請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/29721
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 陳俊宏(Jiun-Hong Chen) | |
dc.contributor.author | Chia-Hua Chen | en |
dc.contributor.author | 陳家嬅 | zh_TW |
dc.date.accessioned | 2021-06-13T01:16:11Z | - |
dc.date.available | 2007-07-23 | |
dc.date.copyright | 2007-07-23 | |
dc.date.issued | 2007 | |
dc.date.submitted | 2007-07-17 | |
dc.identifier.citation | Ali, K., Bilancio, A., Thomas, M., Pearce, W., Gilfillan, A.M., Tkaczyk, C., Kuehn, N., Gray, A., Giddings, J., Peskett, E., Fox, R., Bruce, I., Walker, C., Sawyer, C., Okkenhaug, K., Finan, P., and Vanhaesebroeck, B. (2004). Essential role for the p110ζ phosphoinositide 3-kinase in the allergic response. Nature 431:1007-1011.
Asako, H., Wolf, R.E., and Granger, D.N. (1993). Leukocyte adherence in rat mesenteric venules: effects of adenosine and methotrexate. Gastroenterology 104(1):31-7. Baillie, G.S., Scott, J.D., and Houslay, M.D. (2005). Compartmentalisation of phosphodiesterases and protein kinase A: opposites attract. FEBS Lett. 579:3264–3270. Bank, I., Koltakov, A., Nir-Glickman, E., Goldstein, I., Li, J., Roitelman, J., and Chess, L. (2003). Lovastatin and phospholipase C regulate constitutive and protein kinase C dependent integrin mediated interactions of human T-cells with collagen. Cell. Immunol. 223:35–45. Barber, M.A. and Welch, H.C. (2006). PI3K and Rac signaling in leukocyte and cancer cell migration. Bull. Cancer 93(5):e44-e52. Berridge, M.J. and Irvine, R.F. (1984). Inositol triphosphate, a novel second messenger in cellular signal transduction. Nature 312:315-321. Bershadsky, A.D., Ballestrem, C., Carramusa, L., Zilberman, Y., Gilquin, B., Khochbin, S., Alexandrova, A.Y., Verkhovsky, A.B., Shemesh, T., Kozlov, M.M. (2006). Assembly and mechanosensory function of focal adhesions: experiments and models. Eur. J. Cell Biol. 85:165–173. Bos, J.L. (2003). Epac: a new cAMP target and new avenues in cAMP research. Nat. Rev. Mol. Cell Biol. 4:733–738. Bunney, T.D. and Katan, M. (2006). Phopholipase C epsilon: linking second messengers and small GTPases. Trends Cell Biol. 16(12):640-648. Burridge, K., Fath, K., Kelly, T., Nuckolls, G., and Turner, C. (1988). Focal adhesions – transmembrane junctions between the extracellular-matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487-525. 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(8):505-8. Cai, J., Li, J., 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(1):84-6. Chang, P.H., Kuo, S.T., Lai, S.H., Yang, H.S., Ting, Y.Y., Hsu, C.L., and Chen, H.C. (2005). Herpes-like virus infection causing mortality of cultured abalone Haliotis diversicolor supertexta in Taiwan. Dis. Aquat. Organ. 65(1):23-7. Chen, J.H. (1996). Hemolymph collection in abalone (Haliotis diversicolor). Acta Zoologica. Taiwanica 7:61-72. Chen, J.H. and Bayne, C.J. (1995a). Hemocyte adhesion in the California mussel (Mytilus californianus): regulation by adenosine. Biochim. Biophys. Acta. 1268:178-184. Chen, J.H. and Bayne, C.J. (1995b). Bivalve mollusk hemocyte behaviors: characterization of hemocyte aggregation and adhesion and their inhibition in California mussel (Mytilus californianus). Biol. Bull. 188:255-266. Chen, J. H. and Lee, H. (2002). Lysophospholipids regulate abalone hemocyte adhesion in vitro. Molecular Biology of the Cell, 13 (supplement): 203a. 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(1):31-38. Constantin, G., Majeed, M., Giagulli, C., Piccio, L., Kim, J.Y., Butcher, E.C., and Laudanna, C. (2000). Chemokines trigger immediate β2 integrin affinity and mobility changes: differential regulation and roles in lymphocyte arrest under flow. Immunity 13:759–769. Cooper, D.M. (2005). Compartmentalization of adenylate cyclase and cAMP signalling. Biochem. Soc. Trans. 