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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 陳俊宏 | |
| dc.contributor.author | Tai-Wei Li | en |
| dc.contributor.author | 李岱威 | zh_TW |
| dc.date.accessioned | 2021-06-13T15:36:11Z | - |
| dc.date.available | 2011-08-12 | |
| dc.date.copyright | 2011-08-12 | |
| dc.date.issued | 2011 | |
| dc.date.submitted | 2011-08-10 | |
| dc.identifier.citation | Babcock, D.T., Brock, A.R., Fish, G.S., Wang, Y., Perrin, L., Krasnow, M.A., and Galko, M.J. (2008). Circulating blood cells function as a surveillance system for damaged tissue in Drosophila larvae. Proc. Natl. Acad. Sci. 105: 10017-10022.
Bache`re,E., Gueguen, Y., Gonzalez M., de Lorgeril, J., Garnier J., and Romestand, B. (2004) Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas. Immunol. Rev. 198: 149–168 Baldini, P.M., De Vito P, D'aquilio.F., Vismara, D., Zalfa, F., Bagni, C., Fiaccavento, R., and Di Nardo, P. (2005). Role of atrial natriuretic peptide in the suppression of lysophosphatydic acid-induced rat aortic smooth muscle (RASM) cell growth. Mol. Cell Biochem. 272: 19-28. Ballarin, L., Cima, F., Floreani, M., and Sabbadin A. (2002 a) Oxidative stress induces cytotoxicity during rejection reaction in the compound ascidian Botryllus schlosseri. Comp. Biochem. Physiol. C Toxicol Pharmacol. 133: 411-418. Ballarin, L., Scanferla, M., Cima, F., and Sabbadin, A. (2002 b) Phagocyte spreading and phagocytosis in the compound ascidian Botryllus schlosseri: evidence for an integrin-like, RGD-dependent recognition mechanism. Dev. Comp. Immunol. 26: 345-354. Bedard, K., and Krause, K-H.(2007). The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology. Physiol Rev. 87: 245–313 Blanco, G.A., Malchiodi, E.L., and De Marzi, M.C. (2008). Cellular clot formation in a sipunculan worm: Entrapment of foreign particles, cell death and identification of a PGRP-related protein. J. Invertebr. Pathol. 99: 156-165. Boehm, T. (2011). Design principles of adaptive immune systems. Nat. Rev. Immunol. 11: 307-317. Bokoch, G.M., and Knaus, U.G. (2003). NADPH oxidases: not just for leukocytes anymore! Trends Biochem. Sci. 28: 502-508. Brandes R.P.,and Kreuzer J.(2005). Vascular NADPH oxidases: molecular mechanisms of activation. Cardiovasc. Res. 65: 16-27. Brown, D.I. and Griendling K.K.(2009). Nox proteins in signal transduction. Free Radic Biol. Med. 47: 1239-1253. Bugge, D.M., Hegaret, H., Wikfors, G.H., and Allam, B. (2007). Oxidative burst in hard clam (Mercenaria mercenaria) haemocytes. Fish & Shellfish Immunology 23: 188-196. Cai, J., Chen, H., Thompson, K.D., and Li, C. (2006). Isolation and identification of Shewanella alga and its pathogenic effects on post-larvae of abalone Haliotis diversicolor supertexta. J. Fish. Dis. 29: 505-508. Cai, J., Chen, H., Thompson, K.D., Li, C., and Han, H. (2007). Isolation and characterization of pathogenic Vibrio parahaemolyticus from diseased post-larvae of abalone Haliotis diversicolor supertexta. J. Basic Microbiol. 47: 84-86. Chen, C.H.(2006). Adenosine-like receptor mediates the intracellular signaling transduction on hemocyte adhesion in abalones (Haliotis diversicolor). Master thesis, National Taiwan University, Taipei. : 13-20. Chen, J.H.(1996). Hemolymph collection in abalone (Haliotis diversicolor). Acta Zoologica. Taiwanica 7: 61-72. Chen, J.H. and Bayne, C.J. (1995). Hemocyte adhesion in California mussel (Mytilus californianus): regulation by adenosine. Biochim. Biophys. Acta. 1268: 178-184. Chen, J.H., Yang, H.Y., Peng, S.W., Chen, Y.J., and Tasi, K.Y. (1996). Characterization of abalone (Haliotis diversicolor) hemocytes in vitro. Biol. Bull. NTNU. 31:31-38. Chiarugi, P., Pani, G., Giannoni, E., Taddei, L., Colavitti, R., Raugei, G., Symons, M., Borrello, S., Galeotti, T., and Ramponi, G.