跳到主要內容

臺灣博碩士論文加值系統

(44.192.79.149) 您好!臺灣時間:2023/06/02 23:31
字體大小: 字級放大   字級縮小   預設字形  
回查詢結果 :::

詳目顯示

: 
twitterline
研究生:黃春華
研究生(外文):Huang, Chunhua
論文名稱:利用小片段干擾核醣核酸抑制人類間質金屬蛋白酶 1之表現
論文名稱(外文):Inhibition of Matrix Metalloproteinases 1 Expression by Small Interfering RNAs
指導教授:陳俊宏陳俊宏引用關係江善宗
指導教授(外文):Chen, GenhungJiang, Shanntzong
口試委員:殷儷容曹欽玉
口試委員(外文):Yin, LijungTsao, Chingyu
口試日期:2013-06-14
學位類別:碩士
校院名稱:靜宜大學
系所名稱:化粧品科學系
學門:民生學門
學類:美容學類
論文種類:學術論文
論文出版年:2013
畢業學年度:101
語文別:中文
論文頁數:119
中文關鍵詞:第一型人類間質金屬蛋白酶核醣核酸干擾人類纖維母細胞
外文關鍵詞:Matrix metalloproteinase 1 (MMP1)RNA interference (RNAi)Human Fibroblast
相關次數:
  • 被引用被引用:0
  • 點閱點閱:181
  • 評分評分:
  • 下載下載:5
  • 收藏至我的研究室書目清單書目收藏:0
第一型間質金屬蛋白酶 (Matrix metalloproteinase1, MMP1) 可分解細胞外間質而引起皮膚皺縮老化及癌症之轉移;而 RNAi 技術具有高效性、專一性地阻斷基因表達之功效,被認為是達到哺乳動物細胞基因緘默最有效的利器。本研究將人類纖維母細胞 (Detroit 551, BCRC 60118) 之total RNA萃取後,藉由 RT-PCR 及 PCR 技術已將第一型人類間質金屬蛋白酶的cDNA (MMP1 cDNA) 專一地成功複製。為了讓 RNA 干擾之效率或 MMP1 基因表現效率得以藉由螢光分析法加以偵測或定量,使用具有綠色螢光蛋白 (Green Fluorescent Protein, GFP) 編碼的報導系統做為表現載體,計畫將 MMP1 基因構築於 CMV (Human cytomegalovirus) 啟動子下游,接著將此構築好之 MMP1 - pAcGFP1-N3 表現載體轉染入人類黑色素瘤細胞 (MeWo, BCRC 60540) 中,然後再將化學合成的 siRNA 傳遞到細胞中,經過48小時培養後,於螢光分析儀中進行螢光數值的讀取。本研究至今已依據人類間質金屬蛋白酶第一型之 mRNA 序列及 RNA 干擾效率影響因子設計了 26 段高專一性的小片段雙股 RNA,每段的大小約 19 至 25 個核苷酸且 GC 含量約 30 至 50% 。其中 3 段小雙股 RNA 已由 Invitrogen 生技公司合成-357, 710 和 742 siRNAs。由報導系統的螢光數值結果顯示三段 siRNA 皆具有抑制螢光蛋白表現的能力,其中第710 siRNA的干擾效果更高達 90% 。接著將具有基因沉默效果的 siRNA 藉由轉染試劑的作用直接轉染入哺乳類細胞中,並藉由即時定量 PCR 與西方墨點法來分析是否具有抑制細胞中內生性 MMP1 基因的效果。此研究結果不只提供了 siRNA 研究技術之基礎數據,更提供了可抑制人類間質金屬蛋白酶第一型基因表現的 RNAi 資料。
Matrix metalloproteinase 1 (MMP1) degrading the extracellular matrix protein would cause skin wrinkle and play an important role on the malignant tumor metastasis. Small Interfering RNAs (RNAi), which could block gene expression specifically and efficiently, are considered to be the most powerful way of gene silencing in mammalian system. In this study, the total RNAs of human skin fibroblast (Detroit 551, BCRC 60118) have been extracted. After RT-PCR and PCR reactions, the recombinant human MMP1 cDNA (MMP1 cDNA) has been specifically amplified. For the purpose of detection and quantitation of the efficiency of RNA interference and MMP1 gene expression by fluorescence, one MMP1 GFP expression system has been successfully created by the following way: the MMP1 DNA was cloned into the pAcGFP1-N3 expression vector, which encodes a green fluorescent protein (GFP), under the control of CMV (Human cytomegalovirus) promoter, finally the MMP1-pAcGFP1-N3 expression vector was transfected into malignant melanoma (MeWo, BCRC 60540) and the GFP was detected after 48h. To now, 26 small double