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  1. NTU Theses and Dissertations Repository
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請用此 Handle URI 來引用此文件: http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75015
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dc.contributor.authorJun-An Chenen
dc.contributor.author陳俊安zh_TW
dc.date.accessioned2021-07-01T08:11:22Z-
dc.date.available2021-07-01T08:11:22Z-
dc.date.issued1999
dc.identifier.citation粘光明(1995)國立台灣大學生化科學研究所 碩士論文
黃憲祿(1999)國立台灣大學生化科學研究所 博士論文
• Agarwal C, Hembree JR, Rorke EA, Eckert RL(1994).Transforming growth factor beta 1 regulation of metalloproteinase production in cultured human cervical epithelial cells. Cancer Res .54,943-9.
• Anuradha P, Thampan RV. (1993). Hormonal regulation of rat uterine collagenase. Arch Biochem Biophys 303,81-9.
• Backstrom JR, Lim GP, Cullen MJ, Tokes ZA(1996)Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1-40).J Neurosci 1996.16,7910-9
• Benaud C, Dickson RB, Thompson EW.(1998).Roles of the matrix metalloproteinases in mammary gland development and cancer. Breast Cancer Res Treat 50,97-116.
• Braunhut SJ, Moses MA(1994). Retinoids modulate endothelial cell production of matrix-degrading proteases and tissue inhibitors of metalloproteinases (TIMP).J Biol Chem 269,13472-9.
• Chu ST, Lin HJ, Huang HL, Chen YH.(1998).The hydrophobic pocket of 24p3 protein from mouse uterine luminal fluid: fatty acid and retinol binding activity and predicted structural similarity to lipocalins. J Pept Res 52,390-7.
• Collier JE, Wilhelm SM, Eisen AZ, Marmer BL, Grant GA, Seltzer JL, Kronberger A, He CS, Bauer EA, Goldberg GI. (1988). H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J Biol Chem263,6579-87.
• Edwards DR, Murphy G, Reynolds JJ, Whitham SE, Docherty AJ, Angel P, Heath JK.(1987). Transforming growth factor beta modulates the expression of collagenase and metalloproteinase inhibitor. EMBO J 6,1899-904.
• Fini ME, Parks WC, Rinehart WB, Girard MT, Matsubara M, Cook JR, West-Mays JA, Sadow PM, Burgeson RE, Jeffrey JJ, Raizman MB, Krueger RR, Zieske JD.(1996).Role of matrix metalloproteinases in failure to re-epithelialize after corneal injury. Am J Pathol .149,1287-302.
• Fridman R, Fuerst TR, Bird RE, Hoyhtya M, Oelkuct M, Kraus S, Komarek D, Liotta LA, Berman ML, Stetler-Stevenson WG.(1992). Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions. J Biol Chem 267 ,15398-405.
• Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP. (1997).Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol,111-22.
• Greene J, Wang M, Liu YE, Raymond LA, Rosen C, Shi YE.(1996).Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4.J Biol Chem 271,30375-80.
• Gross, J. and Larpiere, C. M. (1962).Collagenolytic activity in amphibian tissue: a tissue remodeling. Proc. Natl. Acad. Sci. USA 54, 1194-1204.
• Hibbs MS, Hasty KA, Seyer JM, Kang AH, Mainardi CL.(1985).Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J Biol Chem 260,2493-500
• Howard EW, Banda MJ.(1991).Binding of tissue inhibitor of metalloproteinases 2 to two distinct sites on human 72-kDa gelatinase. Identification of a stabilization site. J Biol Chem 266,17972-7.
• Huhtala P, Chow LT, Tryggvason K(1990).Structure of the human type IV collagenase gene. J Biol Chem 265,11077-82.
• Hulboy DL, Rudolph LA, Matrisian LM.(1997).Matrix metalloproteinases as mediators of reproductive function. Mol Hum Reprod 3,27-45.