(2003). Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion. J. Cell Biol. 161: 933-944 Cunnick, J.M., Dorsey, J.F., Standley, T., Turkson, J., Kraker, A.J., Fry, D.W., Jove, R., and Wu, J. (1998).Role of tyrosine kinase activity of epidermal growth factor receptor in the lysophosphatidic acid-stimulated mitogen-activated protein kinase pathway. J. Biol. Chem. 273: 14468-14475. D'Autreaux, B., and Toledano, M.B. (2007). ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat. Rev. Mol. Cell Biol. 8: 813-824. de Wit, R., Capello, A., Boonstra, J., Verkleij, A.J., and Post, J.A.(2000) Hydrogen peroxide inhibits epidermal growth factor receptor internalization in human fibroblasts. Free Radic Biol. Med . 28: 28-38. Donaghy, L., Hong, H.-K., Lambert, C., Park, H.-S., Shim, W.J., and Choi, K.-S. (2010). First characterisation of the populations and immune-related activities of hemocytes from two edible gastropod species, the disk abalone, Haliotis discus discus and the spiny top shell, Turbo cornutus. Fish & Shellfish Immunology 28: 87-97. Du, J., Sun, C., Hu, Z., Yang, Y., Zhu, Y., Zheng, D., Gu, L., and Lu, X. (2010) Lysophosphatidic acid induces MDA-MB-231 breast cancer cells migration through activation of PI3K/PAK1/ERK signaling. PLoS One 5: e15940. Engelmann, P., Pal, J., Berki, T., Cooper, E., and Nemeth, P. (2002). Earthworm leukocytes react with different mammalian antigen-specific monoclonal antibodies. Zoology 105: 257-265. Fauvarque, M.O. and Williams, M. J. (2011). Drosophila cellular immunity: a story of migration and adhesion. J. Cell Sci. 124: 1373-1382. Flajnik, M., and Dupasquier, L. (2004). Evolution of innate and adaptive immunity: can we draw a line? Trends in Immunology 25: 640-644. Franc, N.C. (1999). Requirement for Croquemort in Phagocytosis of Apoptotic Cells in Drosophila. Science 284: 1991-1994. Gianni, D., Diaz, B., Taulet, N., Fowler, B., Courtneidge, S.A., and Bokoch, G.M. (2009). Novel p47phox-Related Organizers Regulate Localized NADPH Oxidase 1 (Nox1) Activity. Science Signaling 2: ra54-ra54. Giannoni, E., Taddei, M.L., and Chiarugi, P. (2010). Src redox regulation: again in the front line. Free Radic Biol. Med. 49: 516-527. Gillespie J.P., Kanost M.R. and Trenczek T. (1997) Biological mediators of insect immunity. Annu. Rev. Entomol. 42: 611-643. Gorbushin A.M., Panchin Y.V., and Iakovleva N.V. (2010) In search of the origin of FREPs: characterization of Aplysia californica fibrinogen-related proteins. Dev. Comp. Immunol. 34: 465-467 Hartenstein, Volker. (2006) Blood cells and blood cell development in the animal kingdom. Annu. Rev. Cell Dev. Biol. 22: 677–712 Hattori, H., Subramanian, K.K., Sakai, J., Jia, Y., Li, Y., Porter, T.F., Loison, F., Sarraj, B., Kasorn, A., Jo, H., Blanchard, C., Zirkle, D., McDonald, D., Pai, S.Y., Serhan, C.N., and Hausenloy, D.J. (2004). Ischemic preconditioning protects by activating prosurvival kinases at reperfusion. Am. J. Physiol. Heart Circ. Physiol. 288: 971-976. Jiang, Z., Hu, Z., Zeng, L., Lu, W., Zhang, H., Li, T., and Xiao, H. (2011). The role of the Golgi apparatus in oxidative stress: is this organelle less significant than mitochondria? Free Radic Biol. Med. 50: 907-917. Johansson, M.W., Keyser, P., Sritunyalucksana. K. and So‥derh‥all, K. (2000) Crustacean haemocytes and haematopoiesis. Aquaculture 191: 45-52 Johnson P.T. (1987) A review of fixed phagocytic and pinocytotic cells of decapod crustaceans, with remarks on hemocytes. Dev. Comp. Immunol 11: 609-704. Jomova, K., and Valko, M. (2011). Advances in metal-induced oxidative stress and human disease. Toxicology 283: 65-87. Kuchel R.P., Raftos D.A., Birch D., and Vella N. (2010). Haemocyte morphology and function in the Akoya pearl oyster, Pinctada imbricata. J. Invertebr. Pathol. 