strand RNAs, each contains 21~23 nucleotides, has high specific to human MMP1 and with 30 - 50% of GC content, were designed according to the mRNA sequence of human MMP1 (NCBI, NM002421) and factors affecting RNA interfering efficiency from previous studies. Among them three siRNAs had synthesised by Invitrogen biotech - 357, 710 and 742 siRNAs. The results of fluorescence showed that all the three siRNAs have the capacities for inhibiting GFP expression, in which the inhibite effect of 710 siRNA is almost 90%, especially. Finally, we directly transfected the effective siRNAs into mammalian cells and analyzed whether the siRNAs have the ability to silence the expression of endogenous MMP1 by real-time quantitative PCR and Western blot. This study not only provides the basic data for the siRNA technology, but also obtains the small interfering RNA with inhibition of MMP1 expression.
中文摘要 I
英文摘要 II
目錄 IV
圖目錄 VI
第一章、前言 1
第二章、 文獻回顧 3
第一節、皮膚構造 3
第二節、皮膚老化 5
第三節、膠原蛋白 6
第四節、間質金屬蛋白酶 14
第五節、第一型間質金屬蛋白酶 26
第六節、核糖核酸干擾 33
第三章、實驗設計 41
第四章、實驗材料與方法 42
第一節、實驗材料 42
第二節、實驗方法 45
第三節、人類纖維母細胞之cDNA取得 48
第四節、帶有目標基因之質體的構築 51
第五節、利用報導系統進行siRNA之篩選:質體與siRNA共轉染 59
第六節、觀察細胞之螢光表現 60
第七節、將siRNA轉染到細胞中誘發內生性MMP1基因沉默 60
第八節、即時定量PCR 61
第九節、西方墨點法 62
第五章、結果與討論 64
第六章、結論與未來展望 71
參考文獻 72
中文部分:
徐善慧, 黃. 湯. (2003). 揭開膠原蛋白的神秘面紗. 科學發展, 362。
陳一村 (2008a). 核醣核酸干擾術及其應用. 生物醫學期刊, 1(3), 276-283。
鄭金松 核醣核酸干擾:從意外發現到功能基因體學的應用. 中央研究院週報, 1179。

英文部分:
Agrawal, N., Dasaradhi, P. V., Mohmmed, A., Malhotra, P., Bhatnagar, R. K.&Mukherjee, S. K. (2003). RNA interference: biology, mechanism, and applications. Microbiol Mol Biol Rev, 67(4), 657-685.
Aimes, R. T.&Quigley, J. P. (1995). Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J Biol Chem, 270(11), 5872-5876.
Ala-aho, R.&Kahari, V. M. (2005). Collagenases in cancer. Biochimie,87(3-4), 273-286.
Allan, J. A., Docherty, A. J., Barker, P. J., Huskisson, N. S., Reynolds, J. J.&Murphy, G. (1995). Binding of gelatinases A and B to type-I collagen and other matrix components. Biochem J, 309 ( Pt 1), 299-306.
Arendt, C. W., Tang, G.&Zilberstein, A. (2003). Vector systems for the delivery of small interfering RNAs: managing the RISC. Chembiochem, 4(11), 1129-1136.
Atkinson, S. J., Roghi, C.&Murphy, G. (2006). MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells. Biochem J, 398(1), 15-22.
Bernards, R. (2006). Exploring the uses of RNAi--gene knockdown and the Nobel Prize. N Engl J Med, 355(23), 2391-2393.
Birkedal-Hansen, H., Moore, W. G., Bodden, M. K., Windsor, L. J., Birkedal-Hansen, B., DeCarlo, A.&Engler, J. A. (1993). Matrix metalloproteinases: a review. Crit Rev Oral Biol Med, 4(2), 197-250.
