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Volumn 90, Issue 2-3, 2011, Pages 249-260

Upregulation of paxillin and focal adhesion signaling follows Dystroglycan Complex deletions and promotes a hypertensive state of differentiation

Author keywords

Adhesion; Contractility; Differentiation; Glucocorticoid; Hypertensive; Muscular dystrophy; Paxillin

Indexed keywords

DYSTROGLYCAN; FOCAL ADHESION KINASE; MITOGEN ACTIVATED PROTEIN KINASE; MUTANT PROTEIN; MYOSIN II; PAXILLIN; VINCULIN;

EID: 79151469576     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2010.06.005     Document Type: Article
Times cited : (21)

References (78)
  • 1
    • 4444306357 scopus 로고    scopus 로고
    • Genetic compensation for sarcoglycan loss by integrin {alpha}7{beta}1 in muscle
    • Allikian M.J., Hack A.A., Mewborn S., Mayer U., McNally E.M. Genetic compensation for sarcoglycan loss by integrin {alpha}7{beta}1 in muscle. J. Cell Sci. 2004, 117:3821-3830.
    • (2004) J. Cell Sci. , vol.117 , pp. 3821-3830
    • Allikian, M.J.1    Hack, A.A.2    Mewborn, S.3    Mayer, U.4    McNally, E.M.5
  • 3
    • 0036823748 scopus 로고    scopus 로고
    • A web-accessible complete transcriptome of normal human and DMD muscle
    • Bakay M.Z.P., Chen J., Hoffman E.P. A web-accessible complete transcriptome of normal human and DMD muscle. Neuromuscul. Disord. 2002, Suppl. 1:S125-S141.
    • (2002) Neuromuscul. Disord. , Issue.SUPPL. 1
    • Bakay, M.Z.P.1    Chen, J.2    Hoffman, E.P.3
  • 4
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: adapting to change
    • Brown M.C., Turner C.E. Paxillin: adapting to change. Physiol. Rev. 2004, 84:1315-1339.
    • (2004) Physiol. Rev. , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 5
    • 11144231268 scopus 로고    scopus 로고
    • Transgenic expression of {alpha}7{beta}1 integrin maintains muscle integrity, increases regenerative capacity, promotes hypertrophy, and reduces cardiomyopathy in dystrophic mice
    • Burkin D.J., Wallace G.Q., Milner D.J., Chaney E.J., Mulligan J.A., Kaufman S.J. Transgenic expression of {alpha}7{beta}1 integrin maintains muscle integrity, increases regenerative capacity, promotes hypertrophy, and reduces cardiomyopathy in dystrophic mice. Am. J. Pathol. 2005, 166:253-263.
    • (2005) Am. J. Pathol. , vol.166 , pp. 253-263
    • Burkin, D.J.1    Wallace, G.Q.2    Milner, D.J.3    Chaney, E.J.4    Mulligan, J.A.5    Kaufman, S.J.6
  • 6
    • 0028914964 scopus 로고
    • Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage
    • Campbell K.P. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 1995, 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 7
    • 33747165320 scopus 로고    scopus 로고
    • Homozygous mutation of focal adhesion kinase in embryonic stem cell derived neurons: normal electrophysiological and morphological properties in vitro
    • Charlesworth P., Komiyama N.H., Grant S.G. Homozygous mutation of focal adhesion kinase in embryonic stem cell derived neurons: normal electrophysiological and morphological properties in vitro. BMC Neurosci. 2006, 7:47-57.
    • (2006) BMC Neurosci. , vol.7 , pp. 47-57
    • Charlesworth, P.1    Komiyama, N.H.2    Grant, S.G.3
  • 8
    • 0033814140 scopus 로고    scopus 로고
    • Molecular basis of muscular dystrophies
    • Cohn R.D., Campbell K.P. Molecular basis of muscular dystrophies. Muscle Nerve 2000, 23:1456-1471.
