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Volumn 302, Issue 6, 2012, Pages

Laminin-α 1 LG4-5 domain binding to dystroglycan mediates muscle cell survival, growth, and the AP-1 and NF-κb transcription factors but also has adverse effects

Author keywords

Activator protein 1; Apoptosis; Dystroglycan; Laminin globular (LG) 4 5 domains; Nuclear factor B

Indexed keywords

DYSTROPHIN; GLYCOPROTEIN; LAMININ ALPHA1; LAMININ BINDING PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR RELA; UNCLASSIFIED DRUG;

EID: 84863288240     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00118.2011     Document Type: Article
Times cited : (5)

References (48)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 60549085643 scopus 로고    scopus 로고
    • Meta-analysis of expression signatures of muscle atrophy: Gene interaction networks in early and late stages
    • Calura E, Cagnin S, Raffaello A, Laveder P, Lanfranchi G, Romualdi C. Meta-analysis of expression signatures of muscle atrophy: gene interaction networks in early and late stages. BMC Genomics 9: 630-650, 2008.
    • (2008) BMC Genomics , vol.9 , pp. 630-650
    • Calura, E.1    Cagnin, S.2    Raffaello, A.3    Laveder, P.4    Lanfranchi, G.5    Romualdi, C.6
  • 6
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • Colognato H, Winkelmann DA, Yurchenco PD. Laminin polymerization induces a receptor-cytoskeleton network. J Cell Biol 145: 619-631, 1999.
    • (1999) J Cell Biol , vol.145 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.D.3
  • 8
    • 54249119561 scopus 로고    scopus 로고
    • JNK signaling in apoptosis
    • Dhanasekaran DN, Reddy EP. JNK signaling in apoptosis. Oncogene 27: 6245-6251, 2008.
    • (2008) Oncogene , vol.27 , pp. 6245-6251
    • Dhanasekaran, D.N.1    Reddy, E.P.2
  • 9
    • 33746579821 scopus 로고    scopus 로고
    • Regulation of phosphatidylinositol 3-kinase (PI3K)/Akt and nuclear factor-kappa B signaling pathways in dystrophin-deficient skeletal muscle in response to mechanical stretch
    • Dogra C, Changotra H, Wergedal JE, Kumar A. Regulation of phosphatidylinositol 3-kinase (PI3K)/Akt and nuclear factor-kappa B signaling pathways in dystrophin-deficient skeletal muscle in response to mechanical stretch. J Cell Physiol 208: 575-585, 2006.
    • (2006) J Cell Physiol , vol.208 , pp. 575-585
    • Dogra, C.1    Changotra, H.2    Wergedal, J.E.3    Kumar, A.4
  • 10
    • 33748070833 scopus 로고    scopus 로고
    • Progressive nuclear factor-kappaB activation resistant to inhibition by contraction and curcumin in mdx mice
    • Durham WJ, Arbogast S, Gerken E, Li YP, Reid MB. Progressive nuclear factor-kappaB activation resistant to inhibition by contraction and curcumin in mdx mice. Muscle Nerve 34: 298-303, 2006.
    • (2006) Muscle Nerve , vol.34 , pp. 298-303
    • Durham, W.J.1    Arbogast, S.2    Gerken, E.3    Li, Y.P.4    Reid, M.B.5
  • 11
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophinglycoprotein complex
    • Ervasti JM, Campbell KP. Membrane organization of the dystrophinglycoprotein complex. Cell 66: 1121-1131, 1991.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 12
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122: 809-823, 1993.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 13
    • 4444354572 scopus 로고    scopus 로고
    • Laminin alpha1 chain reduces muscular dystrophy in laminin alpha2 chain deficient mice
    • Gawlik K, Miyagoe-Suzuki Y, Ekblom P, Takeda S, Durbeej M. Laminin alpha1 chain reduces muscular dystrophy in laminin alpha2 chain deficient mice. Hum Mol Genet 13: 1775-1784, 2004.
    • (2004) Hum Mol Genet , vol.13 , pp. 1775-1784
    • Gawlik, K.1    Miyagoe-Suzuki, Y.2    Ekblom, P.3    Takeda, S.4    Durbeej, M.5
  • 14
    • 77954104087 scopus 로고    scopus 로고
    • Transgenic overexpression of laminin alpha1 chain in laminin alpha2 chain-deficient mice rescues the disease throughout the lifespan
