메뉴 건너뛰기




Volumn 8, Issue 11, 2010, Pages 1501-1512

Clinical implications of the influence of Ehm2 on the aggressiveness of breast cancer cells through regulation of matrix metalloproteinase-9 expression

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; EZRIN; GELATINASE B; HAMMERHEAD RIBOZYME; MESSENGER RNA; MOESIN; PROTEIN EHM2; PROTEIN NF2; RADIXIN; UNCLASSIFIED DRUG;

EID: 78649661907     PISSN: 15417786     EISSN: 15573125     Source Type: Journal    
DOI: 10.1158/1541-7786.MCR-10-0186     Document Type: Article
Times cited : (16)

References (42)
  • 1
    • 70349862896 scopus 로고    scopus 로고
    • The Janus-faced role of ezrin in "linking" cells to either normal or metastatic phenotype
    • Brambilla D, Fais S. The Janus-faced role of ezrin in "linking" cells to either normal or metastatic phenotype. Int J Cancer 2009;125:2239-45.
    • (2009) Int J Cancer , vol.125 , pp. 2239-2245
    • Brambilla, D.1    Fais, S.2
  • 2
    • 5444221173 scopus 로고    scopus 로고
    • Novel technologies and recent advances in metastasis research
    • Crnic I, Christofori G. Novel technologies and recent advances in metastasis research. Int J Dev Biol 2004;48:573-81.
    • (2004) Int J Dev Biol , vol.48 , pp. 573-581
    • Crnic, I.1    Christofori, G.2
  • 3
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • Pearson MA, Reczek D, Bretscher A, Karplus PA. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 2000;101:259-70.
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 4
    • 0037155867 scopus 로고    scopus 로고
    • Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain
    • Shimizu T, Seto A, Maita N, Hamada K, Tsukita S, Hakoshima T. Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain. J Biol Chem 2002;277:10332-6.
    • (2002) J Biol Chem , vol.277 , pp. 10332-10336
    • Shimizu, T.1    Seto, A.2    Maita, N.3    Hamada, K.4    Tsukita, S.5    Hakoshima, T.6
  • 5
    • 0038136972 scopus 로고    scopus 로고
    • Structure of the active N-terminal domain of ezrin. Conformational and mobility changes identify keystone interactions
    • Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA. Structure of the active N-terminal domain of ezrin. Conformational and mobility changes identify keystone interactions. J Biol Chem 2003;278:4949-56.
    • (2003) J Biol Chem , vol.278 , pp. 4949-4956
    • Smith, W.J.1    Nassar, N.2    Bretscher, A.3    Cerione, R.A.4    Karplus, P.A.5
  • 6
    • 0037077282 scopus 로고    scopus 로고
    • The phosphotyrosine binding-like domain of talin activates integrins
    • Calderwood DA, Yan B, de Pereda JM, et al. The phosphotyrosine binding-like domain of talin activates integrins. J Biol Chem 2002;277:21749-58.
    • (2002) J Biol Chem , vol.277 , pp. 21749-21758
    • Calderwood, D.A.1    Yan, B.2    De Pereda, J.M.3
  • 7
    • 40449121624 scopus 로고    scopus 로고
    • Dual role of the Jak1 FERM and kinase domains in cytokine receptor binding and in stimulation-dependent Jak activation
    • Haan S, Margue C, Engrand A, et al. Dual role of the Jak1 FERM and kinase domains in cytokine receptor binding and in stimulation-dependent Jak activation. J Immunol 2008;180:998-1007.
    • (2008) J Immunol , vol.180 , pp. 998-1007
    • Haan, S.1    Margue, C.2    Engrand, A.3
  • 9
    • 0029569120 scopus 로고
    • Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets
    • Nakamura F, Amieva MR, Furthmayr H. Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets. J Biol Chem 1995;270:31377-85.
    • (1995) J Biol Chem , vol.270 , pp. 31377-31385
    • Nakamura, F.1    Amieva, M.R.2    Furthmayr, H.3
  • 10
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M, Sato N, Kondo T, et al. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol 1996;135:37-51.
