메뉴 건너뛰기




Volumn 44, Issue 11, 2008, Pages 1587-1595

Pentoxifylline impedes migration in B16F10 melanoma by modulating Rho GTPase activity and actin organisation

Author keywords

Actin organisation; B16F10 melanoma; Migration; Pentoxifylline; Protein Kinase A; Rho GTPase

Indexed keywords

ACTIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; PENTOXIFYLLINE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 46049105906     PISSN: 09598049     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejca.2008.04.009     Document Type: Article
Times cited : (33)

References (36)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., and Weinberg R.A. The hallmarks of cancer. Cell 100 1 (2000) 57-70
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 3
    • 0029166671 scopus 로고
    • Rho, rac and cdc42 GTPases: regulators of actin structures, cell adhesion and motility
    • Nobes C.D., and Hall A. Rho, rac and cdc42 GTPases: regulators of actin structures, cell adhesion and motility. Biochem Soc Trans 23 3 (1995) 456-459
    • (1995) Biochem Soc Trans , vol.23 , Issue.3 , pp. 456-459
    • Nobes, C.D.1    Hall, A.2
  • 4
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: coordinating cell responses
    • Ridley A.J. Rho family proteins: coordinating cell responses. Trends Cell Biol 11 12 (2001) 471-477
    • (2001) Trends Cell Biol , vol.11 , Issue.12 , pp. 471-477
    • Ridley, A.J.1
  • 5
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • Bokoch G.M., Bohl B.P., and Chuang T.H. Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J Biol Chem 269 50 (1994) 31674-31679
    • (1994) J Biol Chem , vol.269 , Issue.50 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.H.3
  • 6
    • 0037805583 scopus 로고    scopus 로고
    • Serine phosphorylation negatively regulates RhoA in vivo
    • Ellerbroek S.M., Wennerberg K., and Burridge K. Serine phosphorylation negatively regulates RhoA in vivo. J Biol Chem 278 21 (2003) 19023-19031
    • (2003) J Biol Chem , vol.278 , Issue.21 , pp. 19023-19031
    • Ellerbroek, S.M.1    Wennerberg, K.2    Burridge, K.3
  • 7
    • 0037113097 scopus 로고    scopus 로고
    • PTP-PEST controls motility through regulation of Rac1
    • Sastry S.K., Lyons P.D., Schaller M.D., et al. PTP-PEST controls motility through regulation of Rac1. J Cell Sci 115 Pt 22 (2002) 4305-4316
    • (2002) J Cell Sci , vol.115 , Issue.PART 22 , pp. 4305-4316
    • Sastry, S.K.1    Lyons, P.D.2    Schaller, M.D.3
  • 8
    • 0028129146 scopus 로고
    • PTP-PEST: a protein tyrosine phosphatase regulated by serine phosphorylation
    • Garton A.J., and Tonks N.K. PTP-PEST: a protein tyrosine phosphatase regulated by serine phosphorylation. Embo J 13 16 (1994) 3763-3771
    • (1994) Embo J , vol.13 , Issue.16 , pp. 3763-3771
    • Garton, A.J.1    Tonks, N.K.2
  • 9
    • 18844363699 scopus 로고    scopus 로고
    • ILK mediates actin filament rearrangements and cell migration and invasion through PI3K/Akt/Rac1 signaling
    • Qian Y., Zhong X., Flynn D.C., et al. ILK mediates actin filament rearrangements and cell migration and invasion through PI3K/Akt/Rac1 signaling. Oncogene 24 19 (2005) 3154-3165
    • (2005) Oncogene , vol.24 , Issue.19 , pp. 3154-3165
    • Qian, Y.1    Zhong, X.2    Flynn, D.C.3
  • 10
    • 0023764256 scopus 로고
    • Pentoxifylline inhibits granulocyte and platelet function, including granulocyte priming by platelet activating factor
    • Hammerschmidt D.E., Kotasek D., McCarthy T., et al. Pentoxifylline inhibits granulocyte and platelet function, including granulocyte priming by platelet activating factor. J Lab Clin Med 112 2 (1988) 254-263
    • (1988) J Lab Clin Med , vol.112 , Issue.2 , pp. 254-263
    • Hammerschmidt, D.E.1    Kotasek, D.2    McCarthy, T.3
  • 11
    • 0018594632 scopus 로고
    • Studies on platelet aggregation inhibitors in vivo. VIII. Effect of pentoxifylline on spontaneous tumor metastasis.
