메뉴 건너뛰기




Volumn 65, Issue 8, 2013, Pages 1192-1199

Fisetin inhibits matrix metalloproteinases and reduces tumor cell invasiveness and endothelial cell tube formation

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; FISETIN; GELATINASE A; GELATINASE B; INTERSTITIAL COLLAGENASE; MATRILYSIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; STROMELYSIN; TETRACYCLINE;

EID: 84888331607     PISSN: 01635581     EISSN: 15327914     Source Type: Journal    
DOI: 10.1080/01635581.2013.828090     Document Type: Article
Times cited : (27)

References (30)
  • 1
    • 0036728623 scopus 로고    scopus 로고
    • MMPs and TIMPs: An historical perspective
    • Woessner JF Jr: MMPs and TIMPs: an historical perspective. Mol Biotechnol 22, 33-49, 2002.
    • (2002) Mol Biotechnol , vol.22 , pp. 33-49
    • Woessner Jr., J.F.1
  • 2
    • 0033999308 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Biologic activity and clinical implications
    • Nelson AR, Fingleton B, Rothenberg ML, and Matrisian LM: Matrix metalloproteinases: biologic activity and clinical implications. J Clin Oncol 18, 1135-1149, 2000.
    • (2000) J Clin Oncol , vol.18 , pp. 1135-1149
    • Nelson, A.R.1    Fingleton, B.2    Rothenberg, M.L.3    Matrisian, L.M.4
  • 3
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens LM, Fingleton B, and Matrisian LM: Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295, 2387-2392, 2002.
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 4
    • 0029245540 scopus 로고
    • Doxycycline inhibits neutrophil (PMN)-type matrix metalloproteinases in human adult periodontitis gingiva
    • Golub LM, Sorsa T, Lee HM, Ciancio S, Sorbi D, et al.: Doxycycline inhibits neutrophil (PMN)-type matrix metalloproteinases in human adult periodontitis gingiva. J Clin Periodontol 22, 100-109, 1995.
    • (1995) J Clin Periodontol , vol.22 , pp. 100-109
    • Golub, L.M.1    Sorsa, T.2    Lee, H.M.3    Ciancio, S.4    Sorbi, D.5
  • 5
    • 0029688549 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibition in periodontal treatment
    • Ryan ME, Ramamurthy S, and Golub LM: Matrix metalloproteinases and their inhibition in periodontal treatment. Curr Opin Periodontol 3, 85-96, 1996.
    • (1996) Curr Opin Periodontol , vol.3 , pp. 85-96
    • Ryan, M.E.1    Ramamurthy, S.2    Golub, L.M.3
  • 6
    • 0037186958 scopus 로고    scopus 로고
    • Refolding of the catalytic and hinge domains of human MT1-MMP expressed in Escherichia coli and its characterization
    • Koo HM, Kim JH, Hwang IK, Lee SJ, Kim TH, et al.: Refolding of the catalytic and hinge domains of human MT1-MMP expressed in Escherichia coli and its characterization. Mol Cells 13, 118-124, 2002.
    • (2002) Mol Cells , vol.13 , pp. 118-124
    • Koo, H.M.1    Kim, J.H.2    Hwang, I.K.3    Lee, S.J.4    Kim, T.H.5
  • 7
    • 28144440373 scopus 로고    scopus 로고
    • Apolipoprotein C-II is a novel substrate for matrix metalloproteinases
    • Kim SY, Park SM, and Lee S-T: Apolipoprotein C-II is a novel substrate for matrix metalloproteinases. Biochem Biophys Res Commun 339, 47-54, 2006.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 47-54
    • Kim, S.Y.1    Park, S.M.2    Lee, S.-T.3
  • 8
    • 79959413927 scopus 로고    scopus 로고
    • Inhibition of invasion and capillary-like tube formation by retrohydroxamate-based MMP inhibitors
    • Choi S-S, Ji A-R, Yu S-W, Cho B-H, Park JD, et al.: Inhibition of invasion and capillary-like tube formation by retrohydroxamate-based MMP inhibitors. Bull Korean Chem Soc 32, 2032-2038, 2011.
    • (2011) Bull Korean Chem Soc , vol.32 , pp. 2032-2038
    • Choi, S.-S.1    Ji, A.-R.2    Yu, S.-W.3    Cho, B.-H.4    Park, J.D.5
  • 9
    • 0033484579 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-2 inhibits the 4-aminophenylmercuric acetate-induced activation and autodegradation of the free promatrix metalloproteinase-2
    • Jo Y, Yoon D-W, Kim MY, Lee YJ, Kim HJ, et al.: Tissue inhibitor of metalloproteinases-2 inhibits the 4-aminophenylmercuric acetate-induced activation and autodegradation of the free promatrix metalloproteinase-2. J Biolchem Mol Biol 32, 60-66, 1999.
