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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 潘建源(Chien-Yuan Pan) | |
dc.contributor.author | Ruo-Lin Kang | en |
dc.contributor.author | 康若琳 | zh_TW |
dc.date.accessioned | 2021-06-13T03:39:38Z | - |
dc.date.available | 2006-07-29 | |
dc.date.copyright | 2006-07-29 | |
dc.date.issued | 2006 | |
dc.date.submitted | 2006-07-25 | |
dc.identifier.citation | Akaike, N. 1991. T-type calcium channel in mammalian CNS neurones. Comp Biochem Physiol C. 98:31-40.
Artalejo, C., Elhamdani A, Palfrey HC. 1996. Calmodulin is the divalent cation receptor for rapid endocytosis, but not exocytosis, in adrenal chromaffin cells. Neuron. 16:195-205. Carbone, E.L.H.D. 1984. A low voltage-activated, fully inactivating Ca channel in vertebrate sensory neurones. Nature. 310:501-2. Chin, D., Means, A R. 2000. Calmodulin: a prototypical calcium sensor. Trends Cell Biol. 10:322-8. Crill, W.E. 1996. Persistent sodium current in mammalian central neurons. Annu Rev Physiol. 58:349-62. Fanger, C.M., Ghanshani, S., Logsdon, N. J., Rauer, H., Kalman, K., Zhou, J., Beckingham, K., Chandy, K. G., Cahalan, M. D., and Aiyar, J. 1999. Calmodulin mediates calcium-dependent activation of the intermediate conductance KCa channel, IKCa1. J Biol Chem. 274:5746-54. Fatt, P., and B.L. Ginsborg. 1958. The ionic requirements for the production of action potentials in crustacean muscle fibres. J Physiol. 142:516-43. Fatt, P., and B. Katz. 1953. The electrical properties of crustacean muscle fibres. J Physiol. 120:171-204. Garcia-Palomero, E.C.-I., I; Garcia, A G; Renart, J; Albillos, A; Montiel, C. 2000. Greater diversity than previously thought of chromaffin cell Ca2+ channels, derived from mRNA identification studies. FEBS Lett. 481:235-9. Haeseleer, F., Y. Imanishi, T. Maeda, D.E. Possin, A. Maeda, A. Lee, F. Rieke, and K. Palczewski. 2004. Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in photoreceptor synaptic function. Nat Neurosci. 7:1079-87. Haeseleer, F., Imanishi Y, Sokal I, Filipek S, Palczewski K. 2002. Calcium-binding proteins: intracellular sensors from the calmodulin superfamily. Biochem Biophys Res Commun. 290:615-23. Haeseleer, F., I. Sokal, C.L. Verlinde, H. Erdjument-Bromage, P. Tempst, A.N. Pronin, J.L. Benovic, R.N. Fariss, and K. Palczewski. 2000. Five members of a novel Ca(2+)-binding protein (CABP) subfamily with similarity to calmodulin. J Biol Chem. 275:1247-60. Halling, D., Aracena-Parks P, Hamilton SL. 2006. Regulation of voltage-gated Ca2+ channels by calmodulin. Sci STKE. 2006:er1. Higuchi, R. 1990. Recombinant PCR. In: PCR Protocols. A Guide to Methods and Applications (MA Innis, DH Gelfand, JJ Sninsky, TJ White, eds). Academic Press, San Diego, CA.:177-183. Higuchi R, K.B., Saiki RK. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16:7351-7367. Karl, D., Kevin Heist, Richard WT. 1998. Translocation of calmodulin to the nucleus supports CREB phosphorylation in hippocampal neurons. Nature. 392:198-202. Kasri, N., Holmes AM, Bultynck G, Parys JB, Bootman MD, Rietdorf K, Missiaen L, McDonald F, De Smedt H, Conway SJ, Holmes AB, Berridge MJ, Roderick HL. 2004. Regulation of InsP3 receptor activity by neuronal Ca2+-binding proteins. EMBO J. 23:312-21. Epub 2003 Dec 18. Lee, A., Ruth E. Westenbroek, Françoise Haeseleer, Krzysztof Palczewski1, Todd Scheuer, William A. Catterall. 2002. Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1. Nat Neurosci. 5:210-217. Locke, F.S. 1894. Notiz uber den Einfluss, physiologisher Kochsalzlosung auf die Eregbarkeit von Muscel and Nerve. Zentralbl. Physiol. 