    • Gordon S., Witul M., Cohen H., et al. Studies on platelet aggregation inhibitors in vivo. VIII. Effect of pentoxifylline on spontaneous tumor metastasis. J Med 10 6 (1979) 435-443
    • (1979) J Med , vol.10 , Issue.6 , pp. 435-443
    • Gordon, S.1    Witul, M.2    Cohen, H.3
  • 12
    • 0030578913 scopus 로고    scopus 로고
    • Inhibition of lung homing of B16F10 by pentoxifylline, a microfilament depolymerizing agent
    • Gude R.P., Ingle A.D., and Rao S.G. Inhibition of lung homing of B16F10 by pentoxifylline, a microfilament depolymerizing agent. Cancer Lett 106 2 (1996) 171-176
    • (1996) Cancer Lett , vol.106 , Issue.2 , pp. 171-176
    • Gude, R.P.1    Ingle, A.D.2    Rao, S.G.3
  • 13
    • 84988267441 scopus 로고    scopus 로고
    • Inhibition of endothelial cell proliferation and tumor-induced angiogenesis by pentoxifylline
    • Gude R.P., Binda M.M., Boquete A.L., et al. Inhibition of endothelial cell proliferation and tumor-induced angiogenesis by pentoxifylline. J Cancer Res Clin Oncol 127 10 (2001) 625-630
    • (2001) J Cancer Res Clin Oncol , vol.127 , Issue.10 , pp. 625-630
    • Gude, R.P.1    Binda, M.M.2    Boquete, A.L.3
  • 14
    • 33646477131 scopus 로고    scopus 로고
    • Antiproliferative and antiproteolytic activity of pentoxifylline in cultures of B16F10 melanoma cells
    • Dua P., and Gude R.P. Antiproliferative and antiproteolytic activity of pentoxifylline in cultures of B16F10 melanoma cells. Cancer Chemother Pharmacol 58 2 (2006) 195-202
    • (2006) Cancer Chemother Pharmacol , vol.58 , Issue.2 , pp. 195-202
    • Dua, P.1    Gude, R.P.2
  • 15
    • 34548203180 scopus 로고    scopus 로고
    • Suramin augments the antitumor and antimetastatic activity of pentoxifylline in B16F10 melanoma
    • Dua P., Ingle A., and Gude R.P. Suramin augments the antitumor and antimetastatic activity of pentoxifylline in B16F10 melanoma. Int J Cancer 121 7 (2007) 1600-1608
    • (2007) Int J Cancer , vol.121 , Issue.7 , pp. 1600-1608
    • Dua, P.1    Ingle, A.2    Gude, R.P.3
  • 16
    • 42549170102 scopus 로고    scopus 로고
    • Pentoxifylline modulates cell surface integrin expression and integrin mediated adhesion of B16F10 cells to extracellular matrix components
    • Ratheesh A., Ingle A., and Gude R.P. Pentoxifylline modulates cell surface integrin expression and integrin mediated adhesion of B16F10 cells to extracellular matrix components. Cancer Biol Ther 6 11 (2007)
    • (2007) Cancer Biol Ther , vol.6 , Issue.11
    • Ratheesh, A.1    Ingle, A.2    Gude, R.P.3
  • 17
    • 0027077726 scopus 로고
    • Differences in chemotaxis to fibronectin in weakly and highly metastatic tumor cells
    • Murata J., Saiki I., Yoneda J., et al. Differences in chemotaxis to fibronectin in weakly and highly metastatic tumor cells. Jpn J Cancer Res 83 12 (1992) 1327-1333
    • (1992) Jpn J Cancer Res , vol.83 , Issue.12 , pp. 1327-1333
    • Murata, J.1    Saiki, I.2    Yoneda, J.3
  • 18
    • 0035142337 scopus 로고    scopus 로고
    • Migration and metalloproteinases determine the invasive potential of mouse melanoma cells, but not melanin and telomerase
    • Zhao W., Liu H., Xu S., et al. Migration and metalloproteinases determine the invasive potential of mouse melanoma cells, but not melanin and telomerase. Cancer Lett 162 Suppl (2001) S49-S55
    • (2001) Cancer Lett , vol.162 , Issue.SUPPL
    • Zhao, W.1    Liu, H.2    Xu, S.3
  • 19
    • 84988293861 scopus 로고    scopus 로고
    • Studies on the mechanisms responsible for inhibition of experimental metastasis of B16-F10 murine melanoma by pentoxifylline
    • Gude R.P., Binda M.M., Presas H.L., et al. Studies on the mechanisms responsible for inhibition of experimental metastasis of B16-F10 murine melanoma by pentoxifylline. J Biomed Sci 6 2 (1999) 133-141
    • (1999) J Biomed Sci , vol.6 , Issue.2 , pp. 133-141
    • Gude, R.P.1    Binda, M.M.2    Presas, H.L.3
  • 20
    • 0025730646 scopus 로고
    • Pentoxifylline stimulates human sperm motility both in vitro and after oral therapy
