請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76083完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | 方玫貞 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:17:53Z | - |
| dc.date.available | 2021-07-01T08:17:53Z | - |
| dc.date.issued | 1994 | |
| dc.identifier.citation | Ahn, K. Y., Madsen, K. M., Tishen, C. C., Kone, B. C. (1993). Differential expression and cellular distribution of mRNA encoding α and β isoforms of Na, K-ATPase in rat Kidney. Am. J. Physiol., 265, F792-F801.
Baxter - Lowe, L. A., Guo, J. Z., Bergstrom, E. E., Hokin, L. E., (1989).Molecular cloning of the Na, K-ATPase alpha-subunit in developing brain shrimp and seqence comaprision with higuer organisms. FEBS Lett., 257, 181-187 Beckman, B. R., Zaugg, W. S. (1990). Effect of actinomycin-D on gill Na, K-ATPase of juvenile Chinook salman, Oncorhynchus tshawytscha (Walbaum). J. Fish. Biol., 37, 907-911. Bell, M. V., Sargent, J. R. (1979). The partial purification of Na, K-ATPase from the gills of Anguilla anguilla and inhibition by orthovanadate. Biochem. J., 179, 431-438. Bertorello, A. M., Adrian, I. K. (1993). Short-term regulation of renal Na, K-ATPase activity: Physiological relevance and cellular mechanism. Am. J. Physiol., 265, F743-F755. Canfield, V. A., Xu, K. Y., D' aquila, T., Shyjan, A. W., Levenson, R. (1992). Molecular cloning and characterization of Na, K-ATPase from Hydra vulgaris: Implications for enzyme evolution and ouabain sensitivity. New Biol., 4, 339-348. Cretien, M., Pisam, M. (1986). Cell rewewal and differentiation in the gill epithelium of fresh -or salt- water - adapted euryhaline fish as revealed by 〔 H 〕 - thymidine radio autography. Biol. Cell. 56, 137-150. Detomaso, A. W., Xie, Z. J., Liu, G., Mercer, R. W. (1993). Expression, targeting, and assembly of functional Na, K-ATPase polypeptides in baculovirus-infected insect cells. J. Biol. Chem., 268, 1470-1478. Dietmar, K., Karl, J. (1991). Acclimation of chloride cells and. Na, K-ATPase to energy deficiency in tilapia (Oreochromis mossambicus). Zool. Jb. physiol., 95, 39-50 Dietmar, K., Ralf, B., Karl, J. Dietrich, S. (1992). Mitochondria rich (MR) cells and the activities of the Na, K-ATPase and carbonic anhydrase in the gill and opercular epithelium of Oreochromis mossambicus adapted to various salinities. Comp. Biochem. Physiol., 102B, 293-301. Eib, D. W., Hossner, K. L. (1985), The effect of cortisol and actinomycin-D injection on chloride cells and branchial Na, K–ATPase in rainbow trout (Salmo Gairdnen). Gem. Comp. Endocrinol.,59, 449-452. E1izabeth, A. J., Lingrel, J. B. (1991). Comparison of the substrate dependence properties of the rat Na, K-ATPase α1、α2、 α3 isoforms expressed in HeLa cells. J. Biol. Chem., 266, 16925-16930. Epstein, F. H., Manitius, E. W., Katz, A. I., Pickford, G. E. (1969). Sodium-and potassium-activated adenosine triphosphatase in kidney of Fundulus heteroclitus adapted to fresh and salt water. Yale J. Biol. Med., 41, 388-393. Forskett, J. K., Scheffey, C. (1982). The chlorides: definitive identification as the salt-secretory cell in teleosts. Science, 215, 164-166. Frank, K. B., Jensen, B., Andersen, B. B. (1993). Cardiac