    • Gawlik KI, Durbeej M. Transgenic overexpression of laminin alpha1 chain in laminin alpha2 chain-deficient mice rescues the disease throughout the lifespan. Muscle Nerve 42: 30-37, 2010.
    • (2010) Muscle Nerve , vol.42 , pp. 30-37
    • Gawlik, K.I.1    Durbeej, M.2
  • 15
    • 84863251717 scopus 로고    scopus 로고
    • Skeletal muscle laminin and MDC1A: Pathogenesis and treatment strategies
    • Gawlik KI, Durbeej M. Skeletal muscle laminin and MDC1A: pathogenesis and treatment strategies. Skelet Muscle 1:9: 1-13, 2011.
    • (2011) Skelet Muscle , vol.1 , Issue.9 , pp. 1-13
    • Gawlik, K.I.1    Durbeej, M.2
  • 16
    • 33748750613 scopus 로고    scopus 로고
    • Laminin alpha1 chain improves laminin alpha2 chain deficient peripheral neuropathy
    • Gawlik KI, Li JY, Petersen A, Durbeej M. Laminin alpha1 chain improves laminin alpha2 chain deficient peripheral neuropathy. Hum Mol Genet 15: 2690-2700, 2006.
    • (2006) Hum Mol Genet , vol.15 , pp. 2690-2700
    • Gawlik, K.I.1    Li, J.Y.2    Petersen, A.3    Durbeej, M.4
  • 18
    • 0032759070 scopus 로고    scopus 로고
    • Laminins during muscle development and in muscular dystrophies
    • Gullberg D, Tiger CF, Velling T. Laminins during muscle development and in muscular dystrophies. Cell Mol Life Sci 56: 442-460, 1999.
    • (1999) Cell Mol Life Sci , vol.56 , pp. 442-460
    • Gullberg, D.1    Tiger, C.F.2    Velling, T.3
  • 19
    • 33745199637 scopus 로고    scopus 로고
    • Akt regulates basal and induced processing of NF-kappaB2 (p100) to p52
    • Gustin JA, Korgaonkar CK, Pincheira R, Li Q, Donner DB. Akt regulates basal and induced processing of NF-kappaB2 (p100) to p52. J Biol Chem 281: 16473-16481, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 16473-16481
    • Gustin, J.A.1    Korgaonkar, C.K.2    Pincheira, R.3    Li, Q.4    Donner, D.B.5
  • 20
    • 0345826140 scopus 로고    scopus 로고
    • Cell type-specific expression of the IkappaB kinases determines the significance of phosphatidylinositol 3-kinase/ Akt signaling to NF-kappa B activation
    • Gustin JA, Ozes ON, Akca H, Pincheira R, Mayo LD, Li Q, Guzman JR, Korgaonkar CK, Donner DB. Cell type-specific expression of the IkappaB kinases determines the significance of phosphatidylinositol 3-kinase/ Akt signaling to NF-kappa B activation. J Biol Chem 279: 1615-1620, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 1615-1620
    • Gustin, J.A.1    Ozes, O.N.2    Akca, H.3    Pincheira, R.4    Mayo, L.D.5    Li, Q.6    Guzman, J.R.7    Korgaonkar, C.K.8    Donner, D.B.9
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0036842214 scopus 로고    scopus 로고
    • Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells
    • Langenbach KJ, Rando TA. Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells. Muscle Nerve 26: 644-653, 2002.
    • (2002) Muscle Nerve , vol.26 , pp. 644-653
    • Langenbach, K.J.1    Rando, T.A.2
  • 26
    • 52549133171 scopus 로고    scopus 로고
    • Nuclear factor-kappa B signaling in skeletal muscle atrophy
    • Li H, Malhotra S, Kumar A. Nuclear factor-kappa B signaling in skeletal muscle atrophy. J Mol Med 86: 1113-1126, 2008.
    • (2008) J Mol Med , vol.86 , pp. 1113-1126
    • Li, H.1    Malhotra, S.2    Kumar, A.3
  • 27
    • 33947721728 scopus 로고    scopus 로고
    • Linker molecules between laminins and dystroglycan ameliorate laminin-alpha2- deficient muscular dystrophy at all disease stages
    • Meinen S, Barzaghi P, Lin S, Lochmüller H, Ruegg MA. Linker molecules between laminins and dystroglycan ameliorate laminin-alpha2- deficient muscular dystrophy at all disease stages. J Cell Biol 176: 979-993, 2007.
    • (2007) J Cell Biol , vol.176 , pp. 979-993
    • Meinen, S.1    Barzaghi, P.2    Lin, S.3    Lochmüller, H.4    Ruegg, M.A.5
  • 29
    • 73949151885 scopus 로고    scopus 로고