105: 36-48 Kvell K., Cooper E.L, Engelmann P, Bovari J,and Nemeth P. (2007). Blurring borders: innate immunity with adaptive features. Clin. Dev. Immunol. 2007: 83671. Kwon, J. (2004). Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc. Natl. Acad. Sci. 101: 16419-16424. Laurila, J.P., Laatikainen, L.E., Castellone, M.D., and Laukkanen, M.O. (2009). SOD3 reduces inflammatory cell migration by regulating adhesion molecule and cytokine production. PLoS One. 4: e5786. Lavine, M.D., and Strand M.R.(2002) Insect hemocytes and their role in immunity. Insect Biochem Mol. Biol. 32: 1295-1309. Le Foll, F., Rioult, D., Boussa, S., Pasquier, J., Dagher, Z., and Leboulenger, F. (2010). Characterisation of Mytilus edulis hemocyte subpopulations by single cell time-lapse motility imaging. Fish & Shellfish Immunol. 28: 372-386. Li, J.M. (2002). Intracellular Localization and Preassembly of the NADPH Oxidase Complex in Cultured Endothelial Cells. J. Biol. Chem. 277: 19952-19960. Liao, C.M. and Chou, B.Y. (2005). Predictive risk thresholds for survival protection of farmed abalone Haliotis diversicolor supertexta exposed to waterborne zinc. Environ Toxicol. 20: 202-211. Liao, C.M., Lin, M.C., Chen, J.S., and Chen, J.W. (2002). Linking biokinetics and consumer-resource dynamic of zinc accumulation in pond abalone Haliotis diversicolor supertexta. Water Res. 36: 5102-12 Ling, E., and Yu, X. (2006). Cellular encapsulation and melanization are enhanced by immulectins, pattern recognition receptors from the tobacco hornworm Manduca sexta. Dev. Comp. Immunol. 30: 289-299. Luo, H.R. (2010). Small-molecule screen identifies reactive oxygen species as key regulators of neutrophil chemotaxis. Proc. Natl. Acad. Sci. 107: 3546-3551. Manea, A. (2010). NADPH oxidase-derived reactive oxygen species: involvement in vascular physiology and pathology. Cell Tissue Res. 342: 325-339. Marmaras, V.J., and Lampropoulou, M. (2009). Regulators and signalling in insect haemocyte immunity. Cellular Signalling 21: 186-195. McKinsey, T.A., and Kass, D.A. (2007) Small-molecule therapies for cardiac hypertrophy: moving beneath the cell surface. Nat. Rev. Drug Discov. 6: 617-635. Meister M., and Lagueux M.(2003) Drosophila blood cells. Cell Microbiol.5: 573-580 Miller, E.W., Dickinson, B.C., and Chang, C.J. (2010) Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling. Proc. Natl. Acad. Sci. 107: 15681-15686. Moreira, S., Stramer, B., Evans, I., Wood, W., and Martin, P. (2010). Prioritization of Competing Damage and Developmental Signals by Migrating Macrophages in the Drosophila Embryo. Curr. Biol. 20: 464-470. Muller, W.E., Koziol, C., Muller, I.M., and Wiens, M. (1999) Towards an understanding of the molecular basis of immune responses in sponges: the marine demosponge Geodia cydonium as a model. Microsc. Res. Tech. 44: 219-236. Munnamalai,V., and Suter, D.M.(2009). Reactive oxygen species regulate F-actin dynamics in neuronal growth cones and neurite outgrowth. J. Neurochem. 108: 644-661. Nakatogawa, S.-i., Oda, Y., Kamiya, M., Kamijima, T., Aizawa, T., Clark, K.D., Demura, M., Kawano, K., Strand, M.R., and Hayakawa, Y. (2009). A Novel Peptide Mediates Aggregation and Migration of Hemocytes from an Insect. Curr. Biol. 19: 779-785. Nambiar M.P., Fisher C.U., Warke V.G., Krishnan S., Mitchell J.P., Delaney N., and Tsokos G.C. (2003). Reconstitution of deficient T cell receptor zeta chain restores T cell signaling and augments T cell receptor/CD3-induced interleukin-2 production in patients with systemic lupus erythematosus. Arthritis Rheum. 