    • Shen M.R., Chiang P.H., Yang R.C., et al. Pentoxifylline stimulates human sperm motility both in vitro and after oral therapy. Br J Clin Pharmacol 31 6 (1991) 711-714
    • (1991) Br J Clin Pharmacol , vol.31 , Issue.6 , pp. 711-714
    • Shen, M.R.1    Chiang, P.H.2    Yang, R.C.3
  • 21
    • 0030930539 scopus 로고    scopus 로고
    • The effect of pentoxifylline on human neutrophil migration: a possible role for cyclic nucleotides
    • Elferink J.G., Huizinga T.W., and de Koster B.M. The effect of pentoxifylline on human neutrophil migration: a possible role for cyclic nucleotides. Biochem Pharmacol 54 4 (1997) 475-480
    • (1997) Biochem Pharmacol , vol.54 , Issue.4 , pp. 475-480
    • Elferink, J.G.1    Huizinga, T.W.2    de Koster, B.M.3
  • 22
    • 0036554332 scopus 로고    scopus 로고
    • Effect of pentoxifylline on polarization and migration of human leukocytes
    • Dominguez-Jimenez C., Sancho D., Nieto M., et al. Effect of pentoxifylline on polarization and migration of human leukocytes. J Leukoc Biol 71 4 (2002) 588-596
    • (2002) J Leukoc Biol , vol.71 , Issue.4 , pp. 588-596
    • Dominguez-Jimenez, C.1    Sancho, D.2    Nieto, M.3
  • 23
    • 0033511150 scopus 로고    scopus 로고
    • Phosphodiesterase type III inhibitor, cilostazol, inhibits colon cancer cell motility
    • Murata K., Kameyama M., Fukui F., et al. Phosphodiesterase type III inhibitor, cilostazol, inhibits colon cancer cell motility. Clin Exp Metastasis 17 6 (1999) 525-530
    • (1999) Clin Exp Metastasis , vol.17 , Issue.6 , pp. 525-530
    • Murata, K.1    Kameyama, M.2    Fukui, F.3
  • 24
    • 0028081499 scopus 로고
    • Regulation of motility and cytoskeletal organization of rat bladder carcinoma cells by cyclic AMP
    • Morton D.M., and Tchao R. Regulation of motility and cytoskeletal organization of rat bladder carcinoma cells by cyclic AMP. Cell Motil Cytoskeleton 29 4 (1994) 375-382
    • (1994) Cell Motil Cytoskeleton , vol.29 , Issue.4 , pp. 375-382
    • Morton, D.M.1    Tchao, R.2
  • 25
    • 0034580663 scopus 로고    scopus 로고
    • Pentoxifylline potentiates nitric oxide production in interleukin-1beta-stimulated vascular smooth muscle cells through cyclic AMP-dependent protein kinase A pathway
    • Kim N.Y., Pae H.O., Kim Y.C., et al. Pentoxifylline potentiates nitric oxide production in interleukin-1beta-stimulated vascular smooth muscle cells through cyclic AMP-dependent protein kinase A pathway. Gen Pharmacol 35 4 (2000) 205-211
    • (2000) Gen Pharmacol , vol.35 , Issue.4 , pp. 205-211
    • Kim, N.Y.1    Pae, H.O.2    Kim, Y.C.3
  • 26
    • 0034751592 scopus 로고    scopus 로고
    • 1-(5-oxohexyl)-3,7-Dimethylxanthine, a phosphodiesterase inhibitor, activates MAPK cascades and promotes osteoblast differentiation by a mechanism independent of PKA activation (pentoxifylline promotes osteoblast differentiation)
    • Rawadi G., Ferrer C., Spinella-Jaegle S., et al. 1-(5-oxohexyl)-3,7-Dimethylxanthine, a phosphodiesterase inhibitor, activates MAPK cascades and promotes osteoblast differentiation by a mechanism independent of PKA activation (pentoxifylline promotes osteoblast differentiation). Endocrinology 142 11 (2001) 4673-4682
    • (2001) Endocrinology , vol.142 , Issue.11 , pp. 4673-4682
    • Rawadi, G.1    Ferrer, C.2    Spinella-Jaegle, S.3
  • 27
    • 22444431716 scopus 로고    scopus 로고
    • Hot-water extracts from adzuki beans (Vigna angularis) stimulate not only melanogenesis in cultured mouse B16 melanoma cells but also pigmentation of hair color in C3H mice
    • Itoh T., and Furuichi Y. Hot-water extracts from adzuki beans (Vigna angularis) stimulate not only melanogenesis in cultured mouse B16 melanoma cells but also pigmentation of hair color in C3H mice. Biosci Biotechnol Biochem 69 5 (2005) 873-882
    • (2005) Biosci Biotechnol Biochem , vol.69 , Issue.5 , pp. 873-882
    • Itoh, T.1    Furuichi, Y.2
  • 28
    • 29844441290 scopus 로고    scopus 로고
    • Inhibition of melanogenic activity by 4,4'-dihydroxybiphenyl in melanoma cells
