메뉴 건너뛰기




Volumn 290, Issue 6, 2015, Pages 3680-3692

Activity of Plasma Membrane V-ATPases Is Critical for the Invasion of MDA-MB231 Breast Cancer Cells

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CYTOLOGY; DISEASES; MEMBRANES;

EID: 84922454172     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.611210     Document Type: Article
Times cited : (87)

References (55)
  • 1
    • 63049090100 scopus 로고    scopus 로고
    • Metastasis: From dissemination to organ-specific colonization
    • Nguyen, D. X., Bos, P. D., and Massagué, J. (2009) Metastasis: from dissemination to organ-specific colonization. Nat. Rev. Cancer 9, 274-284.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 274-284
    • Nguyen, D.X.1    Bos, P.D.2    Massagué, J.3
  • 2
    • 84859715721 scopus 로고    scopus 로고
    • Tumor microenvironment: A main actor in the metastasis process
    • Spano, D., and Zollo, M. (2012) Tumor microenvironment: A main actor in the metastasis process. Clin. Exp. Metastasis 29, 381-395.
    • (2012) Clin. Exp. Metastasis , vol.29 , pp. 381-395
    • Spano, D.1    Zollo, M.2
  • 3
    • 33751252276 scopus 로고    scopus 로고
    • Cancer metastasis: Building a framework
    • Gupta, G. P., and Massagué, J. (2006) Cancer metastasis: building a framework. Cell 127, 679-695.
    • (2006) Cell , vol.127 , pp. 679-695
    • Gupta, G.P.1    Massagué, J.2
  • 4
  • 6
    • 67649763451 scopus 로고    scopus 로고
    • Voltage-gated sodium channel activity promotes cysteine cathepsin-dependent invasiveness and colony growth of human cancer cells
    • Gillet, L., Roger, S., Besson, P., Lecaille, F., Gore, J., Bougnoux, P., Lalmanach, G., and Le Guennec, J. Y. (2009) Voltage-gated sodium channel activity promotes cysteine cathepsin-dependent invasiveness and colony growth of human cancer cells. J. Biol. Chem. 284, 8680-8691.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8680-8691
    • Gillet, L.1    Roger, S.2    Besson, P.3    Lecaille, F.4    Gore, J.5    Bougnoux, P.6    Lalmanach, G.7    Le Guennec, J.Y.8
  • 7
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007) Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 8
    • 62949218373 scopus 로고    scopus 로고
    • The yeast lysosome-like vacuole: Endpoint and crossroads
    • Li, S. C., and Kane, P. M. (2009) The yeast lysosome-like vacuole: endpoint and crossroads. Biochim. Biophys. Acta 1793, 650-663.
    • (2009) Biochim. Biophys. Acta 1793 , pp. 650-663
    • Li, S.C.1    Kane, P.M.2
  • 9
    • 66449088593 scopus 로고    scopus 로고
    • Regulation of the V-ATPase in kidney epithelial cells: Dual role in acid-base homeostasis and vesicle trafficking
    • Brown, D., Paunescu, T. G., Breton, S., and Marshansky, V. (2009) Regulation of the V-ATPase in kidney epithelial cells: dual role in acid-base homeostasis and vesicle trafficking. J. Exp. Biol. 212, 1762-1772.
    • (2009) J. Exp. Biol. , vol.212 , pp. 1762-1772
    • Brown, D.1    Paunescu, T.G.2    Breton, S.3    Marshansky, V.4
  • 10
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform functionof the V-ATPases
    • Toei, M., Saum, R., and Forgac, M. (2010) Regulation and isoform functionof the V-ATPases. Biochemistry 49, 4715-4723.
    • (2010) Biochemistry , vol.49 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 11
    • 0035861664 scopus 로고    scopus 로고
    • The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis
    • Kawasaki-Nishi, S., Bowers, K., Nishi, T., Forgac, M., and Stevens, T. H. (2001) The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis. J. Biol. Chem. 276, 47411-47420.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47411-47420
    • Kawasaki-Nishi, S.1    Bowers, K.2    Nishi, T.3    Forgac, M.4    Stevens, T.H.5
  • 13
  • 18
    • 67650236818 scopus 로고    scopus 로고
    • Function of a subunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells
    • Hinton, A., Sennoune, S. R., Bond, S., Fang, M., Reuveni, M., Sahagian, G. G., Jay, D., Martinez-Zaguilan, R., and Forgac, M. (2009) Function of a subunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells. J. Biol. Chem. 284, 16400-16408.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16400-16408
    • Hinton, A.1    Sennoune, S.R.2    Bond, S.3    Fang, M.4    Reuveni, M.5    Sahagian, G.G.6    Jay, D.7    Martinez-Zaguilan, R.8    Forgac, M.9
  • 19
    • 84887439107 scopus 로고    scopus 로고