    • (1999) J Biolchem Mol Biol , vol.32 , pp. 60-66
    • Jo, Y.1    Yoon, D.-W.2    Kim, M.Y.3    Lee, Y.J.4    Kim, H.J.5
  • 10
    • 33644548658 scopus 로고    scopus 로고
    • Characterization of plasma gelsolin as a substrate for matrix metalloproteinases
    • Park SM, Hwang IK, Kim SY, Lee SJ, Park KS, et al.: Characterization of plasma gelsolin as a substrate for matrix metalloproteinases. Proteomics 6, 1192-1199, 2006.
    • (2006) Proteomics , vol.6 , pp. 1192-1199
    • Park, S.M.1    Hwang, I.K.2    Kim, S.Y.3    Lee, S.J.4    Park, K.S.5
  • 11
    • 0021677785 scopus 로고
    • Tetracyclines inhibit tissue collagenase activity. A new mechanism in the treatment of periodontal disease
    • Golub LM, Ramamurthy N, McNamara TF, Gomes B, Wolff M, et al.: Tetracyclines inhibit tissue collagenase activity. A new mechanism in the treatment of periodontal disease. J Periodontal Res 19, 651-655, 1984.
    • (1984) J Periodontal Res , vol.19 , pp. 651-655
    • Golub, L.M.1    Ramamurthy, N.2    McNamara, T.F.3    Gomes, B.4    Wolff, M.5
  • 12
    • 0027414257 scopus 로고
    • Tetracycline and doxycycline inhibit pleural fluid metalloproteinases A possible mechanism for chemical pleurodesis
    • Hurewitz AN, Wu CL, Mancuso P, and Zucker S: Tetracycline and doxycycline inhibit pleural fluid metalloproteinases. A possible mechanism for chemical pleurodesis. Chest 103, 1113-1117, 1993.
    • (1993) Chest , vol.103 , pp. 1113-1117
    • Hurewitz, A.N.1    Wu, C.L.2    Mancuso, P.3    Zucker, S.4
  • 13
    • 0015822275 scopus 로고
    • Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria
    • Jaffe EA, Nachman RL, Becker CG, and Minick CR: Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J Clin Invest 52, 2745-2756, 1973.
    • (1973) J Clin Invest , vol.52 , pp. 2745-2756
    • Jaffe, E.A.1    Nachman, R.L.2    Becker, C.G.3    Minick, C.R.4
  • 14
    • 0024595042 scopus 로고
    • Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill
    • Hansen MB, Nielsen SE, and Berg K: Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill. J Immunol Methods 119, 203-210, 1989.
    • (1989) J Immunol Methods , vol.119 , pp. 203-210
    • Hansen, M.B.1    Nielsen, S.E.2    Berg, K.3
  • 15
    • 44149096894 scopus 로고    scopus 로고
    • Soluble PTK7 inhibits tube formation, migration, and invasion of endothelial cells and angiogenesis
    • Shin WS, Maeng YS, Jung JW, Min JK, Kwon YG, et al.: Soluble PTK7 inhibits tube formation, migration, and invasion of endothelial cells and angiogenesis. Biochem Biophys Res Commun 371, 793-798, 2008.
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 793-798
    • Shin, W.S.1    Maeng, Y.S.2    Jung, J.W.3    Min, J.K.4    Kwon, Y.G.5
  • 16
    • 48949086474 scopus 로고    scopus 로고
    • Cleavage and functional loss of human apolipoprotein e by digestion of matrix metalloproteinase-14
    • Park JH, Park SM, Park SH, Cho KH, and Lee S-T: Cleavage and functional loss of human apolipoprotein E by digestion of matrix metalloproteinase-14. Proteomics 8, 2926-2935, 2008.
    • (2008) Proteomics , vol.8 , pp. 2926-2935
    • Park, J.H.1    Park, S.M.2    Park, S.H.3    Cho, K.H.4    Lee, S.-T.5
  • 17
    • 0031800674 scopus 로고    scopus 로고
    • Elevated cyclic AMP suppresses ConA-induced MT1-MMP expression in MDA-MB-231 human breast cancer cells
    • Yu M, Sato H, Seiki M, Spiegel S, and Thompson EW: Elevated cyclic AMP suppresses ConA-induced MT1-MMP expression in MDA-MB-231 human breast cancer cells. Clin Exp Metastasis 16, 185-191, 1998.
    • (1998) Clin Exp Metastasis , vol.16 , pp. 185-191
    • Yu, M.1    Sato, H.2    Seiki, M.3    Spiegel, S.4    Thompson, E.W.5
  • 18
    • 0035923669 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis
    • Jiang A, Lehti K, Wang X, Weiss SJ, Keski-Oja J, et al.: Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis. Proc Natl Acad Sci USA 98, 13693-13698, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13693-13698
    • Jiang, A.1    Lehti, K.2    Wang, X.3    Weiss, S.J.4    Keski-Oja, J.5
  • 19
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • KessenbrockK, PlaksV, andWerb Z: Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 141, 52-67, 2010.