33:1319–1322. Cronstein, B.M. (2006). Adensoine receptors and wound healing, revised. ScientificWorldJournal 6:984-991. Cronstein, B.N. (1994). Adenosine, an endogenous anti-inflammatory agent. J. Appl. Physiol. 76:5-13. Cronstein, B.N., Duguma, L., Nicholls, D., Hutchison, A., and Williams, M. (1990). The adenosine/neutrophil paradox resolved. Human neutrophils possess both A1 and A2 receptors which promote chemotaxis and inhibit O2- generation, respectively. J. Clin. Invest. 85:1150-1157. Cronstein, B.N., Haines, K.A., Kolasinski, S.L., and Reibman, J. (1991). Gs linked receptors (beta-adrenergic and adenosine A2) uncouple chemoattractant receptors from G proteins. Clin. Res. 39:343A. Cronstein, B.N., Kramer, S.B., Weissmann, G., and Hirschhorn, R. (1983). Adenosine: physiological modulator of superoxide anion generation by human neutrophils. J. Exp. Med. 158:1160-1177. Cronstein, B.N., Levin, R.I., Belanoff, J., Weissmann, G., and Hirschhorn, R. (1986). Adenosine: an endogenus inhibitor of neutrophil-mediated injury to endothelial cells. J. Clin. Invest. 78:760-770. Cronstein, B.N., Levin, R.I., Philips, M., Hirschhorn, R., Abramson, S.B., and Weissmann, G. (1992). Neutrophil adherence to endothelium is enhanced via adenosine A1 receptors and inhibited via adenosine A2 receptors. J. Immunol. 148:2201-2206. Cronstein, B.N., Rosenstein, E.D, Kramer, S.B., Weissmann, G., and Hirschhorn, R. (1985). Adenosine: a physiologic modulator of superoxide anion generation by human neutrophils. Adenosine acts via an A2 receptor on human neutrophil. J. Immunol. 135:1366-1371. Downward, J. (1998). Mechanisms and consequences of activation of protein kinase B/Akt. Curr. Opin. Cell Biol. 10:262-267. Feoktistov, I. and Biaggioni, I. (1997). Adenosine A2B receptors. Pharmacol. Rev. 49:381-402. Franzini, E., Sellak, H., Marquetty, C., Babin-Chevaye, C., Hakim, J., and Pasquier, C. (1996). Inhibition of human neutrophil binding to hydrogen peroxide-treated endothelial cells by cAMP and hydroxyl radical scavengers. Free Radic. Biol. Med. 21(1):15-23. Fredholm, B.B., Arslan, G., Halldner, L., Kull, B., Schulte, G., and Wasserman, W. (2000). Structure and function of adenosine receptors and their genes. Naunyn-Schmiedeberg’s Arch Pharmacol. 362:364-374. Fredholm, B.B., Ijzerman, A.P., Jacobson, K.A., Klotz, K.N., Linden, J. (2001). International Union of Pharmacology. XXV. Nomenclature and classification of adenosine receptors. Pharmacol. Rev. 53:527-52. Geiger, B., Bershadsky, A., Pankov, R., and Yamada, K.M. (2001). Transmembrane extracellular matrix-cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2:793–805. Gessi, S., Varani, K., Merighi, S., Ongini, E., Borea, P.A.. (2000). A(2A) adenosine receptors in human peripheral blood cells. Br. J. Pharmacol. 129:2-11. Grabovsky, V., Feigelson, S., Chen, C., Bleijs, D.A., Peled, A., Cinamon, G., Baleux, F., Arenzana-Seisdedos, F., Lapidot, T., van Kooyk, Y., Lobb, R.R., and Alon R. (2000). Subsecond induction of alpha4 integrin clustering by immobilized chemokines stimulates leukocyte tethering and rolling on endothelial vascular cell adhesion molecule 1 under flow conditions. J Exp Med. 192:495-506. Hemler, M.E. (1990). VLA proteins in the integrin family: structures, functions, and their role on leukocytes. Annu. Rev. Immunol. 8:365–400. Hoebe, K., Jansen, E. and Beutler, B. (2004). The interface between innate and adaptive immunity. Nat. Immunol. 5:971-974. Hughes, P.E. and Pfaff, M. (1998). Integrin affinity modulation. Trends Cell Biol. 8:359-364. Hyduk, S.J., Chan, J.R., Duffy, S.T., Chen, M., Peterson, M.D., Waddell, T.K., Digby, G.C., Szaszi, K., Kapus, A., and Cybulsky, M.I. (2007). Phospholipase C, calcium, and calmodulin are critical for α4β1 integrin affinity up-regulateion and monocyte arrest triggered by chemoattractants. Blood 109(1):176-184. Imhof, B.A. and Aurrand-Lions, M. (2004). Adhesion mechanisms regulating the migration of monocytes. Nat. Rev. Immunol. 