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Volumn 39, Issue 4, 2016, Pages 353-363

TNF-α promotes breast cancer cell migration and enhances the concentration of membrane-associated proteases in lipid rafts

Author keywords

DPPIV CD26; DRM; FAP F19 seprase; MMP2; MMP9; MT1 MMP MMP14; TNF

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; DIPEPTIDYL PEPTIDASE IV; GELATIN; GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE 14; MITOGEN ACTIVATED PROTEIN KINASE; SEPRASE; TUMOR NECROSIS FACTOR ALPHA; PEPTIDE HYDROLASE; TUMOR NECROSIS FACTOR;

EID: 84962163395     PISSN: 22113428     EISSN: 22113436     Source Type: Journal    
DOI: 10.1007/s13402-016-0280-x     Document Type: Article
Times cited : (92)

References (43)
  • 1
    • 84555179609 scopus 로고    scopus 로고
    • Extracellular matrix degradation and remodeling in development and disease
    • PID: 21917992
    • P. Lu, K. Takai, V. M. Weaver, Z. Werb, Extracellular matrix degradation and remodeling in development and disease. Cold Spring Harb. Perspect. Biol. 3, a005058 (2011)
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. a005058
    • Lu, P.1    Takai, K.2    Weaver, V.M.3    Werb, Z.4
  • 2
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: innovations for the post-trial era
    • COI: 1:CAS:528:DC%2BD38Xmslamsro%3D, PID: 12209155
    • C. M. Overall, C. López-Otín, Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat. Rev. Cancer 2, 657–672 (2002)
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    López-Otín, C.2
  • 3
    • 0028280991 scopus 로고
    • Expression of tumour necrosis factor (TNF-α) and its receptors in benign and malignant breast tissue
    • COI: 1:STN:280:DyaK2c7msVOgsg%3D%3D, PID: 8119765
    • D. W. Miles, L. C. Happerfield, M. S. Naylor, L. G. Bobrow, R. D. Rubens, F. R. Balkwill, Expression of tumour necrosis factor (TNF-α) and its receptors in benign and malignant breast tissue. Int. J. Cancer 56, 777–782 (1994)
    • (1994) Int. J. Cancer , vol.56 , pp. 777-782
    • Miles, D.W.1    Happerfield, L.C.2    Naylor, M.S.3    Bobrow, L.G.4    Rubens, R.D.5    Balkwill, F.R.6
  • 4
    • 0141990957 scopus 로고    scopus 로고
    • TNF-alpha increases human melanoma cell invasion and migration in vitro: the role of proteolytic enzymes
    • COI: 1:CAS:528:DC%2BD3sXntVKnsrs%3D, PID: 12966436
    • E. Katerinaki, G. S. Evans, P. C. Lorigan, S. MacNeil, TNF-alpha increases human melanoma cell invasion and migration in vitro: the role of proteolytic enzymes. Br. J. Cancer 89, 1123–1129 (2003)
    • (2003) Br. J. Cancer , vol.89 , pp. 1123-1129
    • Katerinaki, E.1    Evans, G.S.2    Lorigan, P.C.3    MacNeil, S.4
  • 5
    • 0028064723 scopus 로고
    • Modulation of proteases and their inhibitors in immortal human osteoblast-like cells by tumor necrosis factor-alpha in vitro
    • COI: 1:CAS:528:DyaK2cXlsFGgurY%3D, PID: 8088923
    • F. S. Panagakos, S. Kumar, Modulation of proteases and their inhibitors in immortal human osteoblast-like cells by tumor necrosis factor-alpha in vitro. Inflammation 18, 243–265 (1994)
    • (1994) Inflammation , vol.18 , pp. 243-265
    • Panagakos, F.S.1    Kumar, S.2
  • 6
    • 84877783846 scopus 로고    scopus 로고
    • Tumour necrosis factor and cancer
    • COI: 1:CAS:528:DC%2BC3sXpt1elsbc%3D, PID: 23460481
    • J. P. Waters, J. S. Pober, J. R. Bradley, Tumour necrosis factor and cancer. J. Pathol. 230, 241–248 (2013)