    • LG4-5 domains of laminin-2 binds α-dystroglycan to allow myotube attachment and prevent anoikis
    • Munoz J, Zhou Y, Jarrett HW. LG4-5 domains of laminin-2 binds α-dystroglycan to allow myotube attachment and prevent anoikis. J Cell Physiol 222: 111-119, 2010.
    • (2010) J Cell Physiol , vol.222 , pp. 111-119
    • Munoz, J.1    Zhou, Y.2    Jarrett, H.W.3
  • 30
    • 0141960276 scopus 로고    scopus 로고
    • Skeletal muscle signaling pathway through the dystrophin glycoprotein complex and Rac1
    • Oak SA, Zhou YW, Jarrett HW. Skeletal muscle signaling pathway through the dystrophin glycoprotein complex and Rac1. J Biol Chem 278: 39287-39295, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 39287-39295
    • Oak, S.A.1    Zhou, Y.W.2    Jarrett, H.W.3
  • 31
    • 0023875632 scopus 로고
    • Laminin alters cell shape and stimulates motility and proliferation of murine skeletal myoblasts
    • Ocalan M, Goodman SL, Kuhl U, Hauschka SD, von der Mark K. Laminin alters cell shape and stimulates motility and proliferation of murine skeletal myoblasts. Dev Biol 125: 158-167, 1988.
    • (1988) Dev Biol , vol.125 , pp. 158-167
    • Ocalan, M.1    Goodman, S.L.2    Kuhl, U.3    Hauschka, S.D.4    von der Mark, K.5
  • 32
    • 53949103308 scopus 로고    scopus 로고
    • Skeletal muscle diseases, inflammation, and NF-kappaB signaling: Insights and opportunities for therapeutic intervention
    • Peterson JM, Guttridge DC. Skeletal muscle diseases, inflammation, and NF-kappaB signaling: insights and opportunities for therapeutic intervention. Int Rev Immunol 27: 375-387, 2008.
    • (2008) Int Rev Immunol , vol.27 , pp. 375-387
    • Peterson, J.M.1    Guttridge, D.C.2
  • 33
    • 66049117408 scopus 로고    scopus 로고
    • Laminin-111 protein therapy prevents muscle disease in the mdx mouse model for Duchenne muscular dystrophy
    • Rooney JE, Gurpur P, Burkin DJ. Laminin-111 protein therapy prevents muscle disease in the mdx mouse model for Duchenne muscular dystrophy. Proc Natl Acad Sci USA 106: 7991-7996, 2009.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7991-7996
    • Rooney, J.E.1    Gurpur, P.2    Burkin, D.J.3
  • 36
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins
    • Talts JF, Andac Z, Gohring W, Brancaccio A, Timpl R. Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins. EMBO J 18: 863-870, 1999.
    • (1999) EMBO J , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Gohring, W.3    Brancaccio, A.4    Timpl, R.5
  • 37
    • 0032502958 scopus 로고    scopus 로고
    • Structural analysis and proteolytic processing of recombinant G domain of mouse laminin alpha2 chain
    • Talts JF, Mann K, Yamada Y, Timpl R. Structural analysis and proteolytic processing of recombinant G domain of mouse laminin alpha2 chain. FEBS Lett 426: 71-76, 1998.
    • (1998) FEBS Lett , vol.426 , pp. 71-76
    • Talts, J.F.1    Mann, K.2    Yamada, Y.3    Timpl, R.4
  • 38
    • 78649319656 scopus 로고    scopus 로고
    • Activation by phosphorylation and purification of human c-Jun N-terminal kinase (JNK) isoforms in milligram amounts
    • Thévenin AF, Zony CL, Bahnson BJ, Colman RF. Activation by phosphorylation and purification of human c-Jun N-terminal kinase (JNK) isoforms in milligram amounts. Protein Expr Purif 75: 138-146, 2011.
    • (2011) Protein Expr Purif , vol.75 , pp. 138-146
    • Thévenin, A.F.1    Zony, C.L.2    Bahnson, B.J.3    Colman, R.F.4
  • 39
    • 0030612270 scopus 로고    scopus 로고
    • Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle development and in muscular dystrophies
    • Tiger CF, Champliaud MF, Pedrosa-Domellof F, Thornell LE, Ekblom P, Gullberg D. Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle development and in muscular dystrophies. J Biol Chem 272: 28590-28595, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 28590-28595