4:432-444. Iwanaga, S. and Lee, B.L. (2005). Recent advances in the innate immunity of invertebrate animals. J Biochem Mol Biol. 38(2):128-50. Jackson, S.F. and Schoenwaelder, S.M. (2006). Type I phosphoinositide 3-kinases: potential antithrombotic targets? Cell. Mol. Life Sci. 63:1085-1090. Jones, S.L. (2002). Protein kinase A regulates β2 integrin avidity in neutrophils. J. Leukoc. Biol. 71:1042-1048. Kandel, E.S. and Hay, N. (1999). The regulation and activities of the multifunctional serine/threonine kinase Akt/PKB. Exp. Cell. Res. 253:210-229. Katagiri, K., Hattori, M., Minato, N., Irie, S., Takatsu, K., and Kinashi, T. (2000). Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase. Mol. Cell. Biol. 20:1956–1969. Katan, M. (2005). New insights into the families of PLC enzymes: looking back and going forward. Biochem. J. 391:e7-e9. Kinashi, T. (2005). Intracellular signalling controlling integrin activation in lymphocytes. Nat. Rev. Immunol. 5:546-559. Kinashi, T., Asaoka, T., Setoguchi, R., and Takatsu, K. (1999). Affinity modulation of very late antigen-5 through phosphatidylinositol 3-kinase in mast cells. J. Immunol. 162:2850–2857. Kinashi, T., Escobedo, J.A., Williams, L.T., Takatsu, K., and Springer, T.A. (1995). Receptor tyrosine kinase stimulates cellmatrix adhesion by phosphatidylinositol 3 kinase and phospholipase C-γ1 pathways. Blood 86:2086–2090. Kirchner, J., Kam, Z., Tzur, G., Bershadsky, A.D., and Geiger, B. (2003). Live-cell monitoring of tyrosine phosphorylation in focal adhesions following microtubule disruption. J. Cell. Sci. 278:975-986. Klinger, M., Freissmuth, M., and Nanoff, C. (2002). Adenosine receptors: G protein-mediated signalling and the role of accessory proteins. Cell. Signal. 14:99-108. Klotz, K.N. (2000). Adenosine receptors and their ligands. Naunyn-Schmiedeberg’s Arch Pharmacol. 362:382-391. Krjukova, J., Holmqvist, T., Danis, A.S., Akerman, K.E., and Kukkonen, J.P. (2004). Phospholipase C activator m-3M3FBS affacts Ca2+ homeostasis independently of phospholipase C activation. Br. J. Pharmacol. 143:3-7. Lai, CP. (2004). The cell-matrix adhesion of hemocytes in abalone (Haliotis diversicolor) is regulated by protein kinase a signal transduction pathway. Master thesis, National Taiwan University. Lal, H., Guleria, R.S., Foster, D.M., Lu, G., Watson, L.E., Sanghi, S., Smith, M., and Dostal, D.E. (2007). Integrins: Novel therapeutic tagets for cardiovascular diseases. Cardiovasc. Hematol. Agents Med. Chem. 5:109-132. Lavine, M.D. and Strand, M.R. (2002). Insect hemocytes and their role in immunity. Insect Biochem Mol Biol. 32(10):1295-309. Lee, K.K., Liu, P.C., and Huang, C.Y. (2003). Vibrio parahaemolyticus infectious for both humans and edible mollusk abalone. Microbes Infect. 5(6):481-5. 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(2):202-11. Liao, C.M. and Ling, M.P. (2004). Probabilistic risk assessment of abalone Haliotis diversicolor supertexta exposed to waterborne zinc. Environ Pollut. 127(2):217-27. Liao, C.M., Lin, M.C., Chen, J.S., and Chen, J.W. (2002). Linking biokinetics and consumer-resource dynamics of zinc accumulation in pond abalone Haliotis diversicolor supertexta. Water Res. 36(20):5102-12. Libersan, D., Rousseau, G., and Merhi, Y. (2003). Differential regulation of P-selectin expression by protein kinase A and protein kinase G in thrombin-stimulated human platelets. Thromb. Haemost. 