    • (1996) J Cell Biol , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3
  • 11
    • 33646541349 scopus 로고    scopus 로고
    • A FERM-adjacent (FA) region defines a subset of the 4.1 superfamily and is a potential regulator of FERM domain function
    • Baines AJ. A FERM-adjacent (FA) region defines a subset of the 4.1 superfamily and is a potential regulator of FERM domain function. BMC Genomics 2006;7:85.
    • (2006) BMC Genomics , vol.7 , pp. 85
    • Baines, A.J.1
  • 12
    • 0029850487 scopus 로고    scopus 로고
    • Identification of genes differentially expressed in association with metastatic potential of K-1735 murine melanoma by messenger RNA differential display
    • Hashimoto Y, Shindo-Okada N, Tani M, Takeuchi K, Toma H, Yokota J. Identification of genes differentially expressed in association with metastatic potential of K-1735 murine melanoma by messenger RNA differential display. Cancer Res 1996;56:5266-71.
    • (1996) Cancer Res , vol.56 , pp. 5266-5271
    • Hashimoto, Y.1    Shindo-Okada, N.2    Tani, M.3    Takeuchi, K.4    Toma, H.5    Yokota, J.6
  • 13
    • 0034655545 scopus 로고    scopus 로고
    • Molecular cloning of a novel NF2/ERM/4.1 superfamily gene, Ehm2, that is expressed in high-metastatic K1735 murine melanoma cells
    • Shimizu K, Nagamachi Y, Tani M, et al. Molecular cloning of a novel NF2/ERM/4.1 superfamily gene, Ehm2, that is expressed in high-metastatic K1735 murine melanoma cells. Genomics 2000;65:113-20.
    • (2000) Genomics , vol.65 , pp. 113-120
    • Shimizu, K.1    Nagamachi, Y.2    Tani, M.3
  • 14
    • 0346463080 scopus 로고    scopus 로고
    • Androgen control of cell proliferation and cytoskeletal reorganization in human fibrosarcoma cells: Role of RhoB signaling
    • Chauhan S, Kunz S, Davis K, et al. Androgen control of cell proliferation and cytoskeletal reorganization in human fibrosarcoma cells: role of RhoB signaling. J Biol Chem 2004;279:937-44.
    • (2004) J Biol Chem , vol.279 , pp. 937-944
    • Chauhan, S.1    Kunz, S.2    Davis, K.3
  • 15
    • 0141682080 scopus 로고    scopus 로고
    • Androgen regulation of the human FERM domain encoding gene EHM2 in a cell model of steroid-induced differentiation
    • Chauhan S, Pandey R, Way JF, et al. Androgen regulation of the human FERM domain encoding gene EHM2 in a cell model of steroid-induced differentiation. Biochem Biophys Res Commun 2003;310:421-32.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 421-432
    • Chauhan, S.1    Pandey, R.2    Way, J.F.3
  • 16
    • 33750486853 scopus 로고    scopus 로고
    • Increased expression of the metastasis-associated gene Ehm2 in prostate cancer
    • Wang J, Cai Y, Penland R, Chauhan S, Miesfeld RL, Ittmann M. Increased expression of the metastasis-associated gene Ehm2 in prostate cancer. Prostate 2006;66:1641-52.
    • (2006) Prostate , vol.66 , pp. 1641-1652
    • Wang, J.1    Cai, Y.2    Penland, R.3    Chauhan, S.4    Miesfeld, R.L.5    Ittmann, M.6
  • 17
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 2003;31:3406-15.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 18
    • 0024388166 scopus 로고
    • Colorimetric growth assay for epidermal cell cultures by their crystal violet binding capacity
    • Bonnekoh B, Wevers A, Jugert F, Merk H, Mahrle G. Colorimetric growth assay for epidermal cell cultures by their crystal violet binding capacity. Arch Dermatol Res 1989;281:487-90.
