메뉴 건너뛰기




Volumn 312, Issue 19, 2006, Pages 3857-3871

ROCK signaling mediates the adoption of different modes of migration and invasion in human mammary epithelial tumor cells

Author keywords

Breast cancer; Invasion; Migration; MMP; ROCK

Indexed keywords

COFILIN; MYOSIN LIGHT CHAIN KINASE; RHO KINASE;

EID: 33750289641     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2006.08.025     Document Type: Article
Times cited : (50)

References (73)
  • 2
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: a physically integrated molecular process
    • Lauffenburger D.A., and Horwitz A.F. Cell migration: a physically integrated molecular process. Cell 84 (1996) 359-369
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 4
    • 8344250882 scopus 로고    scopus 로고
    • Membrane ruffles in cell migration: indicators of inefficient lamellipodia adhesion and compartments of actin filament reorganization
    • Borm B., Requardt R.P., Herzog V., and Kirfel G. Membrane ruffles in cell migration: indicators of inefficient lamellipodia adhesion and compartments of actin filament reorganization. Exp. Cell Res. 302 (2005) 83-95
    • (2005) Exp. Cell Res. , vol.302 , pp. 83-95
    • Borm, B.1    Requardt, R.P.2    Herzog, V.3    Kirfel, G.4
  • 5
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M., and Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat. Rev., Cancer 2 (2002) 161-174
    • (2002) Nat. Rev., Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 6
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood J.D., and Cheresh D.A. Role of integrins in cell invasion and migration. Nat. Rev., Cancer 2 (2002) 91-100
    • (2002) Nat. Rev., Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 7
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes C.D., and Hall A. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144 (1999) 1235-1244
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 10
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou M., and Hall A. Cell migration: Rho GTPases lead the way. Dev. Biol. 265 (2004) 23-32
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 12
    • 0037484137 scopus 로고    scopus 로고
    • Coupling membrane protrusion and cell adhesion
    • DeMali K.A., and Burridge K. Coupling membrane protrusion and cell adhesion. J. Cell Sci. 116 (2003) 2389-2397
    • (2003) J. Cell Sci. , vol.116 , pp. 2389-2397
    • DeMali, K.A.1    Burridge, K.2
  • 13
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge K., and Wennerberg K. Rho and Rac take center stage. Cell 116 (2004) 167-179
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 14
    • 0027227425 scopus 로고
    • Maximal migration of human smooth muscle cells on fibronectin and type IV collagen occurs at an intermediate attachment strength
    • DiMilla P.A., Stone J.A., Quinn J.A., Albelda S.M., and Lauffenburger D.A. Maximal migration of human smooth muscle cells on fibronectin and type IV collagen occurs at an intermediate attachment strength. J. Cell Biol. 122 (1993) 729-737
    • (1993) J. Cell Biol. , vol.122 , pp. 729-737
    • DiMilla, P.A.1    Stone, J.A.2    Quinn, J.A.3    Albelda, S.M.4    Lauffenburger, D.A.5
  • 15
    • 0031976733 scopus 로고    scopus 로고
    • Physical and biochemical regulation of integrin release during rear detachment of migrating cells
    • Palecek S.P., Huttenlocher A., Horwitz A.F., and Lauffenburger D.A. Physical and biochemical regulation of integrin release during rear detachment of migrating cells. J. Cell Sci. 111 Pt. 7 (1998) 929-940
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 7 , pp. 929-940
    • Palecek, S.P.1    Huttenlocher, A.2    Horwitz, A.F.3    Lauffenburger, D.A.4
  • 16
    • 0035152391 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the Rho family of GTPases
    • Cox E.A., Sastry S.K., and Huttenlocher A. Integrin-mediated adhesion regulates cell polarity and membrane protrusion through the Rho family of GTPases. Mol. Biol. Cell 12 (2001) 265-277
    • (2001) Mol. Biol. Cell , vol.12 , pp. 265-277
    • Cox, E.A.1    Sastry, S.K.2    Huttenlocher, A.3
  • 17