89:310-317. Liu, D.Z., Liang, H.J., Chen, C.H., Lin, S.Y., Zhong, W.B., Ho, F.M., Hou, W.C., Lo, J.L., Ho, Y.S., Lin, P.J., Hung, L.F., and Liang, Y.C. (2007). Switch activation of PI-PLC downstream signals in activated macrophages with wortmannin. Biochim. Biophy. Acta in press. Loftus, J.C., Smith, J.W., and Ginsberg, M.H. (1994). Integrin-mediated cell adhesion – The extracellular face. J. Biol. Chem. 269:25235-25238. Lorenowicz, M.J., van Gils, J., de Boer, M., Hordijk, P.L., and Fernandez-Borja, M. (2006). Epac1-Rap1 signaling regulates monocyte adhesion and chemotaxis. J. Leukoc. Biol. 80:1542-1552. Magazanik, L.G. and Fedorova, I.M. (2003). Modulatory role of adenosine receptors in insect motor nerve terminals. Neurochem. Res. 28:617-624. Maier, L.S. and Bers, D.M. (2002). Calcium, Calmodulin, and Calcium-Calmodulin Kinase II: Heartbeat to Heartbeat and Beyond. J Mol Cell Cardiol 34:919-939. Merighi, S., Mirandola, P., Varani, K., Gessi, S., Leung, E., Baraldi, P.G., Tabrizi, M.A., Borea, P.A.. (2003). A glance at adenosine receptors: novel target for antitumor therapy. Pharmacol. Ther. 100:31-48. Parsons, J.T. (2003). Focal adhesion kinase: the first ten years. J. Cell Sci. 116:1409-1416. Plow, E.F., Haas, T.A., Zhang, L., Loftus, J., and Smith, J.W. (2000). Ligand binding to integrins. J. Biol. Chem. 275: 21785-21788. Plows, L.D., Cook, R.T., Davies, A.J., and Walker, A.J. (2006). Integrin engagement modulates the phosphorylation of focal adhesion kinase, phagocytosis, and cell spreading in molluscan defense cells. Biochim. Biophy. Acta 1763:779-786. Ralevic, V. and Burnstock, G. (1998). Receptors for purines and pyrimidines. Pharmacol. Rev. 50:413-492. Rangarajan, S., Enserink, J.M., Kuiperij, H.B., de Rooij, J., Price, L.S., Schwede, F., and Bos, J.L. (2003). Cyclic AMP induces integrin-mediated cell adhesion through Epac and Rap1 upon stimulation of the ß2-adrenergic receptor. J. Cell Biol. 160(4):487-493. Revan, S., Montesinos, M.C., Naime, D., Landau, S., and Cronstein, B.N. (1996). Adenosine A2 receptor occupancy regulates stimulated neutrophil function via activation of a serine/threonine protein phosphatase. J. Biol. Chem. 271:17114-17118. Romer, L.H., Birukov, K.G., and Garcia, J.G. (2006). Focal Adhesions: Paradigm for a Signaling Nexus. Circ. Res. 98;606-616. Rose, F.R., Hirschhorn, R., Weissmann, G., and Cronstein, B.N. (1988). Adenosine promotes neutrophil chemotaxis. J. Exp. Med. 167:1186-1194. Salmon, J.E. and Cronstein, B.N. (1990). Fcgamma receptor-mediated functions in neutrophils are modulated by adenosine receptor occupancy: A1 receptors are stimulatory and A2 receptors are inhibitory. J. Immunol. 145:2235-2240. Santellal, C. and Carafoli, E. (1997). Calcium signaling in the cell nucleus. FASEB J. 11:1091-1109. Schaller, M.D. (2001). Paxillin: a focal adhesion-associated adaptor protein. Oncogene 20:6459-6472. Schulte, G. and Fredholm, B.B. (2003). Signalling from adenosine receptors to mitogen-activated protein kinases. Cell. Signal. 15:813-827. Shimizu, Y., Mobley, J.L., Finkelstein, L.D., and Chan, A.S. (1995). A role for phosphatidylinositol 3-kinase in the regulation of β1 integrin activity by the CD2 antigen. J. Cell Biol. 131:1867–1880. Sminia, T. and van der Knaap, W.P. (1987). Cells and molecules in molluscan immunology. Develop. Comp. Immunol. 11:17-28. Smith, R.J., Justen, J.M., McNab, A.R., Rosenbloom, C.L., Steele, A.N., Detmers, P.A., Anderson, D.C., and Manning, A.M. (1996). U-73122: a potent inhibitor of human polymorphonuclear neutrophil adhesion on biological surfaces and adhesion-related effector functions. J. Pharmacol. Exp. Ther. 278:320-329. Spaargaren, M., Beuling, E.A., Rurup, M.L., Meijer, H.P., Klok, M.D., Middendorp, S., Hendriks, R.W., and Pals, S.T. (2003). The B cell antigen receptor controls integrin avidity through Btk and PLCγ2. J. Exp. Med. 198(10):1539-1550. Steeber, D.A., Venturi, G.M., and Tedder, T.F. (2005). A new twist to the leukocyte adhesion cascade: intimate cooperation is key. Trends Immunol. 