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Volumn 8, Issue 7, 2013, Pages

The Bacterial Protein Azurin Impairs Invasion and FAK/Src Signaling in P-Cadherin-Overexpressing Breast Cancer Cell Models

Author keywords

[No Author keywords available]

Indexed keywords

AZURIN; CADHERIN; FOCAL ADHESION KINASE; GELATINASE A; P CADHERIN; PROTEIN TYROSINE KINASE; UVOMORULIN;

EID: 84880423678     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0069023     Document Type: Article
Times cited : (29)

References (30)
  • 1
    • 77950931419 scopus 로고    scopus 로고
    • Matrix Metalloproteinases: Regulators of the Tumor Microenvironment
    • doi: 10.1016/j.cell.2010.03.015
    • Kessenbrock K, Plaks V, Werb Z, (2010) Matrix Metalloproteinases: Regulators of the Tumor Microenvironment. Cell 141: 52-67 doi:10.1016/j.cell.2010.03.015.
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 2
    • 67651085772 scopus 로고    scopus 로고
    • Signal transduction by focal adhesion kinase in cancer
    • doi: 10.1007/s10555-008-9165-4
    • Zhao J, Guan J-L, (2009) Signal transduction by focal adhesion kinase in cancer. Cancer metastasis reviews 28: 35-49 doi:-10.1007/s10555-008-9165-4.
    • (2009) Cancer Metastasis Reviews , vol.28 , pp. 35-49
    • Zhao, J.1    Guan, J.-L.2
  • 3
    • 84861800037 scopus 로고    scopus 로고
    • Epithelial E- and P-cadherins: role and clinical significance in cancer
    • doi: 10.1016/j.bbcan.2012.05.002
    • Paredes J, Figueiredo J, Albergaria A, Oliveira P, Carvalho J, et al. (2012) Epithelial E- and P-cadherins: role and clinical significance in cancer. Biochimica et biophysica acta 1826: 297-311 doi:10.1016/j.bbcan.2012.05.002.
    • (2012) Biochimica Et Biophysica Acta , vol.1826 , pp. 297-311
    • Paredes, J.1    Figueiredo, J.2    Albergaria, A.3    Oliveira, P.4    Carvalho, J.5
  • 4
    • 23844489449 scopus 로고    scopus 로고
    • P-cadherin overexpression is an indicator of clinical outcome in invasive breast carcinomas and is associated with CDH3 promoter hypomethylation
    • doi: 10.1158/1078-0432.CCR-05-0059
    • Paredes J, Albergaria A, Oliveira JT, Jerónimo C, Milanezi F, et al. (2005) P-cadherin overexpression is an indicator of clinical outcome in invasive breast carcinomas and is associated with CDH3 promoter hypomethylation. Clinical cancer research 11: 5869-5877 doi:--10.1158/1078-0432.CCR-05-0059.
    • (2005) Clinical Cancer Research , vol.11 , pp. 5869-5877
    • Paredes, J.1    Albergaria, A.2    Oliveira, J.T.3    Jerónimo, C.4    Milanezi, F.5
  • 6
    • 75149183984 scopus 로고    scopus 로고
    • Extracellular cleavage and shedding of P-cadherin: a mechanism underlying the invasive behaviour of breast cancer cells
    • doi: 10.1038/onc.2009.338
    • Ribeiro A, Albergaria A, Sousa B, Correia A, Bracke M, et al. (2010) Extracellular cleavage and shedding of P-cadherin: a mechanism underlying the invasive behaviour of breast cancer cells. Oncogene 29: 392-402 doi:10.1038/onc.2009.338.
    • (2010) Oncogene , vol.29 , pp. 392-402
    • Ribeiro, A.1    Albergaria, A.2    Sousa, B.3    Correia, A.4    Bracke, M.5
  • 7
    • 76849100707 scopus 로고    scopus 로고
    • Focal adhesion kinase: a prominent determinant in breast cancer initiation, progression and metastasis
    • doi: 10.1016/j.canlet.2009.07.005
    • Luo M, Guan JL, (2010) Focal adhesion kinase: a prominent determinant in breast cancer initiation, progression and metastasis. Cancer letters 289: 127-139 doi:10.1016/j.canlet.2009.07.005.
    • (2010) Cancer Letters , vol.289 , pp. 127-139