    • The function of vacuolar ATPase (VATPase) a subunit isoforms in invasiveness of MCF10a and MCF10CA1a human breast cancer cells
    • Capecci, J., and Forgac, M. (2013) The function of vacuolar ATPase (VATPase) a subunit isoforms in invasiveness of MCF10a and MCF10CA1a human breast cancer cells. J. Biol. Chem. 288, 32731-32741.
    • (2013) J. Biol. Chem. , vol.288 , pp. 32731-32741
    • Capecci, J.1    Forgac, M.2
  • 22
    • 84869502676 scopus 로고    scopus 로고
    • Inhibitors of vacuolar ATPase proton pumps inhibit human prostate cancer cell invasion and prostate-specific antigen expression and secretion
    • Michel, V., Licon-Munoz, Y., Trujillo, K., Bisoffi, M., and Parra, K. J. (2013) Inhibitors of vacuolar ATPase proton pumps inhibit human prostate cancer cell invasion and prostate-specific antigen expression and secretion. Int. J. Cancer. 132, E1-E10.
    • (2013) Int. J. Cancer. , vol.132 , pp. E1-E10
    • Michel, V.1    Licon-Munoz, Y.2    Trujillo, K.3    Bisoffi, M.4    Parra, K.J.5
  • 27
    • 0019554835 scopus 로고
    • Intracellular pH
    • Roos, A., and Boron, W. F. (1981) Intracellular pH. Physiol. Rev. 61, 296-434.
    • (1981) Physiol. Rev. , vol.61 , pp. 296-434
    • Roos, A.1    Boron, W.F.2
  • 28
    • 84892639521 scopus 로고    scopus 로고
    • Regulated assembly of vacuolar ATPase is increased during cluster disruption-induced maturation of dendritic cells through a phosphatidylinositol 3-kinase/mTOR-dependent pathway
    • Liberman, R., Bond, S., Shainheit, M. G., Stadecker, M. J., and Forgac, M. (2014) Regulated assembly of vacuolar ATPase is increased during cluster disruption-induced maturation of dendritic cells through a phosphatidylinositol 3-kinase/mTOR-dependent pathway. J. Biol. Chem. 289, 1355-1363.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1355-1363
    • Liberman, R.1    Bond, S.2    Shainheit, M.G.3    Stadecker, M.J.4    Forgac, M.5
  • 29
    • 80055109363 scopus 로고    scopus 로고
    • An in vitro FluoroBlok tumor invasion assay
    • Partridge, J., and Flaherty, P. (2009) An in vitro FluoroBlok tumor invasion assay. J. Vis. Exp. 29, 1475.
    • (2009) J. Vis. Exp. , vol.29 , pp. 1475
    • Partridge, J.1    Flaherty, P.2
  • 30
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 31
    • 84881261944 scopus 로고    scopus 로고
    • Structural analysis of the N-terminal domain of subunit a of the yeast vacuolar ATPase (V-ATPase) using accessibility of single cysteine substitutions to chemical modification
    • Liberman, R., Cotter, K., Baleja, J. D., and Forgac, M. (2013) Structural analysis of the N-terminal domain of subunit a of the yeast vacuolar ATPase (V-ATPase) using accessibility of single cysteine substitutions to chemical modification. J. Biol. Chem. 288, 22798-22808.
    • (2013) J. Biol. Chem. , vol.288 , pp. 22798-22808
    • Liberman, R.1    Cotter, K.2    Baleja, J.D.3    Forgac, M.4
  • 32
    • 0026688602 scopus 로고
    • +)-ATPase upon modification by sulfhydryl reagents
    • +)-ATPase upon modification by sulfhydryl reagents. J. Biol. Chem. 267, 5817-5822.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5817-5822
    • Feng, Y.1    Forgac, M.2
  • 33
    • 4544289322 scopus 로고    scopus 로고
    • Topological characterization of the c, c, and c subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae
    • Flannery, A. R., Graham, L. A., and Stevens, T. H. (2004) Topological characterization of the c, c, and c subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae. J. Biol. Chem. 279, 39856-39862.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39856-39862
    • Flannery, A.R.1    Graham, L.A.2    Stevens, T.H.3
  • 34
    • 0034604676 scopus 로고    scopus 로고
    • Molecular characterization of the yeast vacuolar H+-ATPase proton pore
    • Powell, B., Graham, L. A., and Stevens, T. H. (2000) Molecular characterization of the yeast vacuolar H+-ATPase proton pore. J. Biol. Chem. 275, 23654-23660.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23654-23660
    • Powell, B.1    Graham, L.A.2    Stevens, T.H.3
  • 35
    • 0031597366 scopus 로고    scopus 로고
    • +-ATPase is an unconventional glucose- induced effect
    • +-ATPase is an unconventional glucose- induced effect. Mol. Cell Biol. 18, 7064-7074.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 7064-7074
    • Parra, K.J.1    Kane, P.M.2
  • 36
