跳到主要內容

臺灣博碩士論文加值系統

(3.229.137.68) 您好!臺灣時間:2021/07/25 18:11
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

我願授權國圖
: 
twitterline
研究生:王心慧
研究生(外文):AriunaaSampilvanjil
論文名稱:基質金屬蛋白酵素在血管窄化誘發腹主動脈瘤之角色
論文名稱(外文):The role of matrix metalloproteinases in coarctation-induced abdominal aortic aneurysm
指導教授:江美治江美治引用關係
指導教授(外文):Meei-Jyh Jiang
學位類別:碩士
校院名稱:國立成功大學
系所名稱:細胞生物及解剖學研究所
學門:醫藥衛生學門
學類:醫學學類
論文種類:學術論文
論文出版年:2012
畢業學年度:100
語文別:英文
論文頁數:92
外文關鍵詞:Matrix MetalloproteinasesAbdominal Aortic AneurysmTIMPs
相關次數:
  • 被引用被引用:0
  • 點閱點閱:89
  • 評分評分:
  • 下載下載:0
  • 收藏至我的研究室書目清單書目收藏:1
Abdominal aortic aneurysm (AAA) is a common dilating disorder of the aorta and a major cause of death upon rupture. The key processes leading to AAA formation includes degradation of extracellular matrix (ECM), inflammation and smooth muscle cell (SMC) death. Our laboratory developed a coarctation-induced AAA model in Taiwanese Lanyu mini pigs characterized by high induction rate and elastic fiber degradation. Coarctation was performed in the infrarenal abdominal aorta (AA) for 4 weeks (4w), 8 weeks (8w), or 12 weeks (12w). AAA was detected in the AA segment distal to the coarctation at 12w post-coarctation. This study examined the role of matrix metalloproteinase-2 (MMP-2) and MMP-9 in the coarctation-induced AAA. The expression and activity of MMP-2 and MMP-9 were examined in three AA segments, i.e. suprarenal AA, proximal AA and distal AA. Suprarenal AA is located proximal to the renal arteries and is less likely to be affected by coarctation. Proximal AA is located proximal to the coarctation, which has laminar flow but is exposed to lower shear stress after coarctation. Messenger RNA levels, protein expression and activity levels of MMP-2 and MMP-9 were detected at 4w, 8w, and 12w post-coarctation with reverse transcription-polymerase chain reaction (RT-PCR), immunoblotting, and gelatinase zymography, respectively. In the distal AA segment, MMP-2 and MMP-9 mRNA levels were higher at 8w post-coarctation. Protein expression and activity levels of MMP-9 were higher at 4w post-coarctation while those of MMP-2 didn’t vary. In the proximal AA segment, MMP-2 mRNA expression was up-regulated throughout the experimental period but no change in protein expression and activity was detected after coarctation. MMP-9 activity was markedly higher at 8w post-coarctation. In the suprarenal AA segment, no difference in MMP-2 mRNA, protein or activity levels was detected between experimental and sham control groups whereas MMP-9 expression and activity were barely detectable. Comparison among the three AA segments revealed that both MMP-9 protein expression and activity in the distal AA were higher at 4w post-coarctation. Because MMP activities in vivo are regulated by tissue inhibitors of MMPs (TIMPs), the activities of TIMPs were examined by reverse zymography. The activities of TIMP-1, -2, -3, and -4 in all three AA segments did not change compared with the sham control. Interestingly, the proximal AA segment showed higher TIMP activity compared with other AA segments. TIMPs inhibit MMPs by forming 1:1 enzyme-inhibitor complex. Therefore, we assessed MMP/TIMP ratios to determine effective activity levels of MMP-2 and -9. In the distal AA segment, MMP-2/TIMP-2 and MMP-9/TIMP-3/4 ratios were elevated at 4w post-coarctation compared with sham control. Furthermore, MMPs/TIMPs ratios in the distal AA segment were higher than those of the other AA segments. Interestingly, in sham group, the distal AA also exhibited higher MMP-2/TIMP-2 and MMP-2/TIMP-3/4 ratios compared with other two AA segments. Plasmin activity is essential for MMPs activation and plasmin activator uPA plays important role in AAA formation, thus, we examined mRNA expression of uPA and tPA. In the distal AA segment, uPA mRNA levels increased at 4w post-coarctation and were higher than those of other AA segments. In contrast, tPA mRNA expression did not differ among AA segments and treatment groups. These results suggest that MMP-2 and -9 in combinations with TIMPs play important roles in the coarctation-induced AAA formation.
