請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/4434
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 潘建源 | |
dc.contributor.author | Yun He | en |
dc.contributor.author | 何芸 | zh_TW |
dc.date.accessioned | 2021-05-14T17:42:14Z | - |
dc.date.available | 2015-08-25 | |
dc.date.available | 2021-05-14T17:42:14Z | - |
dc.date.copyright | 2015-08-25 | |
dc.date.issued | 2015 | |
dc.date.submitted | 2015-08-19 | |
dc.identifier.citation | Bennett, M.K., Erondu, N.E., and Kennedy, M.B. (1983). Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain. J Biol Chem 258, 12735-12744.
Berridge, M.J. (1998). Neuronal calcium signaling. Neuron 21, 13-26. Blochl, A., and Thoenen, H. (1995). Characterization of nerve growth factor (NGF) release from hippocampal neurons: evidence for a constitutive and an unconventional sodium-dependent regulated pathway. Eur J Neurosci 7, 1220-1228. Bootman, M.D., Collins, T.J., Peppiatt, C.M., Prothero, L.S., MacKenzie, L., De Smet, P., Travers, M., Tovey, S.C., Seo, J.T., Berridge, M.J., et al. (2001). Calcium signalling--an overview. Semin Cell Dev Biol 12, 3-10. Bradshaw, J.M., Hudmon, A., and Schulman, H. (2002). Chemical quenched flow kinetic studies indicate an intraholoenzyme autophosphorylation mechanism for Ca2+/calmodulin-dependent protein kinase II. J Biol Chem 277, 20991-20998. Burgoyne, R.D. (2007). Neuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signalling. Nat Rev Neurosci 8, 182-193. Chen, M.L., Chen, Y.C., Peng, I.W., Kang, R.L., Wu, M.P., Cheng, P.W., Shih, P.Y., Lu, L.L., Yang, C.C., and Pan, C.Y. (2008). Ca2+ binding protein-1 inhibits Ca2+ currents and exocytosis in bovine chromaffin cells. J Biomed Sci 15, 169-181. Dash, P.K., Moore, A.N., Kobori, N., and Runyan, J.D. (2007). Molecular activity underlying working memory. Learn Mem 14, 554-563. Dupont, G., and Goldbeter, A. (1993). One-pool model for Ca2+ oscillations involving Ca2+ and inositol 1,4,5-trisphosphate as co-agonists for Ca2+ release. Cell Calcium 14, 311-322. Fink, C.C., Bayer, K.U., Myers, J.W., Ferrell, J.E., Jr., Schulman, H., and Meyer, T. (2003). Selective regulation of neurite extension and synapse formation by the beta but not the alpha isoform of CaMKII. Neuron 39, 283-297. Ghosh, A., and Greenberg, M.E. (1995). Calcium signaling in neurons: molecular mechanisms and cellular consequences. Science (New York, NY) 268, 239-247. Giese, K.P., Fedorov, N.B., Filipkowski, R.K., and Silva, A.J. (1998). Autophosphorylation at Thr286 of the alpha calcium-calmodulin kinase II in LTP and learning. Science (New York, NY) 279, 870-873. Haeseleer, F., Imanishi, Y., Maeda, T., Possin, D.E., Maeda, A., Lee, A., Rieke, F., and Palczewski, K. (2004). Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in photoreceptor synaptic function. Nat Neurosci 7, 1079-1087. Haeseleer, F., Sokal, I., Verlinde, C.L., Erdjument-Bromage, H., Tempst, P., Pronin, A.N., Benovic, J.L., Fariss, R.N., and Palczewski, K. (2000). Five members of a novel Ca(2+)-binding protein (CABP) subfamily with similarity to calmodulin. J Biol Chem 275, 1247-1260. Hanson, P.I., Meyer, T., Stryer, L., and Schulman, H. (1994). Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals. Neuron 12, 943-956. Hayashi, Y., Shi, S.H., Esteban, J.A., Piccini, A., Poncer, J.C., and Malinow, R. (2000). Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science (New York, NY) 287, 2262-2267. Haynes, L.P., Tepikin, A.V., and Burgoyne, R.D. (2004). Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphosphate-mediated calcium signaling. J Biol Chem 279, 547-555. Hoeflich, K.P., and Ikura, M. (2002). Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108, 739-742. Irving, A.J., Collingridge, G.L., and Schofield, J.G. (1992). Interactions between Ca2+ mobilizing mechanisms in cultured rat cerebellar granule cells. The Journal of physiology 456, 667-680. Kasri, N.N., Holmes, A.M., Bultynck, G., Parys, J.B., Bootman, M.D., Rietdorf, K., Missiaen, L., McDonald, F., De Smedt, H., Conway, S.J., et al. (2004). Regulation of InsP3 receptor activity by neuronal Ca2+-binding proteins. EMBO J 23, 312-321. Konur, S., and Ghosh, A. (2005). Calcium signaling and the control of dendritic development. Neuron 46, 401-405. Lee, A., Westenbroek, R.E., Haeseleer, F., Palczewski, K., Scheuer, T., and Catterall, W.A. (2002). Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1. Nat Neurosci 5, 210-217. Li, Z., and Hatton, G.I. (1997). Ca2+ release from internal stores: role in generating depolarizing after-potentials in rat supraoptic neurones. The Journal of physiology 498 ( Pt 2), 339-350. Maeda, T., Lem, J., Palczewski, K., and Haeseleer, F. (2005). A critical role of CaBP4 in the cone synapse. Invest Ophthalmol Vis Sci 46, 4320-4327. McAllister, A.K., Katz, L.C., and Lo, D.C. (1996). Neurotrophin regulation of cortical dendritic growth requires activity. Neuron 17, 1057-1064. McCue, H.V., Burgoyne, R.D., and Haynes, L.P. (2009). Membrane targeting of the EF-hand containing calcium-sensing proteins CaBP7 and CaBP8. Biochem Biophys Res Commun 380, 825-831. Mikhaylova, M., Reddy, P.P., Munsch, T., Landgraf, P., Suman, S.K., Smalla, K.H., Gundelfinger, E.D., Sharma, Y., and Kreutz, M.R. (2009). Calneurons provide a calcium threshold for trans-Golgi network to plasma membrane trafficking. Proc Natl Acad Sci U S A 106, 9093-9098. Mikhaylova, M., Sharma, Y., Reissner, C., Nagel, F., Aravind, P., Rajini, B., Smalla, K.H., Gundelfinger, E.D., and Kreutz, M.R. (2006). Neuronal Ca2+ signaling via caldendrin and calneurons. Biochim Biophys Acta 1763, 1229-1237. Miller, R.J. (1988). Calcium signalling in neurons. Trends Neurosci 11, 415-419. Mukherji, S., and Soderling, T.R. (1994). Regulation of Ca2+/calmodulin-dependent protein kinase II by inter- and intrasubunit-catalyzed autophosphorylations. J Biol Chem 269, 13744-13747. Redmond, L., Kashani, A.H., and Ghosh, A. (2002). Calcium regulation of dendritic growth via CaM kinase IV and CREB-mediated transcription. Neuron 34, 999-1010. Rieke, F., Lee, A., and Haeseleer, F. (2008). Characterization of Ca2+-binding protein 5 knockout mouse retina. Invest Ophthalmol Vis Sci 49, 5126-5135. Rongo, C., and Kaplan, J.M. (1999). CaMKII regulates the density of central glutamatergic synapses in vivo. Nature 402, 195-199. Sah, P., and McLachlan, E.M. (1991). Ca(2+)-activated K+ currents underlying the afterhyperpolarization in