    • Luo, M.1    Guan, J.L.2
  • 8
    • 0033760251 scopus 로고    scopus 로고
    • Secreted products of a nonmucoid Pseudomonas aeruginosa strain induce two modes of macrophage killing: external-ATP- dependent, P2Z-receptor-mediated necrosis apoptosis
    • Zaborina O, Dhiman N, Chen ML, Kostal J, Holder IA, et al. (2000) Secreted products of a nonmucoid Pseudomonas aeruginosa strain induce two modes of macrophage killing: external-ATP- dependent, P2Z-receptor-mediated necrosis apoptosis. Microbiology 146: 2521-2530.
    • (2000) Microbiology , vol.146 , pp. 2521-2530
    • Zaborina, O.1    Dhiman, N.2    Chen, M.L.3    Kostal, J.4    Holder, I.A.5
  • 9
    • 0037195175 scopus 로고    scopus 로고
    • Bacterial redox protein azurin, tumor suppressor protein p53, and regression of cancer
    • doi: 10.1073/pnas.222539699
    • Yamada T, Goto M, Punj V, Zaborina O, Chen ML, et al. (2002) Bacterial redox protein azurin, tumor suppressor protein p53, and regression of cancer. PNAS 99: 14098-14103 doi:10.1073/pnas.222539699.
    • (2002) PNAS , vol.99 , pp. 14098-14103
    • Yamada, T.1    Goto, M.2    Punj, V.3    Zaborina, O.4    Chen, M.L.5
  • 10
    • 1842687879 scopus 로고    scopus 로고
    • Apoptosis or growth arrest: modulation of tumor suppressor p53 specificity by bacterial redox protein azurin, Proc
    • Yamada T, Hiraoka Y, Ikehata M, Kimbara K, Avner BS, et al. (2004) Apoptosis or growth arrest: modulation of tumor suppressor p53 specificity by bacterial redox protein azurin, Proc. PNAS 101: 4770-4775.
    • (2004) PNAS , vol.101 , pp. 4770-4775
    • Yamada, T.1    Hiraoka, Y.2    Ikehata, M.3    Kimbara, K.4    Avner, B.S.5
  • 11
    • 1842484823 scopus 로고    scopus 로고
    • Bacterial cupredoxin azurin as an inducer of apoptosis and regression in human breast cancer
    • Punj V, Bhattacharyya S, Saint-dic D, Vasu C, Cunningham EA, et al. (2004) Bacterial cupredoxin azurin as an inducer of apoptosis and regression in human breast cancer. Oncogene 23: 2367-2378.
    • (2004) Oncogene , vol.23 , pp. 2367-2378
    • Punj, V.1    Bhattacharyya, S.2    Saint-dic, D.3    Vasu, C.4    Cunningham, E.A.5
  • 12
    • 25144449123 scopus 로고    scopus 로고
    • Internalization of bacterial redox protein azurin in mammalian cells: entry domain and specificity
    • doi: 10.1111/j.1462-5822.2005.00567.x
    • Yamada T, Fialho AM, Punj V, Bratescu L, Gupta TK Das, et al. (2005) Internalization of bacterial redox protein azurin in mammalian cells: entry domain and specificity. Cellular microbiology 7: 1418-1431 doi:-10.1111/j.1462-5822.2005.00567.x.
    • (2005) Cellular Microbiology , vol.7 , pp. 1418-1431
    • Yamada, T.1    Fialho, A.M.2    Punj, V.3    Bratescu, L.4    Gupta, T.K.D.5
  • 13
    • 58349113855 scopus 로고    scopus 로고
    • Noncationic peptides obtained from azurin preferentially enter cancer cells
    • doi: 10.1158/0008-5472.CAN-08-2932
    • Taylor BN, Mehta RR, Yamada T, Lekmine F, Christov K, et al. (2009) Noncationic peptides obtained from azurin preferentially enter cancer cells. Cancer research 69: 537-546 doi:--10.1158/0008-5472.CAN-08-2932.
    • (2009) Cancer Research , vol.69 , pp. 537-546
    • Taylor, B.N.1    Mehta, R.R.2    Yamada, T.3    Lekmine, F.4    Christov, K.5
  • 14
    • 70350236724 scopus 로고    scopus 로고
    • A peptide fragment of azurin induces a p53-mediated cell cycle arrest in human breast cancer cells
    • doi: 10.1158/1535-7163.MCT-09-0444
    • Yamada T, Mehta RR, Lekmine F, Christov K, King ML, et al. (2009) A peptide fragment of azurin induces a p53-mediated cell cycle arrest in human breast cancer cells. Molecular cancer therapeutics 8: 2947-2958 doi:--10.1158/1535-7163.MCT-09-0444.
