메뉴 건너뛰기




Volumn 29, Issue 3, 2013, Pages 1147-1153

Suppression of carbonic anhydrase IX leads to aberrant focal adhesion and decreased invasion of tumor cells

Author keywords

Carbonic anhydrase IX; Focal adhesion; Hypoxia; Microarray; ShRNA silencing

Indexed keywords

CARBONATE DEHYDRATASE IX; SHORT HAIRPIN RNA;

EID: 84872811693     PISSN: 1021335X     EISSN: 17912431     Source Type: Journal    
DOI: 10.3892/or.2013.2226     Document Type: Article
Times cited : (40)

References (36)
  • 1
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - A key regulatory factor in tumour growth
    • Harris AL: Hypoxia - a key regulatory factor in tumour growth. Nat Rev Cancer 2: 38-47, 2002. (Pubitemid 37328806)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.1 , pp. 38-47
    • Harris, A.L.1
  • 3
    • 0028111173 scopus 로고
    • Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment
    • Pastorek J, Pastorekova S, Callebaut I, et al: Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment. Oncogene 9: 2877-2888, 1994.
    • (1994) Oncogene , vol.9 , pp. 2877-2888
    • Pastorek, J.1    Pastorekova, S.2    Callebaut, I.3
  • 5
    • 2542601328 scopus 로고    scopus 로고
    • Hypoxia inducible carbonic anhydrase IX, marker of tumor hypoxia, survival pathway and therapy target
    • Potter C and Harris AL: Hypoxia inducible carbonic anhydrase IX, marker of tumour hypoxia, survival pathway and therapy target. Cell Cycle 3: 164-167, 2004. (Pubitemid 40268690)
    • (2004) Cell Cycle , vol.3 , Issue.2 , pp. 164-167
    • Potter, C.1    Harris, A.L.2
  • 7
    • 78650308850 scopus 로고    scopus 로고
    • New insights into the physiological role of carbonic anhydrase IX in tumour pH regulation
    • Swietach P, Hulikova A, Vaughan-Jones RD and Harris AL: New insights into the physiological role of carbonic anhydrase IX in tumour pH regulation. Oncogene 29: 6509-6521, 2010.
    • (2010) Oncogene , vol.29 , pp. 6509-6521
    • Swietach, P.1    Hulikova, A.2    Vaughan-Jones, R.D.3    Harris, A.L.4
  • 8
    • 8844224030 scopus 로고    scopus 로고
    • Microenvironmental and cellular consequences of altered blood flow in tumours
    • DOI 10.1259/bjr/12913493, Angiogenesis Imaging
    • Raghunand N, Gatenby RA and Gillies RJ: Microenvironmental and cellular consequences of altered blood flow in tumours. Br J Radiol 76 Spec No 1: S11-S22, 2003. (Pubitemid 39530312)
    • (2003) British Journal of Radiology , vol.76 , Issue.SPEC. ISS. 1
    • Raghunand, N.1    Gatenby, R.A.2    Gillies, R.J.3
  • 10
    • 84856237720 scopus 로고    scopus 로고
    • Carbonic anhydrase IX interacts with bicarbonate transporters in lamellipodia and increases cell migration via its catalytic domain
    • Svastova E, Witarski W, Csaderova L, et al: Carbonic anhydrase IX interacts with bicarbonate transporters in lamellipodia and increases cell migration via its catalytic domain. J Biol Chem 287: 3392-3402, 2012.
    • (2012) J Biol Chem , vol.287 , pp. 3392-3402
    • Svastova, E.1    Witarski, W.2    Csaderova, L.3
  • 12
    • 33846562017 scopus 로고    scopus 로고
    • Extracellular acidosis elevates carbonic anhydrase IX in human glioblastoma cells via transcriptional modulation that does not depend on hypoxia
    • Ihnatko R, Kubes M, Takacova M, et al: Extracellular acidosis elevates carbonic anhydrase IX in human glioblastoma cells via transcriptional modulation that does not depend on hypoxia. Int J Oncol 29: 1025-1033, 2006.
    • (2006) Int J Oncol , vol.29 , pp. 1025-1033
    • Ihnatko, R.1    Kubes, M.2    Takacova, M.3
  • 13
    • 0037374179 scopus 로고    scopus 로고
    • Expression of the hypoxia marker carbonic anhydrase IX is critically dependent on SP1 activity. Identification of a novel type of hypoxia-responsive enhancer
    • Kaluz S, Kaluzova M and Stanbridge EJ: Expression of the hypoxia marker carbonic anhydrase IX is critically dependent on SP1 activity. Identification of a novel type of hypoxia-responsive enhancer. Cancer Res 63: 917-922, 2003. (Pubitemid 36278419)
    • (2003) Cancer Research , vol.63 , Issue.5 , pp. 917-922
    • Kaluz, S.1    Kaluzova, M.2    Stanbridge, E.J.3
  • 14
    • 31744445721 scopus 로고    scopus 로고