guinea pig vagal neurons: a role for Ca(2+)-activated Ca2+ release. Neuron 7, 257-264. Schrauwen, I., Helfmann, S., Inagaki, A., Predoehl, F., Tabatabaiefar, M.A., Picher, M.M., Sommen, M., Seco, C.Z., Oostrik, J., Kremer, H., et al. (2012). A mutation in CABP2, expressed in cochlear hair cells, causes autosomal-recessive hearing impairment. Am J Hum Genet 91, 636-645. Shih, P.Y., Lin, C.L., Cheng, P.W., Liao, J.H., and Pan, C.Y. (2009). Calneuron I inhibits Ca(2+) channel activity in bovine chromaffin cells. Biochem Biophys Res Commun 388, 549-553. Silva, A.J., Paylor, R., Wehner, J.M., and Tonegawa, S. (1992). Impaired spatial learning in alpha-calcium-calmodulin kinase II mutant mice. Science (New York, NY) 257, 206-211. Tippens, A.L., and Lee, A. (2007). Caldendrin, a neuron-specific modulator of Cav/1.2 (L-type) Ca2+ channels. J Biol Chem 282, 8464-8473. Verkhratsky, A., and Shmigol, A. (1996). Calcium-induced calcium release in neurones. Cell Calcium 19, 1-14. Waterhouse, A.L., Pessah, I.N., Francini, A.O., and Casida, J.E. (1987). Structural aspects of ryanodine action and selectivity. J Med Chem 30, 710-716. Wu, G.Y., and Cline, H.T. (1998). Stabilization of dendritic arbor structure in vivo by CaMKII. Science (New York, NY) 279, 222-226. Wu, Y.Q., Lin, X., Liu, C.M., Jamrich, M., and Shaffer, L.G. (2001). Identification of a human brain-specific gene, calneuron 1, a new member of the calmodulin superfamily. Mol Genet Metab 72, 343-350. Zeitz, C., Kloeckener-Gruissem, B., Forster, U., Kohl, S., Magyar, I., Wissinger, B., Matyas, G., Borruat, F.X., Schorderet, D.F., Zrenner, E., et al. (2006). Mutations in CABP4, the gene encoding the Ca2+-binding protein 4, cause autosomal recessive night blindness. Am J Hum Genet 79, 657-667. Zirpel, L., Nathanson, N.M., Rubel, E.W., and Hyson, R.L. (1994). Glutamate-stimulated phosphatidylinositol metabolism in the avian cochlear nucleus. Neurosci Lett 168, 163-166. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/4434 | - |
dc.description.abstract | 在神經生理中,鈣離子訊號複雜的模式與參與在鈣離子訊號傳遞中的鈣離子結合蛋白 (CaBPs) 有相當大的關聯。CaBP8,又稱為Calneuron I (CalnI),會參與在鈣離子訊號傳遞中並抑制N型鈣離子通道的電流。CaMKII則是在神經突觸的發育與突觸可塑性中扮演重要的角色。在先前的研究中,CalnI與CaMKIIβ被指出可能有交互作用。為了確認CalnI對神經傳導的影響,將CalnI表現在初級培養的神經細胞中,並使用鈣離子影像技術紀錄其神經傳導的情形。除此之外,也利用Sholl analysis來分析表現CalnI的神經細胞其形態是否有所改變。另外在人類胚腎細胞 293T中同時表現CFP-CalnI及YFP-CaMKIIβ來觀察CalnI是否會影響CaMKIIβ在細胞內的分布情形。在表現CalnI的神經細胞中,神經傳導的功能被明顯的阻斷,而鈣離子誘導鈣釋放以及代謝型麩胺酸受體訊息路徑也會受到影響而使細胞內的鈣離子反應減弱。在神經細胞的形態上,神經元突起在遠端的分支數量也因為表現CalnI而明顯減少或變短。而在同時表現CFP-CalnI及YFP-CaMKIIβ的HEK 293T細胞中則發現CalnI確實會影響CaMKIIβ在細胞內的分布情形。綜合以上可知,CalnI會調控鈣離子通道並影響神經傳導,且很有可能與CaMKIIβ交互作用進一步影響突觸發育或可塑性。 | zh_TW |
dc.description.abstract | The complex patterns of Calcium (Ca2+) signals in neuronal physiology can be largely attributed to calcium binding proteins (CaBPs) which participates in Ca2+ signaling pathway. CaBP8, also referred to as calneuron I (CalnI), is involved in transduction of Ca2+ signaling and inhibiting N-type Ca2+ channel currents. Ca2+/calmodulin-dependent protein kinase II (CaMKII) plays an important role in regulating synaptic development and plasticity. According to a previous study in our lab, a possible interaction between CalnI and CaMKIIβ was indicated