Brew, K., Dinakarpandian, D.&Nagase, H. (2000). Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta, 1477(1-2), 267-283.
Buduneli, E., Mantyla, P., Emingil, G., Tervahartiala, T., Pussinen, P., Baris, N., Akilli, A., Atilla, G.&Sorsa, T. (2011). Acute myocardial infarction is reflected in salivary matrix metalloproteinase-8 activation level. J Periodontol, 82(5), 716-725.
Butler, G. S., Tam, E. M.&Overall, C. M. (2004). The canonical methionine 392 of matrix metalloproteinase 2 (gelatinase A) is not required for catalytic efficiency or structural integrity: probing the role of the methionine-turn in the metzincin metalloprotease superfamily. J Biol Chem, 279(15), 15615-15620.
Chung, J. H., Seo, J. Y., Choi, H. R., Lee, M. K., Youn, C. S., Rhie, G., Cho, K. H., Kim, K. H., Park, K. C.&Eun, H. C. (2001). Modulation of skin collagen metabolism in aged and photoaged human skin in vivo. J Invest Dermatol, 117(5), 1218-1224.
Dunsmore, S. E., Saarialho-Kere, U. K., Roby, J. D., Wilson, C. L., Matrisian, L. M., Welgus, H. G.&Parks, W. C. (1998). Matrilysin expression and function in airway epithelium. J Clin Invest, 102(7),
1321-1331.
E. Kohl, * J. Steinbauer, M. Landthaler, R.-M. Szeimies (2011). Skin Skin. Journal of the European Academy of Dermatology and Venereology, 25, 873–884.
Egeblad, M.&Werb, Z. (2002). New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer, 2(3), 161-174.
Elbashir, S. M., Harborth, J., Weber, K.&Tuschl, T. (2002). Analysis of gene function in somatic mammalian cells using small interfering RNAs. Methods, 26(2), 199-213.
Eleftherios, V. C. Y., Spyridoula, D., ZOE, S., Stavros, V., Emeka, N., Vassilis, R., Antonis, V., Sofia, S., Christos, T., Athanasios, Y., Christina, T., Friedrich, W.&Efstratios, P. (2007). Association of Matrix Metalloproteinase-1 (-1607 1G/2G) Polymorphism with Increased Risk for Oral Squamous Cell Carcinoma. Anticancer researcch, 27, 459-464.
Eulalio, A., Huntzinger, E.&Izaurralde, E. (2008). Getting to the root of miRNA-mediated gene silencing. Cell, 132(1), 9-14.
Fire, A., Xu, S., Montgomery, M. K., Kostas, S. A., Driver, S. E.&Mello, C. C. (1998). Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature, 391(6669), 806-811.
Folgueras, A. R., Pendas, A. M., Sanchez, L. M.&Lopez-Otin, C. (2004). Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies. Int J Dev Biol, 48(5-6), 411-424.
Gelse, K., Poschl, E.&Aigner, T. (2003). Collagens--structure, function, and biosynthesis. Adv Drug Deliv Rev, 55(12), 1531-1546.
Griffiths, M. M., Wang, J., Joe, B., Dracheva, S., Kawahito, Y., Shepard, J. S., Reese, V. R., McCall-Vining, S., Hashiramoto, A., Cannon, G. W., Remmers, E. F.&Wilder, R. L. (2000). Identification of four new quantitative trait loci regulating arthritis severity and one new quantitative trait locus regulating autoantibody production in rats with collagen-induced arthritis. Arthritis Rheum, 43(6), 1278-1289.
Guo, S.&Kemphues, K. J. (1995). par-1, a gene required for establishing polarity in C. elegans embryos, encodes a putative Ser/Thr kinase that is asymmetrically distributed. Cell, 81(4), 611-620.
Gvozdev, V. A. (2003). [Mobile genes and RNA interference]. Genetika,39(2), 151-156.
Hamilton, A. J.&Baulcombe, D. C. (1999). A species of small antisense RNA in posttranscriptional gene silencing in plants. Science, 286(5441), 950-952.