    • (2013) J. Pathol. , vol.230 , pp. 241-248
    • Waters, J.P.1    Pober, J.S.2    Bradley, J.R.3
  • 7
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • COI: 1:CAS:528:DC%2BD38Xis1KktL8%3D, PID: 11990853
    • M. Egeblad, Z. Werb, New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2, 161–174 (2002)
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 8
    • 19344366798 scopus 로고    scopus 로고
    • Gelatinase-mediated migration and invasion of cancer cells
    • PID: 15907591
    • M. Björklund, E. Koivunen, Gelatinase-mediated migration and invasion of cancer cells. Biochim. Biophys. Acta 1755, 37–69 (2005)
    • (2005) Biochim. Biophys. Acta , vol.1755 , pp. 37-69
    • Björklund, M.1    Koivunen, E.2
  • 9
    • 84938555944 scopus 로고    scopus 로고
    • S. Shahrabi, M. Shahjahani, N. Saki, The bone marrow metastasis niche in retinoblastoma
    • COI: 1:CAS:528:DC%2BC2MXhtVKlsrrL
    • A. Khosravi, S. Shahrabi, M. Shahjahani, N. Saki, The bone marrow metastasis niche in retinoblastoma. Cell. Oncol. 38, 253–263 (2015)
    • (2015) Cell. Oncol. , vol.38 , pp. 253-263
    • Khosravi, A.1
  • 10
    • 33749535260 scopus 로고    scopus 로고
    • MT1-MMP: a key regulator of cell migration in tissue
    • COI: 1:CAS:528:DC%2BD28XhtlGqsLfM, PID: 17050376
    • Y. Itoh, MT1-MMP: a key regulator of cell migration in tissue. IUBMB Life 58, 589–596 (2006)
    • (2006) IUBMB Life , vol.58 , pp. 589-596
    • Itoh, Y.1
  • 12
    • 0041592501 scopus 로고    scopus 로고
    • R Fridman, Pro-MMP-9 activation by the MT1-MMP/MMP-2 axis and MMP-3: role of TIMP-2 and plasma membranes
    • COI: 1:CAS:528:DC%2BD3sXlvFGgsr8%3D, PID: 12901881
    • M. Toth, I. Chvyrkova, M. M. Bernardo, S. Hernandez-Barrantes, R Fridman, Pro-MMP-9 activation by the MT1-MMP/MMP-2 axis and MMP-3: role of TIMP-2 and plasma membranes. Biochem. Biophys. Res. Commun. 308, 386–395 (2003)
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 386-395
    • Toth, M.1    Chvyrkova, I.2    Bernardo, M.M.3    Hernandez-Barrantes, S.4
  • 14
    • 0038702525 scopus 로고    scopus 로고
    • Seprase complexes in cellular invasiveness
    • PID: 12785000
    • W. T. Chen, T. Kelly, Seprase complexes in cellular invasiveness. Cancer Metastasis Rev. 22, 259–269 (2003)
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 259-269
    • Chen, W.T.1    Kelly, T.2
  • 15
    • 53149100519 scopus 로고    scopus 로고
    • Seprase: an overview of an important matrix serine protease
    • PID: 18262497
    • P. O'Brien, B. F. O'Connor, Seprase: an overview of an important matrix serine protease. Biochim. Biophys. Acta 1784, 1130–1145 (2008)
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1130-1145
    • O'Brien, P.1    O'Connor, B.F.2
  • 16
    • 41549161073 scopus 로고    scopus 로고
    • Assembly and biological role of podosomes and invadopodia
    • COI: 1:CAS:528:DC%2BD1cXks1Gnu7k%3D, PID: 18337078
    • M. Gimona, R. Buccione, S. A. Courtneidge, S. Linder, Assembly and biological role of podosomes and invadopodia. Curr. Opin. Cell Biol. 20, 235–241 (2008)
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 235-241
    • Gimona, M.1    Buccione, R.2    Courtneidge, S.A.3    Linder, S.4
  • 17
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • COI: 1:CAS:528:DC%2BD3MXivVGjtbo%3D, PID: 11413487