48: 1948-55 Niethammer, P., Grabher, C., Look, A.T., and Mitchison, T.J. (2009). A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish. Nature 459: 996-999. Nimnual, A.S., Taylor, L. J., and Bar-Sagi, D. (2003). Redoxdependent downregulation of Rho by Rac. Nat. Cell Biolog. 5: 236–241. Nitti, M., Furfaro, A.L., Cevasco, C., Traverso, N., Marinari, U.M., Pronzato, M.A., and Domenicotti, C. (2010). PKC delta and NADPH oxidase in retinoic acid-induced neuroblastoma cell differentiation. Cellular Signalling 22: 828-835. Owusu-Ansah, E., and Banerjee, U. (2009). Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation. Nature 461: 537-541. Rasmussen, I., Pedersen, L.H., Byg, L., Suzuki, K., Sumimoto, H., and Vilhardt, F. (2010). Effects of F/G-actin ratio and actin turn-over rate on NADPH oxidase activity in microglia. BMC Immunology 11: 44. Ryter S.W., Kim H.P., Hoetzel A., Park J.W., Nakahira K., Wang X., and Choi A.M. (2007). Mechanisms of cell death in oxidative stress. Antioxid. Redox Signal. 9: 49-89 Salzet, M., Tasiemski, A., and Cooper, E.(2006). Innate immunity in Lophotrochozoans: the Annelids. Current Pharmaceutical Design 12: 3043-3050. Schmid-Hempel, P. (2005). Evolutionary Ecology of Insect Immune Defenses. Annual Review of Entomology 50: 529-551. Segal, A.W. (2007). The function of the NADPH oxidase of phagocytes and its relationship to other NOXs in plants, invertebrates, and mammals. Int. J. Biochem. Cell Biol. 40: 604-618. Shandala, T., Woodcock, J.M., Ng, Y., Biggs, L., Skoulakis, E.M.C., Brooks, D.A., and Lopez, A.F. (2011). Drosophila 14-3-3 has a crucial role in anti-microbial peptide secretion and innate immunity. J. Cell Sci. 124: 2165-2174. Shao, D., Segal, A.W., and Dekker, L.V. (2010). Subcellular localisation of the p40phox component of NADPH oxidase involves direct interactions between the Phox homology domain and F-actin. Int. J. Biochem. Cell Biol. 42: 1736-1743. Shinohara, M., Shang, W.H., Kubodera, M., Harada, S., Mitsushita, J., Kato, M., Miyazaki, H., Sumimoto, H., and Kamata, T. (2007). Nox1 Redox Signaling Mediates Oncogenic Ras-induced Disruption of Stress Fibers and Focal Adhesions by Down-regulating Rho. J. Biol. Chem. 282: 17640-17648. Shinohara, M., Adachi, Y., Mitsushita, J., Kuwabara, M., Nagasawa, A., Harada, S., Furuta, S., Zhang, Y., Seheli, K., Miyazaki, H., and Kamata, T. (2009). Reactive oxygen generated by NADPH oxidase 1 (Nox1) contributes to cell invasion by regulating matrix metalloprotease-9 production and cell migration. J. Biol. Chem. 285: 4481-4488 Sideri, M., Tsakas, S., Markoutsa, E., Lampropoulou, M., and Marmaras, V.J. (2008). Innate immunity in insects: surface-associated dopa decarboxylase-dependent pathways regulate phagocytosis, nodulation and melanization in medfly haemocytes. Immunology 123: 528-537. Silva, A., Girio, A., Cebola, I., Santos, CI., Antunes, F., and Barata, J.T. (2011). Intracellular reactive oxygen species are essential for PI3K/Akt/mTOR-dependent IL-7-mediated viability of T-cell acute lymphoblastic leukemia cells. Leukemia. Epub ahead of print . Sminia, T and van der Knaap, W.P.W. (1987). Cell and molecules in mollusan immunology. Develop. Comp. Immunol. 11: 17-28. Van Buul, J.D., Fernandez-Borja, M., Anthony, E.C., and Hordijk, P.L. (2005). Production and localization of NOX2 and NOX4 in primary human endothelial cells. Antioxid Redox Signal. 