    • Tiger, C.F.1    Champliaud, M.F.2    Pedrosa-Domellof, F.3    Thornell, L.E.4    Ekblom, P.5    Gullberg, D.6
  • 41
    • 59649104233 scopus 로고    scopus 로고
    • The IkappaB kinases IKKalpha and IKKbeta are necessary and sufficient for skeletal muscle atrophy
    • Van Gammeren D, Damrauer JS, Jackman RW, Kandarian SC. The IkappaB kinases IKKalpha and IKKbeta are necessary and sufficient for skeletal muscle atrophy. FASEB J 23: 362-370, 2009.
    • (2009) FASEB J , vol.23 , pp. 362-370
    • van Gammeren, D.1    Damrauer, J.S.2    Jackman, R.W.3    Kandarian, S.C.4
  • 42
    • 0037155254 scopus 로고    scopus 로고
    • Alternative splice variants of alpha 7 beta 1 integrin selectively recognize different laminin isoforms
    • von der Mark H, Williams I, Wendler O, Sorokin L, von der Mark K, Poschl E. Alternative splice variants of alpha 7 beta 1 integrin selectively recognize different laminin isoforms. J Biol Chem 277: 6012-6016, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 6012-6016
    • von der Mark, H.1    Williams, I.2    Wendler, O.3    Sorokin, L.4    von der Mark, K.5    Poschl, E.6
  • 43
    • 34250218193 scopus 로고    scopus 로고
    • NF-kappaB regulation of YY1 inhibits skeletal myogenesis through transcriptional silencing of myofibrillar genesNF-kappaB regulation of YY1 inhibits skeletal myogenesis through transcriptional silencing of myofibrillar genes
    • Wang H, Hertlein E, Bakkar N, Sun H, Acharyya S, Wang J, Carathers M, Davuluri R, Guttridge DC. NF-kappaB regulation of YY1 inhibits skeletal myogenesis through transcriptional silencing of myofibrillar genesNF-kappaB regulation of YY1 inhibits skeletal myogenesis through transcriptional silencing of myofibrillar genes. Mol Cell Biol 27: 4374-4387, 2007.
    • (2007) Mol Cell Biol , vol.27 , pp. 4374-4387
    • Wang, H.1    Hertlein, E.2    Bakkar, N.3    Sun, H.4    Acharyya, S.5    Wang, J.6    Carathers, M.7    Davuluri, R.8    Guttridge, D.C.9
  • 44
    • 62149088572 scopus 로고    scopus 로고
    • Dystrophin glycoprotein complexassociated Gbetagamma subunits activate phosphatidylinositol-3-kinase/ Akt signaling in skeletal muscle in a laminin-dependent manner
    • Xiong Y, Zhou Y, Jarrett HW. Dystrophin glycoprotein complexassociated Gbetagamma subunits activate phosphatidylinositol-3-kinase/ Akt signaling in skeletal muscle in a laminin-dependent manner. J Cell Physiol 219: 402-414, 2009.
    • (2009) J Cell Physiol , vol.219 , pp. 402-414
    • Xiong, Y.1    Zhou, Y.2    Jarrett, H.W.3
  • 45
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida M, Ozawa E. Glycoprotein complex anchoring dystrophin to sarcolemma. J Biochem 108: 748-752, 1990.
    • (1990) J Biochem , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2
  • 46
    • 37349039361 scopus 로고    scopus 로고
    • Laminin-Induced Activation of Rac1 and JNKp46 Is Initiated by Src Family Kinases and Mimics the Effects of Skeletal Muscle Contraction
    • Zhou Y, Jiang D, Thomason DB, Jarrett HW. Laminin-Induced Activation of Rac1 and JNKp46 Is Initiated by Src Family Kinases and Mimics the Effects of Skeletal Muscle Contraction. Biochemistry 46: 14907-14916, 2007.
    • (2007) Biochemistry , vol.46 , pp. 14907-14916
    • Zhou, Y.1    Jiang, D.2    Thomason, D.B.3    Jarrett, H.W.4
  • 48
    • 33144482572 scopus 로고    scopus 로고
    • Binding of laminin alpha1-chain LG4-5 domain to alpha-dystroglycan causes tyrosine phosphorylation of syntrophin to initiate Rac1 signaling
    • Zhou YW, Thomason DB, Gullberg D, Jarrett HW. Binding of laminin alpha1-chain LG4-5 domain to alpha-dystroglycan causes tyrosine phosphorylation of syntrophin to initiate Rac1 signaling. Biochemistry 45: 2042-2052, 2006.
    • (2006) Biochemistry , vol.45 , pp. 2042-2052
    • Zhou, Y.W.1    Thomason, D.B.2    Gullberg, D.3    Jarrett, H.W.4


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