메뉴 건너뛰기




Volumn 6, Issue 3, 2011, Pages

The ras antagonist, farnesylthiosalicylic acid (FTS), decreases fibrosis and improves muscle strength in dy2j/dy2j mouse model of muscular dystrophy

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; GELATINASE A; GELATINASE B; MITOGEN ACTIVATED PROTEIN KINASE; RAS PROTEIN; SALIRASIB; DRUG DERIVATIVE; FARNESOL; PRIMER DNA; SALICYLIC ACID DERIVATIVE;

EID: 79952954167     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018049     Document Type: Article
Times cited : (19)

References (49)
  • 1
    • 4444234437 scopus 로고    scopus 로고
    • The congenital muscular dystrophies in 2004: a century of exciting progress
    • Muntoni F, Voit T, (2004) The congenital muscular dystrophies in 2004: a century of exciting progress. Neuromuscul Disord 14: 635-649.
    • (2004) Neuromuscul Disord , vol.14 , pp. 635-649
    • Muntoni, F.1    Voit, T.2
  • 3
    • 0028135436 scopus 로고
    • Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene
    • Xu H, Wu XR, Wewer UM, Engvall E, (1994) Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene. Nat Genet 8: 297-302.
    • (1994) Nat Genet , vol.8 , pp. 297-302
    • Xu, H.1    Wu, X.R.2    Wewer, U.M.3    Engvall, E.4
  • 5
    • 0033581703 scopus 로고    scopus 로고
    • The laminin alpha2 expressed by dystrophic dy(2J) mice is defective in its ability to form polymers
    • Colognato H, Yurchenco PD, (1999) The laminin alpha2 expressed by dystrophic dy(2J) mice is defective in its ability to form polymers. Curr Biol 9: 1327-1330.
    • (1999) Curr Biol , vol.9 , pp. 1327-1330
    • Colognato, H.1    Yurchenco, P.D.2
  • 7
    • 0028788685 scopus 로고
    • Demyelinating peripheral neuropathy in merosin-deficient congenital muscular dystrophy
    • Shorer Z, Philpot J, Muntoni F, Sewry C, Dubowitz V, (1995) Demyelinating peripheral neuropathy in merosin-deficient congenital muscular dystrophy. J Child Neurol 10: 472-475.
    • (1995) J Child Neurol , vol.10 , pp. 472-475
    • Shorer, Z.1    Philpot, J.2    Muntoni, F.3    Sewry, C.4    Dubowitz, V.5
  • 9
    • 33749248495 scopus 로고    scopus 로고
    • Congenital muscular dystrophies and the extracellular matrix
    • Schessl J, Zou Y, Bonnemann CG, (2006) Congenital muscular dystrophies and the extracellular matrix. Semin Pediatr Neurol 13: 80-89.
    • (2006) Semin Pediatr Neurol , vol.13 , pp. 80-89
    • Schessl, J.1    Zou, Y.2    Bonnemann, C.G.3
  • 10
    • 0027232605 scopus 로고
    • Emerging concepts in the Ras superfamily of GTP-binding proteins
    • Bokoch GM, Der CJ, (1993) Emerging concepts in the Ras superfamily of GTP-binding proteins. FASEB J 7: 750-759.
    • (1993) FASEB J , vol.7 , pp. 750-759
    • Bokoch, G.M.1    Der, C.J.2
  • 11
    • 0034104590 scopus 로고    scopus 로고
    • The Ras branch of small GTPases: Ras family members don't fall far from the tree
    • Reuther GW, Der CJ, (2000) The Ras branch of small GTPases: Ras family members don't fall far from the tree. Curr Opin Cell Biol 12: 157-165.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 157-165
    • Reuther, G.W.1    Der, C.J.2
  • 12
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants
    • Scheffzek K, Ahmadian MR, Kabsch W, Wiesmuller L, Lautwein A, et al. (1997) The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277: 333-338.