    • K. Simons, D. Toomre, Lipid rafts and signal transduction. Nat. Rev. Mol. Cell Biol. 1, 31–39 (2000)
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 19
    • 84872973963 scopus 로고    scopus 로고
    • Membrane domains and the "lipid raft" concept
    • COI: 1:CAS:528:DC%2BC3sXjvFOms70%3D, PID: 23150999
    • S. Sonnino, A. Prinetti, Membrane domains and the "lipid raft" concept. Curr. Med. Chem. 20, 4–21 (2013)
    • (2013) Curr. Med. Chem. , vol.20 , pp. 4-21
    • Sonnino, S.1    Prinetti, A.2
  • 20
    • 41949099869 scopus 로고    scopus 로고
    • Dissecting lipid raft facilitated cell signaling pathways in cancer
    • COI: 1:CAS:528:DC%2BD1cXkvFWlur8%3D, PID: 18166162
    • S. K. Patra, Dissecting lipid raft facilitated cell signaling pathways in cancer. Biochim. Biophys. Acta 1785, 182–206 (2008)
    • (2008) Biochim. Biophys. Acta , vol.1785 , pp. 182-206
    • Patra, S.K.1
  • 21
    • 72249116890 scopus 로고    scopus 로고
    • Lipid rafts and caveolin-1 are required for invadopodia formation and extracellular matrix degradation by human breast cancer cells
    • COI: 1:CAS:528:DC%2BD1MXhtl2rsbbJ, PID: 19887621
    • H. Yamaguchi, Y. Takeo, S. Yoshida, Z. Kouchi, Y. Nakamura, et al., Lipid rafts and caveolin-1 are required for invadopodia formation and extracellular matrix degradation by human breast cancer cells. Cancer Res. 69, 8594–8602 (2009)
    • (2009) Cancer Res. , vol.69 , pp. 8594-8602
    • Yamaguchi, H.1    Takeo, Y.2    Yoshida, S.3    Kouchi, Z.4    Nakamura, Y.5
  • 22
    • 84867399470 scopus 로고    scopus 로고
    • Pathological roles of invadopodia in cancer invasion and metastasis
    • COI: 1:CAS:528:DC%2BC38XotVehurY%3D, PID: 22658792
    • H. Yamaguchi, Pathological roles of invadopodia in cancer invasion and metastasis. Eur. J. Cell Biol. 91, 902–907 (2012)
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 902-907
    • Yamaguchi, H.1
  • 23
    • 84892178225 scopus 로고    scopus 로고
    • Interaction of membrane/lipid rafts with the cytoskeleton: impact on signaling and function: membrane/lipid rafts, mediators of cytoskeletal arrangement and cell signaling
    • COI: 1:CAS:528:DC%2BC3sXitVWntr%2FJ, PID: 23899502
    • B. P. Head, H. H. Patel, P. A. Insel, Interaction of membrane/lipid rafts with the cytoskeleton: impact on signaling and function: membrane/lipid rafts, mediators of cytoskeletal arrangement and cell signaling. Biochim. Biophys. Acta 1838, 532–545 (2014)
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 532-545
    • Head, B.P.1    Patel, H.H.2    Insel, P.A.3
  • 24
    • 76949084622 scopus 로고    scopus 로고
    • TNF-alpha/NF-kappaB/Snail pathway in cancer cell migration and invasion
    • COI: 1:CAS:528:DC%2BC3cXitVWgtLo%3D, PID: 20087353
    • Y. Wu, B. P. Zhou, TNF-alpha/NF-kappaB/Snail pathway in cancer cell migration and invasion. Br. J. Cancer 102, 639–644 (2010)
    • (2010) Br. J. Cancer , vol.102 , pp. 639-644
    • Wu, Y.1    Zhou, B.P.2
  • 25
    • 33144484539 scopus 로고    scopus 로고
    • TNFalpha increases in vitro migration of human HPV18-positive SW756 cervical carcinoma cells
    • COI: 1:CAS:528:DC%2BD28Xjt1Giu74%3D, PID: 16524252
    • K. Hidalgo, I. G. Rojas, A. B. Penissi, M. I. Rudolph, TNFalpha increases in vitro migration of human HPV18-positive SW756 cervical carcinoma cells. Biocell 29, 303–311 (2005)
    • (2005) Biocell , vol.29 , pp. 303-311
    • Hidalgo, K.1    Rojas, I.G.2    Penissi, A.B.3    Rudolph, M.I.4