    • (2000) Muscle Nerve , vol.23 , pp. 1456-1471
    • Cohn, R.D.1    Campbell, K.P.2
  • 9
    • 0036783749 scopus 로고    scopus 로고
    • Apparent elastic modulus and hysteresis of skeletal muscle cells throughout differentiation
    • Collinsworth A.M., Zhang S., Kraus W.E., Truskey G.A. Apparent elastic modulus and hysteresis of skeletal muscle cells throughout differentiation. Am. J. Physiol. Cell Physiol. 2002, 283:C1219-C1227.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.283
    • Collinsworth, A.M.1    Zhang, S.2    Kraus, W.E.3    Truskey, G.A.4
  • 10
    • 25144454071 scopus 로고    scopus 로고
    • Eosinophil adhesion under flow conditions activates mechanosensitive signaling pathways in human endothelial cells
    • Cuvelier S.L., Paul S., Shariat N., Colarusso P., Patel K.D. Eosinophil adhesion under flow conditions activates mechanosensitive signaling pathways in human endothelial cells. J. Exp. Med. 2005, 202:865-876.
    • (2005) J. Exp. Med. , vol.202 , pp. 865-876
    • Cuvelier, S.L.1    Paul, S.2    Shariat, N.3    Colarusso, P.4    Patel, K.D.5
  • 11
    • 33646768213 scopus 로고    scopus 로고
    • Potentiation of a survival signal in the ischemic heart by resveratrol through p38 mitogen-activated protein kinase/mitogen- and stress-activated protein kinase 1/cAMP response element-binding protein signaling
    • Das S., Tosaki A., Bagchi D., Maulik N., Das D.K. Potentiation of a survival signal in the ischemic heart by resveratrol through p38 mitogen-activated protein kinase/mitogen- and stress-activated protein kinase 1/cAMP response element-binding protein signaling. J. Pharmacol. Exp. Ther. 2006, 317:980-988.
    • (2006) J. Pharmacol. Exp. Ther. , vol.317 , pp. 980-988
    • Das, S.1    Tosaki, A.2    Bagchi, D.3    Maulik, N.4    Das, D.K.5
  • 12
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • Discher D.E., Janmey P., Wang Y.L. Tissue cells feel and respond to the stiffness of their substrate. Science 2005, 310:1139-1143.
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.L.3
  • 14
    • 4544264684 scopus 로고    scopus 로고
    • Myotubes differentiate optimally on substrates with tissue-like stiffness: pathological implications for soft or stiff microenvironments
    • Engler A.J., Griffin M.A., Sen S., Bonnemann C.G., Sweeney H.L., Discher D.E. Myotubes differentiate optimally on substrates with tissue-like stiffness: pathological implications for soft or stiff microenvironments. J. Cell Biol. 2004, 166:877-887.
    • (2004) J. Cell Biol. , vol.166 , pp. 877-887
    • Engler, A.J.1    Griffin, M.A.2    Sen, S.3    Bonnemann, C.G.4    Sweeney, H.L.5    Discher, D.E.6
  • 17
    • 0032810190 scopus 로고    scopus 로고
    • Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle
    • Fluck M., Carson J.A., Gordon S.E., Ziemiecki A., Booth F.W. Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle. Am. J. Physiol. 1999, 277:152-162.
    • (1999) Am. J. Physiol. , vol.277 , pp. 152-162
    • Fluck, M.1    Carson, J.A.2    Gordon, S.E.3    Ziemiecki, A.4    Booth, F.W.5
  • 18
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta Y., Ilic D., Kanazawa S., Takeda N., Yamamoto T., Aizawa S. Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene 1995, 11:1989-1995.
    • (1995) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 21
    • 17844404025 scopus 로고    scopus 로고
    • {gamma}-Sarcoglycan deficiency increases cell contractility, apoptosis and MAPK pathway activation but does not affect adhesion
    • Griffin M.A., Feng H., Tewari M., Acosta P., Kawana M., Sweeney H.L., Discher D.E. {gamma}-Sarcoglycan deficiency increases cell contractility, apoptosis and MAPK pathway activation but does not affect adhesion. J. Cell Sci. 2005, 118:1405-1416.
    • (2005) J. Cell Sci. , vol.118 , pp. 1405-1416
    • Griffin, M.A.1    Feng, H.2    Tewari, M.3    Acosta, P.4    Kawana, M.5    Sweeney, H.L.6    Discher, D.E.7
  • 22
    • 12344318545 scopus 로고    scopus 로고
    • Adhesion-contractile balance in myocyte differentiation
    • Griffin M.A., Sen S., Sweeney H.L., Discher D.E. Adhesion-contractile balance in myocyte differentiation. J. Cell Sci. 2004, 117:5855-5863.