ACKNOWLEDGEMENTS -I
ABSTRACT -II
TABLE OF CONTENTS -IV
LIST OF FIGURES-VII
CHAPTER ONE INTRODUCTION -1
1.1 Abdominal aortic aneurysm -1
1.2 Structural properties of the normal aorta and their role in AAA -2
1.3 Pathogenesis and risk factors of the AAA -4
1.4 Histopathologic features of the AAA -5
1.5 The role of extracellular matrix degradation in AAA -6
1.5.1 Matrix metalloproteinase-2: Structure, activation and regulation -7
1.5.2 Matrix metalloproteinase-9: Structure, activation and regulation -9
1.5.3 Tissue inhibitors of metalloproteinases (TIMPs)-11
1.6 Medial smooth muscle cell loss in AAA -12
1.7 Animal models in AAA -12
CHAPTER TWO RESEARCH OBJECTIVE -14
CHAPTER THREE MATERIALS AND METHODS -15
3.1 Materials: -15
3.1.1 Experimental animals -15
3.1.2 Chemicals -16
3.1.3 Solution preparation -20
3.2 Methods:-28
3.2.1 RNA extraction and reverse transcription polymerase chain reaction (RT-PCR)-28
3.2.2 Extraction of gelatinases from aortic tissue -32
3.2.3 Western blotting -32
3.2.4 Gelatin zymography -36
3.2.5 Casein zymography -38
3.2.6 Reverse zymography -39
3.2.7 TUNEL staining -41
3.2.8 Statistic analysis -42
CHAPTER FOUR RESULTS -43
4.1 Coarctation-induced AAA formation -43
4.2 Changes in elastic lamellae during AAA formation -43
4.3 MMP-2 and MMP-9 expression and activity in the suprarenal AA segment -44
4.4 MMP-2 and MMP-9 expression and activity in the proximal AA segment -44
4.5 MMP-2 and MMP-9 expression and activity in the distal AA segment -45
4.6 MMP-2 and MMP-9 expression and activity comparison among different AA segments -45
4.7 Coarctation didn't change TIMPs activity in AA segments -46
4.8 MMP/TIMP ratios are increased in the distal AA segment -46
4.9 Coarctation increased uPA mRNA expression in the distal AA segment -47
4.10 Plasma levels of MMP-2 and -9 gelatinase activity after coarctation -48
4.11 The effect of coarctation on cell apoptosis in AA segments -48
CHAPTER FIVE DISCUSSION -49
REFERENCES -55
FIGURES -70
APPENDICES -92
Appendix 1: -92
1.Prisant LM and Mondy JS, Abdominal Aortic Aneurysm. The Journal of Clinical Hypertension, 2004. 6(2): p. 85-89.
2.Gillum RF, Epidemiology of aortic aneurysm in the United States. Journal of Clinical Epidemiology, 1995. 48 (11): p. 1289-1298.
3.Jayr C, et al., Preoperative and intraoperative factors associated with prolonged mechanical ventilation. A study in patients following major abdominal vascular surgery. Chest, 1993. 103(4): p. 1231-1236.
4.El-Hamamsy, et al., Cellular and molecular mechanisms of thoracic aortic aneurysms. Nat Rev Cardiol, 2009. 6(12): p. 771-786.
5.Glagov S, et al., New concepts of the relation of structure to function in the arterial wall. Proc Inst Med Chic, 1968. 27(5): p. 106.
6.Silver F, et al., Relationship between hierarchical structure and mechanical properties of the arteries. Functional abnormalities of the aorta, ed. H. Boudoulas, P. Toutouzas, and C. Wooley. 1996, Armonk (NY): Futura Publishing Company.