  • 26
    • 30644479827 scopus 로고    scopus 로고
    • Modulation of autocrine TNF-alpha-stimulated matrix metalloproteinase 9 (MMP-9) expression by mitogen-activated protein kinases in THP-1 monocytic cells
    • COI: 1:CAS:528:DC%2BD28XhsVKjt70%3D, PID: 16497166
    • M. Heidinger, H. Kolb, H. W. Krell, M. Jochum, C. Ries, Modulation of autocrine TNF-alpha-stimulated matrix metalloproteinase 9 (MMP-9) expression by mitogen-activated protein kinases in THP-1 monocytic cells. Biol. Chem. 387, 69–78 (2006)
    • (2006) Biol. Chem. , vol.387 , pp. 69-78
    • Heidinger, M.1    Kolb, H.2    Krell, H.W.3    Jochum, M.4    Ries, C.5
  • 27
    • 78649264325 scopus 로고    scopus 로고
    • Cordycepin suppresses TNF-alpha-induced invasion, migration and matrix metalloproteinase-9 expression in human bladder cancer cells
    • COI: 1:CAS:528:DC%2BC3MXltlegug%3D%3D, PID: 20564512
    • E. J. Lee, W. J. Kim, S. K. Moon, Cordycepin suppresses TNF-alpha-induced invasion, migration and matrix metalloproteinase-9 expression in human bladder cancer cells. Phytother. Res. 24, 1755–1761 (2010)
    • (2010) Phytother. Res. , vol.24 , pp. 1755-1761
    • Lee, E.J.1    Kim, W.J.2    Moon, S.K.3
  • 28
    • 0036178923 scopus 로고    scopus 로고
    • Chemokine stimulation of monocyte matrix metalloproteinase-9 requires endogenous TNF-alpha
    • COI: 1:CAS:528:DC%2BD38XhvVeht7w%3D, PID: 11813159
    • S. C. Robinson, K. A. Scott, F. R. Balkwill, Chemokine stimulation of monocyte matrix metalloproteinase-9 requires endogenous TNF-alpha. Eur. J. Immunol. 32, 404–412 (2002)
    • (2002) Eur. J. Immunol. , vol.32 , pp. 404-412
    • Robinson, S.C.1    Scott, K.A.2    Balkwill, F.R.3
  • 29
    • 3342904989 scopus 로고    scopus 로고
    • Enhanced invasiveness of breast cancer cell lines upon co-cultivation with macrophages is due to TNF-alpha dependent up-regulation of matrix metalloproteases
    • COI: 1:CAS:528:DC%2BD2cXmtF2ntrk%3D, PID: 15044327
    • T. Hagemann, S. C. Robinson, M. Schulz, L. Trümper, F. R. Balkwill, C. Binder, Enhanced invasiveness of breast cancer cell lines upon co-cultivation with macrophages is due to TNF-alpha dependent up-regulation of matrix metalloproteases. Carcinogenesis 25, 1543–1549 (2004)
    • (2004) Carcinogenesis , vol.25 , pp. 1543-1549
    • Hagemann, T.1    Robinson, S.C.2    Schulz, M.3    Trümper, L.4    Balkwill, F.R.5    Binder, C.6
  • 30
    • 78549269153 scopus 로고    scopus 로고
    • Localization of uPAR and MMP-9 in lipid rafts is critical for migration, invasion and angiogenesis in human breast cancer cells
    • H. Raghu, P. K. Sodadasu, R. R. Malla, C. S. Gondi, N. Estes, J. S. Rao, Localization of uPAR and MMP-9 in lipid rafts is critical for migration, invasion and angiogenesis in human breast cancer cells. BMC Cancer 24, 10–647 (2010)
    • (2010) BMC Cancer , vol.24 , pp. 10-647
    • Raghu, H.1    Sodadasu, P.K.2    Malla, R.R.3    Gondi, C.S.4    Estes, N.5    Rao, J.S.6
  • 31
    • 0042424548 scopus 로고    scopus 로고
    • Activated integrin alphavbeta3 cooperates with metalloproteinase MMP-9 in regulating migration of metastatic breast cancer cells
    • COI: 1:CAS:528:DC%2BD3sXmtlykurs%3D, PID: 12874388
    • M. Rolli, E. Fransvea, J. Pilch, A. Saven, B. Felding-Habermann, Activated integrin alphavbeta3 cooperates with metalloproteinase MMP-9 in regulating migration of metastatic breast cancer cells. Proc. Natl. Acad. Sci. U. S. A. 100, 9482–9487 (2003)