    • 0037040244 scopus 로고    scopus 로고
    • Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site
    • Bowman, B. J., and Bowman, E. J. (2002) Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site. J. Biol. Chem. 277, 3965-3972.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3965-3972
    • Bowman, B.J.1    Bowman, E.J.2
  • 38
    • 0038606551 scopus 로고    scopus 로고
    • Subunit rotation of vacuolar-type proton pumping ATPase: Relative rotation of the G and C subunits
    • Hirata, T., Iwamoto-Kihara, A., Sun-Wada, G. H., Okajima, T., Wada, Y., and Futai, M. (2003) Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and C subunits. J. Biol. Chem. 278, 23714-23719.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23714-23719
    • Hirata, T.1    Iwamoto-Kihara, A.2    Sun-Wada, G.H.3    Okajima, T.4    Wada, Y.5    Futai, M.6
  • 39
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • Gocheva, V., and Joyce, J. A. (2007) Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle. 6, 60-64.
    • (2007) Cell Cycle , vol.6 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 40
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk, B., Turk, D., and Turk, V. (2000) Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta 1477, 98-111.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 42
    • 81155127516 scopus 로고    scopus 로고
    • Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion
    • Victor, B. C., Anbalagan, A., Mohamed, M. M., Sloane, B. F., and Cavallo- Medved, D. (2011) Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion. Breast Cancer Res. 13, R115-8P.
    • (2011) Breast Cancer Res , vol.13 , pp. R115-R118
    • Victor, B.C.1    Anbalagan, A.2    Mohamed, M.M.3    Sloane, B.F.4    Cavallo- Medved, D.5
  • 43
    • 0037442576 scopus 로고    scopus 로고
    • Intracellular and extracellular cathepsin B facilitate invasion of MCF-10A neoT cells through reconstituted extracellular matrix in vitro
    • Premzl, A., Zavasnik-Bergant, V., Turk, V., and Kos, J. (2003) Intracellular and extracellular cathepsin B facilitate invasion of MCF-10A neoT cells through reconstituted extracellular matrix in vitro. Exp. Cell Res. 283, 206-214.
    • (2003) Exp. Cell Res. , vol.283 , pp. 206-214
    • Premzl, A.1    Zavasnik-Bergant, V.2    Turk, V.3    Kos, J.4
  • 44
    • 0038215389 scopus 로고    scopus 로고
    • Pericellular cathepsin B and malignant progression
    • Roshy, S., Sloane, B. F., and Moin, K. (2003) Pericellular cathepsin B and malignant progression. Cancer Metastasis Rev. 22, 271-286.
    • (2003) Cancer Metastasis Rev , vol.22 , pp. 271-286
    • Roshy, S.1    Sloane, B.F.2    Moin, K.3
  • 46
    • 77955920079 scopus 로고    scopus 로고
    • Targeting MMP-9, uPAR, and cathepsin B inhibits invasion, migration and activates apoptosis in prostate cancer cells
    • Nalla, A. K., Gorantla, B., Gondi, C. S., Lakka, S. S., and Rao, J. S. (2010) Targeting MMP-9, uPAR, and cathepsin B inhibits invasion, migration and activates apoptosis in prostate cancer cells. Cancer Gene Ther. 17, 599-613.
    • (2010) Cancer Gene Ther. , vol.17 , pp. 599-613
    • Nalla, A.K.1    Gorantla, B.2    Gondi, C.S.3    Lakka, S.S.4    Rao, J.S.5
  • 48
    • 84880853645 scopus 로고    scopus 로고
    • Investigating mechanisms of alkalinization for reducing primary breast tumor invasion
    • Robey, I. F., and Nesbit, L. A. (2013) Investigating mechanisms of alkalinization for reducing primary breast tumor invasion. Biomed. Res. Int. 2013, 485196.
    • (2013) Biomed. Res. Int. 2013 , pp. 485196
    • Robey, I.F.1    Nesbit, L.A.2
  • 49
    • 0032855505 scopus 로고    scopus 로고
    • +-ATPase and microfilaments during osteoclast activation
    • +-ATPase and microfilaments during osteoclast activation. J. Biol. Chem. 274, 29164-29171.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29164-29171
    • Lee, B.S.1    Gluck, S.L.2    Holliday, L.S.3
  • 54
    • 84898644325 scopus 로고    scopus 로고
    • Atp6v1c1 may regulate filament actin arrangement in breast cancer cells
    • Cai, M., Liu, P., Wei, L., Wang, J., Qi, J., Feng, S., and Deng, L. (2014) Atp6v1c1 may regulate filament actin arrangement in breast cancer cells. PLoS One 9, e84833.
    • (2014) PLoS One , vol.9 , pp. e84833
    • Cai, M.1    Liu, P.2    Wei, L.3    Wang, J.4    Qi, J.5    Feng, S.6    Deng, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.