메뉴 건너뛰기




Volumn 119, Issue 18, 2006, Pages 3822-3832

Multifunctional roles of MT1-MMP in myofiber formation and morphostatic maintenance of skeletal muscle

Author keywords

ECM remodeling; MT1 MMP; Myogenesis; Myopathy

Indexed keywords

CELL MARKER; FIBRONECTIN; LAMININ; LAMININ 4; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE INHIBITOR; MEROSIN; UNCLASSIFIED DRUG;

EID: 33750325693     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.03158     Document Type: Article
Times cited : (108)

References (41)
  • 1
    • 0034839336 scopus 로고    scopus 로고
    • Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: A role in TGFbeta-dependent matrix deposition
    • Akimov, S. S. and Belkin, A. M. (2001). Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: a role in TGFbeta-dependent matrix deposition. J. Cell Sci. 114, 2989-3000.
    • (2001) J. Cell Sci. , vol.114 , pp. 2989-3000
    • Akimov, S.S.1    Belkin, A.M.2
  • 2
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker, A. H., Edwards, D. R. and Murphy, G. (2002). Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell Sci. 115, 3719-3727.
    • (2002) J. Cell Sci. , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 3
    • 0035947675 scopus 로고    scopus 로고
    • Matrix-dependent proteolysis of surface transglutarninase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    • Belkin, A. M., Akimov, S. S., Zaritskaya, L. S., Ratnikov, B. L, Deryugina, E. I. and Strongin, A. Y. (2001). Matrix-dependent proteolysis of surface transglutarninase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion. J. Biol. Chem. 276, 18415-18422.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18415-18422
    • Belkin, A.M.1    Akimov, S.S.2    Zaritskaya, L.S.3    Ratnikov, B.L.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 4
    • 0022614137 scopus 로고
    • A satellite cell mitogen from crushed adult muscle
    • Bischoff, P., (1986). A satellite cell mitogen from crushed adult muscle. Dev. Biol. 115, 140-147.
    • (1986) Dev. Biol. , vol.115 , pp. 140-147
    • Bischoff, P.1
  • 5
    • 0025869184 scopus 로고
    • Differential trans-activation of a muscle-specific enhancer by myogenic, helix-loop-helix proteins is separable from DNA binding
    • Chakraborty, T., Brennan, T. and Olson, E. (1991). Differential trans-activation of a muscle-specific enhancer by myogenic, helix-loop-helix proteins is separable from DNA binding. J. Biol. Chem. 266, 2878-2882.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2878-2882
    • Chakraborty, T.1    Brennan, T.2    Olson, E.3
  • 6
    • 0017600299 scopus 로고
    • Alteration in cell surface LETS protein during myogenesis
    • Chen, L. B. (1977). Alteration in cell surface LETS protein during myogenesis. Cell 10, 393-400.
    • (1977) Cell , vol.10 , pp. 393-400
    • Chen, L.B.1
  • 7
    • 0033814140 scopus 로고    scopus 로고
    • Molecular basis of muscular dystrophies
    • Cohn, R. D. and Campbell, K. P. (2000). Molecular basis of muscular dystrophies. Muscle Nerve 23, 1456-1471.
    • (2000) Muscle Nerve , vol.23 , pp. 1456-1471
    • Cohn, R.D.1    Campbell, K.P.2
  • 8
    • 0032841707 scopus 로고    scopus 로고
    • In vivo satellite cell activation via Myf5 and MyoD in regenerating mouse skeletal muscle
    • Cooper, R. N., Tajbakhsh, S., Mouly, V., Cossu, G., Buckingham, M. and Butler-Browne, G. S. (1999). In vivo satellite cell activation via Myf5 and MyoD in regenerating mouse skeletal muscle. J. Cell Sci. 112, 2895-2901.
    • (1999) J. Cell Sci. , vol.112 , pp. 2895-2901
    • Cooper, R.N.1    Tajbakhsh, S.2    Mouly, V.3    Cossu, G.4    Buckingham, M.5    Butler-Browne, G.S.6
  • 9
    • 0020689882 scopus 로고
    • Rat myoblast fusion requires metalloendoprotease activity
    • Couch, C. B. and Strittinatter, W. J. (1983). Rat myoblast fusion requires metalloendoprotease activity. Cell 32, 257-265.