8:166-167. Meldolesi, J., Pozzan T. 1987. Pathways of Ca2_ influx at the plasma membrane: voltage-, receptor-, and second messenger-operated channels. Exp Cell Res. 171:271-283. Meves, H. 1968. The ionic requirements for the production of action potentials in helix pomatia neurones. Pflugers Arch. 304:215-241. Miller, R. 1987. Multiple calcium channels and neuronal function. . Science 235:46-52. Overton, E. 1904. Beitrage zur allgemeinen Muskel- und Nerven physiologie. III. Mittheilung. Studien uber die Wirkung der Alkali- und Erdkali-salze auf Skeletalmuskeln und Nerven. Pflugers Arch. 155:176-290. Pan CY, K.L. 1997. Catecholamine secretion from bovine adrenal chromaffin cells: the role of the Na+/Ca2+ exchanger and the intracellular Ca2+ pool. J. Neurochem. 69:1085-1092. Peterson, B.Z., DeMaria, C. D., and Yue, D. T. 1999. Calmodulin is the Ca2+ sensor for Ca2+ -dependent inactivation of L-type calcium channels. Neuron. 22:549-58. Polans, A., Baehr, W., and Palczewski, K. 1996. Turned on by Ca2+! The physiology and pathology of Ca(2+)-binding proteins in the retina. Trends Neurosci. 19:547-54. Ringer, S. 1883. A further contribution regarding the influence of different constituents of the blood on the contractions of the heart. J. Physiol. (Lond.). 4:29-43. Ringer, S. 1886. Further experiments regarding the influence of small quantities of lime, potassium and other salts on muscular tissue. J. Physiol. (Lond.). 7:291-308. Ringer, S., H. Sainsbury. 1894. The action of potassium, sodium and calcium salts on Tubifex rivulorum. J. Physiol. (Lond.). 16:1-9. Ringer, S., L.W. Buxton. 1887. Concerning the action of calcium, potassium and sodium salts upon the eel’s heart and upon skeletal muscles of the frog. J. Physiol. (Lond.). 8:15-19. Rizzuto, R., Pozzan T. 2006. Microdomains of intracellular Ca2+: molecular determinants and functional consequences. Physiol Rev. 86:369-408. S. Hagiwara, S.N. 1966a. Differences in Na and Ca spikes as examined by application of tetrodotoxin, procaine, and manganese ions. J. Gen. Physiol. 49:793-806. S. Hagiwara, S.N. 1966b. Effects of the intracellular Ca ion concentration upon the excitability of the muscle fiber membrane of a barnacle. J. Gen. Physiol. 49:807-818. V. Gerasimov, P.K., V. Maisky. 1964. Excitability of giant nerve cells of various representatives of pulmonary molluscs in the sodium-free solutions. Bull. Exp. Biol. Med. Moscow 58:3-7. Wilson SP, L.F., Wilson RE, Housley R. 1995. Optimization of calcium phosphate transfection for bovine chromaffin cells: relationship to calcium phosphate precipitate formation. Anal Biochem. 226:212-20. Y. Oomura, S.O., T. Maeno. 1961. Electrical activity of a giant nerve cell under abnormal conditions. Nature. 191:1265-1267. Zhou, H., Kim SA, Kirk EA, Tippens AL, Sun H, Haeseleer F, Lee A. 2004. Ca2+- binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-Type) Ca2+ Channels. Journal of Neuroscience. 24:4698-4708. Zuhlke, R.D., Pitt, G. S., Deisseroth, K., Tsien, R. Y., and Reuter, H. 1999. Calmodulin supports both inactivation and facilitation of L-type calcium channels. Nature. 399:159-62. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/32264 | - |
dc.description.abstract | 鈣離子結合蛋白 (Ca2+-binding protein 1-5, CaBP1-5) 是一群與calmodulin有高度相似性結構的蛋白質,目前僅知CaBP1及CaBP4會調控鈣離子通道的活性,而其它蛋白的功能則尚不清楚。本篇報告中,我們以PCR技術從大鼠 (Rattus norvegicus) 胚胎的大腦組織中選殖出CaBP5基因,再予以表現於兩類型興奮性細胞中,來探討其對刺激-分泌耦合機轉的調控。細胞螢光染色結果顯示,CaBP5-EYFP主要分布於細胞質中,有些則會集中於細胞核。利用細胞電生理技術,我們發現 CaBP5的大量表現會使神經細胞的鈣離子通道的開啟降低至較負電位,失去第一個 EF-hand正常功能的突變型 (5EF1) 則沒有作用。但在牛腎上腺嗜鉻細胞 (bovine chromaffin cell) 中,CaBP5對其鈣離子通道沒有同樣影響,藉由測量細胞膜電容的變化發現CaBP5的表現,也不會影響胞吐和胞吞作用。在牛腎上腺嗜鉻細胞中,CaBP5對鈣離子通道沒有同樣的作用,也沒有對胞吐 (exocytosis) 和胞吞作用 (endocytosis) 造成明顯的影響;另外,CaBP5對鈉離子電流沒有影響,但5EF1的表現增強了鈉離子電流。以上觀察顯示CaBP5可能參與神經細胞膜的鈣離子電流調控,而對鈉離子電流的影響不明顯;但在牛腎上腺嗜鉻細胞,5EF1增強了鈉離子電流的大小。 | zh_TW |
