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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 朱善德 | |
| dc.contributor.author | Hsien-Yeh Chou | en |
| dc.contributor.author | 周賢曄 | zh_TW |
| dc.date.accessioned | 2021-06-13T06:50:33Z | - |
| dc.date.available | 2008-07-30 | |
| dc.date.copyright | 2005-07-30 | |
| dc.date.issued | 2005 | |
| dc.date.submitted | 2005-07-28 | |
| dc.identifier.citation | 李倍慈 (2004) 國立台灣大學生化科學研究所 碩士論文
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(1999) Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21, pp396-399 Li, Y., Loike, J. D., Ember, J. A., Cleary, P. P., Lu, E., Budhu, S., Cao, L., Silverstein, S. C. (2002) The bacterial peptide N-formyl-Met-Leu-Phe inhibits Killing of Staphylococcus epidermidis by human neutrophils in fibein gels. Journal of immunology 168, pp816-824 Liu, Q. and Nilsen-Hamilton, M. (1995) Identification of a new acute phase protein. J. Biol. Chem. 270 pp22565-22570 Liu, Q., Ryon, J., Nilsen-Hamilton, M. (1997) Uterocalin: A mouse acute phase protein expressed in the uterus around birth. Moleculae reproduction and development 46, pp507-514 Lobert S., Vulevic B., and Correia J. J. (1996) Interaction of Vinca Alkaloid with tubulin: A comparison of Vinblastine, vincristine, and Vinorelbine. Biochemistry 35, pp6806-6814 Maetz-Boutigue, M. H., Jolles, J., Mazurier, J., Schoentgen, F., Legrand, D., Spik, G., Montreuiul, J., and Jolles, P. (1984) Human lactotransferrin: amino acid sequence and structural comarisons with other transferrins. Eur. J. Biochem. 145, pp659-676 Martinez, L. O., Jacquet, S., Esteve, J. P., Rolland, C., Cabezon, E., Champagne, E., Pineau, T., Georgeaud, V., Walker, J. E., Terce, F., Collet, X., Perret, B., Barbaras, R. (2004) Ectopic β- chain of ATP synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis. Nature 421, pp75-79 Masson, P.L., and Heremans J.F. (1966) Studies on lactoferrin, the ironbinding proteins of secretions. Biol. Fluids proc. Colloq. Bruges. 12, pp115-124 Masson, P.L., Heremans, J.F., Schonne, E. (1969) Lactoferrin, an iron-binding proteib in neutrophilic leukocytes. J. Exp. Med. 130, pp643-658 Meheus, L. A., Fransen, L. M., Raymackers, J. G., Blockx, H. A., Van Beeumen, J. J., Van Bun, S. M., Van de Voorde, A. (1993) Identification by microsequencing of lipopolysaccharide-induced proteins secreted by mouse macrophages. J. Immunol 151, pp1535-1547 Michikawa, Y., Baba, T., Arai, Y., Sakakura, T., Kusakabe, M. (1993) Structure and organization of the gene encoding a mouse mitochondrial stress-70 protein. FEBS 1, pp27-33 Moser, T. L., Stack, M. S., Asplin, I., Enghild, J. J., Hojrup, P., Everitt, L., Hubchak, S., Schnaper, H. W., Pizzo, S. V. (1999) Angiostatin binds ATP synthase on the surface of human endothelial cells. Proc. Natl. Acad. Sc. USA 96, pp2811-2816 Murray, J. W. and Wolkoff A. W. (2003) Roles of the cytoskeleton and motor proteins in endocytic sorting. Adv. Drug Delivery Rew 55, pp1385-1403 Newbold, R. B., Teng, C. T., Beckman, W. C., Jr., Jefferson, W. N., Hanson, R. B., Miller, J. V., and McLacjlan, J. A. (1992) Fluctuations of lactofererin protein and messenger ribonucleic acid in the reproductive tract of the mouse during te estrous cycle. Biol. Reprod. 47, pp903-915 Nilsen-Hamilton, M., Hamilton, R. T., Adams, G. A. (1982) Rapid selective stimulation by growth factors of the incorporation by BALB/C 3T3 cells of [35S]methionine into a glycoprotein and five superinducible proteins. Biochem Biophys Res Commun. 108, pp158-166 Nilsen-Hamilton, M., Liu, Q., Ryon, J., Lee, B., Lepont, P., and Chang, Q. (2003) Tissue involution and the acute phase response. Ann.N.Y.Acad.Sci 995, pp94-108 Pederson, P. L., and Amzel L. M. (1993) ATP synthases. Structure, reaction center, mechanism, and regulateon of one of nature’s most unique mechanism. J. Biol. Chem. 268, pp9937-9940 Pentecost, B. T., and Teng, C.T. (1987) Lactotransferrin is the major estrogen inducible protein of mouse uterine secretion. J. Biol. Chem. 262, pp10134-10139 Ryon, J., Bendickson, L., Nilsen-Hamilton, M. (2002) High expression in involuting reproductive tissue of uterocalin/24p3, a lipocalin and acute phase protein. Biochem. J. 367, pp271-277 Saito, A., Pietromonacom S., Loo, A.K. and Farquhar, M.G. (1994) Complete cloning and sequencing of rat gp330/'megalin', a distinctive membrane of the low density lipoprotein receptor gene family. Proc. Natl. Acad. Sc. USA 91, pp9725-9729 Scheiber, B., and goldenberg, H. (1993) NAD(P)H: ferric iron reductase in endisomal membranes from rat liver. Arch. Biochem. Biophys. 