by Yeast Two-Hybrid screening. To verify the effects of CalnI on neurotransmission, CalnI and related mutants were overexpressed in primary cultured neurons, and calcium imaging experiments were applied to characterize neurotransmission. In addition, CalnI overexpressed neurons were analyzed by Sholl analysis to investigate if there were any changes in morphology. In addition, CFP-CalnI and YFP-CaMKIIβ co-expressed HEK293T cells were examined to determine whether CalnI affects the localization of CaMKIIβ. The overexpression of CalnI in neurons caused significant deficits in neurotransmission, also decreased the Ca2+ responses in calcium-induced calcium release (CICR) and metabotropic glutamate receptor (mGluR) signaling pathway. In neuronal morphology, the distal branches of neurites in CalnI overexpressed neurons were obviously decreased. Moreover, the fluorescence imaging of CFP-CalnI and YFP-CaMKIIβ co-expressed HEK293T cells shows that the expression of CalnI does affect the localization of CaMKIIβ. Taken together, CalnI may regulate Ca2+ channels to influence neurotransmission, and possibly interacts with CaMKIIβ to further affect the synaptic development or plasticity. | en |
dc.description.provenance | Made available in DSpace on 2021-05-14T17:42:14Z (GMT). No. of bitstreams: 1 ntu-104-R02b21021-1.pdf: 1382751 bytes, checksum: 0527be8cdfc8febbd414969b42da269b (MD5) Previous issue date: 2015 | en |
dc.description.tableofcontents | Acknowledgement i
摘要 ii Abstract iii 1. Introduction 1 1.1 Ca2+ signaling and synaptic transmission 1 1.2 CaBPs and Calneuron I 2 1.3 Ca2+/calmodulin-dependent protein kinase II 4 1.4 Ca2+ signaling and neuronal morphology 6 2. Aims 7 3. Materials and Methods 8 3.1 Chemicals 8 3.2 Cell preparation 8 3.3 Plasmid construction 9 3.4 Transfection 10 3.5 Calcium imaging 11 3.6 Fluorescence imaging 12 3.7 Data analysis 13 4. Results 14 4.1 CalnI inhibits Ca2+ responses and neurotransmission 14 4.2 CalnI reduces CICR 15 4.3 CalnI affects mGluR but not AMPA receptor 17 4.4 CalnI reduces the distal neurite number of primary cortical neurons 17 4.5 CalnI affects the localization of CaMKIIβ in HEK293T cells 19 5. Discussion 20 5.1 CalnI inhibits Ca2+ response and neurotransmission 20 5.2 CalnI interferes with CICR pathway 22 5.3 CalnI inhibits mGluR signaling pathway 23 5.4 Morphology of CalnI expressing neurons 24 5.5 CalnI and CaMKIIβ interact with each other 25 6. Conclusion 27 7. References 28 Figures 35 | |
dc.language.iso | en | |
dc.title | Calneuron I與CaMKIIβ對於神經訊息傳遞的影響 | zh_TW |
dc.title | Effects of Calneuron I and CaMKIIβ on Neurotransmission | en |
dc.type | Thesis | |
dc.date.schoolyear | 103-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 王致恬,林崇智 | |
dc.subject.keyword | Calneuron I,CaMKIIβ,鈣離子誘導鈣釋放,人類胚腎細胞株293T,突觸傳導, | zh_TW |
dc.subject.keyword | Calneuron I,CaMKIIβ,CICR,HEK293T cell,synaptic transmission, | en |
dc.relation.page | 48 | |
dc.rights.note | 同意授權(全球公開) | |
dc.date.accepted | 2015-08-19 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 生命科學系 | zh_TW |
顯示於系所單位: | 生命科學系 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-104-1.pdf | 1.35 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。