7.Narayanan AS, et al., Elastin Synthesis in Arterial Smooth Muscle Cell Culture. The Journal of Cell Biology pages 1976 68(9): p. 411-419
8.Davidson JM, et al., Control of elastin synthesis: molecular and cellular aspects. Regulation of matrix accumulation, ed. R. Mecham. 1986, New York: Academic Press. 177-216.
9.Parks W, et al., Elastin. Adv Molec Cell Biol, 1993. 6: p. 133-182.
10.Linsenmayer TF, Collagen. Cell biology of extracellular matrix ed. E. Hay. 1991, New York: Plenum Press.
11.Procop D, et al., Biosyntseis of collagen and its disorders (part I). N Engl J Med, 1979. 301: p. 13-24.
12.Prockop D, et al., The biosynthesis of collagen and its disorders (part II). N Engl J Med, 1979. 301: p. 77-85.
13.Tilson MJ, J. Elefraides and C. Brophy, Tensile strength and collagen in abdominal aortic aneurysm disease. The cause and management of aneurysms, ed. R. Greenhsalgh, J. Mannick, and J. Powell. 1990, London: Saunders. 97-104.
14.Dorbin PB, Baker WH., Elastolytic and collagenolytic studies of arteries: implications for the mechanical properties of aneurysms. Arch Surg, 1984. 119: p. 405-9.
15.Dorbin PB, et al., Failure of elastin or collagen as possible critical connective tissue alterations underlying aneurysmal dilatation. Cardiovasc Surg, 1994. 2: p. 484-8.
16.Powell JT., A textbook for vascular surgeons. Mechanisms of vascular disease, ed. R. Fitridge and M.M. Thompson. 2007, Cambridge: Cambridge university press. 226-234.
17.Shah PK., Inflammation, Metalloproteinases, and Increased Proteolysis : An Emerging Pathophysiological Paradigm in Aortic Aneurysm. Circulation Research, 1997. 96(7): p. 2115-2117.
18.Herron GS, et al., Connective tissue proteinases and inhibitors in abdominal aortic aneurysms. Involvement of the vasa vasorum in the pathogenesis of aortic aneurysms. Arteriosclerosis, Thrombosis, and Vascular Biology, 1991. 11(6): p. 1667-1677.
19.Holmes DR, et al., Medial neovascularization in abdominal aortic aneurysms: A histopathologic marker of aneurysmal degeneration with pathophysiologic implications. Journal of Vascular Surgery, 1995. 21(5): p. 761-772.
20.MacSweeney STR, PoweL JT, Pathogenesis of abdominal aortic aneurysm. British Journal of Surgery, 1994. 81(7): p. 935-941.
21.Abraham M, et al., The role of IL-18 and IL-12 in the modulation of matrix metalloproteinases and their tissue inhibitors in monocytic cells. . Int Immunol, 2002. 14: p. 1449-57.
22.Christopher P. Cheng, David Parker, and CA Taylor, Quantification of Wall Shear Stress in Large Blood Vessels Using Lagrangian Interpolation Functions with Cine Phase-Contrast Magnetic Resonance Imaging. Annals of Biomedical Engineering, 2002. 30: p. 1020–1032.
23.Vardulaki KA, et al., Quantifying the risks of hypertension, age, sex and smoking in patients with abdominal aortic aneurysm. British Journal of Surgery, 2000. 87(2): p. 195-200.
24.Brown LC, et al., Risk Factors for Aneurysm Rupture in Patients Kept Under Ultrasound Surveillance. Annals of Surgery, 1999. 230(3): p. 289.
25.Kuivaniemi H, et al., Familial abdominal aortic aneurysms: Collection of 233 multiplex families. Journal of Vascular Surgery, 2003. 37(2): p. 340-345.
26.Pleumeekers HJ, et al., Aneurysms of the Abdominal Aorta in Older Adults. American Journal of Epidemiology, 1995. 142(12): p. 1291-1299.
27.Castleden WM, et al., Abdominal aortic aneurysms in Western Australia: Descriptive epidemiology and patterns of rupture. British Journal of Surgery, 1985. 72(2): p. 109-112.