dc.description.abstract | Ca2+ -binding proteins 1-5 (CaBP1-5) are a group of proteins with structure similar to calmodulin. CaBP1 and CaBP4 have been reported to modulate the Ca2+ currents and synaptic plasticity of neurons; however, functions of other proteins have not been extensively investigated. In this report, functions of CaBP5 in excitable cells were studied. CaBP5 was cloned from rat (Rattus norvegicus) embryonic brain tissue and inserted into pEYFP-N1 for expression. Normally it was localized in the cytosol, but it may concentrat in the nucleus in some cells. We applied whole-cell patch clamping technique to monitor the electrophysiological properties of excitable cells. The results show that CaBP5 shifted the activation of Ca2+ channels to hyperpolarized voltages in primary neuron culture, but mutant CaBP5 with the first nonfunctional EF-hand didn’t have the same effect. When CaBP5 was expressed in cultured bovine adrenal chromaffin cells, neither the Ca2+ currents nor the exocytosis was affected, but the Na+ currents were enhanced. These observations indicate that CaBP5 may be involved in regulation of Ca2+ channels in neurons but enhanced Na+ currents in chromaffin cells. | en |
dc.description.provenance | Made available in DSpace on 2021-06-13T03:39:38Z (GMT). No. of bitstreams: 1 ntu-95-R92b41017-1.pdf: 461945 bytes, checksum: 6aeab7c4211b93b91d36dcae610cbc0c (MD5) Previous issue date: 2006 | en |
dc.description.tableofcontents | 1.摘要
1.1 中文摘要..................................................... 1 1.2 英文摘要.....................................................2 2.前言 2.1 Calmodulin...................................................3 2.2 鈣離子結合蛋白...............................................4 2.3 實驗目標.....................................................5 3. 材料與方法 3.1 溶液........................................................ 7 3.2 RNA 製備與 cDNA 合成..................................... 7 3.3 CaBP5 轉接入 pEYFP-N1 載體與核苷酸點突變合成.............8 3.4 神經細胞與牛腎上腺嗜鉻細胞培養...............................9 3.5 基因轉殖 (Gene Transfection) 與細胞螢光染色................... 9 3.6 細胞電生理技術..............................................10 3.7 統計分析....................................................11 4. 結果 4.1 CaBP5 表現於大鼠的視網膜與胎鼠的大腦組織中................ 12 4.2 CaBP5 主要是均勻分布於神經細胞中,少數集中於細胞核內...... 12 4.3 CaBP5使神經細胞的鈣離子通道的開啟降低至較負電位...........13 4.4 CaBP5對神經細胞的鈉離子電流沒有影響.......................13 4.5 CaBP5 對牛腎上腺嗜鉻細胞的鈣離子電流沒有同樣影響.......... 14 4.6 CaBP5對牛腎上腺嗜鉻細胞的鈉離子電流有增強的效果........... 14 4.7 CaBP5 對牛腎上腺嗜鉻細胞的胞吐和胞吞作用沒有影響.......... 15 5. 討論...........................................................16 6. 致謝...........................................................20 7. 圖表...........................................................21 8. 參考文獻...................................................... 32 | |
dc.language.iso | zh-TW | |
dc.title | 鈣離子結合蛋白5在興奮性細胞的生理功能研究 | zh_TW |
dc.title | Functions of Ca2+-Binding Protein 5 in Excitable Cells | en |
dc.type | Thesis | |
dc.date.schoolyear | 94-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 陳建璋(Chien-Chang Chen),閔明源(Ming-Yuan Min),林崇智(Chung-Chih Lin) | |
dc.subject.keyword | 鈣離子結合蛋白,神經細胞,牛腎上腺嗜鉻細胞,鈣離子通道,鈉離子通道,分泌作用, | zh_TW |
dc.subject.keyword | Ca2+ -binding protein 5,neuron,bovine chromaffin cell,voltage-gated Ca2+ channel,voltage-gated Na+ chabnnel,exocytosis,endocytosis, | en |
dc.relation.page | 35 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2006-07-27 | |
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 |
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