26(1):9-12. Stein, R.C. and Waterfield, M.D. (2000). PI3-kinase inhibition: a target for drug development? Mol. Med. Today 6:347-357. Stephens, L., Ellson, C., and Hawkins, P. (2002). Roles of PI3Ks in leukocyte chemotaxis and phagocytosis. Curr. Opin. Cell Biol. 14:203-213. Streb, H., Irvine, R.F., Berridge, M.J., and Schulz, I. (1983). Release of Ca2+ from a nonmitochondrial store of pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature 306:67–69. Suematsu, E., Hirata, M., Hashimoto, T., and Kuriyama, H. (1984). Inositol 1,4,5-trisphosphate releases Ca2+ from intracellular store sites in skinned single cells of porcine coronary artery. Biochem. Biophys. Res. Commun. 120:481–485. Sullivan, G.W., Lee, D.D., Ross, W.G., DiVietro, J.A., Lappas, C.M., Lawrence, M.B., and Linden, J. J. (2004). Activation of A2A adenosine receptors inhibits expression of alpha 4/beta 1 integrin (very late antigen-4) on stimulated human neutrophils. J. Leukoc. Biol. 75(1):127-134. Tachibana, K., Urano, T., Fujita, H., Ohashi, Y., Kamiguchi, K., Iwata, S., Hirai, H., and Morimoto, C. (1997). Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates. J. Biol. Chem. 272:29083-29090. Takahashi, H.K., Iwagaki, H., Hamano, R., Kanke, T., Liu, K., Sadamori, H., Yagi, T., Yoshino, T., Sendo, T., Tanaka, N., and Nishibori, M. (2007). Effect of adenosine receptor subtypes stimulation on mixed lymphocyte reaction. Eur. J. Pharmacol. 564:204–210. Taylor, C.W. and Laude, A.J. (2002). IP3 receptors and their regulation by calmodulin and cytosolic Ca2+. Cell Calcium 32(5-6):321-334. Toutenhoofd, S.L. and Strehler, E.E. (2000). The calmodulin multigene family as a unique case of genetic redundancy: multiple levels of regulation to provide spatial and temporal control of calmodulin pools? Cell Calcium 28: 83-96. Tsai, J.W., Chou, Y.H., Chen, B.C., Liang, H.M., and Liao, C.M. (2004). Growth toxicity bioassays of abalone Haliotis diversicolor supertexta exposed to waterborne zinc. Bull. Environ. Contam. Toxicol. 72(1):70-7. Tu, L.C., Chou, C.K., Chen, H.C., Yeh, S.F. (2001). Protein kinase C-mediated tyrosine phosphotylation of paxillin and focal adhesion kinase requires cytoskeletal integrity and is uncoupled to mitogen-activated protein kinase activation in human hepatoma cells. J. Biomed. Sci 8:184-190. Tumbarello, D.A., Brown, M.C., and Turner, C.E. (2002). The paxillin LD motifs. FEBS Letters 513:114-118. Tvorogov, D., Wang, X.J., Zent, R., and Carpenter, G. (2005). Integrin-dependent PLC-γ1 phosphorylation mediates fibronectin-dependent adhesion. J. Cell Sci. 118:601-610. van der Flier, A. and Sonnenberg, A. (2001). Function and interactions of integrins. Cell Tissue Res. 305:285-598. Vanhaesebroeck, B. and Alessi, D.R. (2000). The PI3K-PDK1 connection: more than just a road to PKB. Biochem. J. 346:561-576. Wang, J. and Brown, E.J. (1999). Immune complex-induced integrin activation and L-plastin phosphorylation require protein kinase A. J. Biol. Chem. 274(34):24349-24356. Watanabe, T., Tokuyama, S., Yasuda, M., Sasaki, T., and Yamamoto, T. (2002). Involvement of adenosine A2 receptors in the changes of tissue factor-dependent coagulant activity induced by polymorphonuclear leukocytes in endothelial cells. Jpn. J. Pharmacol. 88:407-413. Wong, W. and Scott, J.D. (2004). AKAP signaling complexes: focal points in space and time. Nat. Rev. Mol. Cell Biol. 5:959-970. Wozniak, M.A., Modzelewska, K., Kwong, L., Keely, P.J. (2004). Focal adhesion regulation of cell behavior. Biochim. Biolphy. Acta 1692:103-119. Yoshida, N., Yoshikawa, T., Manabe, H., Terasawa, Y., Kondo, M., Noguchi, N., and Niki, E. (1999). Vitamin E against polymorphonuclear leukocyte-dependent adhesion to endothelial cells. J. Leukoc. Biol. 65:757-763. Zell, T., Hunt, S.W., Mobley, J.L., Finkelstein, L.D., and Shimizu, Y. (1996). CD28-mediated up-regulation of β1-integrin adhesion involves phosphatidylinositol 3-kinase. J. Immunol. 156:883–886. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/29721 | - |