28.Reed W, et al., , Learning From the Last Ultrasound: A PopulationBased Study of Patients With Abdominal Aortic Aneurysm. Arch Intern Med, 1997. 157(18): p. 2064-2068.
29.McFarlane MJ, The Epidemiologic Necropsy for Abdominal Aortic Aneurysm. The Journal of the American Medical Association, 1991. 256(16): p. 2085-2088.
30.Lederle FA, et al., Prevalence and Associations of Abdominal Aortic Aneurysm Detected through Screening. Annals of Internal Medicine, 1997. 126(6): p. 441-449.
31.Shimizu K, Mitchell RN, and Libby P, Inflammation and cellular immune responses in abdominalaorticaneurysms. Arterioscler Thromb Vasc Biol, 2006. 26(5): p. 987-994.
32.Menashi S, et al., Collagen in abdominalaorticaneurysm: typing, content, and degradation. J Vasc Surg, 1987. 6(6): p. 578-582.
33.Lopez-Candales A, et al., Decreased vascular smooth muscle cell density in medial degeneration of human abdominalaorticaneurysms. Am J Pathol, 1997. 150(3): p. 993-1007.
34.Choke E, et al., Abdominalaorticaneurysm rupture is associated with increased medial neovascularization and overexpression of proangiogenic cytokines. Arterioscler Thromb Vasc Biol, 2006. 26(9): p. 2077-82.
35.Campa JS, Greenhalgh RM, Elastin degradation in abdominal aortic aneurysms. Atherosclerosis, 1987. 65(1–2): p. 13-21.
36.Vine NP, et al., Metalloproteinases in degenerative aortic disease. Clin Sci, 1991. 81: p. 233-9.
37.Thompson RW, et al., Role of matrix metalloproteinases in abdominal aortic aneurysms. Ann NY Acad Sci, 1996. 800: p. 157-74.
38.Knox JB, et al., Evidence for Altered Balance Between Matrix Metalloproteinases and Their Inhibitors in Human Aortic Diseases Circulation Research, 1997. 95: p. 205-212.
39.Newman KM, et al., Identification of matrix metalloproteinases 3 (stromelysin-1) and 9 (gelatinase B) in abdominal aortic aneurysm. Arterioscler Thromb Vasc Biol, 1994. 14: p. 1315-1320.
40.Curci JA, et al., Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms. J Clin Invest, 1998. 102: p. 1900-1910.
41.Mao D, et al., Expression of collagenase-3 (MMP-13) in human abdominal aortic aneurysms and vascular smooth muscle cells in culture. Biochem Biophys Res Commun, 1999. 261: p. 904-910.
42.Schneiderman J, et al., Expression of fibrinolytic genes in atherosclerotic abdominal aortic aneurysm wall. A possible mechanism for aneurysm expansion. J Clin Invest, 1995. 96: p. 639-645.
43.Reilly JM, Sicard GA, Abnormal expression of plasminogen activators in aortic aneurysmal and occlusive disease. J Vasc Surg, 1994. 19: p. 865-872.
44.Jean-Claude J, et al., Possible key for plasmin in the pathogenesis of abdominal aortic aneurysms. . Surgery, 1994. 116: p. 472-478.
45.Sukhova GK, et al., J Clin Invest, 1998. 102: p. 576-583.
46.Keeling WB, et al., An overview of matrix metalloproteinases in the pathogenesis and treatment of abdominal aortic aneurysms. Vascular and Endovascular Surgery, 2005. 39: p. 457-464.
47.McMillan WD, et al., Size matters: the relationship between MMP-9 expression and aortic diameter. Circulation Research, 1997. 96: p. 2228-2232.
48.McMillan WD, et al., Increased plasma levels of metalloproteinase-9 are associated with abdominal aortic aneurysms. J Vasc Surg, 1999. 29: p. 122-7.
49.Hovsepian DM, et al., Elevated plasma levels of matrix metalloproteinase-9 (MMP-9) in patients with abdominal aortic aneurysms: a circulating marker of degenerative aneurysm disease. J Vasc Intervent Radiol, 2000. 11: p. 1345-52.