    • (2004) J. Cell Sci. , vol.117 , pp. 5855-5863
    • Griffin, M.A.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 23
    • 0036142219 scopus 로고    scopus 로고
    • The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling
    • Hagel M., George E.L., Kim A., Tamimi R., Opitz S.L., Turner C.E., Imamoto A., Thomas S.M. The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol. Cell. Biol. 2002, 22:901-915.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 901-915
    • Hagel, M.1    George, E.L.2    Kim, A.3    Tamimi, R.4    Opitz, S.L.5    Turner, C.E.6    Imamoto, A.7    Thomas, S.M.8
  • 26
    • 4344621091 scopus 로고    scopus 로고
    • Sequential activation of RhoA and FAK/paxillin leads to ATP release and actin reorganization in human endothelium
    • Hirakawa M., Oike M., Karashima Y., Ito Y. Sequential activation of RhoA and FAK/paxillin leads to ATP release and actin reorganization in human endothelium. J. Physiol. (Lond.) 2004, 558:479-488.
    • (2004) J. Physiol. (Lond.) , vol.558 , pp. 479-488
    • Hirakawa, M.1    Oike, M.2    Karashima, Y.3    Ito, Y.4
  • 27
    • 0030809116 scopus 로고    scopus 로고
    • Altered expression of the alpha7beta1 integrin in human and murine muscular dystrophies
    • Hodges B.L., Hayashi Y.K., Nonaka I., Wang W., Arahata K., Kaufman S.J. Altered expression of the alpha7beta1 integrin in human and murine muscular dystrophies. J. Cell Sci. 1997, 110:2873-2881.
    • (1997) J. Cell Sci. , vol.110 , pp. 2873-2881
    • Hodges, B.L.1    Hayashi, Y.K.2    Nonaka, I.3    Wang, W.4    Arahata, K.5    Kaufman, S.J.6
  • 31
    • 0347915657 scopus 로고    scopus 로고
    • Loss of dystrophin causes aberrant mechanotransduction in skeletal muscle fibers
    • Kumar A., Khandelwal N., Malya R., Reid M.B., Boriek A.M. Loss of dystrophin causes aberrant mechanotransduction in skeletal muscle fibers. FASEB J. 2004, 18:102-113.
    • (2004) FASEB J. , vol.18 , pp. 102-113
    • Kumar, A.1    Khandelwal, N.2    Malya, R.3    Reid, M.B.4    Boriek, A.M.5
  • 32
    • 0028264218 scopus 로고
    • Talin, vinculin and DRP (utrophin) concentrations are increased at mdx myotendinous junctions following onset of necrosis
    • Law D.J., Allen D.L., Tidball J.G. Talin, vinculin and DRP (utrophin) concentrations are increased at mdx myotendinous junctions following onset of necrosis. J. Cell Sci. 1994, 107(Pt 6):1477-1483.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 6 , pp. 1477-1483
    • Law, D.J.1    Allen, D.L.2    Tidball, J.G.3
  • 33
    • 33644901594 scopus 로고    scopus 로고
    • Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells
    • Lele T.P., Pendse J., Kumar S., Salanga M., Karavitis J., Ingber D.E. Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells. J. Cell. Physiol. 2006, 207:187-194.
    • (2006) J. Cell. Physiol. , vol.207 , pp. 187-194
    • Lele, T.P.1    Pendse, J.2    Kumar, S.3    Salanga, M.4    Karavitis, J.5    Ingber, D.E.6
  • 34
    • 0031722943 scopus 로고    scopus 로고
    • The sarcoglycan complex in limb-girdle muscular dystrophy
    • Lim L.E., Campbell K.P. The sarcoglycan complex in limb-girdle muscular dystrophy. Curr. Opin. Neurol. 1998, 11:443-452.
    • (1998) Curr. Opin. Neurol. , vol.11 , pp. 443-452
    • Lim, L.E.1    Campbell, K.P.2
  • 35
    • 12344311038 scopus 로고    scopus 로고
    • Focal adhesion kinase antisense oligodeoxynucleotides inhibit human pulmonary artery smooth muscle cells proliferation and promote human pulmonary artery smooth muscle cells apoptosis
    • Lin C.L., Zhang Z.X., Xu Y.J., Ni W., Chen S.X. Focal adhesion kinase antisense oligodeoxynucleotides inhibit human pulmonary artery smooth muscle cells proliferation and promote human pulmonary artery smooth muscle cells apoptosis. Chin. Med. J. (Engl.) 2005, 118(1):20-26.