dc.description.abstract | 細胞防禦機制,例如:細胞吞噬(phagocytosis)以及囊包作用(encapsulation),是先天免疫中主要的一類免疫反應機制,而血球細胞附著是細胞防禦機制的起始步驟。相對於在哺乳動物血球細胞中已有的詳細研究,無脊椎血液細胞的附著機制尚未清楚了解。在這篇研究中,九孔(Haliotis diversicolor)血液細胞處理咖啡因(caffeine)和其他的腺苷酸受體促效劑(adenosine receptor agonists)會影響血液細胞的附著。腺苷酸(adenosine)、咖啡因以及A1和A3腺苷酸受體促效劑會抑制九孔血液細胞附著,在另一方面,CGS21680(A2A腺苷酸受體促效劑)可以回復受到腺苷酸所抑制的血液細胞附著。除此之外,ZM241385(A2A腺苷酸受體對抗劑; Adenosine A2A receptor antagonist)與腺苷酸同時作用能更抑制九孔血液細胞的附著。這些實驗結果顯示,可能有多種不同的類型的腺苷酸受體存在於九孔血液細胞上,且類A1腺苷酸受體活化可能是造成九孔血液細胞附著受抑制的原因。腺苷酸受體是G 蛋白耦合性受體(G-protein coupled receptor)家族的一員,此受體主要的下游訊息傳導路徑為環苷腺酸-蛋白激酶A(cAMP-PKA)和磷脂酶C(PLC)相關的訊息傳導路徑。在這篇研究中,當九孔血液細胞處理R-PIA(A1腺苷酸受體促效劑)時,細胞內的環苷腺酸濃度會下降,但並沒有顯著影響蛋白激酶A的活性。增加細胞內的環苷腺酸濃度並不能回復R-PIA造成的附著受到抑制,顯示環苷腺酸-蛋白激酶A的訊息傳導路徑可能不是調控類A1腺苷酸受體活化後造成九孔血液細胞附著下降的主要原因。但以磷脂酶C的活化劑m-3M3FBS處理九孔血液細胞,可以回復CHA所抑制的九孔血液細胞附著,而且單獨以U73122(磷脂酶C的抑制劑)處理來抑制細胞的磷脂酶C的活性,會降低九孔血液細胞的附著。這些結果指出九孔血液細胞附著需要磷脂酶C的活性,又在九孔血液細胞中,磷脂酶C可能位於活化的類A1腺苷酸受體訊息傳遞的下游。以PMA(蛋白激酶C活化劑)會增進九孔血液細胞的附著,但蛋白激酶C抑制劑並不影響九孔血液細胞的附著。另一方面,用A23187(鈣離子通道)增加胞內鈣離子的濃度卻可以增加九孔血液細胞的附著。又,以wortmannin和LY294002抑制PI3K (phosphoinositide-3-kinase)的活性會降低九孔血液細胞的附著。這些研究結果顯示,類A1腺苷酸受體可能經由抑制磷脂酶C-鈣離子或PI3K的訊息傳導路徑來降低九孔血液細胞的附著。環苷腺酸-蛋白激酶A訊息傳導路徑和蛋白激酶C參與在九孔血液細胞附著的調控中,但可能不是主要影響類A1腺苷酸受體活化後抑制九孔血液細胞附著的原因。在九孔血液細胞中的Focal adhesion蛋白質,例如:paxillin和FAK,可以被西方點墨法(Western blot)、免疫沉澱法(immunoprecipitation)和免疫螢光染色(immunocytochemistry)偵測到。此外,免疫螢光染色的螢光在細胞的邊緣呈現點狀分布,且類似focal adhesion的螢光點也可以在細胞邊緣較靠近細胞中心點的地方被發現。Integrin β1和αVβ3如同focal adhesion蛋白質一樣,可以被免疫螢光染色偵測到,顯示在哺乳動物中調控細胞附著的重要分子也存在於九孔血液細胞中。 | zh_TW |
dc.description.abstract | Cellular defenses are the principal responses of innate immunity, and blood cell adhesion is the very first step to perform those cellular defenses like phagocytosis and encapsulation. Unlike well-known mechanisms in mammalian blood cells, little is known about hemocyte adhesion in invertebrates. Here, I report that caffeine and other adenosine receptor agonists affected hemocyte adhesion in abalones (Haliotis diversicolor). Adenosine, caffeine and adenosine A1 and A3 receptor agonists all inhibit the hemocyte adhesion. On the other hand, CGS21680, an adenosine A2A receptor agonist, can recover the adenosine inhibited hemocyte adhesion. In addition, ZM241385 (an adenosine A2A receptor antagonist) synergistically inhibited hemocyte adhesion with adenosine. The result suggests that several subtypes of adenosine receptors exist in hemocytes, and adenosine A1-like receptor may be responsible for the adhesion inhibitory effect. Adenosine receptors have been recognized as the members of G-protein coupled receptor family, and the major intracellular signaling transduction pathways downstream of the receptors are cAMP-PKA and PLC related signaling pathways. In this study, the treatment of R-PIA (an adenosine A1 receptor agonist) decreased intracellular cAMP concentration, but not PKA activity. Increasing intracellular cAMP concentration could not overcome the inhibitory effect of R-PIA, which suggests that the cAMP-PKA signaling pathway may not be the key factor that regulates adhesion inhibition upon adenosine A1-like receptor activation. However, treating hemocytes with PLC activator, m-3M3FBS, can increase the CHA-inhibited hemocyte adhesion, and inhibition of PLC activity alone decreased hemocyte adhesion. These data indicate the requirement of PLC activity in hemocyte adhesion, and PLC might locate downstream of adenosine A1-like receptor activation. While PMA (a PKC activator) increased hemocyte adhesion, the PKC inhibitors treatment left hemocyte adhesion unaffected. On the other hand, increasing