activity, ventilation rate and acid-base regulation in rainbow trout exposed to hypoxia and combined hypoxia and hypercapnia. Fish Physiol. Biochem., 12, 101-110. Gallis, J. L., Lasserre, P., Belloc, F. (1979). Freshwater adaptation in the euryhaline teleost ,Chelon labrosus. Effects of adaptation, prolacten, cortisol, and actionomycin-D on plasma osmotic balance and Na, K-ATPase in gill and kidney. Gen. Comp. Endocrinol., 38, 1-10. Geering, K. (1992). Subunit assembly and post translational processing of Na-pump. Acta. Physical. Scand., 146, 177-181. Gick, G. G., Hatula, M. A. Chon, D. Faramarz, I. B. (1993). Na, K-ATPase in several tissues of the rat: Tissue-specific expression of subunit mRNAs and enzyme activity. J. Membr. Biol., 131, 229-236. Goss, G. G., Perry, S. F., Wood, C. M., Laurent, P (1992). Mechanism of ion and acid-base regulation at the gills of freshwater fish.J. Exp. Biol., 263, 143-159. Hara, Y., Urayama, O., Kawakami, K., Nojima, H., Nagamune, Ho Kojima, T., Ohta, T., Nagano, K., Nakao, M. (1987). Primary structure of two types of alpha-subunit of rat brain Na, K-ATPase deduced from cDNA sequence. J. Biochem., 102, 43-58. Herrera, V. L. M., Emanuel, J. R., Ruiz-opazo, N., Levenson, R. Nadal-Ginard, B. (1987). Three differentially expressed Na, K-ATPase α subunit isoforms: Structural and functional implications. J. Cell Biol., 105, 1855-1865. Ho, S. M., Chan, D. K. O. (1979). Branchial ATPase and ionic transport in the eel Anguilla Japonica-I. Na, K-ATPase. Comp. Biochem. Physiol., 66B, 255-260. Horowitz, B., Hensley, C. B., Quintero, M., Azuma, K. K., Putnam, D., MaDonough, A. A. (1990). Differential regulation of Na, K-ATPase α1, α2 and β subunit mRNA and protein level by thyroid hormone. J. Biol. Chem., 265, 14308-14314. Hwang, P. P., Sun, C. M., Wu, S. M. (1989). Changes of plasma osmolatity, chloride concentration and gill Na, K-ATPase activity in tilapia Oreochromis concentration during seawater acclimation Marine Biol., 100, 295-299. Hwang, P. P., Wu, S. M. (1988). Salinity effects on cytometrical parameters of the kidney in the euryhaline teleost Oreochromis mossambicus peter. J. Fish Biol., 33, 89-95. Jaisser, F., Canessa, C., Horisberger, J., Rossier, B. C. (1992). Primary sequence and functional expression of a novel ouabain-resisttant Na, K-ATPase. J. Biol. Chem., 267, 16895-16903. Jewell, E. A. and Lingrel, J. B. (1991). Comparison of the substrate dependence properties of the rat Na, K-ATPase α1, α2, and α3 isoforms expressed in HeLa cells., J. Biol. Chem., 266, 16925-16930. Jewell, E. A., Shamraj, O. I., Lingrel, J. B. (1992). Isoforms of the α Subunit of Na, K-ATPase and their significance. Acta. Physiol. Scamd., 146, 161-169. Kawakami, K. Noguchi, S., Noda, M., Takahashi, H., Otha, T., Kawamura, M., Nojima, H., Nagano, K., Hirose, T., Inayama, S., Hayashida, H., Miyata, T., Numa, S. (1985). Primary structure of the α-subunit of Torpedo californica Na, K-ATPase doduced from cDNA sequence. Nature, 316, 733-736. Kawakami. K., Ohta, T., Nojima, H., Nagano, K. (1986). Primary structure of the α-subunit of Human Na, K-ATPase deduced from cDNA Sequence. J. Biochem., 100, 