305, pp225-230 Teng, C.T., Pentecost, B.T., Chen, Y.H., Newbold, R.R., Eddy, E.M., and McLachlan, J.A. (1989) Lactoferrin gene expression in the mouse uterus and mammary gland. Endocrinology 124, pp992-999 Teng, C.T., Walker, M. P., Bhattacharyya, S.N., Klapper, D.G., DiAugustine, R.P., and McLachlan, J.A. (1986) Purification and properties of an oestrogen-stimulated mouse uterine glycoprotein. Biochem. 240, pp413-422 Triebel S., Blaser J., Reinke H. and Tschesche H. (1992) A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase. FEBS Letters 341, pp386-388 Trif, M., Sekine, K., Kuhara, T., Takasuka, N., Iigo, M., and Tsuda H. (1998) Liposomes as possible carrier foe lectoferrin in the local treatment of inflammatory diseases. Exp. Biol. Med 226, pp559-564 Urbanik, E. (1989) Actin filament capping and cleaving actiyity of cytochalasins B, D, E, and H. Archives of biochemistry and biophysics 269, pp181-187 Van Leuven, F., Cassiman, J. J., Van Den Berghe, H. (1980) Primary amines inhibit recycling of α2M receptors in fibroblaste. Cell 20, pp37-43 Walmer, D.K., Wrona, M.A., Hughes, C.L., and Nelson, K.G. (1992) Latofreein expression in the mouse reproductive tract during the natural estrous cycle: correlation with circulatng estradiol and progesterone. Endocrinology 131, pp1458-1466 Ward, P., Mendoza-Meneses, M., Mulac-Jericevic, B., Cunningham, G., Saucedo-Cardenas, O., Teng, C., and Conneely, O. (1999) Restricted spatiotemporal expression of lactoferrin during nurine embryonic development. Endocrinology 140, pp1852-1860 Wojnar, P,, Lechner, M., Redlm B. (2003) Antisense Down-regulation of Lipocalin-interacting Membrane Receptor Expression Inhibits Cellular Internalization of Lipocalin-1 in Human NT2 Cells. J. Biol. Chem 278, pp16209-16215 Yang, J., Goetz, D., Li, J. Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., Barasch, J. (2002) An iron dilivery pathway mediated by a liprocalin. Molecular Cell 10, pp1045-1056 Yu, L. C. and Chen, Y. H. (1993) The developmental profile of lactoferrin in mouse epididymis. Biochem J. 296, pp107-11 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/35385 | - |
| dc.description.abstract | 24p3蛋白為分子量25.8 kD的醣蛋白，屬於疏水性分子結合蛋白家族中的一員。24p3蛋白會在雌鼠動情前期之子宮組織表現並分泌至子宮腔內。小鼠副睪是雄鼠唯一發現24p3蛋白表現的生殖系統組織。此蛋白可結合於精蟲的頭端，增強其活動性，但抑制由牛血清蛋白引發的精蟲獲能作用並減低小鼠受孕能力。在血球細胞上被認為與環境壓力和細胞凋亡有關，但在生物體確實的功能至今尚未明瞭。
疏水性分子結合蛋白家族可能是藉由細胞表面受體調控的內吞作用攜帶疏水性分子進入細胞中促成進一步的訊號傳遞，因此推測24p3蛋白會與細胞表面蛋白結合，引發細胞生理作用的改變。實驗室之前的研究中發現24p3蛋白可進入小鼠結締組織細胞株L929，有引發細胞凋亡的可能，因此利用L929細胞株探討24p3蛋白進入細胞的路徑及尋找細胞上未知的24p3蛋白結合蛋白，以期待未來24p3蛋白對傳遞分子訊息的研究有所幫助。本實驗證實了24p3蛋白確實會與L929細胞表面進行專一性結合。實驗中使用影響受體調控內吞作用的藥物則可影響24p3蛋白在細胞內的傳遞，確實了解24p3蛋白進入細胞之路徑。由24p3蛋白與溶酶體膜上的Lamp-2蛋白在L929細胞內的結合位置一致的觀察結果，以及內吞至細胞內biotin標記24p3蛋白的減少，顯示24p3蛋白可能內吞至細胞後進入分解的階段。萃取細胞膜蛋白進行二維電泳後，轉漬到PVDF膜，進行24p3蛋白結合實驗結果顯示有一較強的結合蛋白，並利用24p3蛋白建立的親和性管柱分析，分離出幾個可能和24p3蛋白結合的膜蛋白，希望未來能藉由質譜儀定序的結果找出L929細胞膜上與24p3蛋白結合的蛋白質，提供24p3蛋白在細胞功能研究的基礎。 | zh_TW |
| dc.description.abstract | 24p3 protein is a 25.8 kD glycoprotein which belongs to the lipocalin superfamily. It is expressed and secreted from uterine endometrial epithelia during the proestrous phase of female mice, but is constitutively expressed in epididymis. The protein could associate with sperm head and then enhance the sperm motility, but was suggested as a stressor of sperm capacitation and fertility. It was also considered as an apoptotic factor or inflammatory factor in blood cells. The real function is unclear. Our previous studies showed that 24p3 protein could internalize into the cell and had effects on mouse connective tissue cell line, L929.