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9482-9487
    • Rolli, M.1    Fransvea, E.2    Pilch, J.3    Saven, A.4    Felding-Habermann, B.5
  • 32
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • COI: 1:CAS:528:DyaK1MXnvF2gtg%3D%3D, PID: 9887098
    • Q. Yu, I. Stamenkovic, Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev. 13, 35–48 (1999)
    • (1999) Genes Dev. , vol.13 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2
  • 33
    • 58149266689 scopus 로고    scopus 로고
    • The hemopexin domain of matrix metalloproteinase-9 activates cell signaling and promotes migration of schwann cells by binding to low-density lipoprotein receptor-related protein
    • COI: 1:CAS:528:DC%2BD1cXhtlOgt77E, PID: 18987193
    • E. Mantuano, G. Inoue, X. Li, K. Takahashi, A. Gaultier, S. L. Gonias, W. M. Campana, The hemopexin domain of matrix metalloproteinase-9 activates cell signaling and promotes migration of schwann cells by binding to low-density lipoprotein receptor-related protein. J. Neurosci. 28, 11571–11582 (2008)
    • (2008) J. Neurosci. , vol.28 , pp. 11571-11582
    • Mantuano, E.1    Inoue, G.2    Li, X.3    Takahashi, K.4    Gaultier, A.5    Gonias, S.L.6    Campana, W.M.7
  • 34
    • 84884935919 scopus 로고    scopus 로고
    • Lipid rafts control human melanoma cell migration by regulating focal adhesion disassembly
    • COI: 1:CAS:528:DC%2BC3sXhvVWgtL3F, PID: 24055995
    • R. Wang, J. Bi, K. K. Ampah, X. Ba, W. Liu, X. Zeng, Lipid rafts control human melanoma cell migration by regulating focal adhesion disassembly. Biochim. Biophys. Acta 1833, 3195–3205 (2013)
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 3195-3205
    • Wang, R.1    Bi, J.2    Ampah, K.K.3    Ba, X.4    Liu, W.5    Zeng, X.6
  • 35
    • 79957521262 scopus 로고    scopus 로고
    • Membrane lipids in invadopodia and podosomes: key structures for cancer invasion and metastasis
    • PID: 21307399
    • H. Yamaguchi, T. Oikawa, Membrane lipids in invadopodia and podosomes: key structures for cancer invasion and metastasis. Oncotarget 1, 320–328 (2010)
    • (2010) Oncotarget , vol.1 , pp. 320-328
    • Yamaguchi, H.1    Oikawa, T.2
  • 36
    • 30444432840 scopus 로고    scopus 로고
    • Local proteolytic activity in tumor cell invasion and metastasis
    • COI: 1:CAS:528:DC%2BD2MXht1Olur%2FJ, PID: 16237672
    • T. Ludwig, Local proteolytic activity in tumor cell invasion and metastasis. BioEssays 27, 1181–1191 (2005)
    • (2005) BioEssays , vol.27 , pp. 1181-1191
    • Ludwig, T.1
  • 37
    • 0035252979 scopus 로고    scopus 로고
    • Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains
    • COI: 1:CAS:528:DC%2BD3MXhtlOrsLk%3D, PID: 11171051
    • B. Annabi, M. Lachambre, N. Bousquet-Gagnon, M. Pagé, D. Gingras, R. Béliveau, Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains. Biochem. J. 353, 547–553 (2001)
    • (2001) Biochem. J. , vol.353 , pp. 547-553
    • Annabi, B.1    Lachambre, M.2    Bousquet-Gagnon, N.3    Pagé, M.4    Gingras, D.5    Béliveau, R.6
  • 38
    • 0038279762 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (CD26) activity in the hematopoietic system: differences between the membrane-anchored and the released enzyme activity
    • COI: 1:CAS:528:DC%2BD3sXkvFGmsLc%3D, PID: 12715075