389-397. Kisen, G., Gallais, C., Auperin, B., Klungland, H., Sandra, O., Patrick. p., Andersen, O. (1994). Northern blot analysis of the Na, K-ATPase α subunit in salmonids. Comp. Biochem. Physiol., 107B, 255-259. Laurent, P. (1984). Gill internal morphology. In Fish physiology (Hoar, W. S. and Randall, D. J. eds.). Academic Press, New York., 10A, 73-183. Lafluer, G. T., Thomas, P. (1991). Evidence for a role of Na, K-ATPase in the hydration of atlantic croaker and spotted seatroutoocytes during final maturation. J. Exp. Zool., 258, 126-136. Lebovitz, R. M., Takeyase, K., Fambrough, D. M. (1989). Molecular characterisation and expression of the Na, K-ATPase alpha-subunit in Drosophila melangaster. EMBO J., 8, 193-202. Lingrel, J. B, (1992). Na, K-ATPase: isoform structure, function, and expression. J. Bioenerg. Biomembr., 24, 263-270. Lingrel, J. B., Orlowski. J., Shull, M. M. Price, E. M. (1990). Molecular genetic of Na, K-ATPase. Prog. Nucleic Acid Res.Mol. Biol., 38, 37-89. MacGregor, S. E., Walker, J. M. (1993), Inhibitors of the Na, K–ATPse. Comp. Biochem. Physiol., 105C, l-9. Macias, M. T. Martinez, J. L., Palmero, I. Sastre, L., (1990). Cloning of a cDNA encoding an Artermia franciscana Na, K-ATPase α subunit Gene, 105, 197-208. Mercer, R. W. (1993). Structure of the Na, K-ATPase. Int. Rev. Cytol.,173C, 139-168. Motais, R. (1969). Effect of actinomycin D on the branchial Na, K–dependent ATPase activity in relation to sodium balance of the eel. Comp. Biochem. Physiol., 34, 497-501. Mocharla, H., Mocharla, R., Hodes, M. E. (1990). Coupled reverse transcription-polymerase chain reaction (RT-PCR) as sensitive and rapid method for isozyme genotyping. Gene, 93, 271-275. Monastyrskaya, G. S., Broude, N. E. Melkov, A. M., Smirnov, Y. V., Malyshev, I. V., Arsenyan, S. G., Salomatina, I. S., Sverdlov, V. E., Grishin, A. V., Petrukhin, K. E., Modyanov, N. N. (1987). The primary structure of the alpha-subunit of Na, K-ATPase III. The completenucleotide seqence corresponding to the coding part of the gene. Bioorg. Khim., 13, 20-26. Orlowski, J., Lingrel, J. B. (1988a). Tissue-specific and developmental regulation of rat Na, K-ATPase catalytic α isoform and β subunit mRNAs. J. Biol. Chem., 263, 10436-10442. Orlowski, J,, Lingrel, J B. (1988b). Differential expression of the Na, K-ATPase α1, and α2 subunit genes in a murine myogenic cell Line. J. Biol. Chem., 263, 17817-17821. Orlowski, J., Lingrel, J, B. (1990). Thyroid and glucocorticoid hormone regulate the expression of multiple Na, K-ATPase genes in cutlured neonatal rat cardiac myocytes. J. Biol. Chem., 265, 3462-3472. Ovchinnikov, Y. A. Modyanov, N. N., Broude, N. E., Petrukhin, K. E., Grishin, A. V., Arzamazova, N. M. Aldanova, N. A., Monastyrskaya, G. S., Sverdlov E. D. (1986). Pig kidney Na, K-ATPase. FEBS Lett., 201, 237-245. Ovchinnikov, Y. A., Monastyrskaya, G. S., Broude, N, E., Ushkaryov, Y. A., Melkov, A. M., Smirnov, Y. V., Malyshev, I. V., Allikmets, R. L., Kostina, M. B., Dulubova, I. E., Kiyatkin, N. I., Grishin, A. V., Modyanov, N. N., Sverdlov, E. D. (1988). Human Na, K-ATPase alpha III. FEBS Lett., 233, 87-94. Pagliarani, A., Ventrella, V., Ballestrazzi, R., Trombetti, F., Pirimi, M., Trigari, G, (1991). Salinity-dependence