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: diversity and escape mechanisms
    • Friedl P., and Wolf K. Tumour-cell invasion and migration: diversity and escape mechanisms. Nat. Rev., Cancer 3 (2003) 362-374
    • (2003) Nat. Rev., Cancer , vol.3 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 19
    • 0042354574 scopus 로고    scopus 로고
    • Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis
    • Sahai E., and Marshall C.J. Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis. Nat. Cell Biol. 5 (2003) 711-719
    • (2003) Nat. Cell Biol. , vol.5 , pp. 711-719
    • Sahai, E.1    Marshall, C.J.2
  • 20
    • 0041695159 scopus 로고    scopus 로고
    • New dimensions in cell migration
    • Webb D.J., and Horwitz A.F. New dimensions in cell migration. Nat. Cell Biol. 5 (2003) 690-692
    • (2003) Nat. Cell Biol. , vol.5 , pp. 690-692
    • Webb, D.J.1    Horwitz, A.F.2
  • 21
    • 0347383715 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their tissue inhibitors direct cell fate during cancer development
    • Hojilla C.V., Mohammed F.F., and Khokha R. Matrix metalloproteinases and their tissue inhibitors direct cell fate during cancer development. Br. J. Cancer 89 (2003) 1817-1821
    • (2003) Br. J. Cancer , vol.89 , pp. 1817-1821
    • Hojilla, C.V.1    Mohammed, F.F.2    Khokha, R.3
  • 22
    • 0033603826 scopus 로고    scopus 로고
    • Quantifying lamella dynamics of cultured cells by SACED, a new computer-assisted motion analysis
    • Hinz B., Alt W., Johnen C., Herzog V., and Kaiser H.W. Quantifying lamella dynamics of cultured cells by SACED, a new computer-assisted motion analysis. Exp. Cell Res. 251 (1999) 234-243
    • (1999) Exp. Cell Res. , vol.251 , pp. 234-243
    • Hinz, B.1    Alt, W.2    Johnen, C.3    Herzog, V.4    Kaiser, H.W.5
  • 24
    • 0021601213 scopus 로고
    • Cytoskeleton of mouse embryo fibroblasts. Electron microscopy of platinum replicas
    • Svitkina T.M., Shevelev A.A., Bershadsky A.D., and Gelfand V.I. Cytoskeleton of mouse embryo fibroblasts. Electron microscopy of platinum replicas. Eur. J. Cell Biol. 34 (1984) 64-74
    • (1984) Eur. J. Cell Biol. , vol.34 , pp. 64-74
    • Svitkina, T.M.1    Shevelev, A.A.2    Bershadsky, A.D.3    Gelfand, V.I.4
  • 26
    • 1342326910 scopus 로고    scopus 로고
    • Relevance of breast cancer cell lines as models for breast tumours: an update
    • Lacroix M., and Leclercq G. Relevance of breast cancer cell lines as models for breast tumours: an update. Breast Cancer Res. Treat. 83 (2004) 249-289
    • (2004) Breast Cancer Res. Treat. , vol.83 , pp. 249-289
    • Lacroix, M.1    Leclercq, G.2
  • 27
    • 0035569896 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) in breast cancer cell lines of different tumorigenicity
    • Bachmeier B.E., Nerlich A.G., Lichtinghagen R., and Sommerhoff C.P. Matrix metalloproteinases (MMPs) in breast cancer cell lines of different tumorigenicity. Anticancer Res. 21 (2001) 3821-3828
    • (2001) Anticancer Res. , vol.21 , pp. 3821-3828
    • Bachmeier, B.E.1    Nerlich, A.G.2    Lichtinghagen, R.3    Sommerhoff, C.P.4
  • 28
    • 0032826846 scopus 로고    scopus 로고
    • Breast cancer cells express cathepsins B and L but not cathepsins K or H
    • Ishibashi O., Mori Y., Kurokawa T., and Kumegawa M. Breast cancer cells express cathepsins B and L but not cathepsins K or H. Cancer Biochem. Biophys. 17 (1999) 69-78
    • (1999) Cancer Biochem. Biophys. , vol.17 , pp. 69-78
    • Ishibashi, O.1    Mori, Y.2    Kurokawa, T.3    Kumegawa, M.4
  • 29
    • 0344845003 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and pathologies
    • Thiery J.P. Epithelial-mesenchymal transitions in development and pathologies. Curr. Opin. Cell Biol. 15 (2003) 740-746
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 740-746
    • Thiery, J.P.1
  • 30
    • 14744304060 scopus 로고    scopus 로고
    • Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion
    • Wilkinson S., Paterson H.F., and Marshall C.J. Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion. Nat. Cell Biol. 7 (2005) 255-261
    • (2005) Nat. Cell Biol. , vol.7 , pp. 255-261