• Imada K, Ito A, Sato T, Namiki M, Nagase H, Mori Y.(1997).Hormonal regulation of matrix metalloproteinase 9/gelatinase B gene expression in rabbit uterine cervical fibroblasts. Biol Reprod 56,575-80.
• Itoh Y, Nagase H.(1995).Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase. J Biol Chem 270,16518-21.
• Kleiner DE Jr, Unsworth EJ, Krutzsch HC, Stetler-Stevenson WG. (1992).Higher-order complex formation between the 72-kilodalton type IV collagenase and tissue inhibitor of metalloproteinases-2.Biochemistry 31,1665-72.
• Kleiner DE Jr, Tuuttila A, Tryggvason K, Stetler-Stevenson WG(1993).Stability analysis of latent and active 72-kDa type IV collagenase: the role of tissue inhibitor of metalloproteinases-2 (TIMP-2) .Biochemistry 32,1583-92.
• Kolkenbrock H, Hecker-Kia A, Orgel D, Kinawi A, Ulbrich N.(1996). Progelatinase B forms from human neutrophils. complex formation of monomer/lipocalin with TIMP-1.Biol Chem 377,529-33.
• Liotta LA, Tryggvason K, Garbisa S, Hart I, Foltz CM, Shafie S. (1980). Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 284,67-8.
• Mainardi CL, Hibbs MS, Hasty KA, Seyer JM.(1984).Purification of a type V collagen degrading metalloproteinase from rabbit alveolar macrophages. Coll Relat Res 6,479-92.
• Marbaix E, Donnez J, Courtoy PJ, Eeckhout Y.(1992).Progesterone regulates the activity of collagenase and related gelatinases A and B in human endometrial explants. Proc Natl Acad Sci USA 89,11789-93.
• Massova I, KotraL. P, Fridman R, MobasheryS. (1998). Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 12,1075-95.
• Masure S, Nys G, Fiten P, Van Damme J, Opdenakker G.(1993).Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation. Eur J Biochem 218,129-41
• Matrisian LM. (1994)Matrix metalloproteinase gene expression. Ann N Y Acad Sci 732,42-50.
• Matsubara M, Zieske JD, Fini ME. (1991).Mechanism of basement membrane dissolution preceding comeal ulceration. Invest Ophthalmol Vis Sci .32,3221-37.
• Mohan R, Rinehart WB, Bargagna-Mohan P, Fini ME.(1998). Gelatinase B/lacZ transgenic mice, a model for mapping gelatinase B expression during developmental and injury-related tissue remodeling. J Biol Chem 273,25903-14.
• Moll UM, Youngleib GL, Rosinski KB, Quigley JP.(1990).Tumor promoter-stimulated Mr 92,000 gelatinase secreted by normal and malignant human cells: isolation and characterization of the enzyme from HT1O8O tumor cells. Cancer Res 50,6162-70.
• Murphy G, Crabbe T.(1995).Gelatinases A and B. Methods Enzymol 248,470-84
• Nagase H. (1997). Activation mechanisms of matrix metalloproteinases. Biol Chem 378,151-60.
• Ogata Y, Itoh Y, Nagase H.(1995).Steps involved in activation of the promatrix metalloproteinase 9 (progelatinase B)-tissue inhibitor of metalloproteinases-1 complex by 4-aminophenylmercuric acetate and proteinases. J Biol Chem 270,18506-11.
• Opdenakker G, Masure S, Proost P, Billiau A, van Damme J.(1991).Natural human monocyte gelatinase and its inhibitor. FEBS Lett 284,73-8.
• Overall CM, Limeback H.(1988).Identification and characterization of enamel proteinases isolated from developing enamel. Amelogeninolytic serine proteinases are associated with enamel maturation in pig. Biochem J 256,965-72.
• Overall CM, Wrana JL, Sodek J.(1991).Induction of formative and resorptive cellular phenotypes in human gingival fibroblasts by TGF-beta 1 and concanavalin A: regulation of matrix metalloproteinases and TIMP.J Periodontal Res .26(3 Pt2):279-82.