50.Pyo R, et al., Targeted gene disruption of matrix metalloproteinase-9 (gelatinase B) suppresses development of experimental abdominal aortic aneurysms. J Clin Invest, 2000. 105: p. 1641-1649.
51.Carmeliet P, et al., Urokinase-generated plasmin activates matrix metalloproteinases during aneurysm formation. Nat Genet, 1997. 17(4): p. 439-444.
52.Banyai L, Tordai H., The gelatin-binding site of human 72 kDa type IV collagenase (gelatinase A). Biochem J. , 1994 298((Pt 2)): p. 403-7.
53.Overall CM, Wrana JL., Transcriptional and post-transcriptional regulation of 72-kDa gelatinase/type IV collagenase by transforming growth factor-beta 1 in human fibroblasts. Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression. J Biol Chem, 1991. 266(21): p. 14064-71.
54.Brown PD, et al., Independent expression and cellular processing of Mr 72,000 type IV collagenase and interstitial collagenase in human tumorigenic cell lines. Cancer Res, 1990. 50(19): p. 6184-91.
55.Collier IE, et al., H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J Biol Chem, 1988. 263(14): p. 6579-87.
56.Overall CM, et al., Concanavalin A produces a matrix-degradative phenotype in human fibroblasts. Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of the tissue inhibitor of matrix metalloproteinases. J Biol Chem, 1990. 265(34): p. 21141-51.
57.Matrisian LM., Matrix metalloproteinase gene expression. Ann N Y Acad Sci, 1994. 732: p. 42-50.
58.Tomita T, et al., Granulocyte-macrophage colonystimulating factor upregulates matrix metalloproteinase-2 (MMP-2) and membrane type-1 MMP (MT1-MMP) in human head and neck cancer cells. Cancer Lett, 2000. 156: p. 83-91.
59.Sugimoto C, et al., Granulocyte colony-stimulating factor (G-CSF)-mediated signaling regulates type IV collagenase activity in head and neck cancer cells. Int J Cancer, 2001. 93: p. 42-6.
60.Cipollone F, et al., Overexpression of functionally coupled cyclooxygenase-2 and prostaglandin E synthase in symptomatic atherosclerotic plaques as a basis of prostaglandin E(2)-dependent plaque instability. . Circulation Research, 2001. 104: p. 921-7.
61.Kleiner D E, et al., Stability analysis of latent and active 72-kDa type IV collagenase: the role of tissue inhibitor of metalloproteinase -2 (TIMP-2). Biochemistry, 1993. 32: p. 1583-1592.
62.Ginestra A, et al., Urokinase plasminogen activator and gelatinases are associated with membrane vesicles shed by human HT1080 fibrosarcoma cells. J Biol Chem, 1997. 272: p. 17216-17222.
63.Mazzieri R, et al., Control of type IV collagenase activity by components of the urokinase-plasmin system: A regulatory mechanism with cell-bound reactants. EMBO J., 1997. 16: p. 2319-2332.
64.Zucker S et al., Thrombin induces the activation of progelatinase A in vascular endothelial cells. Physiologic regulation of angiogenesis. J Biol Chem, 1995. 270: p. 23730-23738.
65.Rajagopalan S, et al., Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation.Contribution to alterations of vasomotor tone. J Clin Invest., 1996. 97: p. 1916-23.
66.Philip S and Bulbule A., Osteopontin stimulates tumor growth and activation of promatrix metalloproteinase-2 through nuclear factor-kappa Bmediated induction of membrane type 1 matrix metalloproteinase in murine melanoma cells. . J Biol Chem, 2001. 276: p. 44926-35.
67.Philip S, et al., Osteopontin induces nuclear factor kappa B-mediated promatrix metalloproteinase-2 activation through I kappa B alpha /IKK signaling pathways, and curcumin (diferulolylmethane) down-regulates these pathways. J Biol Chem, 2003. 278: p. 14487-97.
68.Bruemmer D, et al., Angiotensin II-accelerated atherosclerosis and aneurysm formation is attenuated in osteopontin-deficient mice. . J Clin Invest., 2003. 112: p. 1318-31.