    • Wilkinson, S.1    Paterson, H.F.2    Marshall, C.J.3
  • 32
    • 0034194578 scopus 로고    scopus 로고
    • A critical step in metastasis: in vivo analysis of intravasation at the primary tumor
    • Wyckoff J.B., Jones J.G., Condeelis J.S., and Segall J.E. A critical step in metastasis: in vivo analysis of intravasation at the primary tumor. Cancer Res. 60 (2000) 2504-2511
    • (2000) Cancer Res. , vol.60 , pp. 2504-2511
    • Wyckoff, J.B.1    Jones, J.G.2    Condeelis, J.S.3    Segall, J.E.4
  • 33
    • 0032935495 scopus 로고    scopus 로고
    • An essential part for Rho-associated kinase in the transcellular invasion of tumor cells
    • Itoh K., Yoshioka K., Akedo H., Uehata M., Ishizaki T., and Narumiya S. An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nat. Med. 5 (1999) 221-225
    • (1999) Nat. Med. , vol.5 , pp. 221-225
    • Itoh, K.1    Yoshioka, K.2    Akedo, H.3    Uehata, M.4    Ishizaki, T.5    Narumiya, S.6
  • 34
    • 0035123728 scopus 로고    scopus 로고
    • Inhibition of intrahepatic metastasis of human hepatocellular carcinoma by Rho-associated protein kinase inhibitor Y-27632
    • Takamura M., Sakamoto M., Genda T., Ichida T., Asakura H., and Hirohashi S. Inhibition of intrahepatic metastasis of human hepatocellular carcinoma by Rho-associated protein kinase inhibitor Y-27632. Hepatology 33 (2001) 577-581
    • (2001) Hepatology , vol.33 , pp. 577-581
    • Takamura, M.1    Sakamoto, M.2    Genda, T.3    Ichida, T.4    Asakura, H.5    Hirohashi, S.6
  • 35
    • 0031459917 scopus 로고    scopus 로고
    • Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K
    • Keely P.J., Westwick J.K., Whitehead I.P., Der C.J., and Parise L.V. Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(3)K. Nature 390 (1997) 632-636
    • (1997) Nature , vol.390 , pp. 632-636
    • Keely, P.J.1    Westwick, J.K.2    Whitehead, I.P.3    Der, C.J.4    Parise, L.V.5
  • 36
    • 0036599583 scopus 로고    scopus 로고
    • Reversion of RhoC GTPase-induced inflammatory breast cancer phenotype by treatment with a farnesyl transferase inhibitor
    • van Golen K.L., Bao L., DiVito M.M., Wu Z., Prendergast G.C., and Merajver S.D. Reversion of RhoC GTPase-induced inflammatory breast cancer phenotype by treatment with a farnesyl transferase inhibitor. Mol. Cancer Ther. 1 (2002) 575-583
    • (2002) Mol. Cancer Ther. , vol.1 , pp. 575-583
    • van Golen, K.L.1    Bao, L.2    DiVito, M.M.3    Wu, Z.4    Prendergast, G.C.5    Merajver, S.D.6
  • 37
    • 0141482096 scopus 로고    scopus 로고
    • p38 kinase is a key signaling molecule for H-Ras-induced cell motility and invasive phenotype in human breast epithelial cells
    • Kim M.S., Lee E.J., Kim H.R., and Moon A. p38 kinase is a key signaling molecule for H-Ras-induced cell motility and invasive phenotype in human breast epithelial cells. Cancer Res. 63 (2003) 5454-5461
    • (2003) Cancer Res. , vol.63 , pp. 5454-5461
    • Kim, M.S.1    Lee, E.J.2    Kim, H.R.3    Moon, A.4
  • 38
    • 0037072731 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells
    • Chen B.H., Tzen J.T., Bresnick A.R., and Chen H.C. Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells. J. Biol. Chem. 277 (2002) 33857-33863
    • (2002) J. Biol. Chem. , vol.277 , pp. 33857-33863
    • Chen, B.H.1    Tzen, J.T.2    Bresnick, A.R.3    Chen, H.C.4
  • 39
    • 12544252253 scopus 로고    scopus 로고
    • The COOH-terminal end of R-Ras alters the motility and morphology of breast epithelial cells through Rho/Rho-kinase
    • Jeong H.W., Nam J.O., and Kim I.S. The COOH-terminal end of R-Ras alters the motility and morphology of breast epithelial cells through Rho/Rho-kinase. Cancer Res. 65 (2005) 507-515
    • (2005) Cancer Res. , vol.65 , pp. 507-515
    • Jeong, H.W.1    Nam, J.O.2    Kim, I.S.3
  • 40
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo K.A., Dembo M., Kaverina I., Small J.V., and Wang Y.L. Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J. Cell Biol. 153 (2001) 881-888
    • (2001) J. Cell Biol. , vol.153 , pp. 881-888
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, Y.L.5
  • 41