    • (1989) Arch Dermatol Res , vol.281 , pp. 487-490
    • Bonnekoh, B.1    Wevers, A.2    Jugert, F.3    Merk, H.4    Mahrle, G.5
  • 19
    • 23844431620 scopus 로고    scopus 로고
    • Targeting matrilysin and its impact on tumor growth in vivo: The potential implications in breast cancer therapy
    • Jiang WG, Davies G, Martin TA, et al. Targeting matrilysin and its impact on tumor growth in vivo: the potential implications in breast cancer therapy. Clin Cancer Res 2005;11:6012-9.
    • (2005) Clin Cancer Res , vol.11 , pp. 6012-6019
    • Jiang, W.G.1    Davies, G.2    Martin, T.A.3
  • 20
    • 0028941798 scopus 로고
    • Inhibition of hepatocyte growth factor-induced motility and in vitro invasion of human colon cancer cells by γ-linolenic acid
    • Jiang WG, Hiscox S, Hallett MB, Scott C, Horrobin DF, Puntis MC. Inhibition of hepatocyte growth factor-induced motility and in vitro invasion of human colon cancer cells by γ-linolenic acid. Br J Cancer 1995;71:744-52.
    • (1995) Br J Cancer , vol.71 , pp. 744-752
    • Jiang, W.G.1    Hiscox, S.2    Hallett, M.B.3    Scott, C.4    Horrobin, D.F.5    Puntis, M.C.6
  • 21
    • 0032713122 scopus 로고    scopus 로고
    • Antagonistic effect of NK4, a novel hepatocyte growth factor variant, on in vitro angiogenesis of human vascular endothelial cells
    • Jiang WG, Hiscox SE, Parr C, et al. Antagonistic effect of NK4, a novel hepatocyte growth factor variant, on in vitro angiogenesis of human vascular endothelial cells. Clin Cancer Res 1999;5:3695-703.
    • (1999) Clin Cancer Res , vol.5 , pp. 3695-3703
    • Jiang, W.G.1    Hiscox, S.E.2    Parr, C.3
  • 22
    • 0027989808 scopus 로고
    • Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis
    • Koopman G, Reutelingsperger CP, Kuijten GA, Keehnen RM, Pals ST, van Oers MH. Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis. Blood 1994;84:1415-20.
    • (1994) Blood , vol.84 , pp. 1415-1420
    • Koopman, G.1    Reutelingsperger, C.P.2    Kuijten, G.A.3    Keehnen, R.M.4    Pals, S.T.5    Van Oers, M.H.6
  • 23
    • 34447119556 scopus 로고    scopus 로고
    • Podocalyxin increases the aggressive phenotype of breast and prostate cancer cells in vitro through its interaction with ezrin
    • Sizemore S, Cicek M, Sizemore N, Ng KP, Casey G. Podocalyxin increases the aggressive phenotype of breast and prostate cancer cells in vitro through its interaction with ezrin. Cancer Res 2007;67:6183-91.
    • (2007) Cancer Res , vol.67 , pp. 6183-6191
    • Sizemore, S.1    Cicek, M.2    Sizemore, N.3    Ng, K.P.4    Casey, G.5
  • 24
    • 33747834891 scopus 로고    scopus 로고
    • The FERM protein Yurt is a negative regulatory component of the Crumbs complex that controls epithelial polarity and apical membrane size
    • Laprise P, Beronja S, Silva-Gagliardi NF, et al. The FERM protein Yurt is a negative regulatory component of the Crumbs complex that controls epithelial polarity and apical membrane size. Dev Cell 2006;11:363-74.
    • (2006) Dev Cell , vol.11 , pp. 363-374
    • Laprise, P.1    Beronja, S.2    Silva-Gagliardi, N.F.3
  • 25
    • 0034672418 scopus 로고    scopus 로고
    • BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration
    • Aguiar RC, Yakushijin Y, Kharbanda S, Salgia R, Fletcher JA, Shipp MA. BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration. Blood 2000;96:4328-34.