• Reponen P, Sahlberg C, Huhtala P, Hurskainen T, Thesleff I, Tryggvason K. (1992).Molecular cloning of murine 72-kDa type IV collagenase and its expression during mouse development. J Biol Chem 267,7856-62.
• Roberts Rugh.(1994) The mouse its reproduction and development, Oxford.
• Rodgers WH, Matrisian LM, Giudice LC, Dsupin B, Cannon P, Svitek C, Gorstein F, Osteen KG.(1994).Patterns of matrix metalloproteinase expression in cycling endometrium imply differential functions and regulation by steroid hormones. J Clin Invest 94,946-53.
• Rudolph-Owen LA, Hulboy DL, Wilson CL, Mudgett J, Matrisian LM.(1997). Coordinate expression of matrix metalloproteinase family members in the uterus of normal, matrilysin-deficient, and stromelysin-1-deficient mice. Endocrinology 138,4902-11.
• Sato H, Seiki M.(1996).Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis. J Biochem (Tokyo) 119,209-15.
• Takino T, Sato H, Shinagawa A, Seiki M(1995).Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. J Biol Chem 270,23013-20.
• Tanaka H, Hojo K, Yoshida H, Yoshioka T, Sugita K.(1993).Molecular cloning and expression of the mouse 105-kDa gelatinase cDNA. Biochem Biophys Res Commun 190,732-40.
• Triebel S, Blaser J, Reinke H, Tschesche H.(1992).A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase. FEBS Lett 314,386-8.
• Tyagi SC, Matsubara L, Weber KT.(1993).Direct extraction and estimation of collagenase(s) activity by zymography in microquantities of rat myocardium and uterus. Clin Biochem 26,191-8.
• Vassalli JD, Sappino AP, Belin D.(1991)The plasminogen activator/plasmin system. J Clin Invest 88,1067-72.
• Van Wart HE, 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 87.5578-82.
• Walmer DK, Wrona MA, Hughes CL, Nelson KG.(1992). Lactoferrin expression in the mouse reproductive tract during the natural estrous cycle: correlation with circulating estradiol and progesterone. Endocrinology 131,1458-66.
• Wick M, Burger C, Brusselbach S, Lucibello FC, Muller R.(1994).A novel member of human tissue inhibitor of metalloproteinases (TIMP) gene family is regulated during GI progression, mitogenic stimulation, differentiation, and senescence. J Biol Chem 269,18953-60.
• Wilhelm SM, Collier IE, Marmer BL, Eisen AZ, Grant GA, Goldberg GI. (1989).SV4O-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J Biol Chem 264,17213-21.
• Woessner JF Jr. (1991). Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB Journal. 5, 2145-54.
• Woessner JF Jr. (1994). The family of matrix metalloproteinases. Annals of the New York Academy of Sciences. 732:11-21.
dc.identifier.urihttp://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75015-
dc.description.abstract成熟雌鼠排卵、受精卵著床、分娩及子宮組織在動情週期的重組等生理變化過程中,都需要胞外間質成份的降解和重新合成。胞外間質帶金屬離子蛋白?(MMP)家族成員則是擔任調控胞外間質平衡的重要角色。胞外間質帶金屬離子蛋白?以潛伏蛋白(proenzyme)的形式分泌到細胞外進行活化,其活性會受到專一性的胞外金屬?抑制蛋白(TIMP)所調控。
本論文中,我們觀察MMP家族中的gelatinase B(MMP-9)基因和蛋白在雌鼠子宮動情週期各階段表現。從 Zymography 和RT-PCR的結果顯示,gelatinase B在動情前期和動情期有較強的表現,而動情間期的表現減少,動情後期則幾乎不表現。Gelatinase B的表現可能受到黃體素的抑制。我們推論gelatinase B在雌鼠子宮動情前期和動情期的表現可能會參與子宮組織降解和重組,而TIMP-1在動情週期的表現幾乎沒有變化。
zh_TW
dc.description.abstractIn the adult female, some of the most actively changing tissues are the reproductive organs. For example, ovulation, implantation, parturition, and uterus continually remodels throughout the estrous cycle. All of these processes require both breakdown and resynthesis of the extracellular matrix (ECM) components. Matrix metalloproteinase (MMP) are believed to be primary contributors to the process. Secreted as proenzymes, the MMPs undergo conversion to a catalytic active form that can be regulated by specific endogenous tissue inhibitors of metalloproteinases (TIMPs).