    • 2442606429 scopus 로고    scopus 로고
    • Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility
    • Subauste M.C., Pertz O., Adamson E.D., Turner C.E., Junger S., and Hahn K.M. Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility. J. Cell Biol. 165 (2004) 371-381
    • (2004) J. Cell Biol. , vol.165 , pp. 371-381
    • Subauste, M.C.1    Pertz, O.2    Adamson, E.D.3    Turner, C.E.4    Junger, S.5    Hahn, K.M.6
  • 43
    • 0037175385 scopus 로고    scopus 로고
    • Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion and migration
    • Tsubouchi A., Sakakura J., Yagi R., Mazaki Y., Schaefer E., Yano H., and Sabe H. Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion and migration. J. Cell Biol. 159 (2002) 673-683
    • (2002) J. Cell Biol. , vol.159 , pp. 673-683
    • Tsubouchi, A.1    Sakakura, J.2    Yagi, R.3    Mazaki, Y.4    Schaefer, E.5    Yano, H.6    Sabe, H.7
  • 47
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: the first ten years
    • Parsons J.T. Focal adhesion kinase: the first ten years. J. Cell Sci. 116 (2003) 1409-1416
    • (2003) J. Cell Sci. , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 48
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley A.J. Rho GTPases and cell migration. J. Cell Sci. 114 (2001) 2713-2722
    • (2001) J. Cell Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.J.1
  • 49
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung T., Chen X.Q., Manser E., and Lim L. The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16 (1996) 5313-5327
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 53
    • 0035833247 scopus 로고    scopus 로고
    • RhoA is required for monocyte tail retraction during transendothelial migration
    • Worthylake R.A., Lemoine S., Watson J.M., and Burridge K. RhoA is required for monocyte tail retraction during transendothelial migration. J. Cell Biol. 154 (2001) 147-160
    • (2001) J. Cell Biol. , vol.154 , pp. 147-160
    • Worthylake, R.A.1    Lemoine, S.2    Watson, J.M.3    Burridge, K.4
  • 54
    • 0032583123 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase in cytokinesis; mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments
    • Yasui Y., Amano M., Nagata K., Inagaki N., Nakamura H., Saya H., Kaibuchi K., and Inagaki M. Roles of Rho-associated kinase in cytokinesis; mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments. J. Cell Biol. 143 (1998) 1249-1258
    • (1998) J. Cell Biol. , vol.143 , pp. 1249-1258
    • Yasui, Y.1    Amano, M.2    Nagata, K.3    Inagaki, N.4    Nakamura, H.5    Saya, H.6    Kaibuchi, K.7    Inagaki, M.8
  • 55
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: multifunctional kinases in cell behaviour
    • Riento K., and Ridley A.J. Rocks: multifunctional kinases in cell behaviour. Nat. Rev., Mol. Cell Biol. 4 (2003) 446-456
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 56
    • 0036168355 scopus 로고    scopus 로고
    • Characterization of RhoC expression in benign and malignant breast disease: a potential new marker for small breast carcinomas with metastatic ability
    • Kleer C.G., van Golen K.L., Zhang Y., Wu Z.F., Rubin M.A., and Merajver S.D. Characterization of RhoC expression in benign and malignant breast disease: a potential new marker for small breast carcinomas with metastatic ability. Am. J. Pathol. 160 (2002) 579-584
    • (2002) Am. J. Pathol. , vol.160 , pp. 579-584
    • Kleer, C.G.1    van Golen, K.L.2    Zhang, Y.3    Wu, Z.F.4    Rubin, M.A.5    Merajver, S.D.6
  • 57
    • 0037817325 scopus 로고    scopus 로고
    • Significant association of Rho/ROCK pathway with invasion and metastasis of bladder cancer
    • Kamai T., Tsujii T., Arai K., Takagi K., Asami H., Ito Y., and Oshima H. Significant association of Rho/ROCK pathway with invasion and metastasis of bladder cancer. Clin. Cancer Res. 9 (2003) 2632-2641
    • (2003) Clin. Cancer Res. , vol.9 , pp. 2632-2641
    • Kamai, T.1    Tsujii, T.2    Arai, K.3    Takagi, K.4    Asami, H.5    Ito, Y.6    Oshima, H.7
  • 58
    • 0038679226 scopus 로고    scopus 로고
    • Up-regulation of small GTPases, RhoA and RhoC, is associated with tumor progression in ovarian carcinoma
