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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | Fan Jun 一 Huei | en |
| dc.contributor.author | 範潤薈 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:12:47Z | - |
| dc.date.available | 2021-07-01T08:12:47Z | - |
| dc.date.issued | 2002 | |
| dc.identifier.citation | Akiyama S.K. 1996. Integrins in cell adhesion and signaling. Hum Cell. 3: 181-186.
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75348 | - |
| dc.description.abstract | 本論文藉由S-ras (Q61K) Balb / 3T3細胞，去探討當細胞內膽固醇的生合成路徑遭到阻礙時，細胞內與訊息傳導相關的蛋白integrin βl , caveolin-l (Cav-l）以及FAK之間的交互作用。 本論文首先利用不同濃度的SB-14分次萃取pcDNA 3.1 Balb/3T3細胞以及shrimp-ras (Q61K) pcDNA3.1 Balb/3T3轉型細胞之膜蛋白，發現無論在pcDNA 3.1Balb/3T3細胞中或者 shrimp-ras (Q61K) pcDNA3.1 Balb/3T3轉型細胞中，絕大多數(~99%）的integrinβ1都出現在以0.1% SB-14處理後的細胞膜之蛋白液中。當細胞分別處理10μM mevastatin以阻斷 mevalonate pathway，在0.1% SB-14所抽取的pcDNA 3.1 Balb/3T3細胞之細胞膜蛋白萃取液中，Cav-l的量上升。在免疫沈澱法實驗中，未處理過mevastatin的shrimp-ras(Q61K) pcDNA 3.1 Balb/3T3轉型細胞，其在integrin βl上有Cav-l量的增加而形成 integrin βl-Cav-l complex，以及integrin βl上降解的FAK；經由mevastatin的處理後，在轉殖pcDNA 3.1質體的Balb/3T3細胞中的integrin β1上也有Cav-1量的增加，形成integin βl-Cav-1 complex，同樣integrin βl上也出現降解的FAK。推論經過mevastatin處理的pcDNA 3.1 Balb/3T3細胞，在0.1% SB-14所抽取的細胞膜之蛋白液中增加的Cav-l，可能用以協助細胞形成integrin βl-Cav-1 complex。 PKD為golgi 中參與蛋白質傳遞的分子，而細胞中的Cav-l必須經由golgi傳送。為了推測integrin complex上增量的Cav-1來自於何處，所以分別將經過或未經過mevastatin處理的細胞染測PKD以及phospho-PKD。結果顯示pc DNA 3.1 Balb/3T3細胞和S-ras (Q61K) Balb/3T3轉型細胞中，存在未磷酸化的PKD，此種PKD不具有運輸蛋白質的能力以推論integrin complex上增量的Cav-l是由Caveolae而來。再進一步以GGTI-286以及FTI-277處理細胞。實驗結果顯示，經過GGTI-286或FTI-277抑制prenylation作用後的轉殖或未轉殖S-ras (Q61K）的細胞中，染測不到活化的integrin complex。所以推論當細胞中prenylation 作用被抑制後，Cav-1無法在膜上被傳送。 | zh_TW |
| dc.description.abstract | BALB/3T3 cells transfected with DNA encoding shrimp Penaeus japonicus S-ras (Q61K) were transformed successfully. The interaction among integrin βl, caveolin-1 (Cav-1), and focal adhesion kinase (FAK) was studied while the biosynthesis of cholesterol was blocked. The amount of caveolin-1 in the membrane fraction of the transformed BALB/3T3 cells that was extractable with 0.1% Sulfobetaine-14 was significant larger than in pcDNA 3.l-transfected BALA/3T3 cells. The possible interaction of caveolin-1 with β1 integrin was investigated. Most of the caveolin-1 in the 0.1% Sulfobetaine-14 lysates of S-ras(Q61)-transformed BALB/3T3 cells was associated with β1 integrin, but the signal transmission of βl integrin-FAK was inhibited by the proteolysis of FAK. On the other hand, caveolin-1 in the 0.1% Sulfobetaine-14 lysates of mock-transfected BALB/3T3 cells was found to be free from binding with β1 integrin and the β1 integrin-FAK was intact for signal transmission. Following treatment by mevastatin ( a HMG -CoA reductase inhibitor) to prevent the mevalonate pathwav, mock-transfected BALB/3T3 cells exhibited additional amounts of caveolin-1 in the 0.1% Sulfobetaine-14 extractable membrane lysates, but transformed BALB/3T3 cells did not. Most of the 0.1% Sulfobetaine-1-extractable caveolin-1 in the mock-transfected and mevastatin treated BALB/3T3 was bound with β1 integrin, but the signal transmission of β1 integrin-FAK was inhibited by the proteolysis of FAK, mimicking the results in cells transformed with S-ras (Q61K). However, electron microscopy revealed no morphological identity between mevastatin-treated and S-ras (Q61K）-transformed BALB/3T3 cells. In