Lipocalin has been proposed internalizing into the cells via receptor-mediated endocytosis and triggering further signal transduction. The unclearity of the 24p3 protein interacting molecule in cell membrane encouraged us to find out the interacting molecule(s) from the cell. Using L929 cell line as a model, we attempted to demonstrate the unknown interacting protein and transition pathway. The competition assay and endocytosis inhibition studies indicated that 24p3 protein could bind to the cell surface specifically and transport into the cell via receptor-mediated endocytosis pathway. Observation the locations of FITC-LAMP-2 Ab(lysosome- associated membrane protein-2 antibody) and the Alexa555-24p3 protein under fluorescence microscope revealed that the 24p3 protein should be localized in lysosome. The degradation of internalized 24p3 protein in L929 cells coincided with the colocalization of 24p3 and lysosome. Western blotting analysis of L929 cell membrane protein extract with 24p3 protein showed stress-70 protein might be the interacting protein of 24p3 protein in the PVDF membrane. We constructed a 24p3 protein-coupled affinity column to separate several 24p3 protein associated-membrane protein candidates after flow in the L929 cell membrane protein extract. Furthermore, we will identify the interacting protein of 24p3 protein from L929 cell line by the mass spectrum analysis and elucidate the 24p3 protein signal transduction in the cells. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T06:50:33Z (GMT). No. of bitstreams: 1 ntu-94-R92b46032-1.pdf: 687729 bytes, checksum: e9238adc1ef00b47cc7f6ac115095866 (MD5) Previous issue date: 2005 | en |
| dc.description.tableofcontents | 目錄…………………………………………………1
圖表目錄……………………………………………………………3 中文摘要………………………………………………………………4 英文摘要…………………………………………………………………5 縮寫表……………………………………………………………………6 第一章 緒論 24p3蛋白…………………………………………………………………8 研究背景……………………………………………………………… 9 本實驗室研究成果…………………………………………………12 本論文研究方向………………………………………………………13 第二章 實驗材料與方法 材料…………………………………………………………………16 方法 小白鼠結締組織細胞株 (ATCC CCL-1，L929) 細胞培養……20 小白鼠子宮液的製備……………………………………………21 小白鼠子宮液中24p3蛋白質純化………………………………21 蛋白質定量……………………………………………………23 24p3蛋白標記…………………………………………………24 24p3蛋白與L929細胞株之結合…………………………………26 24p3蛋白的內吞作用……………………………………………26 影響內吞作用之分子……………………………………………27 Lamp-2免疫螢光染色……………………………………………27 SDS-聚丙烯醯胺膠體電泳………………………………………28 Sypro®Ruby染色………………………………………………30 銀染………………………………………………………………31 西方轉漬法(Western blotting) ……………………………31 蛋白質沉澱……………………………………………………3１ 24p3蛋白於細胞內結果觀察……………………………………33 L929細胞膜蛋白萃取……………………………………………34 Biotin標記L929細胞膜蛋白……………………………………35 二維電泳…………………………………………………………35 24p3親和性管柱…………………………………………………３7 蛋白質身分鑑定…………………………………………………38 第三章 實驗結果 24p3蛋白與L929細胞株之結合…………………………………41 24p3蛋白在L929細胞內可能的傳遞路徑…………………………41 與24p3蛋白作用之L929細胞膜蛋白………………………………44 第四章 討論 討論…………………………………………………………………59 參考文獻………………………………………………………………65 | |
| dc.language.iso | zh-TW | |
| dc.title | 利用結締組織細胞株L929探討小白鼠子宮分泌24p3蛋白質的內吞作用機制 | zh_TW |
| dc.title | Mechanism of 24p3 Protein, Mouse Uterine Secretory Protein Internalizes to L929 Cell Line | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 93-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 曾婉芳,余榮熾,張?仁 | |
| dc.subject.keyword | 子宮分泌蛋白質,24p3蛋白質,L929細胞株,內吞作用, | zh_TW |
| dc.subject.keyword | Uterine secretory protein,24p3 protein,L929 cell line,endocytosis, | en |
| dc.relation.page | 74 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2005-07-28 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科學研究所 | zh_TW |
| 顯示於系所單位： | 生化科學研究所 | |
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