Hammond, S. M., Caudy, A. A.&Hannon, G. J. (2001). Post-transcriptional gene silencing by double-stranded RNA. Nat Rev Genet, 2(2), 110-119.
Hu, J., Van den Steen, P. E., Sang, Q. X.&Opdenakker, G. (2007). Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nat Rev Drug Discov, 6(6), 480-498.
Hurst, R. E. (1994). Structure, function, and pathology of proteoglycans and glycosaminoglycans in the urinary tract. World J Urol, 12(1), 3-10.
Iatridis, J. C., Wu, J., Yandow, J. A.&Langevin, H. M. (2003). Subcutaneous tissue mechanical behavior is linear and viscoelastic under uniaxial tension. Connect Tissue Res, 44(5), 208-217.
Imai, K., Yokohama, Y., Nakanishi, I., Ohuchi, E., Fujii, Y., Nakai, N.&Okada, Y. (1995). Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction
with other matrix metalloproteinases and enzymic properties. J Biol Chem, 270(12), 6691-6697.
Iorns, E., Lord, C. J., Turner, N.&Ashworth, A. (2007). Utilizing RNA interference to enhance cancer drug discovery. Nat Rev Drug Discov, 6(7), 556-568.
Itoh, F., Yamamoto, H., Hinoda, Y.&Imai, K. (1996). Enhanced secretion and activation of matrilysin during malignant conversion of human colorectal epithelium and its relationship with invasive potential of colon cancer cells. Cancer, 77(8 Suppl), 1717-1721.
Iyer, S., Visse, R., Nagase, H.&Acharya, K. R. (2006). Crystal structure of an active form of human MMP-1. J Mol Biol, 362(1), 78-88.
Jackson, A. L., Burchard, J., Schelter, J., Chau, B. N., Cleary, M., Lim, L.&Linsley, P. S. (2006). Widespread siRNA "off-target" transcript silencing mediated by seed region sequence complementarity. RNA, 12(7), 1179-1187.
Jacob, M. P. (2003). Extracellular matrix remodeling and matrix metalloproteinases in the vascular wall during aging and in pathological conditions. Biomed Pharmacother, 57(5-6), 195-202.
Jiang, X., Dutton, C. M., Qi, W. N., Block, J. A., Garamszegi, N.&Scully, S. P. (2005). siRNA mediated inhibition of MMP-1 reduces invasive potential of a human chondrosarcoma cell line. J Cell Physiol, 202(3), 723-730.
Joey E. Lai-Cheong, J. A. M. (2009). Structure and function of skin, hair and nails. Medicine, 37(5), 223-226. Johansson, N., Ala-aho, R., Uitto, V., Grenman, R., Fusenig, N. E., Lopez-Otin, C.&Kahari, V. M. (2000). Expression of collagenase-3 (MMP-13) and collagenase-1 (MMP-1) by transformed keratinocytes is dependent on the activity of p38 mitogen-activated protein kinase. J Cell Sci, 113 Pt 2, 227-235.
Khavkin, J.&Ellis, D. A. (2011). Aging skin: histology, physiology, and pathology. Facial Plast Surg Clin North Am, 19(2), 229-234.
Khvorova, A., Reynolds, A.&Jayasena, S. D. (2003). Functional siRNAs and miRNAs exhibit strand bias. Cell, 115(2), 209-216.
Kim, D. H.&Rossi, J. J. (2007). Strategies for silencing human disease using RNA interference. Nat Rev Genet, 8(3), 173-184.
Kren, L., Goncharuk, V. N., Krenova, Z., Stratil, D., Hermanova, M., Skrickova, J., Sheehan, C. E.&Ross, J. S. (2006). Expression of matrix metalloproteinases 3, 10 and 11 (stromelysins 1, 2 and 3) and matrix metalloproteinase 7 (matrilysin) by cancer cells in non-small cell lung neoplasms. Clinicopathologic studies. Cesk Patol, 42(1), 16-19.
Lee, Y., Ahn, C., Han, J., Choi, H., Kim, J., Yim, J., Lee, J., Provost, P., Radmark, O., Kim, S.&Kim, V. N. (2003). The nuclear RNase III Drosha initiates microRNA processing. Nature, 425(6956), 415-419.