addition, the recruitment of caveoli-1 with β1 integrin was not detectable after further incubation of S-ras (Q61K)-transformed BALB/3T3 cells with 10μM mevastatin for 3.5 hrs. However, the signal transmission of βl integrin-FAK was sustained, as arrested by the proteolysis of FAK. In other words, the recruitment of caveolin-1 with β1 integrin functions as a molecular switch that responds to cholesterol deprivation, but the proteolytic degradation of FAK does not. Furthermore, pcDNA3.l-transfected BALA/3T3 cells and S-ras(Q61K)- transformed Balb/3T3 cells were treated with 10μM GGTI-286 or 10μM GGTI-277 for 1 hr. The results show that there is no active integrin complex in pcDNA3.l-transfected BALB/3T3 cells and S-ras (Q6lK)-transformed BALB/3T3 cells. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:12:47Z (GMT). No. of bitstreams: 0 Previous issue date: 2002 | en |
| dc.description.tableofcontents | 致謝………………………………………………………………………………………………………………1 目錄………………………………………………………………………………………………………………3 中文摘要…………………………………………………………………………………………………………5 英文摘要…………………………………………………………………………………………………………7 引言………………………………………………………………………………………………………………9 Caveolin的作用……………………………………………………………………………………………9 Integrin complex…………………………………………………………………………………………10 PDK 的生理活性……………………………………………………………………………………………12 膽固醇的生合成路徑之簡介………………………………………………………………………………13 Mevastatin、GGTI-286以及 FTI-277的簡介……………………………………………………………14 S-ras（Q61K)的細胞特性…………………………………………………………………………………15 實驗方法…………………………………………………………………………………………………………17 細胞培養……………………………………………………………………………………………………17 蛋白質膠體電泳及染色……………………………………………………………………………………18 西方墨點法…………………………………………………………………………………………………19 免疫沉澱法…………………………………………………………………………………………………20 西方墨點法與免疫沉澱法的比較…………………………………………………………………………21 分次萃取細胞膜蛋白的方法………………………………………………………………………………22 蛋白質定量…………………………………………………………………………………………………23 結果………………………………………………………………………………………………………………24 細胞外形……………………………………………………………………………………………………24 用不同濃度的 SB-14分次萃取細胞膜蛋白………………………………………………………………24 抑制mevalonate pathway時，pcDNA 3.1Balb/3T3細胞內之Cav-1量增加……………………………25 Shrimp-ras(Q16K）pcDNA3.1Balb/3T3轉型細胞內，其integrinβ-1上有Cav-1量的增加…………27 在以mevastatin處理後的pcDNA 3.1 Balb/3T3細胞裡, 其integrinβl上也有Cav-1量的增加……27 FAK的降解跟integrinβl上 Cav-1量的增加之情形無關………………………………………………28 電子顯微鏡下分析經由mevastatin處理後的細胞外形…………………………………………………29 Mevastatin誘使pcDNA3.1 Balb/3T3細胞中之PKD增加…………………………………………………29 經過GGTI-286或FTI-277抑制 prenylation作用後，細胞內染測不到活化的integrin complex……30 討論………………………………………………………………………………………………………………32 S-ras ( Q61K) Balb/3T3轉型細胞的生理變化…………………………………………………………32 以mevastatin 阻斷mevalonate pathway後，細胞內Cav-1量之表現…………………………………32 FAK降解(degradation)之生理意義…………………………………………………………………………33 抑制 prenylation作用對細胞造成的影響………………………………………………………………33 未磷酸化的 PKD之生理意義………………………………………………………………………………34 Integrin Complex上的 Cav-1來自於何處………………………………………………………………36 結論………………………………………………………………………………………………………………36 參考文獻…………………………………………………………………………………………………………37 圖表說明…………………………………………………………………………………………………………54 | |
| dc.language.iso | zh-TW | |
| dc.title | Caveolin-1與Integrin Complex在S-ras (Q61K ) Balb/3T3轉型細胞中的互動 | zh_TW |
| dc.title | The Interaction between Caveolin-1 and Integrin Complex in S-ras (Q61K) Balb/3T3 cells | en |
| dc.date.schoolyear | 90-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 83 | |
| dc.rights.note | 未授權 | |
| dc.contributor.author-dept | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 動物學研究所 | zh_TW |
| 顯示於系所單位： | 動物學研究所 | |
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