    • (1997) Science , vol.277 , pp. 333-338
    • Scheffzek, K.1    Ahmadian, M.R.2    Kabsch, W.3    Wiesmuller, L.4    Lautwein, A.5
  • 13
  • 14
    • 0037377992 scopus 로고    scopus 로고
    • Ras antagonist farnesylthiosalicylic acid (FTS) reduces glomerular cellular proliferation and macrophage number in rat thy-1 nephritis
    • Clarke HC, Kocher HM, Khwaja A, Kloog Y, Cook HT, et al. (2003) Ras antagonist farnesylthiosalicylic acid (FTS) reduces glomerular cellular proliferation and macrophage number in rat thy-1 nephritis. J Am Soc Nephrol 14: 848-854.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 848-854
    • Clarke, H.C.1    Kocher, H.M.2    Khwaja, A.3    Kloog, Y.4    Cook, H.T.5
  • 15
    • 0035652626 scopus 로고    scopus 로고
    • Treatment of MRL/lpr mice, a genetic autoimmune model, with the Ras inhibitor, farnesylthiosalicylate (FTS)
    • Katzav A, Kloog Y, Korczyn AD, Niv H, Karussis DM, et al. (2001) Treatment of MRL/lpr mice, a genetic autoimmune model, with the Ras inhibitor, farnesylthiosalicylate (FTS). Clin Exp Immunol 126: 570-577.
    • (2001) Clin Exp Immunol , vol.126 , pp. 570-577
    • Katzav, A.1    Kloog, Y.2    Korczyn, A.D.3    Niv, H.4    Karussis, D.M.5
  • 16
    • 0032937404 scopus 로고    scopus 로고
    • Modulation of the immune response and tumor growth by activated Ras
    • Weijzen S, Velders MP, Kast WM, (1999) Modulation of the immune response and tumor growth by activated Ras. Leukemia 13: 502-513.
    • (1999) Leukemia , vol.13 , pp. 502-513
    • Weijzen, S.1    Velders, M.P.2    Kast, W.M.3
  • 18
    • 0028981375 scopus 로고
    • Selective inhibition of Ras-dependent cell growth by farnesylthiosalisylic acid
    • Marom M, Haklai R, Ben-Baruch G, Marciano D, Egozi Y, et al. (1995) Selective inhibition of Ras-dependent cell growth by farnesylthiosalisylic acid. J Biol Chem 270: 22263-22270.
    • (1995) J Biol Chem , vol.270 , pp. 22263-22270
    • Marom, M.1    Haklai, R.2    Ben-Baruch, G.3    Marciano, D.4    Egozi, Y.5
  • 19
    • 0033803477 scopus 로고    scopus 로고
    • RAS inhibitors: potential for cancer therapeutics
    • Kloog Y, Cox AD, (2000) RAS inhibitors: potential for cancer therapeutics. Mol Med Today 6: 398-402.
    • (2000) Mol Med Today , vol.6 , pp. 398-402
    • Kloog, Y.1    Cox, A.D.2
  • 20
    • 0036260550 scopus 로고    scopus 로고
    • Ras processing as a therapeutic target in hematologic malignancies
    • Le DT, Shannon KM, (2002) Ras processing as a therapeutic target in hematologic malignancies. Curr Opin Hematol 9: 308-315.
    • (2002) Curr Opin Hematol , vol.9 , pp. 308-315
    • Le, D.T.1    Shannon, K.M.2
  • 21
    • 0033559885 scopus 로고    scopus 로고
    • Growth inhibition of ras-dependent tumors in nude mice by a potent ras-dislodging antagonist
    • Egozi Y, Weisz B, Gana-Weisz M, Ben-Baruch G, Kloog Y, (1999) Growth inhibition of ras-dependent tumors in nude mice by a potent ras-dislodging antagonist. Int J Cancer 80: 911-918.
    • (1999) Int J Cancer , vol.80 , pp. 911-918
    • Egozi, Y.1    Weisz, B.2    Gana-Weisz, M.3    Ben-Baruch, G.4    Kloog, Y.5
  • 22
    • 4444269015 scopus 로고    scopus 로고
    • Treatment of thioacetamide-induced liver cirrhosis by the Ras antagonist, farnesylthiosalicylic acid
    • Reif S, Aeed H, Shilo Y, Reich R, Kloog Y, et al. (2004) Treatment of thioacetamide-induced liver cirrhosis by the Ras antagonist, farnesylthiosalicylic acid. J Hepatol 41: 235-241.
    • (2004) J Hepatol , vol.41 , pp. 235-241
    • Reif, S.1    Aeed, H.2    Shilo, Y.3    Reich, R.4    Kloog, Y.5
  • 23
    • 0032731750 scopus 로고    scopus 로고
    • The Ras antagonist, farnesylthiosalicylic acid (FTS), inhibits experimentally-induced liver cirrhosis in rats
    • Reif S, Weis B, Aeed H, Gana-Weis M, Zaidel L, et al. (1999) The Ras antagonist, farnesylthiosalicylic acid (FTS), inhibits experimentally-induced liver cirrhosis in rats. J Hepatol 31: 1053-1061.