    • Horiuchi A., Imai T., Wang C., Ohira S., Feng Y., Nikaido T., and Konishi I. Up-regulation of small GTPases, RhoA and RhoC, is associated with tumor progression in ovarian carcinoma. Lab. Invest. 83 (2003) 861-870
    • (2003) Lab. Invest. , vol.83 , pp. 861-870
    • Horiuchi, A.1    Imai, T.2    Wang, C.3    Ohira, S.4    Feng, Y.5    Nikaido, T.6    Konishi, I.7
  • 60
    • 0141829795 scopus 로고    scopus 로고
    • Expression and significance of RhoC gene in hepatocellular carcinoma
    • Wang W., Yang L.Y., Yang Z.L., Huang G.W., and Lu W.Q. Expression and significance of RhoC gene in hepatocellular carcinoma. World J. Gastroenterol. 9 (2003) 1950-1953
    • (2003) World J. Gastroenterol. , vol.9 , pp. 1950-1953
    • Wang, W.1    Yang, L.Y.2    Yang, Z.L.3    Huang, G.W.4    Lu, W.Q.5
  • 61
    • 12344252751 scopus 로고    scopus 로고
    • Mechanisms of cancer cell invasion
    • Sahai E. Mechanisms of cancer cell invasion. Curr. Opin. Genet. Dev. 15 (2005) 87-96
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 87-96
    • Sahai, E.1
  • 65
    • 0036226043 scopus 로고    scopus 로고
    • The rho/rho-kinase pathway is involved in the progression of testicular germ cell tumour
    • Kamai T., Arai K., Sumi S., Tsujii T., Honda M., Yamanishi T., and Yoshida K.I. The rho/rho-kinase pathway is involved in the progression of testicular germ cell tumour. BJU Int. 89 (2002) 449-453
    • (2002) BJU Int. , vol.89 , pp. 449-453
    • Kamai, T.1    Arai, K.2    Sumi, S.3    Tsujii, T.4    Honda, M.5    Yamanishi, T.6    Yoshida, K.I.7
  • 66
    • 0036211023 scopus 로고    scopus 로고
    • Expression of ROCK-1 in human pancreatic cancer: its down-regulation by morpholino oligo antisense can reduce the migration of pancreatic cancer cells in vitro
    • Kaneko K., Satoh K., Masamune A., Satoh A., and Shimosegawa T. Expression of ROCK-1 in human pancreatic cancer: its down-regulation by morpholino oligo antisense can reduce the migration of pancreatic cancer cells in vitro. Pancreas 24 (2002) 251-257
    • (2002) Pancreas , vol.24 , pp. 251-257
    • Kaneko, K.1    Satoh, K.2    Masamune, A.3    Satoh, A.4    Shimosegawa, T.5
  • 67
    • 0034698841 scopus 로고    scopus 로고
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts
    • Totsukawa G., Yamakita Y., Yamashiro S., Hartshorne D.J., Sasaki Y., and Matsumura F. Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J. Cell Biol. 150 (2000) 797-806
    • (2000) J. Cell Biol. , vol.150 , pp. 797-806
    • Totsukawa, G.1    Yamakita, Y.2    Yamashiro, S.3    Hartshorne, D.J.4    Sasaki, Y.5    Matsumura, F.6
  • 68
    • 0842288222 scopus 로고    scopus 로고
    • Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts
    • Totsukawa G., Wu Y., Sasaki Y., Hartshorne D.J., Yamakita Y., Yamashiro S., and Matsumura F. Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts. J. Cell Biol. 164 (2004) 427-439
    • (2004) J. Cell Biol. , vol.164 , pp. 427-439
    • Totsukawa, G.1    Wu, Y.2    Sasaki, Y.3    Hartshorne, D.J.4    Yamakita, Y.5    Yamashiro, S.6    Matsumura, F.7
  • 70
    • 0035808419 scopus 로고    scopus 로고
    • Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase
    • Sumi T., Matsumoto K., and Nakamura T. Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J. Biol. Chem. 276 (2001) 670-676
    • (2001) J. Biol. Chem. , vol.276 , pp. 670-676
    • Sumi, T.1    Matsumoto, K.2    Nakamura, T.3
  • 72
    • 0035819527 scopus 로고    scopus 로고
    • Development of matrix metalloproteinase inhibitors in cancer therapy
    • Hidalgo M., and Eckhardt S.G. Development of matrix metalloproteinase inhibitors in cancer therapy. J. Natl. Cancer Inst. 93 (2001) 178-193
    • (2001) J. Natl. Cancer Inst. , vol.93 , pp. 178-193
    • Hidalgo, M.1    Eckhardt, S.G.2
  • 73
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: innovations for the post-trial era
    • Overall C.M., and Lopez-Otin C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat. Rev., Cancer 2 (2002) 657-672
    • (2002) Nat. Rev., Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.