69.Arenas IA, et al., Angiotensin II-induced MMP-2 release from endothelial cells is mediated by TNF-alpha. Am J Physiol Cell Physiol. , 2004. 286: p. 779-84.
70.Wilhelm SM, et al., SV40-transformed human fibroblasts secrete a 92-kDa type-IV collagenase which is identical to that secreted by normal human macrophages. J Biol Chem, 1989. 264: p. 17213-17221.
71.Van Wart HE, et al., Cysteine switch: A pronciple of regulation of metalloproteinase activity with potential applicability to entire matrix metalloproteinase family. Proc. Natl. Acad. Sci. USA, 1990. 87(14): p. 5578-5582.
72.Reilly JM, Brophy CM., Characterization of an elastase from aneurysmal aorta which degrades intact aortic elastin. Ann Vasc Surg., 1992. 6: p. 499-502.
73.Newman KM and Jean-Claude J., Cellular localization of matrix metalloproteinases in the abdominal aortic aneurysm wall. . J Vasc Surg, 1994. 20: p. 814-20.
74.Newman KM and Ogata Y., Malon AM, Identification of matrix metalloproteinases3 (stromelysin-1) and 9 (gelatinase B) in abdominal aortic aneurysm. Arterioscler Thromb 1994. 14: p. 1315-20.
75.McMillan WD, et al., In situ localization and quantification of mRNA for 92-kD type IV collagenase and its inhibitor in aneurysmal, occlusive, and normal aorta. Arterioscler Thromb Vasc Biol., 1995. 15: p. 1139-44.
76.Welgus HG, Campbell EJ, and Cury JD., Neutral metalloproteinases produced by human mononuclear phagocytes: enzyme profile, regulation, and expression during cellular development. J Clin Invest, 1990. 86: p. 1496-502.
77.Thompson RW, Holmes DR, and Mertens RA, Production and localization of 92-kilodalton gelatinase in abdominal aortic aneurysms: an elastolytic metalloproteinase expressed by aneurysm-infiltrating macrophages. J Clin Invest, 1995. 96: p. 318-26.
78.Gum R, et al., Stimulation of 92-kDa gelatinase B promoter activity by ras is mitogen-activated protein kinase kinase 1-independent and requires multiple transcription factor binding sites including closely spaced PEA3/ets and AP-1 sequences. J Biol Chem, 1996. 271(18): p. 10672-80.
79.Huhtala P, et al., Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells. J Biol Chem. , 1991. 266(25): p. 16485-90.
80.Mercurio F et al., Multiple signals converging on NF-kappaB. Curr Opin Cell Biol., 1999. 11(2): p. 226-32.
81.St-Pierre Y, Couillard J and C. Van Themsche, Regulation of MMP-9 gene expression for the development of novel molecular targets against cancer and inflammatory diseases. Expert Opinion on Therapeutic Targets, 2004. 8(5): p. 473-489.
82.Fähling M, et al., Role of nucleolin in posttranscriptional control of MMP-9 expression. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2005. 1731(1): p. 32-40.
83.Overall CM and Wrana JL., Transcriptional and post-transcriptional regulation of 72-kDa gelatinase/type IV collagenase by transforming growth factor-beta 1 in human fibroblasts. Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression. J Biol Chem., 1991. 266: p. 14064–14071.
84.Hsu JC, Bravo R, and T. R., Interactions among LRF-1, JunB, c-Jun, and c-Fos define a regulatory program in the G1 phase of liver regeneration. Mol Cell Biol., 1992. 12: p. 4654-4665.
85.Ogata Y, Enghild JJ., Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J Biol Chem, 1992. 267(6): p. 3581-4.
86.Okada Y, et al., 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, 1992. 267(30): p. 21712-9.
87.Ramos-DeSimone N, et al., Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion. J Biol Chem., 1999 274(19): p. 13066-76.
88.Fang KC, et al., Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase. J Clin Invest, 1996. 97(7): p. 1589-96.
89.Fridman R, et al., Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2). Cancer Res., 1995 55(12): p. 2548-55.