    • (1999) J Hepatol , vol.31 , pp. 1053-1061
    • Reif, S.1    Weis, B.2    Aeed, H.3    Gana-Weis, M.4    Zaidel, L.5
  • 24
    • 0028959539 scopus 로고
    • Farnesyl derivatives of rigid carboxylic acids-inhibitors of ras-dependent cell growth
    • Marciano D, Ben-Baruch G, Marom M, Egozi Y, Haklai R, et al. (1995) Farnesyl derivatives of rigid carboxylic acids-inhibitors of ras-dependent cell growth. J Med Chem 38: 1267-1272.
    • (1995) J Med Chem , vol.38 , pp. 1267-1272
    • Marciano, D.1    Ben-Baruch, G.2    Marom, M.3    Egozi, Y.4    Haklai, R.5
  • 25
    • 77950954615 scopus 로고    scopus 로고
    • Improved muscle strength and mobility in the dy(2J)/dy(2J) mouse with merosin deficient congenital muscular dystrophy treated with Glatiramer acetate
    • Dadush O, Aga-Mizrachi S, Ettinger K, Tabakman R, Elbaz M, et al. (2010) Improved muscle strength and mobility in the dy(2J)/dy(2J) mouse with merosin deficient congenital muscular dystrophy treated with Glatiramer acetate. Neuromuscul Disord 20: 267-272.
    • (2010) Neuromuscul Disord , vol.20 , pp. 267-272
    • Dadush, O.1    Aga-Mizrachi, S.2    Ettinger, K.3    Tabakman, R.4    Elbaz, M.5
  • 26
    • 0037020243 scopus 로고    scopus 로고
    • Galectin-1 augments Ras activation and diverts Ras signals to Raf-1 at the expense of phosphoinositide 3-kinase
    • Elad-Sfadia G, Haklai R, Ballan E, Gabius HJ, Kloog Y, (2002) Galectin-1 augments Ras activation and diverts Ras signals to Raf-1 at the expense of phosphoinositide 3-kinase. J Biol Chem 277: 37169-37175.
    • (2002) J Biol Chem , vol.277 , pp. 37169-37175
    • Elad-Sfadia, G.1    Haklai, R.2    Ballan, E.3    Gabius, H.J.4    Kloog, Y.5
  • 27
    • 0023779791 scopus 로고
    • Ras oncogene mediated induction of a 92 kDa metalloproteinase; strong correlation with the malignant phenotype
    • Ballin M, Gomez DE, Sinha CC, Thorgeirsson UP, (1988) Ras oncogene mediated induction of a 92 kDa metalloproteinase; strong correlation with the malignant phenotype. Biochem Biophys Res Commun 154: 832-838.
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 832-838
    • Ballin, M.1    Gomez, D.E.2    Sinha, C.C.3    Thorgeirsson, U.P.4
  • 28
    • 33846265912 scopus 로고    scopus 로고
    • Congenital muscular dystrophies: new aspects of an expanding group of disorders
    • Lisi MT, Cohn RD, (2007) Congenital muscular dystrophies: new aspects of an expanding group of disorders. Biochim Biophys Acta 1772: 159-172.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 159-172
    • Lisi, M.T.1    Cohn, R.D.2
  • 30
    • 33750286101 scopus 로고    scopus 로고
    • Signal transduction. Prelude to an anniversary for the RAS oncogene
    • Downward J, (2006) Signal transduction. Prelude to an anniversary for the RAS oncogene. Science 314: 433-434.
    • (2006) Science , vol.314 , pp. 433-434
    • Downward, J.1
  • 31
    • 0036364408 scopus 로고    scopus 로고
    • A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases
    • Quilliam LA, Rebhun JF, Castro AF, (2002) A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases. Prog Nucleic Acid Res Mol Biol 71: 391-444.
    • (2002) Prog Nucleic Acid Res Mol Biol , vol.71 , pp. 391-444
    • Quilliam, L.A.1    Rebhun, J.F.2    Castro, A.F.3
  • 32
    • 38949093546 scopus 로고    scopus 로고
    • Inhibitors of chronically active ras: potential for treatment of human malignancies
    • Blum R, Cox AD, Kloog Y, (2008) Inhibitors of chronically active ras: potential for treatment of human malignancies. Recent Pat Anticancer Drug Discov 3: 31-47.