Luciano, D. J., Mirsky, H., Vendetti, N. J.&Maas, S. (2004). RNA editing of a miRNA precursor. RNA, 10(8), 1174-1177.
Lund, E., Guttinger, S., Calado, A., Dahlberg, J. E.&Kutay, U. (2004). Nuclear export of microRNA precursors. Science, 303(5654), 95-98.
Luo, X. H.&Liao, E. Y. (2001). Progesterone differentially regulates the membrane-type matrix metalloproteinase-1 (MT1 -MMP) compartment of proMMP-2 activation in MG-63 cells. Horm Metab Res, 33(7), 383-388.
Makrantonaki, E.&Zouboulis, C. C. (2007). Molecular mechanisms of skin
aging: state of the art. Ann N Y Acad Sci, 1119, 40-50.
Martignetti, J. A., Aqeel, A. A., Sewairi, W. A., Boumah, C. E., Kambouris, M., Mayouf, S. A., Sheth, K. V., Eid, W. A., Dowling, O., Harris, J., Glucksman, M. J., Bahabri, S., Meyer, B. F.&Desnick, R. J. (2001). Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome. Nat Genet, 28(3), 261-265.
McGuire, J. K., Li, Q.&Parks, W. C. (2003). Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am J Pathol, 162(6), 1831-1843.
McIntush, E. W.&Smith, M. F. (1998). Matrix metalloproteinases and tissue inhibitors of metalloproteinases in ovarian function. Rev Reprod, 3(1), 23-30.
Nagase, H., Visse, R.&Murphy, G. (2006). Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res, 69(3), 562-573.
Nagase, H.&Woessner, J. F., Jr. (1999). Matrix metalloproteinases. J Biol Chem, 274(31), 21491-21494.
Napoli, C., Lemieux, C.&Jorgensen, R. (1990). Introduction of a Chimeric Chalcone Synthase Gene into Petunia Results in Reversible Co-Suppression of Homologous Genes in trans. Plant Cell, 2(4), 279-289.
Naylor, E. C., Watson, R. E.&Sherratt, M. J. (2011). Molecular aspects of skin ageing. Maturitas, 69(3), 249-256.
Ngo, V. N., Davis, R. E., Lamy, L., Yu, X., Zhao, H., Lenz, G., Lam, L. T., Dave, S., Yang, L., Powell, J.&Staudt, L. M. (2006). A loss-of-function RNA interference screen for molecular targets in cancer. Nature, 441(7089), 106-110.
Nishida, Y., Miyamori, H., Thompson, E. W., Takino, T., Endo, Y.&Sato, H. (2008). Activation of matrix metalloproteinase-2 (MMP-2) by membrane type 1 matrix metalloproteinase through an artificial receptor for proMMP-2 generates active MMP-2. Cancer Res, 68(21), 9096-9104.
Ohuchi, E., Imai, K., Fujii, Y., Sato, H., Seiki, M.&Okada, Y. (1997). Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem, 272(4), 2446-2451.
Okada, Y., Gonoji, Y., Naka, K., Tomita, K., Nakanishi, I., Iwata, K., Yamashita, K.&Hayakawa, T. (1992). Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties. J Biol Chem, 267(30), 21712-21719. Osborne, R., Mullins, L. A.&Jarrold, B. B. (2009). Understanding metabolic pathways for skin anti-aging. J Drugs Dermatol, 8(7 Suppl), s4-7.
Pardo, A.&Selman, M. (2005). MMP-1: the elder of the family. Int J Biochem Cell Biol, 37(2), 283-288.
Park, H. I., Ni, J., Gerkema, F. E., Liu, D., Belozerov, V. E.&Sang, Q. X. (2000). Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor. J Biol Chem, 275(27), 20540-20544. Park, H. I., Turk, B. E., Gerkema, F. E., Cantley, L. C.&Sang, Q. X. (2002). Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26. J Biol Chem, 277(38), 35168-35175.
Philips, N., Keller, T., Hendrix, C., Hamilton, S., Arena, R., Tuason, M.&Gonzalez, S. (2007). Regulation of the extracellular matrix remodeling by lutein in dermal fibroblasts, melanoma cells, and ultraviolet radiation exposed fibroblasts. Arch Dermatol Res, 299(8), 373-379.