    • (2009) Molecular Cancer Therapeutics , vol.8 , pp. 2947-2958
    • Yamada, T.1    Mehta, R.R.2    Lekmine, F.3    Christov, K.4    King, M.L.5
  • 15
    • 20444410796 scopus 로고    scopus 로고
    • Unique complex between bacterial azurin and tumor-suppressor protein p53
    • doi: 10.1016/j.bbrc.2005.05.038
    • Apiyo D, Wittung-Stafshede P, (2005) Unique complex between bacterial azurin and tumor-suppressor protein p53. Biochemical and Biophysical Research Communications 332: 965-968 doi:10.1016/j.bbrc.2005.05.038.
    • (2005) Biochemical and Biophysical Research Communications , vol.332 , pp. 965-968
    • Apiyo, D.1    Wittung-Stafshede, P.2
  • 16
    • 33847043161 scopus 로고    scopus 로고
    • Cupredoxin-cancer interrelationship: azurin binding with EphB2, interference in EphB2 tyrosine phosphorylation, and inhibition of cancer growth
    • doi: 10.1021/bi061661x
    • Chaudhari A, Mahfouz M, Fialho AM, Yamada T, Granja AT, et al. (2007) Cupredoxin-cancer interrelationship: azurin binding with EphB2, interference in EphB2 tyrosine phosphorylation, and inhibition of cancer growth. Biochemistry 46: 1799-1810 doi:10.1021/bi061661x.
    • (2007) Biochemistry , vol.46 , pp. 1799-1810
    • Chaudhari, A.1    Mahfouz, M.2    Fialho, A.M.3    Yamada, T.4    Granja, A.T.5
  • 17
    • 80052722389 scopus 로고    scopus 로고
    • A cell penetrating peptide derived from azurin inhibits angiogenesis and tumor growth by inhibiting phosphorylation of VEGFR-2, FAK and Akt
    • doi: 10.1007/s10456-011-9220-6
    • Mehta RR, Yamada T, Taylor BN, Christov K, King ML, et al. (2011) A cell penetrating peptide derived from azurin inhibits angiogenesis and tumor growth by inhibiting phosphorylation of VEGFR-2, FAK and Akt. Angiogenesis 14: 355-369 doi:---10.1007/s10456-011-9220-6.
    • (2011) Angiogenesis , vol.14 , pp. 355-369
    • Mehta, R.R.1    Yamada, T.2    Taylor, B.N.3    Christov, K.4    King, M.L.5
  • 18
    • 0025848088 scopus 로고
    • Retinoic acid modulates both invasion and plasma membrane ruffling of MCF-7 human mammary carcinoma cells in vitro
    • Bracke ME, Van Larebeke N, Vyncke BM, Mareel MM, (1991) Retinoic acid modulates both invasion and plasma membrane ruffling of MCF-7 human mammary carcinoma cells in vitro. British journal of cancer 63: 867-872.
    • (1991) British Journal of Cancer , vol.63 , pp. 867-872
    • Bracke, M.E.1    Van Larebeke, N.2    Vyncke, B.M.3    Mareel, M.M.4
  • 19
    • 33845978786 scopus 로고    scopus 로고
    • Autocrine and juxtacrine effects of amphiregulin on the proliferative, invasive, and migratory properties of normal and neoplastic human mammary epithelial cells
    • doi: 10.1074/jbc.M606532200
    • Willmarth NE, Ethier SP, (2006) Autocrine and juxtacrine effects of amphiregulin on the proliferative, invasive, and migratory properties of normal and neoplastic human mammary epithelial cells. The Journal of biological chemistry 281: 37728-37737 doi:10.1074/jbc.M606532200.
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 37728-37737
    • Willmarth, N.E.1    Ethier, S.P.2
  • 20
    • 8544229187 scopus 로고    scopus 로고
    • P-cadherin is up-regulated by the antiestrogen ICI 182,780 and promotes invasion of human breast cancer cells
    • doi: 10.1158/0008-5472.CAN-04-0795
    • Paredes J, Stove C, Stove V, Milanezi F, Van Marck V, et al. (2004) P-cadherin is up-regulated by the antiestrogen ICI 182,780 and promotes invasion of human breast cancer cells. Cancer research 64: 8309-8317 doi:--10.1158/0008-5472.CAN-04-0795.