intracellular Ca2+ by A23187 (a Ca2+ ionophore) improved hemocyte adhesion. Moreover, inhibiting PI3K activity by wortmannin or LY294002 decreased hemocyte adhesion. Together, hemocyte adhesion that inhibited by activation of adenosine A1-like receptor should be regulated by signaling pathways like PLC-Ca2+ pathway or PI3K. The cAMP-PKA pathway and PKC are involved, but may not be the major signaling pathways that control adhesion inhibitory effect of adenosine A1-like receptor activation. Focal adhesion proteins such as paxillin and FAK could be detected by Western blotting, immunoprecipitation (IP), or immunocytochemistry (ICC) in abalone hemocytes. Furthermore, ICC showed spot-like fluorescence scattering in the edge of cells, and focal adhesion-like spots can also be observed at inner side of cells. As well as focal adhesion proteins, integrin β1 and αVβ3 were also discovered using ICC process, which suggests the critical molecules that are involved in regulation of cell adhesion in mammals are also existence in abalone hemocytes. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T01:16:11Z (GMT). No. of bitstreams: 1 ntu-96-R93b41008-1.pdf: 796722 bytes, checksum: 040cc2a0f77a901fc27a5c1502443da1 (MD5) Previous issue date: 2007 | en |
dc.description.tableofcontents | 口試委員會審定書………………………………………………………………….... i
誌謝………………………………………………………………………………...… ii Abstract (English)………………………………………………………………….... iii Abstract (Chinese)……………………………………………………………………. v 1. Introduction 1.1. Invertebrate immunity and hemocyte adhesion………………………………... 1 1.2. Intracellular signaling pathways involve in hemocyte adhesion………………. 2 1.2.1. cAMP-PKA signaling…………………………..……………………..…. 2 1.2.2. PLC, PKC, and Ca2+ regulate integrin activation and cell adhesion…..… 3 1.2.3. PI3K regulates integrin activation and cell adhesion………..…………… 5 1.3. Integrins………………………………………………………………………... 6 1.4. Focal adhesion……………………………………………………………….… 7 1.5. Adenosine receptors………………………………………………………….... 8 1.6. Adenosine receptors and their functions in blood cells……………………...… 9 1.7. Hemocytes in abalones and current researches………………………………. 10 1.8. Purpose of this study….……………………………………………………… 11 2. Materials and methods 2.1. Animals……………………………………………………………………….. 13 2.2. Hemolymph collection……………………………………………………..… 13 2.3. Chemicals…………………………………………………………………….. 14 2.4. Hemocyte adhesion assay…………………………………………………..… 14 2.5. cAMP measurement………………………………………………………….. 15 2.6. PKA activity assay………………………………………………………….... 16 2.7. Immunoprecipitation (IP)…………………………………………………..… 17 2.8. SDS-PAGE and Western analysis……………………………………………. 18 2.9. Immunocytochemistry (ICC)…………………………………………………. 19 2.10. Statistical analyses……………………………………………………………. 20 3. Results 3.1. The basic phenomena of abalone hemocyte adhesion…………………….….. 21 3.2. Adenosine receptors involved in hemocyte adhesion 3.2.1. Effect of adenosine or caffeine on hemocyte adhesion…………………. 21 3.2.2. Effect of AdoA1R agonists or antagonists on hemocyte adhesion…….... 22 3.2.3. Effect of an AdoA2AR agonist, CGS21680, and an antagonist, ZM241385, on hemocyte adhesion…………………………………………………... 22 3.2.4. Effect of an AdoA3R agonist, IB-MECA, on hemocyte adhesion…….... 23 3.3. The cAMP-PKA signaling pathway regulated hemocyte adhesion. 3.3.1. Effect of R-PIA on the changes of intracellular cAMP concentration and PKA activity…………………………………………………………..… 23 3.3.2. Effect of intracellular cAMP concentration increase on hemocyte adhesion…………………………………………………………………. 24 3.3.3. Inhibition of PKA could not affect hemocyte adhesion……………….... 24 3.4. PLC related signaling molecules controlled hemocyte adhesion. 3.4.1. PLC activity is required for hemocyte adhesion………………………... 24 3.4.2. The influence of PKC activity on hemocyte adhesion………………….. 