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 20
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation
    • Liotta LA, Steeg PS, and Stetler-Stevenson WG: Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell 64, 327-336, 1991.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 21
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato H, Takino T, Okada Y, Cao J, Shinagawa A, et al.: A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 61-51, 1994.
    • (1994) Nature , vol.370 , pp. 61-51
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5
  • 22
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme
    • Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson SJ, et al.: Cellular mechanisms for human procollagenase-3 activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J Biol Chem 271, 17124-17131, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 17124-17131
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3    Smith, B.4    Atkinson, S.J.5
  • 23
    • 0034738824 scopus 로고    scopus 로고
    • Expression of membrane-type 1 matrix metalloproteinase (MT1-MMP) on prostate cancer cell lines
    • Nagakawa O, Murakami K, Yamaura T, Fujiuchi Y, Murata J, et al.: Expression of membrane-type 1 matrix metalloproteinase (MT1-MMP) on prostate cancer cell lines. Cancer Lett 155, 173-179, 2000.
    • (2000) Cancer Lett , vol.155 , pp. 173-179
    • Nagakawa, O.1    Murakami, K.2    Yamaura, T.3    Fujiuchi, Y.4    Murata, J.5
  • 24
    • 0042062324 scopus 로고    scopus 로고
    • Roles of pericellular proteolysis by membrane type-1 matrix metalloproteinase in cancer invasion and angiogenesis
    • Seiki M, and Yana I: Roles of pericellular proteolysis by membrane type-1 matrix metalloproteinase in cancer invasion and angiogenesis. Cancer Sci 94, 569-574, 2003.
    • (2003) Cancer Sci , vol.94 , pp. 569-574
    • Seiki, M.1    Yana, I.2
  • 25
    • 66149148680 scopus 로고    scopus 로고
    • Induction of p53 contributes to apoptosis of HCT-116 human colon cancer cells induced by the dietary compound fisetin
    • Lim DY and Park JHY: Induction of p53 contributes to apoptosis of HCT-116 human colon cancer cells induced by the dietary compound fisetin. Am J Physiol Gastrointest Liver Physiol 296, G1060-G1068, 2009.
    • (2009) Am J Physiol Gastrointest Liver Physiol , vol.296
    • Kang, T.H.1    Tian, Y.H.Y.2
  • 26
    • 78651438001 scopus 로고    scopus 로고
    • Fisetin, a dietary flavonoid, induces cell cycle arrest and apoptosis through activation of p53 and inhibition of NF-kappa B pathways in bladder cancer cells
    • Li J, Cheng Y, Qu W, Sun Y, Wang Z, et al.: Fisetin, a dietary flavonoid, induces cell cycle arrest and apoptosis through activation of p53 and inhibition of NF-kappa B pathways in bladder cancer cells. Basic Clin Pharmacol Toxicol 108, 84-93, 2011.
    • (2011) Basic Clin Pharmacol Toxicol , vol.108 , pp. 84-93
    • Li, J.1    Cheng, Y.2    Qu, W.3    Sun, Y.4    Wang, Z.5
  • 27
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta LA, Tryggvason K, Garbisa S, Hart I, Foltz CM, et al.: Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 284, 67-68, 1980.
    • (1980) Nature , vol.284 , pp. 67-68
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Hart, I.4    Foltz, C.M.5
  • 28
    • 0345487550 scopus 로고    scopus 로고
    • Increased type IV collagen-degrading activity in metastases originating from primary tumors of the human colon
    • Karakiulakis G, Papanikolaou C, Jankovic SM, Aletras A, Papakonstantinou E, et al.: Increased type IV collagen-degrading activity in metastases originating from primary tumors of the human colon. Invasion Metastasis 17, 158-168, 1997.
    • (1997) Invasion Metastasis , vol.17 , pp. 158-168
    • Karakiulakis, G.1    Papanikolaou, C.2    Jankovic, S.M.3    Aletras, A.4    Papakonstantinou, E.5
  • 29
    • 0030242225 scopus 로고    scopus 로고
    • Fighting cancer by attacking its blood supply
    • Folkman J: Fighting cancer by attacking its blood supply. Sci Am 275, 150-154, 1996.
    • (1996) Sci Am , vol.275 , pp. 150-154
    • Folkman, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.