7: 308-317. van der Knaap, W.P.W., Adema, C.M., and Sminia, T. (1993). Invertebrate Blood Cells: Morphological and Functional Aspects of the Haemocytes in the Pond Snail Lymnaea stagnalis. Comp. Haematol. Int. 3: 20-26. Walker, C., Botter, S.A., Mulkern, J., Jerszyk, E., Litvaitis, M., and Lesser, M.(2009). Mass culture and characterization of tumor cells from a naturally occurring invertebrate cancer model: application for human and animal and environment health. Biol. Bull. 216: 23–39. Wang, Z., Li, Y., and Sarkar FH. (2010). Signaling mechanism(s) of reactive oxygen species in Epithelial-Mesenchymal Transition reminiscent of cancer stem cells in tumor progression. Curr. Stem Cell Res. Ther. 5: 74-80. Winterbourn, C.C., (2008). Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol. 4: 278-286. Wood, W. and Jacinto, A. (2007).Drosophila melanogaster embryonic haemocytes: masters of multitasking. Nat. Rev. Mo.l Cell Biol. 8: 542-551 Wu, W.S., Tsai, R.K., Chang, C.H., Wang, S., Wu, J.R., and Chang, Y.X. (2006). Reactive oxygen species mediated sustained activation of protein kinase C alpha and extracellular signal-regulated kinase for migration of human hepatoma cell Hepg2. Mol. Cancer Res. 4: 747-758. Wu, W.S., Wu, J.R., and Hu, C.T. (2008). Signal cross talks for sustained MAPK activation and cell migration: the potential role of reactive oxygen species. Cancer Metastasis Rev. 27: 303-314. Wu, Y., Brock, A.R., Wang, Y., Fujitani, K., Ueda, R., and Galko, M.J. (2009). A Blood-Borne PDGF/VEGF-like Ligand Initiates Wound-Induced Epidermal Cell Migration in Drosophila Larvae. Curr. Biol. 19: 1473-1477. Yarrow, J.C., Perlman, Z.E., Westwood, N.J. and Mitchison, T.J. (2004). A high-throughput cell migration assay using scratch wound healing, a comparison of image-based readout methods. BMC Biotechnol. 4: 21. Yu X.Q., and Kanost M.R. (2004) Immulectin-2, a pattern recognition receptor that stimulates hemocyte encapsulation and melanization in the tobacco hornworm, Manduca sexta. Dev. Comp. Immunol. 28: 891-900. Zhang, S.M. (2004). Diversification of Ig Superfamily Genes in an Invertebrate. Science 305: 251-254. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/37640 | - |
| dc.description.abstract | 在無脊椎動物中,血液細胞的遷移已經知道會參與在幾個重要的生理功能之中,特別是在防禦時的細胞吞噬或傷口修復過程中的血栓形成及免疫調控等,然而,無脊椎動物細胞遷移過程中的細胞趨化現象跟詳細的調控機制都尚未清楚。在近期的研究中指出,活性氧化物(Reactive oxgen species, ROS)雖會對細胞造成危害,但同時也參與並調控了細胞多種的生理反應。在哺乳動物細胞中,ROS會直接調控癌細胞、神經細胞及內皮細胞等細胞遷移行為,ROS也會調控在斑馬魚傷口周圍免疫細胞的趨化,因此,ROS可能也會參與調控無脊椎動物血球細胞之細胞遷移。本研究發現九孔體內的CD3+血球細胞會表現較高量的ROS,移動速度較快,但移動方向較隨機; 而九孔的類巨嗜細胞則表現較低量的ROS,雖然移動速度較慢,但移動較具方向性。當經由diphenyleneiodonium chloride (DPI)抑制ROS表現時,只有CD3+血球細胞的移動能力受到顯著的抑制,同時也會影響血球細胞之移動分佈。標定細胞製造ROS的NADPH氧化酶,發現氧化酶會集中在CD3+血球細胞的絲狀偽足反側;而在類巨嗜細胞中,NADPH氧化酶則是以點狀分佈在細胞裡。在經由Wortmannin及LY294002抑制血球細胞的PI3K訊息傳遞後,細胞擴散分布及ROS表現都受到明顯的抑制,類似於使用抑制劑降低ROS表現的效用,指出PI3K訊息傳遞與細胞內ROS產生有關。故此,我推論ROS在九孔血球的細胞遷移過程中會經由NADPH氧化酶生成,而主要調控血球細胞內的actin的解構作用,並且經由PI3K訊息傳遞調控。 | zh_TW |
| dc.description.abstract | Hemocyte migration in invertebrates has been known to be involved in several important physiological functions such as phagocytosis and wound healing. In addition to chemotaxis or haptotaxis, the regulatory mechanisms on the cell migration are still needed to be clearly unraveled. In recent studies, reactive oxygen species (ROS) are not only generally considered as threat for cells, but also found as important modulators for some cell behaviors. In mammals, ROS can activate migration in different types of cells including neurons, endothelial cells, and cancer cells. ROS also serves as chemoattractants and stimulators for leukocytes in zebra fish. Therefore, ROS may also play crucial roles in invertebrate hemocyte migration.