    • (2005) Chin. Med. J. (Engl.) , vol.118 , Issue.1 , pp. 20-26
    • Lin, C.L.1    Zhang, Z.X.2    Xu, Y.J.3    Ni, W.4    Chen, S.X.5
  • 36
    • 0842344627 scopus 로고    scopus 로고
    • The mechanism of the force response to stretch in human skinned muscle fibres with different myosin isoforms
    • Linari M., Pellegrino B.R., Reconditi M.A., Reggiani M., Lombardi C. The mechanism of the force response to stretch in human skinned muscle fibres with different myosin isoforms. J. Physiol. 2004, 554(Pt 2):335-352.
    • (2004) J. Physiol. , vol.554 , Issue.PART 2 , pp. 335-352
    • Linari, M.1    Pellegrino, B.R.2    Reconditi, M.A.3    Reggiani, M.4    Lombardi, C.5
  • 38
    • 7244229657 scopus 로고    scopus 로고
    • Hyperosmotic stress induces rapid focal adhesion kinase phosphorylation at tyrosines 397 and 577: role of Src family kinases and Rho family GTPases
    • Lunn J.A., Rozengurt E. Hyperosmotic stress induces rapid focal adhesion kinase phosphorylation at tyrosines 397 and 577: role of Src family kinases and Rho family GTPases. J. Biol. Chem. 2004, 279:45266-45278.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45266-45278
    • Lunn, J.A.1    Rozengurt, E.2
  • 39
    • 0022980637 scopus 로고
    • Formation and alignment of Z lines in living chick myotubes microinjected with rhodamine-labeled alpha-actinin
    • McKenna N.M., Johnson C.S., Wang Y.L. Formation and alignment of Z lines in living chick myotubes microinjected with rhodamine-labeled alpha-actinin. J. Cell Biol. 1986, 103:2163-2171.
    • (1986) J. Cell Biol. , vol.103 , pp. 2163-2171
    • McKenna, N.M.1    Johnson, C.S.2    Wang, Y.L.3
  • 40
    • 11144234830 scopus 로고    scopus 로고
    • Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillin
    • Melendez J., Turner C., Avraham H., Steinberg S.F., Schaefer E., Sussman M.A. Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillin. J. Biol. Chem. 2004, 279:53516-53523.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53516-53523
    • Melendez, J.1    Turner, C.2    Avraham, H.3    Steinberg, S.F.4    Schaefer, E.5    Sussman, M.A.6
  • 41
    • 9644266707 scopus 로고    scopus 로고
    • ERK1/2 regulates intracellular ATP levels through alpha-enolase expression in cardiomyocytes exposed to ischemic hypoxia and reoxygenation
    • Mizukami Y., Iwamatsu A., Aki T., Kimura M., Nakamura K., Nao T., Okusa T., Matsuzaki M., Yoshida K., Kobayashi S. ERK1/2 regulates intracellular ATP levels through alpha-enolase expression in cardiomyocytes exposed to ischemic hypoxia and reoxygenation. J. Biol. Chem. 2004, 279:50120-50131.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50120-50131
    • Mizukami, Y.1    Iwamatsu, A.2    Aki, T.3    Kimura, M.4    Nakamura, K.5    Nao, T.6    Okusa, T.7    Matsuzaki, M.8    Yoshida, K.9    Kobayashi, S.10
  • 43
    • 0142249452 scopus 로고    scopus 로고
    • Microtubule assembly in cultured myoblasts and myotubes following nocodazole induced microtubule depolymerisation
    • Musa H., Orton C., Morrison E.E., Peckham M. Microtubule assembly in cultured myoblasts and myotubes following nocodazole induced microtubule depolymerisation. J. Muscle Res. Cell Motil. 2003, 24:301-308.
    • (2003) J. Muscle Res. Cell Motil. , vol.24 , pp. 301-308
    • Musa, H.1    Orton, C.2    Morrison, E.E.3    Peckham, M.4
  • 44
    • 0036894605 scopus 로고    scopus 로고
    • A role for dystroglycan in epithelial polarization: loss of function in breast tumor cells
    • Muschler J., Levy D., Boudreau R., Henry M., Campbell K., Bissell M.J. A role for dystroglycan in epithelial polarization: loss of function in breast tumor cells. Cancer Res. 2002, 62:7102-7109.