Romano, N.&Macino, G. (1992). Quelling: transient inactivation of gene expression in Neurospora crassa by transformation with homologous sequences. Mol Microbiol, 6(22), 3343-3353.
Rutter, J. L., Benbow, U., Coon, C. I.&Brinckerhoff, C. E. (1997). Cell-type specific regulation of human interstitial collagenase-1 gene expression by interleukin-1 beta (IL-1 beta) in human fibroblasts and BC-8701 breast cancer cells. J Cell Biochem, 66(3), 322-336.
Saarialho-Kere, U. K., Crouch, E. C.&Parks, W. C. (1995). Matrix metalloproteinase matrilysin is constitutively expressed in adult human exocrine epithelium. J Invest Dermatol, 105(2), 190-196.
Seggerson, K., Tang, L.&Moss, E. G. (2002). Two genetic circuits repress the Caenorhabditis elegans heterochronic gene lin-28 after translation initiation. Dev Biol, 243(2), 215-225.
Shoulders, M. D.&Raines, R. T. (2009). Collagen structure and stability. Annu Rev Biochem, 78, 929-958. Sjerobabski-Masnec, I.&Situm, M. (2010). Skin aging. Acta Clin Croat, 49(4), 515-518.
Song, J. J., Smith, S. K., Hannon, G. J.&Joshua-Tor, L. (2004). Crystal structure of Argonaute and its implications for RISC slicer activity. Science, 305(5689), 1434-1437.
Suzuki, K., Lees, M., Newlands, G. F., Nagase, H.&Woolley, D. E. (1995). Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II. Biochem J, 305 ( Pt 1), 301-306.
Tam, E. M., Moore, T. R., Butler, G. S.&Overall, C. M. (2004). Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities. J Biol Chem, 279(41), 43336-43344.
Tang, G., Reinhart, B. J., Bartel, D. P.&Zamore, P. D. (2003). A biochemical framework for RNA silencing in plants. Genes Dev, 17(1), 49-63.
Van Wart, H. E.&Birkedal-Hansen, H. (1990). The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A, 87(14), 5578-5582.
Vihinen, P.&Kahari, V. M. (2002). Matrix metalloproteinases in cancer: prognostic markers and therapeutic targets. Int J Cancer, 99(2), 157-166.
Visse, R.&Nagase, H. (2003). Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res, 92(8), 827-839.
Wassenegger, M. (2005). The role of the RNAi machinery in heterochromatin formation. Cell, 122(1), 13-16.
Wood, F. (2012). Tissue engineering of skin. Clin Plast Surg, 39(1), 21-32.
Wyatt, C. A., Geoghegan, J. C. & Brinckerhoff, C. E. (2005). Short hairpin RNA-mediated inhibition of matrix metalloproteinase-1 in MDA-231 cells: effects on matrix destruction and tumor growth. Cancer Res, 65(23), 11101-11108.
Yoon, S. O., Park, S. J., Yun, C. H.&Chung, A. S. (2003). Roles of matrix metalloproteinases in tumor metastasis and angiogenesis. J Biochem Mol Biol, 36(1), 128-137.
Yuan, J., Dutton, C. M.&Scully, S. P. (2005). RNAi mediated MMP-1 silencing inhibits human chondrosarcoma invasion. J Orthop Res, 23(6), 1467-1474.
Yung, S. & Chan, T. M. (2007). Glycosaminoglycans and proteoglycans: overlooked entities? Perit Dial Int, 27 Suppl 2, S104-109.
Zamore, P. D., Tuschl, T., Sharp, P. A.&Bartel, D. P. (2000). RNAi: double-stranded RNA directs the ATP-dependent cleavage of mRNA at 21 to 23 nucleotide intervals. Cell, 101(1), 25-33.
Zeng, Y., Yi, R.&Cullen, B. R. (2003). MicroRNAs and small interfering RNAs can inhibit mRNA expression by similar mechanisms. Proc Natl Acad Sci U S A, 100(17), 9779-9784.
QRCODE
 
 
 
 
 
                                                                                                                                                                                                                                                                                                                                                                                                               
第一頁 上一頁 下一頁 最後一頁 top