of the properties of gill Na, K-ATPase in rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol., 100B, 229-236. Perry, S. F., Goss, G. G., Fenwick, J. C. (1992). Interrelationships between gill chloride cell morphology and calcium uptake in freshwater teleosts. Fish Physiol. Biochem., 10, 327-337. Peterson, G. L., Ewing, R. D., Hootman, S. R., Conte, F. P. (1978). Large scale partial purification and molecular and kinetic properties of the Na, K-ATPase from Artemia salina nauplii. J. Biol. Chem., 253, 4762-4770. Pfeiler, E., Kirschner, L. B. (1972). Studies on gill ATPase of rainbow trout (Salmo gairdneci) Biochim. Biophys. Acta, 282 301-310. Pisam, M., Rambourg, A. (1987). Two types of chloride cells in the gill epithelium of a freshwater-adapted euryhaline fish; Lebistes reticulates; their modification during adaptation to saltwater. Am. J. Anat., 179, 40-50. Pisam, M., Auperin, B., Prunet, D., Delrue, F. R., Ulartial, J., Rambourg, A. (1993). Effects of prolactin on α and β cells in the gill epithelium of the saltwater adapted tilapia Oreochromis niloticus. Anat. Rec., 235, 275-284. Price, E. M., Rice, D. A., Lingrel, J. B. (1990). Structure-function studies of Na, K-ATPase. J. Biol. Chem., 265, 6638-6641. Risinger, C., Larhammar, D. (1993). Multiple loci for synapse protein SNAP-25 in the tetraploid goldfish. Proc. Natt. Acad. Sci. USA, 90, 10598-10602. Schonrock, C., Morley, S. D., Okawasa, Y., Lederis, K., Richter, D. (1991). Sodium and potassium-ATPase of the teleost fish Catostomus comsnersoni: sequence, protein, structure and evolutionary conservation of the alpha subunit. Biol. Chem. Hoppe–Sey1er, 372, 279-286. Silva, P., Solomon, R., Spokes, K., Epstein, F. H. (1977). Ouabain inhibition of gill Na, K-ATPase: Relationship to active chloride transport. J. Exp. Zool., 199, 419-426. Shull, G. E., Schwartz, A., Lingrel, J. B. (1985). Amino-acid sequence of the catalytic subunit of the Na, K-ATPase deduced from a complementary DNA, Nature, 316, 691-695. Shull, G. E., Greek, J., Lingrel, J. B. (1986) .Molecular cloning of three distinct forms of the Na, K-ATPase α subunit from rat brain. Biochemistry, 25, 8125-8132. Shull, G. E. and Lingrel, J. B. (1987). Multiple genes encode the human Na, K-ATPase catalytic subunit. Proc. Natl. Acad. Sci. USA, 84, 4039-4043. Sweadner, K. J. (1989). Isozymes of the Na, K-ATPase. Biochim. Biophy Acta, 988, 185-220. Takeyasu, K., Tamkun, M. M., Renaud, K. J., Fambrough, D. M. (1988).Ouabain-sensitive Na, K-ATPase activity expressed in mourse L Cells by transfections with DNA encoding the alpha-subunit of an avian sodium pump. J. Biol. Chem., 263, 4347-4354. Takeyasu, K., Lemas, V., Fambrough, D. M. (1991). Stability of the Na, K-ATPase alpha-subunit isoforms in evolution. Am. J. Physiol., 259, 619-630. Verbost, P. M., Flik, G., Fenwick, J. C., Gerco, A., Pang, P. K T., Wendelaar Bonga, S. E. (1993). Branchial calcium uptake: possible mechanism of control by stanniocalcin. Fish Physiol. Biochem., 11, 205-215. Yoshikawa, J. S. M., Mccormick, S. D., Young, G., Bern, H. A.