    • (2002) Cancer Res. , vol.62 , pp. 7102-7109
    • Muschler, J.1    Levy, D.2    Boudreau, R.3    Henry, M.4    Campbell, K.5    Bissell, M.J.6
  • 45
    • 8744224517 scopus 로고    scopus 로고
    • Inactivation of Rho/ROCK signaling is crucial for the nuclear accumulation of FKHR and myoblast fusion
    • Nishiyama T., Kii I., Kudo A. Inactivation of Rho/ROCK signaling is crucial for the nuclear accumulation of FKHR and myoblast fusion. J. Biol. Chem. 2004, 279:47311-47319.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47311-47319
    • Nishiyama, T.1    Kii, I.2    Kudo, A.3
  • 46
    • 0842331443 scopus 로고    scopus 로고
    • Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling
    • Palazzo A.F., Eng C.H., Schlaepfer D.D., Marcantonio E.E., Gundersen G.G. Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling. Science 2004, 303:836-839.
    • (2004) Science , vol.303 , pp. 836-839
    • Palazzo, A.F.1    Eng, C.H.2    Schlaepfer, D.D.3    Marcantonio, E.E.4    Gundersen, G.G.5
  • 47
    • 25644445311 scopus 로고    scopus 로고
    • The role of Akt and mitogen-activated protein kinase systems in the protective effect of poly(ADP-ribose) polymerase inhibition in Langendorff perfused and in isoproterenol-damaged rat hearts
    • Palfi A., Toth A., Kulcsar G., Hanto K., Deres P., Bartha E., Halmosi R., Szabados E., Czopf L., Kalai T., Hideg K., Sumegi B., Toth K. The role of Akt and mitogen-activated protein kinase systems in the protective effect of poly(ADP-ribose) polymerase inhibition in Langendorff perfused and in isoproterenol-damaged rat hearts. J. Pharmacol. Exp. Ther. 2005, 315:273-282.
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 273-282
    • Palfi, A.1    Toth, A.2    Kulcsar, G.3    Hanto, K.4    Deres, P.5    Bartha, E.6    Halmosi, R.7    Szabados, E.8    Czopf, L.9    Kalai, T.10    Hideg, K.11    Sumegi, B.12    Toth, K.13
  • 48
    • 0036357414 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration
    • Panetti T.S. Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration. Front. Biosci. Rev. 2002, 7:143-150.
    • (2002) Front. Biosci. Rev. , vol.7 , pp. 143-150
    • Panetti, T.S.1
  • 49
    • 77949754056 scopus 로고    scopus 로고
    • Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation
    • Pasapera A.M., Schneider I.C., Rericha E., Schlaepfer D.D., Waterman C.M. Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation. J. Cell Biol. 2010, 188:877-890.
    • (2010) J. Cell Biol. , vol.188 , pp. 877-890
    • Pasapera, A.M.1    Schneider, I.C.2    Rericha, E.3    Schlaepfer, D.D.4    Waterman, C.M.5
  • 50
    • 0027230425 scopus 로고
    • Prednisolone enhances myogenesis and dystrophin-related protein in skeletal muscle cell cultures from mdx mouse
    • Passaquin A.C., Metzinger L., Leger J.J., Warter J.M., Poindron P. Prednisolone enhances myogenesis and dystrophin-related protein in skeletal muscle cell cultures from mdx mouse. J. Neurosci. Res. 1993, 35:363-372.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 363-372
    • Passaquin, A.C.1    Metzinger, L.2    Leger, J.J.3    Warter, J.M.4    Poindron, P.5
  • 51
    • 0344912596 scopus 로고    scopus 로고
    • Cell locomotion and focal adhesions are regulated by substrate flexibility
    • Pelham R.J., Wang Y. Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:13661-13665.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13661-13665
    • Pelham, R.J.1    Wang, Y.2
  • 53
    • 27744465686 scopus 로고    scopus 로고
    • Microtubule-dependent transport and organization of sarcomeric myosin during skeletal muscle differentiation
    • Pizon V., Gerbal F., Diaz C.C., Karsenti E. Microtubule-dependent transport and organization of sarcomeric myosin during skeletal muscle differentiation. EMBO J. 2005, 24:3781-3792.