    • D. A. Pereira, L. Gomes, M. C. El-Cheikh, R. Borojevic, Dipeptidyl peptidase IV (CD26) activity in the hematopoietic system: differences between the membrane-anchored and the released enzyme activity. Braz. J. Med. Biol. Res. 36, 567–578 (2003)
    • (2003) Braz. J. Med. Biol. Res. , vol.36 , pp. 567-578
    • Pereira, D.A.1    Gomes, L.2    El-Cheikh, M.C.3    Borojevic, R.4
  • 39
    • 77955501414 scopus 로고    scopus 로고
    • MT1-MMP association with membrane lipid rafts facilitates G-CSF–induced hematopoietic stem/progenitor cell mobilization
    • COI: 1:CAS:528:DC%2BC3cXhtVektLbF, PID: 20471446
    • N. Shirvaikar, L. A. Marquez-Curtis, A. R. Shaw, A. R. Turner, A. Janowska-Wieczorek, MT1-MMP association with membrane lipid rafts facilitates G-CSF–induced hematopoietic stem/progenitor cell mobilization. Exp. Hematol. 38, 823–835 (2010)
    • (2010) Exp. Hematol. , vol.38 , pp. 823-835
    • Shirvaikar, N.1    Marquez-Curtis, L.A.2    Shaw, A.R.3    Turner, A.R.4    Janowska-Wieczorek, A.5
  • 40
    • 0033532205 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion
    • COI: 1:CAS:528:DyaK1MXjtFOlsrw%3D, PID: 10224058
    • N. Ramos-DeSimone, E. Hahn-Dantona, J. Sipley, H. Nagase, D. L. French, J. P. Quigley, Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion. J. Biol. Chem. 274, 13066–13076 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 13066-13076
    • Ramos-DeSimone, N.1    Hahn-Dantona, E.2    Sipley, J.3    Nagase, H.4    French, D.L.5    Quigley, J.P.6
  • 41
    • 84908046785 scopus 로고    scopus 로고
    • WAVE3-NFκB interplay is essential for the survival and invasion of cancer cells
    • PID: 25329315
    • G. Davuluri, K. Augoff, W. P. Schiemann, E. F. Plow, K. Sossey-Alaoui, WAVE3-NFκB interplay is essential for the survival and invasion of cancer cells. PLoS One 9, e110627 (2014)
    • (2014) PLoS One , vol.9
    • Davuluri, G.1    Augoff, K.2    Schiemann, W.P.3    Plow, E.F.4    Sossey-Alaoui, K.5
  • 42
    • 0031873178 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)- and scatter factor/hepatocyte growth factor (SF/HGF)- mediated keratinocyte migration is coincident with induction of matrix metalloproteinase (MMP)-9
    • COI: 1:CAS:528:DyaK1cXktVKrurk%3D, PID: 9648913
    • L. J. McCawley, P. O'Brien, L. G. Hudson, Epidermal growth factor (EGF)- and scatter factor/hepatocyte growth factor (SF/HGF)- mediated keratinocyte migration is coincident with induction of matrix metalloproteinase (MMP)-9. J. Cell. Physiol. 176, 255–265 (1998)
    • (1998) J. Cell. Physiol. , vol.176 , pp. 255-265
    • McCawley, L.J.1    O'Brien, P.2    Hudson, L.G.3
  • 43
    • 4043115618 scopus 로고    scopus 로고
    • Calcium-induced matrix metalloproteinase 9 gene expression is differentially regulated by ERK1/2 and p38 MAPK in oral keratinocytes and oral squamous cell carcinoma
    • COI: 1:CAS:528:DC%2BD2cXmtFOisLo%3D, PID: 15180997
    • S. Mukhopadhyay, H. G. Munshi, S. Kambhampati, A. Sassano, L. C. Platanias, M. S. Stack, Calcium-induced matrix metalloproteinase 9 gene expression is differentially regulated by ERK1/2 and p38 MAPK in oral keratinocytes and oral squamous cell carcinoma. J. Biol. Chem. 279, 33139–33146 (2004)
    • (2004) J. Biol. Chem. , vol.279 , pp. 33139-33146
    • Mukhopadhyay, S.1    Munshi, H.G.2    Kambhampati, S.3    Sassano, A.4    Platanias, L.C.5    Stack, M.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.