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Volumn 46, Issue 5, 2012, Pages 810-813

Suramin affects metalloproteinase-9 activity and increases beta-dystroglycan levels in the diaphragm of the dystrophin-deficient mdx MOUSE

Author keywords

Beta dystroglycan; DMD; mdx; Metalloproteinases; Suramin

Indexed keywords

BETA DYSTROGLYCAN; GELATINASE A; GELATINASE B; SURAMIN;

EID: 84867383138     PISSN: 0148639X     EISSN: 10974598     Source Type: Journal    
DOI: 10.1002/mus.23468     Document Type: Article
Times cited : (12)

References (39)
  • 1
    • 0023614188 scopus 로고
    • Dystrophin: the protein product of the Duchenne muscular dystrophy locus
    • Hoffman EP, Brown RH Jr, Kunkel LM. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 1987; 51: 919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown J, R.H.2    Kunkel r, L.M.3
  • 2
    • 0026419948 scopus 로고
    • The mdx mouse diaphragm reproduces the degenerative changes of Duchenne muscular dystrophy
    • Stedman HH, Sweeney HL, Shrager JB, Maguire HC, Panettieri RA, Petrof B, et al. The mdx mouse diaphragm reproduces the degenerative changes of Duchenne muscular dystrophy. Nature 1991; 352: 536-538.
    • (1991) Nature , vol.352 , pp. 536-538
    • Stedman, H.H.1    Sweeney, H.L.2    Shrager, J.B.3    Maguire, H.C.4    Panettieri, R.A.5    Petrof, B.6
  • 3
    • 0000801692 scopus 로고
    • Muscular dystrophies
    • In: Engel AG, Franzini-Armstrong C, editors. New York: McGraw-Hill.
    • Engel AG, Yamamoto M, Fischbeck KH. Muscular dystrophies. In: Engel AG, Franzini-Armstrong C, editors. Myology. New York: McGraw-Hill; 1994. p 1133-1187.
    • (1994) Myology , pp. 1133-1187
    • Engel, A.G.1    Yamamoto, M.2    Fischbeck, K.H.3
  • 4
    • 0029153067 scopus 로고
    • Expression of transforming growth factor-beta1 in dystrophic patient muscles correlates with fibrosis
    • Bernasconi P, Torchiana E, Confalonieri P, Brugnoni R, Barresi R, Mora M, et al. Expression of transforming growth factor-beta1 in dystrophic patient muscles correlates with fibrosis. J Clin Invest 1995; 96: 1137-1144.
    • (1995) J Clin Invest , vol.96 , pp. 1137-1144
    • Bernasconi, P.1    Torchiana, E.2    Confalonieri, P.3    Brugnoni, R.4    Barresi, R.5    Mora, M.6
  • 6
    • 36549043507 scopus 로고    scopus 로고
    • Altered extracellular matrix transcript expression and protein modulation in primary Duchenne muscular dystrophy myotubes
    • Zanotti S, Saredi S, Ruggieri A, Fabbri M, Blasevich F, Romaggi S, et al. Altered extracellular matrix transcript expression and protein modulation in primary Duchenne muscular dystrophy myotubes. Matrix Biol 2007; 26: 615-624.
    • (2007) Matrix Biol , vol.26 , pp. 615-624
    • Zanotti, S.1    Saredi, S.2    Ruggieri, A.3    Fabbri, M.4    Blasevich, F.5    Romaggi, S.6
  • 7
    • 0025375617 scopus 로고
    • Transforming growth factor-beta. Major role in regulation of extracellular matrix
    • Roberts AB, Heine UI, Flanders KC, Sporn MB. Transforming growth factor-beta. Major role in regulation of extracellular matrix. Ann N Y Acad Sci 1990; 580: 225-232.
    • (1990) Ann N Y Acad Sci , vol.580 , pp. 225-232
    • Roberts, A.B.1    Heine, U.I.2    Flanders, K.C.3    Sporn, M.B.4
  • 8
    • 77957669313 scopus 로고    scopus 로고
    • Regulation and dysregulation of fibrosis in skeletal muscle
    • Serrano AL, Munoz-Canoves P. Regulation and dysregulation of fibrosis in skeletal muscle. Exp Cell Res 2010; 316: 3050-3058.
    • (2010) Exp Cell Res , vol.316 , pp. 3050-3058
    • Serrano, A.L.1    Munoz-Canoves, P.2
  • 9
    • 0842326021 scopus 로고    scopus 로고
    • Matrix metalloproteinases and skeletal muscle: a brief review
    • Carmeli E, Moas M, Reznick AZ, Coleman R. Matrix metalloproteinases and skeletal muscle: a brief review. Muscle Nerve 2004; 29: 191-197.
    • (2004) Muscle Nerve , vol.29 , pp. 191-197
    • Carmeli, E.1    Moas, M.2    Reznick, A.Z.3    Coleman, R.4
  • 10
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001; 17: 463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 11
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: they're not just for matrix anymore!
    • McCawley LJ, Matrisian LM. Matrix metalloproteinases: they're not just for matrix anymore!. Curr Opin Cell Biol 2001;13: 534-540.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 12
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodeling
    • Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodeling. Nat Rev Mol Cell Biol 2007; 8: 221-233.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 13
    • 0035878554 scopus 로고    scopus 로고
    • Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex
    • Yamada H, Saito F, Fukuta-Ohi H, Zhong D, Hase A, Arai K, et al. Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex. Hum Mol Genet 2001; 10: 1563-1569.
    • (2001) Hum Mol Genet , vol.10 , pp. 1563-1569
    • Yamada, H.1    Saito, F.2    Fukuta-Ohi, H.3    Zhong, D.4    Hase, A.5    Arai, K.6
  • 15
    • 33646835580 scopus 로고    scopus 로고
    • Characterization of the protease activity that cleaves the extracellular domain of beta-dystroglycan
    • Zhong D, Saito F, Saito Y, Nakamura A, Shimizu T, Matsumura K. Characterization of the protease activity that cleaves the extracellular domain of beta-dystroglycan. Biochem Biophys Res Commun 2006; 345: 867-871.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 867-871
    • Zhong, D.1    Saito, F.2    Saito, Y.3    Nakamura, A.4    Shimizu, T.5    Matsumura, K.6
  • 19
    • 84956848860 scopus 로고
    • Observation on the isolated phrenic nerve diaphragm preparation of rat
    • Bulbring E. Observation on the isolated phrenic nerve diaphragm preparation of rat. Br J Pharmacol 1946; 1: 38-61.
    • (1946) Br J Pharmacol , vol.1 , pp. 38-61
    • Bulbring, E.1
  • 20
    • 0036217615 scopus 로고    scopus 로고
    • Mn(2+) ions reduce the enzymatic and pharmacological activities of bothropstoxin-I, a myotoxic Lys49 phospholipase A(2) homologue from Bothrops jararacussu snake venom
    • Soares AM, Oshima-Franco Y, Vieira CA, Leite GB, Fletcher JE, Jiang MS, et al. Mn(2+) ions reduce the enzymatic and pharmacological activities of bothropstoxin-I, a myotoxic Lys49 phospholipase A(2) homologue from Bothrops jararacussu snake venom. Int J Biochem Cell Biol 2002; 34: 668-677.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 668-677
    • Soares, A.M.1    Oshima-Franco, Y.2    Vieira, C.A.3    Leite, G.B.4    Fletcher, J.E.5    Jiang, M.S.6
  • 22
    • 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, Verdiere-Sahuque M, etal. Expression of matrix metalloproteinases 2 and 9 in regenerating skeletal muscle: a study in experimentally injured and mdx muscles. Dev Biol 1999; 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    Verdiere-Sahuque, M.6
  • 24
    • 33644979210 scopus 로고    scopus 로고
    • Variability and failure of neurotransmission in the diaphragm of mdx mice
    • Personius KE, Sawyer RP. Variability and failure of neurotransmission in the diaphragm of mdx mice. Neuromuscul Disord 2006; 16: 168-177.
    • (2006) Neuromuscul Disord , vol.16 , pp. 168-177
    • Personius, K.E.1    Sawyer, R.P.2
  • 25
    • 66149144404 scopus 로고    scopus 로고
    • Multiple pathological events in exercised dystrophic mdx are targeted by pentoxifylline: outcome of a large array of in vivo and ex vivo tests
    • Burdi R, Rolland JF, Fraysse B, Litvinova K, Cozzoli A, Giannuzzi V, et al. Multiple pathological events in exercised dystrophic mdx are targeted by pentoxifylline: outcome of a large array of in vivo and ex vivo tests. J Appl Physiol 2009; 106: 1311-1324.
    • (2009) J Appl Physiol , vol.106 , pp. 1311-1324
    • Burdi, R.1    Rolland, J.F.2    Fraysse, B.3    Litvinova, K.4    Cozzoli, A.5    Giannuzzi, V.6
  • 27
    • 34447620885 scopus 로고    scopus 로고
    • Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ)
    • Fukushima K, Nakamura A, Ueda H, Yuasa K, Yoshida K, Takeda S, et al. Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ). BMC Musculoskelet Disord 2007; 8: 54-64.
    • (2007) BMC Musculoskelet Disord , vol.8 , pp. 54-64
    • Fukushima, K.1    Nakamura, A.2    Ueda, H.3    Yuasa, K.4    Yoshida, K.5    Takeda, S.6
  • 28
    • 33947544175 scopus 로고    scopus 로고
    • Modulation of p38 mitogen-activated protein kinase cascade and metalloproteinase activity in diaphragm muscle in response to free radical scavenger administration in dystrophin-deficient mdx mice
    • Hnia K, Hugon G, Rivier F, Masmoudi A, Mercier J, Mornet D. Modulation of p38 mitogen-activated protein kinase cascade and metalloproteinase activity in diaphragm muscle in response to free radical scavenger administration in dystrophin-deficient mdx mice. Am J Pathol 2007; 170: 633-643.
    • (2007) Am J Pathol , vol.170 , pp. 633-643