90.Sang QX and Birkedal-Hansen H., Proteolytic and non-proteolytic activation of human neutrophil progelatinase B. Biochim Biophys Acta, 1995. 1251(2): p. 99-108.
91.Okamoto T, et al., Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J Biol Chem, 2001. 276(31): p. 29596-602.
92.Bannikov GA et al., Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide. J Biol Chem, 2002. 277(18): p. 16022-7.
93.Gomez DE, et al., Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol., 1997. 74(2): p. 111-22.
94.Brew K and Dinakarpandian D., Tissue inhibitors of metalloproteinases: evolution, structure and function. . Biochim Biophys Acta., 2000. 1477: p. 267–283.
95.Murphy G, et al., The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry., 1991. 30: p. 8097–8102.
96.Hanemaaijer R, et al., Regulation of matrix metalloproteinase expression in human vein and microvascular endothelial cells: effects of tumor necrosis factor α, interleukin 1 and phorbol ester. Biochem J., 1993. 296: p. 803-809.
97.Galis ZS, et al., Cytokine-stimulated human vascular smooth muscle cells synthesize a complement of enzymes required for extracellular matrix digestion. Circulation Research, 1994. 75: p. 181-189.
98.GalisZS, et al., Matrix Metalloproteinases in Vascular Remodeling and Atherogenesis. Circulation Research, 2002. 90(3): p. 251-262.
99.Steteler-Stevenson and WG, Krutzsch HC., Tissue inhibitor of metalloproteinase-2 (TIMP-2). . J Biol Chem, 1989. 264: p. 17374–17378.
100.Kinoshita T, et al., TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads. J Biol Chem 1998. 273: p. 16098–16103.
101.Kurschat P, et al., Tissue inhibitor of matrix metalloproteinase-2 regulated matrix metalloproteinase-2 activation. . J Biol Chem, 1999. 274: p. 21056–21062.
102.Hutton M, et al., Kinetic analysis of the mechanism of interaction of full-length TIMP-2 and gelatinase A: evidence for the existence of a low-affinity intermediate. . Biochemistry., 1998. 37: p. 10094-8.
103.Tamarina NA, et al., Expression of matrix metalloproteinases and their inhibitors in aneurysms and normal aorta. Surgery, 1997. 122: p. 264-72.
104.Kengo Nishimura, Shigetsugu Ohgi, and E. Nanba., Expression of MMP-2, MMP-9 and TIMP-1 in the Wall of Abdominal Aortic Aneurysms. Yonago Acta medica 2001. 44: p. 25–35.
105.McMIllan WD, et al., Incraesed plasma levels of metalloproteinase-9 are associated with abdominal aortic aneurysms. J Vasc Surg, 1999. 29: p. 122-7.
106.Nakamura M, et al., Circulating biochemical marker levels of collagen metabolism are abnormal in patients with abdominal aortic aneurysm. Angiology, 2000. 51: p. 385-92.
107.Lopez-Candales A, et al., Decreased vascular smooth muscle cell density in medial degeneration of human abdominal aortic aneurysms. Am. J. Pathol. , 1997. 150: p. 993-1007.
108.Lopez-Candales A, et al., Decreased vascular smooth muscle cell density in medial degeneration of human abdominal aortic aneurysms. . Am J Pathol., 1997. 150: p. 993-1007.
109.Henderson EL, et al., Death of smooth muscle cells and expression of mediators of apoptosis by T lymphocytes in human abdominal aortic aneurysms. Circulation. , 1999. 99: p. 96-104.
110.Walton LJ, et al., Inhibition of prostaglandin E2 synthesis in abdominal aortic aneurysms: implications for smooth muscle cell viability, inflammatory processes, and the expansion of abdominal aortic aneurysms. Circulation Research, 1999. 100: p. 48-54.
111.Eliason JL, et al., Neutrophil depletion inhibits experimental abdominal aortic aneurysm formation. . Circulation., 2005. 112: p. 232-240.
112.Sun J, et al., Mast cells modulate the pathogenesis of elastase-induced abdominal aortic aneurysms in mice. J Clin Invest., 2007. 117: p. 3359–3368.