    • (2000) Blood , vol.96 , pp. 4328-4334
    • Aguiar, R.C.1    Yakushijin, Y.2    Kharbanda, S.3    Salgia, R.4    Fletcher, J.A.5    Shipp, M.A.6
  • 26
    • 0031683065 scopus 로고    scopus 로고
    • The FERM domain: A unique module involved in the linkage of cytoplasmic proteins to the membrane
    • Chishti AH, Kim AC, Marfatia SM, et al. The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane. Trends Biochem Sci 1998;23:281-2.
    • (1998) Trends Biochem Sci , vol.23 , pp. 281-282
    • Chishti, A.H.1    Kim, A.C.2    Marfatia, S.M.3
  • 27
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002;2:161-74.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 28
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • Overall CM, Lopez-Otin C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer 2002;2:657-72.
    • (2002) Nat Rev Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 29
    • 0040439972 scopus 로고    scopus 로고
    • The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells
    • Manes S, Llorente M, Lacalle RA, et al. The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells. J Biol Chem 1999;274:6935-45.
    • (1999) J Biol Chem , vol.274 , pp. 6935-6945
    • Manes, S.1    Llorente, M.2    Lacalle, R.A.3
  • 30
    • 0345687153 scopus 로고    scopus 로고
    • Constitutive secretion of MMP9 by early-passage cultured human endothelial cells
    • Arkell J, Jackson CJ. Constitutive secretion of MMP9 by early-passage cultured human endothelial cells. Cell Biochem Funct 2003;21:381-6.
    • (2003) Cell Biochem Funct , vol.21 , pp. 381-386
    • Arkell, J.1    Jackson, C.J.2
  • 31
    • 0000391746 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
    • Bergers G, Brekken R, McMahon G, et al. Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nat Cell Biol 2000;2:737-44.
    • (2000) Nat Cell Biol , vol.2 , pp. 737-744
    • Bergers, G.1    Brekken, R.2    McMahon, G.3
  • 32
    • 0037103183 scopus 로고    scopus 로고
    • Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo
    • McQuibban GA, Gong JH, Wong JP, Wallace JL, Clark-Lewis I, Overall CM. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 2002;100:1160-7.
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1    Gong, J.H.2    Wong, J.P.3    Wallace, J.L.4    Clark-Lewis, I.5    Overall, C.M.6
  • 33
    • 0035940429 scopus 로고    scopus 로고
    • Thrombospondin-1 suppresses spontaneous tumor growth and inhibits activation of matrix metalloproteinase-9 and mobilization of vascular endothelial growth factor
    • Rodriguez-Manzaneque JC, Lane TF, Ortega MA, Hynes RO, Lawler J, Iruela-Arispe ML. Thrombospondin-1 suppresses spontaneous tumor growth and inhibits activation of matrix metalloproteinase-9 and mobilization of vascular endothelial growth factor. Proc Natl Acad Sci U S A 2001;98:12485-90.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12485-12490
    • Rodriguez-Manzaneque, J.C.1    Lane, T.F.2    Ortega, M.A.3    Hynes, R.O.4    Lawler, J.5    Iruela-Arispe, M.L.6
  • 34
    • 47749119594 scopus 로고    scopus 로고
    • Forced expression of MMP9 rescues the loss of angiogenesis and abrogates metastasis of pancreatic tumors triggered by the absence of host SPARC
    • Maywood
    • Arnold S, Mira E, Muneer S, et al. Forced expression of MMP9 rescues the loss of angiogenesis and abrogates metastasis of pancreatic tumors triggered by the absence of host SPARC. Exp Biol Med (Maywood) 2008;233:860-73.
    • (2008) Exp Biol Med , vol.233 , pp. 860-873
    • Arnold, S.1    Mira, E.2    Muneer, S.3
  • 35
    • 0141482154 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: Implications for ascites formation
    • Belotti D, Paganoni P, Manenti L, et al. Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: implications for ascites formation. Cancer Res 2003;63:5224-9.