    • (1983) Cell , vol.32 , pp. 257-265
    • Couch, C.B.1    Strittinatter, W.J.2
  • 10
    • 0028556710 scopus 로고
    • Control of skeletal muscle-specific transcription: Involvement of paired homeodomain and MADS domain transcription factors
    • Duprey, P. and Lesens, C. (1994). Control of skeletal muscle-specific transcription: involvement of paired homeodomain and MADS domain transcription factors. Int. J. Dev. Biol. 38, 591-604.
    • (1994) Int. J. Dev. Biol. , vol.38 , pp. 591-604
    • Duprey, P.1    Lesens, C.2
  • 11
  • 12
    • 0023234520 scopus 로고
    • A laminin substrate promotes myogenesis in rat skeletal muscle cultures: Analysis of replication and development using antidesmin and anti-BrdUrd monoclonal antibodies
    • Foster, R. F., Thompson, I M. and Kaufman, S. I (1987). A laminin substrate promotes myogenesis in rat skeletal muscle cultures: analysis of replication and development using antidesmin and anti-BrdUrd monoclonal antibodies. Dev. Biol. 122, 11-20.
    • (1987) Dev. Biol. , vol.122 , pp. 11-20
    • Foster, R.F.1    Thompson, I.M.2    Kaufman, S.I.3
  • 13
    • 0029127225 scopus 로고
    • Analysis of fibronectin and vitronectin receptors on human fetal skeletal muscle cells upon differentiation
    • Gullberg, D., Sjoberg, G., Velling, T. and Sejersen, T. (1995). Analysis of fibronectin and vitronectin receptors on human fetal skeletal muscle cells upon differentiation. Exp. Cell Res. 220, 112-123.
    • (1995) Exp. Cell Res. , vol.220 , pp. 112-123
    • Gullberg, D.1    Sjoberg, G.2    Velling, T.3    Sejersen, T.4
  • 15
    • 0035195785 scopus 로고    scopus 로고
    • Skeletal muscle cell hypertrophy induced by inhibitors of metalloproteases; myostatin as a potential mediator
    • Huet, C., Li, Z. E, Liu, H. Z., Black, R. A., Galliano, M. R and Engvall, E. (2001). Skeletal muscle cell hypertrophy induced by inhibitors of metalloproteases; myostatin as a potential mediator. Am. J. Physiol. Cell Physiol. 281, C1624-C1634.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Huet, C.1    Li, Z.E.2    Liu, H.Z.3    Black, R.A.4    Galliano, M.R.5    Engvall, E.6
  • 16
    • 28444454893 scopus 로고    scopus 로고
    • MT1-NUVIP: A potent modifier of pericellular microenvironment
    • Itoh, Y. and Seiki, M. (2006). MT1-NUVIP: A potent modifier of pericellular microenvironment. J. Cell Physiol. 206, 1-8.
    • (2006) J. Cell Physiol. , vol.206 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 17
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type I matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita, M., Rob, Y., Chiba, T., Mori, H., Okada, A., Kinoh, H. and Seiki, M. (2001). Membrane-type I matrix metalloproteinase cleaves CD44 and promotes cell migration. J. Cell Biol. 153, 893-904.
    • (2001) J. Cell Biol. , vol.153 , pp. 893-904
    • Kajita, M.1    Rob, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 18
    • 0032947765 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases 2 and 9 in regenerating skeletal muscle: A study in experimentally injured and rndx muscles
    • Kherif, S., Lafuma, C., Dehoupas, M., Lachkar, S., Fournier, J. G., Verdiere-Sahuque, M., Fardeau, M. and Alarneddine, H. S. (1999). Expression of matrix metalloproteinases 2 and 9 in regenerating skeletal muscle: a study in experimentally injured and rndx muscles. Dev. Biol. 205, 158-170.
    • (1999) Dev. Biol. , vol.205 , pp. 158-170
    • Kherif, S.1    Lafuma, C.2    Dehoupas, M.3    Lachkar, S.4    Fournier, J.G.5    Verdiere-Sahuque, M.6    Fardeau, M.7    Alarneddine, H.S.8
  • 19
    • 25844498774 scopus 로고    scopus 로고
    • Regulation of TIMP-2, MT1-MMP, and MMP-2 expression during C2C12 differentiation
    • Lluri, G. and Jaworski, D. M. (2005). Regulation of TIMP-2, MT1-MMP, and MMP-2 expression during C2C12 differentiation. Muscle Nerve 32, 492-499.