    • (2005) EMBO J. , vol.24 , pp. 3781-3792
    • Pizon, V.1    Gerbal, F.2    Diaz, C.C.3    Karsenti, E.4
  • 55
    • 0033514379 scopus 로고    scopus 로고
    • Dimensional and mechanical dynamics of active and stable edges in motile fibroblasts investigated by using atomic force microscopy
    • Rotsch C., Jacobson K., Radmacher M. Dimensional and mechanical dynamics of active and stable edges in motile fibroblasts investigated by using atomic force microscopy. PNAS 1999, 96:921-926.
    • (1999) PNAS , vol.96 , pp. 921-926
    • Rotsch, C.1    Jacobson, K.2    Radmacher, M.3
  • 57
    • 0345096662 scopus 로고    scopus 로고
    • Calcitonin gene-related peptide partly protects cultured smooth muscle cells from apoptosis induced by an oxidative stress via activation of ERK1/2 MAPK
    • Schaeffer C., Vandroux D., Thomassin L., Athias P., Rochette L., Connat J.L. Calcitonin gene-related peptide partly protects cultured smooth muscle cells from apoptosis induced by an oxidative stress via activation of ERK1/2 MAPK. Biochim. Biophys. Acta 2003, 1643:65-73.
    • (2003) Biochim. Biophys. Acta , vol.1643 , pp. 65-73
    • Schaeffer, C.1    Vandroux, D.2    Thomassin, L.3    Athias, P.4    Rochette, L.5    Connat, J.L.6
  • 59
    • 0031283362 scopus 로고    scopus 로고
    • Mechanotransduction and intracellular signaling mechanisms of stretch-induced remodeling in endothelial cells
    • Sokabe M., Naruse K., Sai S., Yamada T., Kawakami K., Inoue M., Murase K., Miyazu M. Mechanotransduction and intracellular signaling mechanisms of stretch-induced remodeling in endothelial cells. Heart Vessels Suppl. 1997, 12:191-193.
    • (1997) Heart Vessels Suppl. , vol.12 , pp. 191-193
    • Sokabe, M.1    Naruse, K.2    Sai, S.3    Yamada, T.4    Kawakami, K.5    Inoue, M.6    Murase, K.7    Miyazu, M.8
  • 61
    • 0030909575 scopus 로고    scopus 로고
    • Muscular dystrophies and the dystrophin-glycoprotein complex
    • Straub V., Campbell K.P. Muscular dystrophies and the dystrophin-glycoprotein complex. Curr. Opin. Neurol. 1997, 10:168-175.
    • (1997) Curr. Opin. Neurol. , vol.10 , pp. 168-175
    • Straub, V.1    Campbell, K.P.2
  • 62
    • 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., Hahn K.M. Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility. J. Cell Biol. 2004, 165:371-381.
    • (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
  • 63
    • 0032418076 scopus 로고    scopus 로고
    • Effect of long-term administration of prednisolone on serum creatine kinase and muscle pathology of mdx mouse
    • Takagi A., Watanabe T., Kojima S., Endo Y. Effect of long-term administration of prednisolone on serum creatine kinase and muscle pathology of mdx mouse. Rinsho Shinkeigaku 1998, 38:724-728.
    • (1998) Rinsho Shinkeigaku , vol.38 , pp. 724-728
    • Takagi, A.1    Watanabe, T.2    Kojima, S.3    Endo, Y.4
  • 64
    • 0037101563 scopus 로고    scopus 로고
    • The focal adhesion protein paxillin regulates contraction in canine tracheal smooth muscle
    • Tang D.D., Wu M.F., Opazo Saez A.M., Gunst S.J. The focal adhesion protein paxillin regulates contraction in canine tracheal smooth muscle. J. Physiol. 2002, 542:501-513.
    • (2002) J. Physiol. , vol.542 , pp. 501-513
    • Tang, D.D.1    Wu, M.F.2    Opazo Saez, A.M.3    Gunst, S.J.4
  • 66
    • 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., Sabe H. Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion and migration. J. Cell Biol. 2002, 159:673-683.