In abalone, CD3+ hemocytes perform high ROS production and active cell mobility with random migrating directions, whereas marcophage-like hemocytes are totally different. The results showed that inhibition of ROS production by diphenyleneiodonium chloride (DPI) significantly reduced CD3+ hemocytes mobility, and also affected the spreading of hemocyte monolayer. NADPH oxidase, the main producer of cellular ROS, was apparently located at the opposite site of the filopodia in the migrating CD3+ hemocyte, but distributed as dot pattern in macrophage-like hemocyte. The spreading of cell-layer and production of ROS were both significantly inhibited by PI3K pathway inhibitors, woermannin or LY294002. Due to the effects of depressing PI3K were similar to suppress the production of cellular ROS, these data inferred that PI3K pathway may regulate ROS generation. Therefore, it was suggested that ROS generated by NADPH oxidase should mediate in actin filament assembling during cell migration under the regulation of PI3K pathway in abalone hemocytes. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T15:36:11Z (GMT). No. of bitstreams: 1 ntu-100-R98b41005-1.pdf: 4546681 bytes, checksum: 412b1ab4463d6213c647854718bfd97b (MD5) Previous issue date: 2011 | en |
| dc.description.tableofcontents | Acknowledgement ii
Abstract (Chinese) iii Abstract (English) iv 1. Introduction 1 1.1Cell types of invertebrate hemocytes 1 1.1.1 Macrophage-like hemocyte 1 1.1.2 Natural killer-like, T cell-like, and other types of cells. 2 1.2 The role of hemocyte migration in invertebrate physiology 3 1.3 ROS production in cells 4 1.4 The role of NADPH oxidase in ROS production 4 1.5 ROS directly regulate cell migration 6 1.6 The ROS-related signaling pathways in cell migration 6 1.7 Purpose of this study 7 2. Materials and methods 9 2.1 Animals 9 2.2 Hemolymph collection 9 2.3 Cell culture of hemocyte 10 2.4 Live time-lapse image of hemocytes 10 2.5 Immunocytochemistry 11 2.5.1 CD3 staining 11 2.5.2 Nox1 protein staining 12 2.5.3 Wright’s staining 12 2.5 Immunocytochemistry 13 2.6 Live ROS image of hemocytes 13 2.7 Measurement of the cell-layer spreading rate 13 2.8 Detection the production of cellular ROS 13 2.9 Statistical analysis 14 3. Results 15 3.1 Two cell types in abalone hemocytes 15 3.2 Difference of ROS production and cell migration in two cell types 16 3.3 Effect on cell migration under regulation of ROS 17 3.4 Distribution of NADPH oxidase in abalone hemocyte 18 3.5 Regulation of hemocyte migration by ROS-related pathway 19 4. Disussion 20 4.1 The hemocyte population in abalone 20 4.2 Cellular ROS regulate hemocyte migration 22 5. References 27 6. Figure 36 7. Supplemental data 48 7.1 Production of ROS in cell aggregation 48 7.2 The distribution of Nox1 in cell aggregation 49 7.3 The mechanism of cell aggregation from single hemocyte 50 7.4 Movie data 51 | |
| dc.language.iso | en | |
| dc.subject | 活性氧化物 | zh_TW |
| dc.subject | 細胞遷移 | zh_TW |
| dc.subject | 血球細胞 | zh_TW |
| dc.subject | 九孔 | zh_TW |
| dc.subject | hemocyte | en |
| dc.subject | cell migration | en |
| dc.subject | abalone | en |
| dc.subject | ROS | en |
| dc.title | 活性氧化物調控九孔(Haliotis diversicolor) 血球細胞
之細胞遷移作用 | zh_TW |
| dc.title | Reactive oxygen species regulate hemocyte migration in abalone (Haliotis diversicolor) | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 99-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 李心予,李士傑,廖秀娟 | |
| dc.subject.keyword | 九孔,活性氧化物,血球細胞,細胞遷移, | zh_TW |
| dc.subject.keyword | abalone,ROS,hemocyte,cell migration, | en |
| dc.relation.page | 52 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2011-08-10 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 動物學研究所 | zh_TW |
| 顯示於系所單位: | 動物學研究所 | |
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