113.Kaschina E et al., Telmisartan prevents aneurysm progression in the rat by inhibiting proteolysis, apoptosis and inflammation. J Hypertens., 2008. 26: p. 2361–2373.
114.Wang YX, et al., A Rho-kinase inhibitor, attenuates angiotensin II-induced abdominal aortic aneurysm in apolipoprotein E-deficient mice by inhibiting apoptosis and proteolysis. Circulation Research, 2005. 111: p. 2219-2226.
115.Allaire E, et al., Vascular smooth muscle cell endovascular therapy stabilizes already developed aneurysms in a model of aortic injury elicited by inflammation and proteolysis. Ann Surg., 2004. 239(3): p. 417-27.
116.Dai Yamanouchi, et al., Effects of Caspase Inhibitor on Angiotensin II-Induced Abdominal Aortic Aneurysm in Apolipoprotein E-deficient mice. Arteriosclerosis, Thrombosis, and Vascular Biology., 2010. 30: p. 702-707.
117.Zaragoza C, et al., Animal Models of Cardiovascular Diseases. Journal of Biomedicine and Biotechnology, 2011. 2011:497841. Epub 2011 Feb 16.
118.Saraff K, et al., Aortic dissection precedes formation of aneurysms and atherosclerosis in angiotensin II-infused, apolipoprotein E-deficient mice. Arterioscler Thromb Vasc Biol., 2003. 23: p. 1621-6.
119.Molácek J, et al., Optimization of the model of abdominal aortic aneurysm--experiment in an animal model. J Vasc Res., 2009. 46(1): p. 1-5.
120.Valerie Davis, et al., Matrix Metalloproteinase-2 Production and Its Binding to the Matrix Are Increased in Abdominal Aortic Aneurysms. Arterioscler Thromb Vasc Biol 1998. 18: p. 1625-1633.
121.Caroline Cheng, et al., Atherosclerotic Lesion Size and Vulnerability Are Determined by Patterns of Fluid Shear Stress. Circulation, 2006. 113: p. 2744-2753.
122.Femke A. M. V. I. Hellenthal, et al., Biomarkers of AAA progression. Part 1: extracellular matrix degeneration. Nature Reviews Cardiology, 2009. 6: p. 464-474.
123.Sakalihasan N, et al., Activated forms of MMP2 and MMP9 in abdominal aortic aneurysms. Journal of Vascular Surgery, 1996. 24(1): p. 127-133.
124.Freestone T, et al., Inflammation and matrix metalloproteinases in the enlarging abdominal aortic aneurysm. Arterioscler Thromb Vasc Biol., 1995. 15(8): p. 1145-51.
125.Petersen E, et al., Activity of matrix metalloproteinase-2 and -9 in abdominal aortic aneurysms. Relation to size and rupture. Eur J Vasc Endovasc Surg., 2000. 20(5): p. 457-61.
126.Crowther M, et al., Localization of matrix metalloproteinase 2 within the aneurysmal and normal aortic wall. British Journal of Surgery, 2000. 87(10): p. 1391-1400.
127.Liapis CD, et al., The pivotal role of matrix metalloproteinases in the development of human abdominal aortic aneurysms. Vasc Med. , 2003. 8(4): p. 267-71.
128.Crowther M, et al., Increased matrix metalloproteinase 2 expression in vascular smooth muscle cells cultured from abdominal aortic aneurysms. J Vasc Surg. , 2000. 32(3): p. 575-83.
129.Rafael Fridman, et al., Cell surface association of matrix metalloproteinase-9 (gelatinase B). Cancer and Metastasis Reviews, 2003. 22: p. 153-166.

連結至畢業學校之論文網頁點我開啟連結
註: 此連結為研究生畢業學校所提供,不一定有電子全文可供下載,若連結有誤,請點選上方之〝勘誤回報〞功能,我們會盡快修正,謝謝!
QRCODE
 
 
 
 
 
                                                                                                                                                                                                                                                                                                                                                                                                               
第一頁 上一頁 下一頁 最後一頁 top