    • (2003) Cancer Res , vol.63 , pp. 5224-5229
    • Belotti, D.1    Paganoni, P.2    Manenti, L.3
  • 36
    • 33745594554 scopus 로고    scopus 로고
    • Expression of MT-1 MMP, MMP2, MMP9 and TIMP2 mRNAs in ductal carcinoma in situ and invasive ductal carcinoma of the breast
    • Kim HJ, Park CI, Park BW, Lee HD, Jung WH. Expression of MT-1 MMP, MMP2, MMP9 and TIMP2 mRNAs in ductal carcinoma in situ and invasive ductal carcinoma of the breast. Yonsei Med J 2006;47:333-42.
    • (2006) Yonsei Med J , vol.47 , pp. 333-342
    • Kim, H.J.1    Park, C.I.2    Park, B.W.3    Lee, H.D.4    Jung, W.H.5
  • 37
    • 38749137345 scopus 로고    scopus 로고
    • Expression and prognostic role of MMP2, MMP9, MMP13, and MMP14 matrix metalloproteinases in sinonasal and oral malignant melanomas
    • Kondratiev S, Gnepp DR, Yakirevich E, et al. Expression and prognostic role of MMP2, MMP9, MMP13, and MMP14 matrix metalloproteinases in sinonasal and oral malignant melanomas. Hum Pathol 2008;39:337-43.
    • (2008) Hum Pathol , vol.39 , pp. 337-343
    • Kondratiev, S.1    Gnepp, D.R.2    Yakirevich, E.3
  • 38
    • 24744464071 scopus 로고    scopus 로고
    • Expression of MMP2, MMP9 and MMP3 in breast cancer brain metastasis in a rat model
    • Mendes O, Kim HT, Stoica G. Expression of MMP2, MMP9 and MMP3 in breast cancer brain metastasis in a rat model. Clin Exp Metastasis 2005;22:237-46.
    • (2005) Clin Exp Metastasis , vol.22 , pp. 237-246
    • Mendes, O.1    Kim, H.T.2    Stoica, G.3
  • 39
    • 33747515210 scopus 로고    scopus 로고
    • Circulating MMP2 and MMP9 in breast cancer - Potential role in classification of patients into low risk, high risk, benign disease and breast cancer categories
    • Somiari SB, Somiari RI, Heckman CM, et al. Circulating MMP2 and MMP9 in breast cancer - potential role in classification of patients into low risk, high risk, benign disease and breast cancer categories. Int J Cancer 2006;119:1403-11.
    • (2006) Int J Cancer , vol.119 , pp. 1403-1411
    • Somiari, S.B.1    Somiari, R.I.2    Heckman, C.M.3
  • 40
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens LM, Fingleton B, Matrisian LM. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002;295:2387-92.
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 41
    • 8744306171 scopus 로고    scopus 로고
    • Prognostic value of matrix metalloproteinases (MMP-2 and MMP-9) in patients with lymph node-negative breast carcinoma
    • Li HC, Cao DC, Liu Y, et al. Prognostic value of matrix metalloproteinases (MMP-2 and MMP-9) in patients with lymph node-negative breast carcinoma. Breast Cancer Res Treat 2004;88:75-85.
    • (2004) Breast Cancer Res Treat , vol.88 , pp. 75-85
    • Li, H.C.1    Cao, D.C.2    Liu, Y.3
  • 42
    • 32244434925 scopus 로고    scopus 로고
    • Plasma concentration and activity of matrix metalloproteinase 2 and 9 in patients with breast disease, breast cancer and at risk of developing breast cancer
    • Somiari SB, Shriver CD, Heckman C, et al. Plasma concentration and activity of matrix metalloproteinase 2 and 9 in patients with breast disease, breast cancer and at risk of developing breast cancer. Cancer Lett 2006;233:98-107.
    • (2006) Cancer Lett , vol.233 , pp. 98-107
    • Somiari, S.B.1    Shriver, C.D.2    Heckman, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.