    • (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
  • 67
    • 0034529411 scopus 로고    scopus 로고
    • Paxillin interactions
    • Turner C.E. Paxillin interactions. J. Cell Sci. 2000, 113:4139-4140.
    • (2000) J. Cell Sci. , vol.113 , pp. 4139-4140
    • Turner, C.E.1
  • 68
    • 0035895915 scopus 로고    scopus 로고
    • Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules
    • van Horck F.P., Ahmadian M.R., Haeusler L.C., Moolenaar W.H., Kranenburg O. Characterization of p190RhoGEF, a RhoA-specific guanine nucleotide exchange factor that interacts with microtubules. J. Biol. Chem. 2001, 276:4948-4956.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4948-4956
    • van Horck, F.P.1    Ahmadian, M.R.2    Haeusler, L.C.3    Moolenaar, W.H.4    Kranenburg, O.5
  • 69
    • 0033538558 scopus 로고    scopus 로고
    • The effect of methylprednisolone on intracellular calcium of normal and dystrophic human skeletal muscle cells
    • Vandebrouck C., Imbert N., Duport G., Cognard C., Raymond G. The effect of methylprednisolone on intracellular calcium of normal and dystrophic human skeletal muscle cells. Neurosci. Lett. 1999, 269:110-114.
    • (1999) Neurosci. Lett. , vol.269 , pp. 110-114
    • Vandebrouck, C.1    Imbert, N.2    Duport, G.3    Cognard, C.4    Raymond, G.5
  • 71
    • 0141865507 scopus 로고    scopus 로고
    • Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2
    • von Wichert G., Haimovich B., Feng G.S., Sheetz M.P. Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2. EMBO J. 2003, 22:5023-5035.
    • (2003) EMBO J. , vol.22 , pp. 5023-5035
    • von Wichert, G.1    Haimovich, B.2    Feng, G.S.3    Sheetz, M.P.4
  • 73
    • 4344632582 scopus 로고    scopus 로고
    • Prednisolone decreases cellular adhesion molecules required for inflammatory cell infiltration in dystrophin-deficient skeletal muscle
    • Wehling-Henricks M., Lee J.J., Tidball J.G. Prednisolone decreases cellular adhesion molecules required for inflammatory cell infiltration in dystrophin-deficient skeletal muscle. Neuromuscul. Disord. 2004, 14:483-490.
    • (2004) Neuromuscul. Disord. , vol.14 , pp. 483-490
    • Wehling-Henricks, M.1    Lee, J.J.2    Tidball, J.G.3
  • 74
    • 33746820549 scopus 로고    scopus 로고
    • Heat shock-induced cardioprotection activates cytoskeletal-based cell survival pathways
    • Wei H., Campbell W., Vander Heide R.S. Heat shock-induced cardioprotection activates cytoskeletal-based cell survival pathways. Am. J. Physiol. Heart Circ. Physiol. 2006, 291:H638-647.
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.291
    • Wei, H.1    Campbell, W.2    Vander Heide, R.S.3
  • 75
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W., Baribault H., Adamson E.D. Vinculin knockout results in heart and brain defects during embryonic development. Development 1998, 125:327-337.
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 76
    • 0030210726 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of pp125FAK and paxillin in aortic endothelial cells induced by mechanical strain
    • Yano Y., Geibel J., Sumpio B.E. Tyrosine phosphorylation of pp125FAK and paxillin in aortic endothelial cells induced by mechanical strain. Am. J. Physiol. 1996, 271:C635-649.
    • (1996) Am. J. Physiol. , vol.271
    • Yano, Y.1    Geibel, J.2    Sumpio, B.E.3
  • 77
    • 0031939073 scopus 로고    scopus 로고
    • Bidirectional signaling between sarcoglycans and the integrin adhesion system in cultured L6 myocytes
    • Yoshida T., Pan Y., Hanada H., Iwata Y., Shigekawa M. Bidirectional signaling between sarcoglycans and the integrin adhesion system in cultured L6 myocytes. J. Biol. Chem. 1998, 273:1583-1590.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1583-1590
    • Yoshida, T.1    Pan, Y.2    Hanada, H.3    Iwata, Y.4    Shigekawa, M.5
  • 78
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • Zaidel-Bar R., Milo R., Kam Z., Geiger B. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J. Cell Sci. 2007, 120:137-148.
    • (2007) J. Cell Sci. , vol.120 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4


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