    • No J.K., Kim Y.J., Lee J.S., et al. Inhibition of melanogenic activity by 4,4'-dihydroxybiphenyl in melanoma cells. Biol Pharm Bull 29 1 (2006) 14-16
    • (2006) Biol Pharm Bull , vol.29 , Issue.1 , pp. 14-16
    • No, J.K.1    Kim, Y.J.2    Lee, J.S.3
  • 29
    • 0033803074 scopus 로고    scopus 로고
    • Photo-induced inactivation of protein kinase calpha by dequalinium inhibits motility of murine melanoma cells
    • Sullivan R.M., Stone M., Marshall J.F., et al. Photo-induced inactivation of protein kinase calpha by dequalinium inhibits motility of murine melanoma cells. Mol Pharmacol 58 4 (2000) 729-737
    • (2000) Mol Pharmacol , vol.58 , Issue.4 , pp. 729-737
    • Sullivan, R.M.1    Stone, M.2    Marshall, J.F.3
  • 30
    • 0034757405 scopus 로고    scopus 로고
    • Atypical protein kinase Czeta suppresses migration of mouse melanoma cells
    • Sanz-Navares E., Fernandez N., Kazanietz M.G., et al. Atypical protein kinase Czeta suppresses migration of mouse melanoma cells. Cell Growth Differ 12 10 (2001) 517-524
    • (2001) Cell Growth Differ , vol.12 , Issue.10 , pp. 517-524
    • Sanz-Navares, E.1    Fernandez, N.2    Kazanietz, M.G.3
  • 31
    • 0042858413 scopus 로고    scopus 로고
    • Ligand-dependent inhibition of B16 melanoma cell migration and invasion via endogenous S1P2 G protein-coupled receptor. Requirement of inhibition of cellular RAC activity.
    • Arikawa K., Takuwa N., Yamaguchi H., et al. Ligand-dependent inhibition of B16 melanoma cell migration and invasion via endogenous S1P2 G protein-coupled receptor. Requirement of inhibition of cellular RAC activity. J Biol Chem 278 35 (2003) 32841-32851
    • (2003) J Biol Chem , vol.278 , Issue.35 , pp. 32841-32851
    • Arikawa, K.1    Takuwa, N.2    Yamaguchi, H.3
  • 32
    • 0034060491 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate inhibits haptotactic motility by overproduction of focal adhesion sites in B16 melanoma cells through EDG-induced activation of Rho
    • Yamamura S., Hakomori S., Wada A., et al. Sphingosine-1-phosphate inhibits haptotactic motility by overproduction of focal adhesion sites in B16 melanoma cells through EDG-induced activation of Rho. Ann N Y Acad Sci 905 (2000) 301-307
    • (2000) Ann N Y Acad Sci , vol.905 , pp. 301-307
    • Yamamura, S.1    Hakomori, S.2    Wada, A.3
  • 33
    • 33750614889 scopus 로고    scopus 로고
    • Dykellic acid inhibits cell migration and tube formation by RhoA-GTP expression
    • Heo J.C., Park J.Y., Woo S.U., et al. Dykellic acid inhibits cell migration and tube formation by RhoA-GTP expression. Biol Pharm Bull 29 11 (2006) 2256-2259
    • (2006) Biol Pharm Bull , vol.29 , Issue.11 , pp. 2256-2259
    • Heo, J.C.1    Park, J.Y.2    Woo, S.U.3
  • 34
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase
    • Ridley A.J., and Hall A. Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase. Embo J 13 11 (1994) 2600-2610
    • (1994) Embo J , vol.13 , Issue.11 , pp. 2600-2610
    • Ridley, A.J.1    Hall, A.2
  • 35
    • 0024221503 scopus 로고
    • Actin depolymerization and inhibition of capping induced by pentoxifylline in human lymphocytes and neutrophils
    • Rao K.M., Crawford J., Currie M.S., et al. Actin depolymerization and inhibition of capping induced by pentoxifylline in human lymphocytes and neutrophils. J Cell Physiol 137 3 (1988) 577-582
    • (1988) J Cell Physiol , vol.137 , Issue.3 , pp. 577-582
    • Rao, K.M.1    Crawford, J.2    Currie, M.S.3
  • 36
    • 0023645738 scopus 로고
    • Protein kinase C and cAMP-dependent protein kinase induce opposite effects on actin polymerizability
    • Ohta Y., Akiyama T., Nishida E., et al. Protein kinase C and cAMP-dependent protein kinase induce opposite effects on actin polymerizability. FEBS Lett 222 2 (1987) 305-310
    • (1987) FEBS Lett , vol.222 , Issue.2 , pp. 305-310
    • Ohta, Y.1    Akiyama, T.2    Nishida, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.