    • (2004) Cancer Research , vol.64 , pp. 8309-8317
    • Paredes, J.1    Stove, C.2    Stove, V.3    Milanezi, F.4    Van Marck, V.5
  • 21
    • 25644451938 scopus 로고    scopus 로고
    • P-cadherin promotes cell-cell adhesion and counteracts invasion in human melanoma
    • doi: 10.1158/0008-5472.CAN-04-4414
    • Van Marck V, Stove C, Van Den Bossche K, Stove V, Paredes J, et al. (2005) P-cadherin promotes cell-cell adhesion and counteracts invasion in human melanoma. Cancer research 65: 8774-8783 doi:--10.1158/0008-5472.CAN-04-4414.
    • (2005) Cancer Research , vol.65 , pp. 8774-8783
    • Van Marck, V.1    Stove, C.2    Van Den Bossche, K.3    Stove, V.4    Paredes, J.5
  • 22
    • 84875054847 scopus 로고    scopus 로고
    • Ribeiro AS, Sousa B, Carreto L, Mendes N, Nobre AR, et al. (2012) P-cadherin functional role is dependent on E-cadherin cellular context: a proof of concept using the breast cancer model. The Journal of pathology. doi:10.1002/path.4143
    • Ribeiro AS, Sousa B, Carreto L, Mendes N, Nobre AR, et al. (2012) P-cadherin functional role is dependent on E-cadherin cellular context: a proof of concept using the breast cancer model. The Journal of pathology. doi:10.1002/path.4143.
  • 24
  • 25
    • 55449113706 scopus 로고    scopus 로고
    • Increased shedding of soluble fragments of P-cadherin in nipple aspirate fluids from women with breast cancer
    • doi: 10.1111/j.1349-7006.2008.00921.x
    • Mannello F, Tonti GA, Medda V, Pederzoli A, Sauter ER, (2008) Increased shedding of soluble fragments of P-cadherin in nipple aspirate fluids from women with breast cancer. Cancer science 99: 2160-2169 doi:-10.1111/j.1349-7006.2008.00921.x.
    • (2008) Cancer Science , vol.99 , pp. 2160-2169
    • Mannello, F.1    Tonti, G.A.2    Medda, V.3    Pederzoli, A.4    Sauter, E.R.5
  • 26
    • 82255186386 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumorigenesis: an evolving paradigm
    • doi: 10.1007/s00018-011-0763-x
    • Hua H, Li M, Luo T, Yin Y, Jiang Y, (2011) Matrix metalloproteinases in tumorigenesis: an evolving paradigm. Cellular and molecular life sciences: CMLS 68: 3853-3868 doi:--10.1007/s00018-011-0763-x.
    • (2011) Cellular and Molecular Life Sciences: CMLS , vol.68 , pp. 3853-3868
    • Hua, H.1    Li, M.2    Luo, T.3    Yin, Y.4    Jiang, Y.5
  • 27
    • 0032031062 scopus 로고    scopus 로고
    • Both Focal Adhesion Kinase and c-Ras Are Required for the Enhanced Matrix Metalloproteinase 9 Secretion by Fibronectin in Ovarian Cancer Cells Advances in Brief Both Focal Adhesion Kinase and c-Ras Are Required for the Enhanced Matrix Metalloproteinase 9
    • Shibata K, Kikkawa F, Nawa A, Thant AA, Naruse K, et al. (1998) Both Focal Adhesion Kinase and c-Ras Are Required for the Enhanced Matrix Metalloproteinase 9 Secretion by Fibronectin in Ovarian Cancer Cells Advances in Brief Both Focal Adhesion Kinase and c-Ras Are Required for the Enhanced Matrix Metalloproteinase 9. Cancer research 58: 900-903.
    • (1998) Cancer Research , vol.58 , pp. 900-903
    • Shibata, K.1    Kikkawa, F.2    Nawa, A.3    Thant, A.A.4    Naruse, K.5
  • 29
    • 75749103348 scopus 로고    scopus 로고
    • Src signaling in cancer invasion
    • doi: 10.1002/jcp.22011
    • Guarino M, (2010) Src signaling in cancer invasion. Journal of cellular physiology 223: 14-26 doi:10.1002/jcp.22011.
    • (2010) Journal of Cellular Physiology , vol.223 , pp. 14-26
    • Guarino, M.1


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