The results of Zymography and RT-PCR revealed that the expression level of gelatinase B appeared intensively at proestrus and estrus during mouse estrous cycle, declined sharply at metestrus, and nearly undetected in diestrus. The expression of gelatinase B may be inhibited by progesterone. We supposed that the expression of gelatinase B in proestrus and estrus might be involved in the tissue remodeling processes of uterus. The expression of TIMP-1 in uterus during mouse estrous cycle was constant.
en
dc.description.provenanceMade available in DSpace on 2021-07-01T08:11:22Z (GMT). No. of bitstreams: 0
Previous issue date: 1999
en
dc.description.tableofcontents目錄…………………i
圖表目錄…………iii
中文摘要……………I
ABSTRACT……………II
縮寫表………………III
第一章 緒論……………1
1.1 胞外間質帶金屬離子蛋白?家族的簡介…1
1.1.1 MMP蛋白的結構……………………2
1.2 明膠?的研究概況……………………3
1.2.1 明膠?的啟動子序列分析…………4
1.2.2 明膠?與胞外金屬?抑制蛋白……5
1.2.3 明膠?的活化……………………6
1.2.4 明膠?與荷爾蒙的調控………7
1.2.5 lipocalin與明膠?的關係……7
1.3 本論文的研究方向…………………8
第二章 實驗設計與方法………………15
2.1 實驗流程大綱……………………15
2.2 方法和材料……………………16
2.2.1 樣品的處理……………………16
2.2.2 雌鼠動情週期的判定……………………16
2.2.3 Total RNA的萃取……………………17
2.2.4 RNA品質的檢定……………………19
2.2.5 逆轉錄-聚合?連鎖反應(RTPCR)……21
2.2.6 聚合?連鎖反(PCR) …………………23
2.2.7 洋菜膠體泳……………………24
2.2.8 DNA片段萃取……………………25
2.2.9 DNA酒精沉澱……………………26
2.2.10 DNA接合反應……………………27
2.2.11 質體轉型……………………28
2.2.12 小量質體抽取…………………30
2.2.13 北方墨點法……………………31
2.2.14 組織蛋白萃取液……………35
2.2.15 蛋白質定量……………………36
2.2.16 SDS-聚丙烯醯胺膠體電泳………38
2.2.17 Serva Blue R染色法……………40
2.2.18 Zymography……………………41
2.2.19 西方墨點法……………………43
第三章 實驗結果……………………48
3.1 明膠?蛋白在雌鼠子宮動情週期的表現……48
3.1.1 Zymography……………48
3.1.2 西方墨點法……………………49
3.2 明膠?塞因在雌鼠子宮動情週期的表現……49
3.2.1 Gelatinase B cDNA的製備………49
3.2.2 北方墨點法……………………49
3.2.3 逆轉錄-聚合?連鎖反應……………50
3.3 明膠?和卵巢荷爾蒙調控的關係………50
第四章 討論…………………59
參考文獻……………………62
附錄一……………………66
附錄二……………………67
附錄三……………………69
附錄四……………………70
dc.language.isozh-TW
dc.title明膠?在雌鼠子宮中動情週期的表現zh_TW
dc.titleThe Expression of Gelatinase B in Mouse Uterus during Estrous Cycleen
dc.date.schoolyear87-2
dc.description.degree碩士
dc.relation.page70
dc.rights.note未授權
dc.contributor.author-dept生命科學院zh_TW
dc.contributor.author-dept生化科學研究所zh_TW
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