ1-42蛋白之影響 30 4.5 暴露MG對C. elegans血清素敏感度之影響 34 4.6 暴露MG對C. elegans體內ROS之影響 36 4.7 暴露MG對C. elegans抗氧化與自噬作用相關基因表達之影響 38 4.8 NOB對MG誘導C. elegans癱瘓行為之功效 43 5. 結論 46 6. 建議 47 7. 參考文獻 48 8. 附錄 70 附錄一、MG對E. coli OP50生長之影響 70 附錄二、暴露MG對C. elegans CL2006不同天數癱瘓行為之比較 72 附錄三、暴露MG對C. elegans抗氧化與自噬作用相關基因表達隨老化之影響 73 " | |
dc.language.iso | zh-TW | |
dc.title | 以秀麗隱桿線蟲為模式探討甲基乙二醛誘導阿茲海默症之毒性效應 | zh_TW |
dc.title | Evaluation of Methylglyoxal Enhanced Alzheimer’s Disease Toxicity in Caenorhabditis elegans | en |
dc.date.schoolyear | 109-2 | |
dc.description.degree | 碩士 | |
dc.contributor.coadvisor | 潘敏雄(Min-Hsiung Pan) | |
dc.contributor.oralexamcommittee | 何元順(Hsin-Tsai Liu),洪偉倫(Chih-Yang Tseng) | |
dc.subject.keyword | 阿茲海默症,類澱粉蛋白,氧化壓力,甲基乙二醛,秀麗隱桿線蟲,川陳皮素,自噬作用, | zh_TW |
dc.subject.keyword | Alzheimer’s disease,Amyloid-β,Oxidative stress,Methylglyoxal,Caenorhabditis elegans,Nobiletin,Autophagy, | en |
dc.relation.page | 74 | |
dc.identifier.doi | 10.6342/NTU202102976 | |
dc.rights.note | 同意授權(限校園內公開) | |
dc.date.accepted | 2021-09-07 | |
dc.contributor.author-college | 公共衛生學院 | zh_TW |
dc.contributor.author-dept | 食品安全與健康研究所 | zh_TW |
dc.date.embargo-lift | 2023-09-03 | - |
顯示於系所單位: | 食品安全與健康研究所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
U0001-0309202114333000.pdf 授權僅限NTU校內IP使用(校園外請利用VPN校外連線服務) | 2.6 MB | Adobe PDF | 檢視/開啟 |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。