    • (2005) Muscle Nerve , vol.32 , pp. 492-499
    • Lluri, G.1    Jaworski, D.M.2
  • 20
    • 13044258437 scopus 로고    scopus 로고
    • MyoR: A muscle-restricted basic helix-loop-helix transcription factor that antagonizes the actions of MyoD
    • Lu, J., Webb, R., Richardson, I A. and Olson, E. N. (1999). MyoR: a muscle-restricted basic helix-loop-helix transcription factor that antagonizes the actions of MyoD. Proc. Natl. Acad Sci. USA 96, 552-557.
    • (1999) Proc. Natl. Acad Sci. USA , vol.96 , pp. 552-557
    • Lu, J.1    Webb, R.2    Richardson, I.A.3    Olson, E.N.4
  • 21
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • Mott, J D. and Werb, Z. (2004). Regulation of matrix biology by matrix metalloproteinases. Curr. Opin. Cell Biol. 16, 558-564.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 22
    • 0027297310 scopus 로고
    • Myogenin gene disruption results in perinatal lethality because of severe muscle defect
    • Nabeshima, Y., Hanaoka, K., Hayasaka, M., Esumi, E., Li, S. and Nonaka, I. (1993). Myogenin gene disruption results in perinatal lethality because of severe muscle defect. Nature 364, 532-535.
    • (1993) Nature , vol.364 , pp. 532-535
    • Nabeshima, Y.1    Hanaoka, K.2    Hayasaka, M.3    Esumi, E.4    Li, S.5    Nonaka, I.6
  • 23
    • 0032705145 scopus 로고    scopus 로고
    • UEF2: A transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation
    • Naya, F. S. and Olson, E. (1999). UEF2: a transcriptional target for signaling pathways controlling skeletal muscle growth and differentiation. Curr. Opin. Cell Biol. 11, 683-688.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 683-688
    • Naya, F.S.1    Olson, E.2
  • 24
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi, E., Imai, K., Fujii, Y., Sato, H., Seikii, M. and Okada, Y. (1997). Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272, 2446-2451.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seikii, M.5    Okada, Y.6
  • 25
    • 0025616093 scopus 로고
    • Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties
    • Okada, Y., Morodomi, T., Enghild, J. J., Suzuki, K., Yasul, A., Nakanishi, I., Salvesen, G. and Nagase, H. (1990). Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194, 721-730.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 721-730
    • Okada, Y.1    Morodomi, T.2    Enghild, J.J.3    Suzuki, K.4    Yasul, A.5    Nakanishi, I.6    Salvesen, G.7    Nagase, H.8
  • 26
    • 2642546699 scopus 로고    scopus 로고
    • Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MTI-NRAP)
    • Osenkowski, P., Toth, M. and Fridman, R. (2004). Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MTI-NRAP). J. Cell Physiol. 200, 2-10.
    • (2004) J. Cell Physiol. , vol.200 , pp. 2-10
    • Osenkowski, P.1    Toth, M.2    Fridman, R.3
  • 27
    • 0036086733 scopus 로고    scopus 로고
    • ECM is required for skeletal muscle differentiation independently of muscle regulatory factor expression
    • Osses, N. and Brandan, E. (2002). ECM is required for skeletal muscle differentiation independently of muscle regulatory factor expression. Am. J. Physiol. Cell Physiol. 282, C383-C394.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Osses, N.1    Brandan, E.2
  • 29
    • 0022413114 scopus 로고
    • Extracellular matrix (ECM) synthesis in muscle cell cultures: Quantitative and qualitative studies during myogenesis
    • Rao, J. S., Beach, R. L. and Festoff, B. W. (1985). Extracellular matrix (ECM) synthesis in muscle cell cultures: quantitative and qualitative studies during myogenesis. Biochem. Biophys. Res. Commun. 130, 440-446.
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 440-446
    • Rao, J.S.1    Beach, R.L.2    Festoff, B.W.3
  • 30
    • 0029257376 scopus 로고
    • The MyoD family of transcription factors and skeletal myogenesis