    • (2008) Recent Pat Anticancer Drug Discov , vol.3 , pp. 31-47
    • Blum, R.1    Cox, A.D.2    Kloog, Y.3
  • 34
    • 0037332586 scopus 로고    scopus 로고
    • Laminin alpha2 deficiency and muscular dystrophy; genotype-phenotype correlation in mutant mice
    • Guo LT, Zhang XU, Kuang W, Xu H, Liu LA, et al. (2003) Laminin alpha2 deficiency and muscular dystrophy; genotype-phenotype correlation in mutant mice. Neuromuscul Disord 13: 207-215.
    • (2003) Neuromuscul Disord , vol.13 , pp. 207-215
    • Guo, L.T.1    Zhang, X.U.2    Kuang, W.3    Xu, H.4    Liu, L.A.5
  • 35
    • 0032717429 scopus 로고    scopus 로고
    • Targeting of K-Ras 4B by S-trans,trans-farnesyl thiosalicylic acid
    • Elad G, Paz A, Haklai R, Marciano D, Cox A, et al. (1999) Targeting of K-Ras 4B by S-trans,trans-farnesyl thiosalicylic acid. Biochim Biophys Acta 1452: 228-242.
    • (1999) Biochim Biophys Acta , vol.1452 , pp. 228-242
    • Elad, G.1    Paz, A.2    Haklai, R.3    Marciano, D.4    Cox, A.5
  • 36
    • 0842326021 scopus 로고    scopus 로고
    • Matrix metalloproteinases and skeletal muscle: a brief review
    • Carmeli E, Moas M, Reznick AZ, Coleman R, (2004) Matrix metalloproteinases and skeletal muscle: a brief review. Muscle Nerve 29: 191-197.
    • (2004) Muscle Nerve , vol.29 , pp. 191-197
    • Carmeli, E.1    Moas, M.2    Reznick, A.Z.3    Coleman, R.4
  • 37
    • 33646537449 scopus 로고    scopus 로고
    • Matrix metalloproteinases and cellular motility in development and disease
    • VanSaun MN, Matrisian LM, (2006) Matrix metalloproteinases and cellular motility in development and disease. Birth Defects Res C Embryo Today 78: 69-79.
    • (2006) Birth Defects Res C Embryo Today , vol.78 , pp. 69-79
    • VanSaun, M.N.1    Matrisian, L.M.2
  • 38
    • 0033981058 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases in the muscle of patients with inflammatory myopathies
    • Choi YC, Dalakas MC, (2000) Expression of matrix metalloproteinases in the muscle of patients with inflammatory myopathies. Neurology 54: 65-71.
    • (2000) Neurology , vol.54 , pp. 65-71
    • Choi, Y.C.1    Dalakas, M.C.2
  • 39
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian LM, (1992) The matrix-degrading metalloproteinases. Bioessays 14: 455-463.
    • (1992) Bioessays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 40
    • 42549110017 scopus 로고    scopus 로고
    • Pattern of metalloprotease activity and myofiber regeneration in skeletal muscles of mdx mice
    • Bani C, Lagrota-Candido J, Pinheiro DF, Leite PE, Salimena MC, et al. (2008) Pattern of metalloprotease activity and myofiber regeneration in skeletal muscles of mdx mice. Muscle Nerve 37: 583-592.
    • (2008) Muscle Nerve , vol.37 , pp. 583-592
    • Bani, C.1    Lagrota-Candido, J.2    Pinheiro, D.F.3    Leite, P.E.4    Salimena, M.C.5
  • 41
    • 0034597464 scopus 로고    scopus 로고
    • Unusual laminin alpha2 processing in myoblasts from a patient with a novel variant of congenital muscular dystrophy
    • Lattanzi G, Muntoni F, Sabatelli P, Squarzoni S, Maraldi NM, et al. (2000) Unusual laminin alpha2 processing in myoblasts from a patient with a novel variant of congenital muscular dystrophy. Biochem Biophys Res Commun 277: 639-642.
    • (2000) Biochem Biophys Res Commun , vol.277 , pp. 639-642
    • Lattanzi, G.1    Muntoni, F.2    Sabatelli, P.3    Squarzoni, S.4    Maraldi, N.M.5
  • 42
    • 0032947765 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases 2 and 9 in regenerating skeletal muscle: a study in experimentally injured and mdx muscles
    • Kherif S, Lafuma C, Dehaupas M, Lachkar S, Fournier JG, et al. (1999) Expression of matrix metalloproteinases 2 and 9 in regenerating skeletal muscle: a study in experimentally injured and mdx muscles. Dev Biol 205: 158-170.