25 3.4.3. The increase of Ca2+ concentration promotes hemocyte adhesion…….... 26 3.5. PI3K activity was required for hemocyte adhesion…………………………... 26 3.6. Focal adhesion proteins and integrins exist in abalone hemocytes 3.6.1. FAK and paxillin in abalone hemocytes………………………………... 27 3.6.2. Intergrin β1 and integrinαVβ3 in abalone hemocytes………………...… 28 3.6.3. Protein tyrosine phosphorylation during hemocyte adhesion………...… 28 4. Discussion 4.1. The existence of adenosine receptor in abalone hemocytes………………….. 30 4.2. The cAMP-PKA signaling pathway regulates hemocyte adhesion…………... 32 4.3. PLC, PKC, and Ca2+ regulate hemocyte adhesion in abalones……………….. 34 4.4. PI3K and related signaling pathway regulate hemocyte adhesion in abalones……………………………………………………………………..… 37 4.5. Focal adhesion and integrins in abalone hemocytes………………………….. 38 5. Conclusion………………………………………………………………….... 41 6. References…………………………………………….……………………... 43 Tables 1. G protein coupling with adenosine receptors and agonists and antagonists of adenosine receptor that is used in this study………………………………..….. f1 Figures 1. Hemocyte adhesion during 45 min incubation………………….……………... f2 2. The effect of adenosine and caffeine on hemocyte adhesion………………..… f3 3. The effect of AdoA1R agonists, CHA and R-PIA, and antagonist, DPCPX, on hemocyte adhesion……………………………………………………………... f4 4. The effect of the AdoA2AR agonist, CGS21680, and antagonist, ZM241385, on hemocyte adhesion………………………………………………………..….… f5 5. The effect of the AdoA3R agonist, IB-MECA, on hemocyte adhesion………... f6 6. Regulation of intracellular cAMP concentration and PKA activity by R-PIA…………………………………………………………………………... f7 7. The effect of dbcAMP, a cAMP analogue, on hemocyte adhesion…………..... f8 8. Effect of intracellular cAMP increase on R-PIA inhibited hemocyte adhesion………………………………………………………………………... f9 9. PKA activity inhibition and hemocyte adhesion regulation………………….. f10 10. Requirement of PLC activity on hemocyte adhesion……………………….… f11 11. Recovering the inhibitory effect of CHA by m-3M3FBS on hemocyte adhesion………………………………………………………………………. f12 12. Hemocyte adhesion in response to activation or inhibition of PKC activity……………………………………………………………………….... f13 13. Increase in CHA inhibited hemocyte adhesion by PMA……………………... f14 14. Increase intracellular Ca2+ regulation of hemocyte adhesion…………….…... f15 15. PI3K regulation of hemocyte adhesion……………………………………...... f16 16. Western blotting and immunoprecipitation of abalone paxillin………………. f17 17. Immunochemistry of paxillin and FAK in abalone hemocytes…………….… f18 18. Immunochemistry of integrin β1 in abalone hemocytes……………………… f20 19. Immunochemistry of αVβ3 in abalone hemocytes…………………………… f21 20. Negative control for Immunochemistry………………………………………. f22 21. Pattern of protein tyrosine phosphorylation during hemocyte adhesion……… f23 22. Signaling pathwayoverview………………………………………………….. f25 | |
dc.language.iso | en | |
dc.title | 類腺苷酸受體調控九孔(Haliotis diversicolor)血液細胞
附著之胞內訊息傳導 | zh_TW |
dc.title | Adenosine-like receptor mediates the intracellular signaling transduction on hemocyte adhesion in abalones (Haliotis diversicolor) | en |
dc.type | Thesis | |
dc.date.schoolyear | 95-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 李心予(Hsin-Yu Lee),李士傑(Shyh-Jye Lee),沈湯龍(Tang-Long Shen) | |
dc.subject.keyword | 先天性免疫反應,九孔,血液細胞,腺苷,酸受體,細胞附著,訊息傳遞, | zh_TW |
dc.subject.keyword | innate immunity,abalones,hemocytes,adenosine receptor,cell adhesion,signaling transduction, | en |
dc.relation.page | 78 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2007-07-19 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 動物學研究研究所 | zh_TW |
顯示於系所單位: | 動物學研究所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-96-1.pdf 目前未授權公開取用 | 778.05 kB | Adobe PDF |
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。