    • Rudnicki, M. A. and Jaenisch, R. (1995). ne Myol) family of transcription factors and skeletal myogenesis. BioEssays 17, 203-209.
    • (1995) BioEssays , vol.17 , pp. 203-209
    • Rudnicki, M.A.1    Jaenisch, R.2
  • 31
    • 0033594107 scopus 로고    scopus 로고
    • Quantitative changes in integrin and focal adhesion signaling regulate myoblast cell cycle withdrawal
    • Sastry, S. K., Lakonishok, M., Wu, S., Truong, T. Q., Huttenlocher, A., Turner, C. E. and Horwitz, A. F. (1999). Quantitative changes in integrin and focal adhesion signaling regulate myoblast cell cycle withdrawal. J. Cell Biol. 144, 1295-1309.
    • (1999) J. Cell Biol. , vol.144 , pp. 1295-1309
    • Sastry, S.K.1    Lakonishok, M.2    Wu, S.3    Truong, T.Q.4    Huttenlocher, A.5    Turner, C.E.6    Horwitz, A.F.7
  • 32
    • 0022271052 scopus 로고
    • Response of satellite cells to focal skeletal muscle injury
    • Schultz, E., Jaryszak, D. L. and Valliere, C. R. (1985). Response of satellite cells to focal skeletal muscle injury. Muscle Nerve 8, 217-222.
    • (1985) Muscle Nerve , vol.8 , pp. 217-222
    • Schultz, E.1    Jaryszak, D.L.2    Valliere, C.R.3
  • 34
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion
    • Seiki, M. (2003). Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion. Cancer Lett. 194, 1 -11.
    • (2003) Cancer Lett. , vol.194 , pp. 1-11
    • Seiki, M.1
  • 36
    • 0035945354 scopus 로고    scopus 로고
    • Cytoplasmic tail-dependent internalization of membrane-type I matrix metalloproteinase is important for its invasion-promoting activity
    • Uekita, T., Rob, Y., Yana, I., Ohno, H. and Seiki, M. (2001). Cytoplasmic tail-dependent internalization of membrane-type I matrix metalloproteinase is important for its invasion-promoting activity. J. Cell Biol. 155, 1345-1356.
    • (2001) J. Cell Biol. , vol.155 , pp. 1345-1356
    • Uekita, T.1    Rob, Y.2    Yana, I.3    Ohno, H.4    Seiki, M.5
  • 37
    • 0030465319 scopus 로고    scopus 로고
    • Merosin/lammin-2 and muscular dystrophy
    • Wewer, U. M. and Engvall, E. (1996). Merosin/lammin-2 and muscular dystrophy. Neuromuscul. Disord. 6, 409-418.
    • (1996) Neuromuscul. Disord. , vol.6 , pp. 409-418
    • Wewer, U.M.1    Engvall, E.2
  • 38
    • 0033023377 scopus 로고    scopus 로고
    • An E-box within the MHC IlB gene is bound by MyoD and is required for gene expression in fast muscle
    • Wheeler, M. T., Snyder, E. C., Patterson, M. N. and Swoap, S. 1 (1999). An E-box within the MHC IlB gene is bound by MyoD and is required for gene expression in fast muscle. Am. J. Physiol. 276, C1069-C1078.
    • (1999) Am. J. Physiol. , vol.276
    • Wheeler, M.T.1    Snyder, E.C.2    Patterson, M.N.3    Swoap, S.4
  • 39
    • 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., Aral, K., Okuyarna, A., Maekawa, R., Shimizu, T. and Matsumura, K. (2001). Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex. Hum. Mol. Genet. 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    Aral, K.6    Okuyarna, A.7    Maekawa, R.8    Shimizu, T.9    Matsumura, K.10
  • 40
    • 0034643284 scopus 로고    scopus 로고
    • Expression of myostatin gene in regenerating skeletal muscle of the rat and its localization
    • Yamanouchi, K., Soeta, C., Naito, K. and Tojo, H. (2000). Expression of myostatin gene in regenerating skeletal muscle of the rat and its localization. Biochem. Biophys. Res. Commun. 270, 510-516.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 510-516
    • Yamanouchi, K.1    Soeta, C.2    Naito, K.3    Tojo, H.4
  • 41
    • 0030945778 scopus 로고    scopus 로고
    • MRF4 can substitute for myogenin during early stages of myogenesis
    • Zhu, Z. and Miller, J. B. (1997). MRF4 can substitute for myogenin during early stages of myogenesis. Dev. Dyn. 209, 233-241.
    • (1997) Dev. Dyn. , vol.209 , pp. 233-241
    • Zhu, Z.1    Miller, J.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.