    • A versatile tool for conditional gene expression and knockdown
    • DOI 10.1038/nmeth846, PII N846
    • Szulc J, Wiznerowicz M, Sauvain MO, Trono D and Aebischer P: A versatile tool for conditional gene expression and knockdown. Nat Methods 3: 109-116, 2006. (Pubitemid 43173309)
    • (2006) Nature Methods , vol.3 , Issue.2 , pp. 109-116
    • Szulc, J.1    Wiznerowicz, M.2    Sauvain, M.-O.3    Trono, D.4    Aebischer, P.5
  • 15
    • 58049215467 scopus 로고    scopus 로고
    • A novel signaling pathway impact analysis
    • Tarca AL, Draghici S, Khatri P, et al: A novel signaling pathway impact analysis. Bioinformatics 25: 75-82, 2009.
    • (2009) Bioinformatics , vol.25 , pp. 75-82
    • Tarca, A.L.1    Draghici, S.2    Khatri, P.3
  • 16
    • 44449091556 scopus 로고    scopus 로고
    • Molecular mechanisms of carbonic anhydrase IX-mediated pH regulation under hypoxia
    • Pastorekova S, Ratcliffe PJ and Pastorek J: Molecular mechanisms of carbonic anhydrase IX-mediated pH regulation under hypoxia. BJU Int 101 (Suppl 4): 8-15, 2008.
    • (2008) BJU Int , vol.101 , Issue.SUPPL. 4 , pp. 8-15
    • Pastorekova, S.1    Ratcliffe, P.J.2    Pastorek, J.3
  • 17
    • 58249094845 scopus 로고    scopus 로고
    • Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH
    • Chiche J, Ilc K, Laferriere J, et al: Hypoxia-inducible carbonic anhydrase IX and XII promote tumor cell growth by counteracting acidosis through the regulation of the intracellular pH. Cancer Res 69: 358-368, 2009.
    • (2009) Cancer Res , vol.69 , pp. 358-368
    • Chiche, J.1    Ilc, K.2    Laferriere, J.3
  • 18
    • 71749105278 scopus 로고    scopus 로고
    • Intact intracellular tail is critical for proper functioning of the tumor-associated, hypoxia-regulated carbonic anhydrase IX
    • Hulikova A, Zatovicova M, Svastova E, et al: Intact intracellular tail is critical for proper functioning of the tumor-associated, hypoxia-regulated carbonic anhydrase IX. FEBS Lett 583: 3563-3568, 2009.
    • (2009) FEBS Lett , vol.583 , pp. 3563-3568
    • Hulikova, A.1    Zatovicova, M.2    Svastova, E.3
  • 19
    • 84255199558 scopus 로고    scopus 로고
    • Phosphorylation of carbonic anhydrase IX controls its ability to mediate extracellular acidification in hypoxic tumors
    • Ditte P, Dequiedt F, Svastova E, et al: Phosphorylation of carbonic anhydrase IX controls its ability to mediate extracellular acidification in hypoxic tumors. Cancer Res 71: 7558-7567, 2011.
    • (2011) Cancer Res , vol.71 , pp. 7558-7567
    • Ditte, P.1    Dequiedt, F.2    Svastova, E.3
  • 20
    • 79953138420 scopus 로고    scopus 로고
    • Carbonic anhydrase IX (CA9) modulates tumor-associated cell migration and invasion
    • Shin HJ, Rho SB, Jung DC, Han IO, Oh ES and Kim JY: Carbonic anhydrase IX (CA9) modulates tumor-associated cell migration and invasion. J Cell Sci 124: 1077-1087, 2011.
    • (2011) J Cell Sci , vol.124 , pp. 1077-1087
    • Shin, H.J.1    Rho, S.B.2    Jung, D.C.3    Han, I.O.4    Oh, E.S.5    Kim, J.Y.6
  • 21
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir E and Geiger B: Molecular complexity and dynamics of cell-matrix adhesions. J Cell Sci 114: 3583-3590, 2001. (Pubitemid 33041040)
    • (2001) Journal of Cell Science , vol.114 , Issue.20 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 22
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • DOI 10.1016/S0092-8674(03)00163-6
    • Tu Y, Wu S, Shi X, Chen K and Wu C: Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 113: 37-47, 2003. (Pubitemid 36411958)
    • (2003) Cell , vol.113 , Issue.1 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 23
    • 54549088877 scopus 로고    scopus 로고
    • Rac activation and inactivation control plasticity of tumor cell movement
    • Sanz-Moreno V, Gadea G, Ahn J, et al: Rac activation and inactivation control plasticity of tumor cell movement. Cell 135: 510-523, 2008.
    • (2008) Cell , vol.135 , pp. 510-523
    • Sanz-Moreno, V.1    Gadea, G.2    Ahn, J.3
  • 24
    • 0036713381 scopus 로고    scopus 로고
    • Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins
    • DOI 10.1038/ncb835