(1993). EffectS of salinity on chloride cells and Na, K-ATPase activity in the teleost Gillichthys mirabilis. Comp. Biocham. Physiol, 105A, 311-317. Young, R. M., Lingrel, J. B. (1987). Tissue distribution of mRNAs encoding the α isoforms and β subunit of rat Na, K-ATPase. Biochem. Biophy. Res. Com., 145, 52-58. Zahler, R., Maureen, G. H., Baldwin, J. C., Franco, K. Benz, E. J. (1993).Expression of α isoforms of the Na, K-ATPase in human heart. Biochim. Biophy. Acta, 1149, 189-194. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76083 | - |
| dc.description.abstract | 本研究探討廣鹽性吳郭魚( Oreochromis mossambicus )鰓是否表現不同型Na, K-ATPase α subunit 基因,以及這些基因是否分別在海水或淡水環境中表現不同的功能。 以 RT-PCR 方法找到吳郭魚至少具有 5 種不同型 Na , K-ATPase α subunit 基因。本實驗確定 TG3 (α1)、 TH23 、 TH6 、 S34-2 、 S34-9 是 Na , K-ATPase α subunit isoform 基因之證據包括: 1、在 GCG bank 作比對,氨基酸相似性最高的前 20 個蛋白質都是 Na , K-ATPase α subunit ,有 75 %-84 %以上相似性。 2、Na , K-ATPase α subunit 的 active site 氨基酸都相同 3、除 TH6 外,以其餘 4 種作 DNA 探針,進行各個組織 RNA 北方式點墨法,都具有 Na , K-ATPase α subunit 相近位置。 此外以 RT-PCR 方法得到一個較大的吳郭魚 Na , K-ATPase α subuni t DNA 片段,長約 1685bp ,命名為 OM α1,可轉譯為一個含 565 個氨基酸的蛋白質,進入 GCG bank 作氨基酸相似性比對,皆與已知動物 Na , K-ATPase α1 subunit 有 85 % 以上的相似性,而且 active site 的氨基酸都相同,因此推測OMαl 是屬於哺乳類 Na , K-ATPase α1 subunit 的相似基因。 本實驗以 2 種方法證明不論是海水或淡水鰓都具有不同型 Na , K-ATPase α subunit 基因表現。海水魚鰓與淡水魚鰓都具有 TG3 (α1)這型 Na, K-ATPase α subunit 而且基因表現量較其他 isoform 高。在 TG3 (α1) isoform,海水魚鰓的基因表現量高於淡水魚鰓。在 TH23 isoform,海水魚鰓基因表現量非常少;淡水魚鰓相對海水魚而言,基因表現量較高。至於 S34-2與S34-9 isoform 基因只表現在淡水魚鰓。淡水魚鰓比海水魚鰓表現較多型 Na , K-ATPase α subunit , 可以解釋淡水魚鰓和海水魚鰓完全不一樣的功能機制。 本實驗是第一次直接證明廣鹽性吳郭魚鰓有不同型 Na , K-ATPase α subunit 基因表現,而且不論是海水或淡水吳郭魚鰓表現最多的 Na , K-ATPase α subunit是α1。 | zh_TW |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:17:53Z (GMT). No. of bitstreams: 0 Previous issue date: 1994 | en |
| dc.description.tableofcontents | 摘要……………………………………………………………………………………………2
壹、前言………………………………………………………………………………………3 貳、材料與方法………………………………………………………………………………6 (1)材料……………………………………………………………………………………6 (2)實驗內容………………………………………………………………………………6 (3)實驗方法………………………………………………………………………………7 參、結果………………………………………………………………………………………16 (1) Na, K-ATPase α subunit cDNA 片斷……………………………………………l6 (2) Na, K-ATPase α sununit 部份 cDNA sequence…………………………………l6 (3) 吳郭魚基因體 DNA ( genomic DNA )的 Southern blot………………………l7 (4) Na, K-ATPase α subunit isoform probe專一性…………………………………17 (5) 淡水與海水吳郭魚鰓 Na, K-ATPase α subunit 基因表現……………………l8 (6) 吳郭魚不同組織器官 Na, K-ATPase α subunit isoform 基因表現 …………l9 (7) 不同鹽度環境,對鰓與腎臟 Na , K-ATPase α subunit 基因表現的影響 ……20 (8) 吳郭魚腎臟及腦的 cDNA library (基因庫)之篩選基因 …………………20 肆、討論………………………………………………………………………………………21 伍、附錄………………………………………………………………………………………26 陸、參考資料…………………………………………………………………………………30 柒、圖表 | |
| dc.language.iso | zh-TW | |
| dc.title | 吳郭魚鰓不同型 Na , K – ATPase α 次單原基因之研究 | zh_TW |
| dc.title | Study on gene of different isoforms of Na , K - ATPase α subunit in the gills of tilapia ( Oreochomis mossambicus ) | en |
| dc.date.schoolyear | 82-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 68 | |
| dc.rights.note | 未授權 | |
| dc.contributor.author-dept | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 漁業科學研究所 | zh_TW |
| 顯示於系所單位: | 漁業科學研究所 | |
文件中的檔案:
沒有與此文件相關的檔案。
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。