    • (1999) Dev Biol , vol.205 , pp. 158-170
    • Kherif, S.1    Lafuma, C.2    Dehaupas, M.3    Lachkar, S.4    Fournier, J.G.5
  • 43
    • 0036116405 scopus 로고    scopus 로고
    • Matrix metalloproteinases in inflammatory myopathies: enhanced immunoreactivity near atrophic myofibers
    • Schoser BG, Blottner D, Stuerenburg HJ, (2002) Matrix metalloproteinases in inflammatory myopathies: enhanced immunoreactivity near atrophic myofibers. Acta Neurol Scand 105: 309-313.
    • (2002) Acta Neurol Scand , vol.105 , pp. 309-313
    • Schoser, B.G.1    Blottner, D.2    Stuerenburg, H.J.3
  • 44
    • 67649851014 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy
    • Li H, Mittal A, Makonchuk DY, Bhatnagar S, Kumar A, (2009) Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum Mol Genet 18: 2584-2598.
    • (2009) Hum Mol Genet , vol.18 , pp. 2584-2598
    • Li, H.1    Mittal, A.2    Makonchuk, D.Y.3    Bhatnagar, S.4    Kumar, A.5
  • 45
    • 33846120591 scopus 로고    scopus 로고
    • Matrix metalloproteinases as valid clinical targets
    • Fingleton B, (2007) Matrix metalloproteinases as valid clinical targets. Curr Pharm Des 13: 333-346.
    • (2007) Curr Pharm Des , vol.13 , pp. 333-346
    • Fingleton, B.1
  • 46
    • 37249069513 scopus 로고    scopus 로고
    • Over-expression of GTP-binding proteins and GTPase activity in mouse astrocyte membranes in response to Theiler's murine encephalomyelitis virus infection
    • Rubio N, Gonzalez-Tirante M, Arevalo MA, Aranguez I, (2008) Over-expression of GTP-binding proteins and GTPase activity in mouse astrocyte membranes in response to Theiler's murine encephalomyelitis virus infection. J Neurochem 104: 100-112.
    • (2008) J Neurochem , vol.104 , pp. 100-112
    • Rubio, N.1    Gonzalez-Tirante, M.2    Arevalo, M.A.3    Aranguez, I.4
  • 47
    • 0034025512 scopus 로고    scopus 로고
    • Expression of a dominant-negative mutant of p21(ras) inhibits induction of nitric oxide synthase and activation of nuclear factor-kappaB in primary astrocytes
    • Pahan K, Liu X, McKinney MJ, Wood C, Sheikh FG, et al. (2000) Expression of a dominant-negative mutant of p21(ras) inhibits induction of nitric oxide synthase and activation of nuclear factor-kappaB in primary astrocytes. J Neurochem 74: 2288-2295.
    • (2000) J Neurochem , vol.74 , pp. 2288-2295
    • Pahan, K.1    Liu, X.2    McKinney, M.J.3    Wood, C.4    Sheikh, F.G.5
  • 48
    • 77955151335 scopus 로고    scopus 로고
    • Fibrosis inhibition and muscle histopathology improvement in laminin-alpha2-deficient mice
    • Nevo Y, Halevy O, Genin O, Moshe I, Turgeman T, et al. (2010) Fibrosis inhibition and muscle histopathology improvement in laminin-alpha2-deficient mice. Muscle Nerve 42: 218-229.
    • (2010) Muscle Nerve , vol.42 , pp. 218-229
    • Nevo, Y.1    Halevy, O.2    Genin, O.3    Moshe, I.4    Turgeman, T.5
  • 49
    • 33846946114 scopus 로고    scopus 로고
    • Angiotensin II type 1 receptor blockade attenuates TGF-beta-induced failure of muscle regeneration in multiple myopathic states
    • Cohn RD, van Erp C, Habashi JP, Soleimani AA, Klein EC, et al. (2007) Angiotensin II type 1 receptor blockade attenuates TGF-beta-induced failure of muscle regeneration in multiple myopathic states. Nat Med 13: 204-210.
    • (2007) Nat Med , vol.13 , pp. 204-210
    • Cohn, R.D.1    van Erp, C.2    Habashi, J.P.3    Soleimani, A.A.4    Klein, E.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.