    • Meller N, Irani-Tehrani M, Kiosses WB, Del Pozo MA and Schwartz MA: Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins. Nat Cell Biol 4: 639-647, 2002. (Pubitemid 34993699)
    • (2002) Nature Cell Biology , vol.4 , Issue.9 , pp. 639-647
    • Meller, N.1    Irani-Tehrani, M.2    Kiosses, W.B.3    Del Pozo, M.A.4    Schwartz, M.A.5
  • 25
    • 0037115488 scopus 로고    scopus 로고
    • Identification of an evolutionary conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity
    • DOI 10.1242/jcs.00219
    • Cote JF and Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleo-tide exchange activity. J Cell Sci 115: 4901-4913, 2002. (Pubitemid 36054642)
    • (2002) Journal of Cell Science , vol.115 , Issue.24 , pp. 4901-4913
    • Cote, J.-F.1    Vuori, K.2
  • 26
    • 65249168811 scopus 로고    scopus 로고
    • Interaction of mono-carboxylate transporter 4 with beta1-integrin and its role in cell migration
    • Gallagher SM, Castorino JJ and Philp NJ: Interaction of mono-carboxylate transporter 4 with beta1-integrin and its role in cell migration. Am J Physiol Cell Physiol 296: C414-C421, 2009.
    • (2009) Am J Physiol Cell Physiol , vol.296
    • Gallagher, S.M.1    Castorino, J.J.2    Philp, N.J.3
  • 27
    • 0037164808 scopus 로고    scopus 로고
    • Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1
    • DOI 10.1083/jcb.200208050
    • Denker SP and Barber DL: Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1. J Cell Biol 159: 1087-1096, 2002. (Pubitemid 36055762)
    • (2002) Journal of Cell Biology , vol.159 , Issue.6 , pp. 1087-1096
    • Denker, S.P.1    Barber, D.L.2
  • 28
    • 68149105927 scopus 로고    scopus 로고
    • Protons make tumor cells move like clockwork
    • Stock C and Schwab A: Protons make tumor cells move like clockwork. Pflugers Arch 458: 981-992, 2009.
    • (2009) Pflugers Arch , vol.458 , pp. 981-992
    • Stock, C.1    Schwab, A.2
  • 29
    • 1542269303 scopus 로고    scopus 로고
    • Integrins: Roles in cancer development and as treatment targets
    • DOI 10.1038/sj.bjc.6601576
    • Jin H and Varner J: Integrins: roles in cancer development and as treatment targets. Br J Cancer 90: 561-565, 2004. (Pubitemid 38297190)
    • (2004) British Journal of Cancer , vol.90 , Issue.3 , pp. 561-565
    • Jin, H.1    Varner, J.2
  • 30
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • DOI 10.1016/j.cardiores.2005.12.002, PII S0008636305005651
    • Nagase H, Visse R and Murphy G: Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 69: 562-573, 2006. (Pubitemid 43139720)
    • (2006) Cardiovascular Research , vol.69 , Issue.3 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 31
    • 59449108662 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2-integrin alpha(v)beta3 binding is required for mesenchymal cell invasive activity but not epithelial locomotion: A computational time-lapse study
    • Rupp PA, Visconti RP, Czirok A, Cheresh DA and Little CD: Matrix metalloproteinase 2-integrin alpha(v)beta3 binding is required for mesenchymal cell invasive activity but not epithelial locomotion: a computational time-lapse study. Mol Biol Cell 19: 5529-5540, 2008.
    • (2008) Mol Biol Cell , vol.19 , pp. 5529-5540
    • Rupp, P.A.1    Visconti, R.P.2    Czirok, A.3    Cheresh, D.A.4    Little, C.D.5
  • 32
    • 0033547831 scopus 로고    scopus 로고
    • Role of His-224 in the anomalous pH dependence of human strome-lysin-1
    • Holman CM, Kan CC, Gehring MR and Van Wart HE: Role of His-224 in the anomalous pH dependence of human strome-lysin-1. Biochemistry 38: 677-681, 1999.
    • (1999) Biochemistry , vol.38 , pp. 677-681
    • Holman, C.M.1    Kan, C.C.2    Gehring, M.R.3    Van Wart, H.E.4
  • 35
    • 0035988813 scopus 로고    scopus 로고
    • Matrix-directed regulation of pericellular proteolysis and tumor progression
    • DOI 10.1016/S1044-579X(02)00026-3
    • Hornebeck W, Emonard H, Monboisse JC and Bellon G: Matrix-directed regulation of pericellular proteolysis and tumor progression. Semin Cancer Biol 12: 231-241, 2002. (Pubitemid 34833066)
    • (2002) Seminars in Cancer Biology , vol.12 , Issue.3 , pp. 231-241
    • Hornebeck, W.1    Emonard, H.2    Monboisse, J.-C.3    Bellon, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.