    • Hnia, K.1    Hugon, G.2    Rivier, F.3    Masmoudi, A.4    Mercier, J.5    Mornet, D.6
  • 30
    • 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. Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum Mol Genet 2009; 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
  • 31
    • 33745088086 scopus 로고    scopus 로고
    • Rapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor
    • Gu BJ, Wiley JS. Rapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor. Blood 2006; 107: 4946-4953.
    • (2006) Blood , vol.107 , pp. 4946-4953
    • Gu, B.J.1    Wiley, J.S.2
  • 32
    • 44849127317 scopus 로고    scopus 로고
    • L-arginine decreases inflammation and modulates the nuclear factor-κB/matrix metalloproteinase cascade in mdx muscle fibers
    • Hnia K, Gayraud J, Hugon G, Ramonatxo M, De La Porte S, Matecki S, et al. L-arginine decreases inflammation and modulates the nuclear factor-κB/matrix metalloproteinase cascade in mdx muscle fibers. Am J Pathol 2008; 172: 1509-1519.
    • (2008) Am J Pathol , vol.172 , pp. 1509-1519
    • Hnia, K.1    Gayraud, J.2    Hugon, G.3    Ramonatxo, M.4    De La Porte, S.5    Matecki, S.6
  • 33
    • 78649716241 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 induces matrix metalloproteinase-9 and cell migration in astrocytes: roles of ROS-dependent ERK- and JNK- NF-κB pathways
    • Hsieh HL, Wang HH, Wu WB, Chu PJ, Yang CM. Transforming growth factor-beta1 induces matrix metalloproteinase-9 and cell migration in astrocytes: roles of ROS-dependent ERK- and JNK- NF-κB pathways. J Neuroinflammation 2010; 7: 88-104.
    • (2010) J Neuroinflammation , vol.7 , pp. 88-104
    • Hsieh, H.L.1    Wang, H.H.2    Wu, W.B.3    Chu, P.J.4    Yang, C.M.5
  • 34
    • 44249095380 scopus 로고    scopus 로고
    • Implications of cross-talk between tumour necrosis factor and insulin-like growth factor-1 signalling in skeletal muscle
    • Grounds MD, Radley HG, Gebski BL, Bogoyevitch MA, Shavlakadze T. Implications of cross-talk between tumour necrosis factor and insulin-like growth factor-1 signalling in skeletal muscle. Clin Exp Pharmacol Physiol 2008; 35: 846-851.
    • (2008) Clin Exp Pharmacol Physiol , vol.35 , pp. 846-851
    • Grounds, M.D.1    Radley, H.G.2    Gebski, B.L.3    Bogoyevitch, M.A.4    Shavlakadze, T.5
  • 35
    • 36348965906 scopus 로고    scopus 로고
    • Enhanced Na+/H+ exchange activity contributes to the pathogenesis of muscular dystrophy via involvement of P2 receptors
    • Iwata Y, Katanosaka Y, Hisamitsu T, Wakabayashi S. Enhanced Na+/H+ exchange activity contributes to the pathogenesis of muscular dystrophy via involvement of P2 receptors. Am J Pathol 2007; 171: 1576-1587.
    • (2007) Am J Pathol , vol.171 , pp. 1576-1587
    • Iwata, Y.1    Katanosaka, Y.2    Hisamitsu, T.3    Wakabayashi, S.4
  • 37
    • 78149469593 scopus 로고    scopus 로고
    • Improvement of the mdx mouse dystrophic phenotype by systemic in utero AAV8 delivery of a minidystrophin gene
    • Koppanati BM, Li J, Reay DP, Wang B, Daood M, Zheng H, et al. Improvement of the mdx mouse dystrophic phenotype by systemic in utero AAV8 delivery of a minidystrophin gene. Gene Ther 2010; 17: 1355-1362.
    • (2010) Gene Ther , vol.17 , pp. 1355-1362
    • Koppanati, B.M.1    Li, J.2    Reay, D.P.3    Wang, B.4    Daood, M.5    Zheng, H.6
  • 38
    • 35948937145 scopus 로고    scopus 로고
    • Distribution of suramin, an antitrypanosomal drug, across the blood-brain and blood-cerebrospinal fluid interfaces in wild-type and P-glycoprotein transporter-deficient mice
    • Sanderson L, Khan A, Thomas S. Distribution of suramin, an antitrypanosomal drug, across the blood-brain and blood-cerebrospinal fluid interfaces in wild-type and P-glycoprotein transporter-deficient mice. Antimicrob Agents Chemother 2007; 51: 3136-3146.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 3136-3146
    • Sanderson, L.1    Khan, A.2    Thomas, S.3
  • 39
    • 77954582762 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor batimastat alleviates pathology and improves skeletal muscle function in dystrophin-deficient mdx mice
    • Kumar A, Bhatnagar S, Kumar A. Matrix metalloproteinase inhibitor batimastat alleviates pathology and improves skeletal muscle function in dystrophin-deficient mdx mice. Am J Pathol 2010; 177: 248-260.
    • (2010) Am J Pathol , vol.177 , pp. 248-260
    • Kumar, A.1    Bhatnagar, S.2    Kumar, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.