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Volumn 62, Issue 5, 2007, Pages 481-489

Age-related increase of insoluble, phosphorylated small heat shock proteins in human skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHOPROTEIN; SMALL HEAT SHOCK PROTEIN;

EID: 34447532418     PISSN: 10795006     EISSN: None     Source Type: Journal    
DOI: 10.1093/gerona/62.5.481     Document Type: Article
Times cited : (40)

References (50)
  • 1
    • 7544233112 scopus 로고    scopus 로고
    • Effects of aging on muscle fiber type and size
    • Deschenes MR. Effects of aging on muscle fiber type and size. Sports Med. 2004;34:809-824.
    • (2004) Sports Med , vol.34 , pp. 809-824
    • Deschenes, M.R.1
  • 2
    • 0036266110 scopus 로고    scopus 로고
    • Attenuated HSP70 response in skeletal muscle of aged rats following contractile activity
    • Vasilaki A, Jackson MJ, McArdle A. Attenuated HSP70 response in skeletal muscle of aged rats following contractile activity. Muscle Nerve. 2002;25:902-905.
    • (2002) Muscle Nerve , vol.25 , pp. 902-905
    • Vasilaki, A.1    Jackson, M.J.2    McArdle, A.3
  • 3
    • 0037444470 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (MAPK) pathway activation: Effects of age and acute exercise on human skeletal muscle
    • Williamson D, Gallagher P, Harber M, Hollon C, Trappe S. Mitogen-activated protein kinase (MAPK) pathway activation: effects of age and acute exercise on human skeletal muscle. J Physiol. 2003;547:977-987.
    • (2003) J Physiol , vol.547 , pp. 977-987
    • Williamson, D.1    Gallagher, P.2    Harber, M.3    Hollon, C.4    Trappe, S.5
  • 4
    • 0030066985 scopus 로고    scopus 로고
    • Effect of aging on insulin receptor, insulin receptor substrate-1, and phosphatidylinositol 3-kinase in liver and muscle of rats
    • Carvalho CR, Brenelli SL, Silva AC, Nunes AL, Velloso LA, Saad MJ. Effect of aging on insulin receptor, insulin receptor substrate-1, and phosphatidylinositol 3-kinase in liver and muscle of rats. Endocrinology. 1996;137:151-159.
    • (1996) Endocrinology , vol.137 , pp. 151-159
    • Carvalho, C.R.1    Brenelli, S.L.2    Silva, A.C.3    Nunes, A.L.4    Velloso, L.A.5    Saad, M.J.6
  • 5
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family, and structure predictions of the conserved "alpha- crystallin domain
    • Caspers GJ, Leunissen JA, de Jong WW. The expanding small heat-shock protein family, and structure predictions of the conserved "alpha- crystallin domain". J Mol Evol. 1995;40:238-248.
    • (1995) J Mol Evol , vol.40 , pp. 238-248
    • Caspers, G.J.1    Leunissen, J.A.2    de Jong, W.W.3
  • 6
    • 0036716317 scopus 로고    scopus 로고
    • Innervation-dependent phosphorylation and accumulation of alpha B-crystallin and Hsp27 as insoluble complex in disused muscle
    • Kato K, Ito H, Kamei K, Iwamoto I, Inaguma Y. Innervation-dependent phosphorylation and accumulation of alpha B-crystallin and Hsp27 as insoluble complex in disused muscle. FASEB J. 2002;16:1432-1434.
    • (2002) FASEB J , vol.16 , pp. 1432-1434
    • Kato, K.1    Ito, H.2    Kamei, K.3    Iwamoto, I.4    Inaguma, Y.5
  • 7
    • 17344361902 scopus 로고    scopus 로고
    • A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • Vicart P, Caron A, Guicheney P, et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet. 1998;20:92-95.
    • (1998) Nat Genet , vol.20 , pp. 92-95
    • Vicart, P.1    Caron, A.2    Guicheney, P.3
  • 8
    • 0034089378 scopus 로고    scopus 로고
    • Fiber-type-specific alphaB-crystallin distribution and its shifts with T(3) and PTU treatments in rat hind limb muscles
    • Atomi Y, Toro K, Masuda T, Hatta H. Fiber-type-specific alphaB-crystallin distribution and its shifts with T(3) and PTU treatments in rat hind limb muscles. J Appl Physiol. 2000;88:1355-1364.
    • (2000) J Appl Physiol , vol.88 , pp. 1355-1364
    • Atomi, Y.1    Toro, K.2    Masuda, T.3    Hatta, H.4
  • 9
    • 0026341897 scopus 로고
    • Alpha B-crystallin in skeletal muscle: Purification and localization
    • Atomi Y, Yamada S, Strohman R, Nonomura Y. Alpha B-crystallin in skeletal muscle: purification and localization. J Biochem (Tokyo). 1991;110:812-822.
    • (1991) J Biochem (Tokyo) , vol.110 , pp. 812-822
    • Atomi, Y.1    Yamada, S.2    Strohman, R.3    Nonomura, Y.4
  • 10
    • 0030724879 scopus 로고    scopus 로고
    • AlphaB-crystallin interacts with intermediate filaments in response to stress
    • Djabali K, de Nechaud B, Landon F, Portier MM. AlphaB-crystallin interacts with intermediate filaments in response to stress. J Cell Sci. 1997;110:2759-2769.
    • (1997) J Cell Sci , vol.110 , pp. 2759-2769
    • Djabali, K.1    de Nechaud, B.2    Landon, F.3    Portier, M.M.4
  • 11
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • Mounier N, Arrigo A. Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones. 2002;7:167-176.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.2
  • 12
    • 0031457379 scopus 로고    scopus 로고
    • Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation
    • Arai H, Atomi Y. Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation. Cell Struct Fund. 1997;22:539-544.
    • (1997) Cell Struct Fund , vol.22 , pp. 539-544
    • Arai, H.1    Atomi, Y.2
  • 13
    • 21744433513 scopus 로고    scopus 로고
    • The decrease of the cytoskeleton tubulin follows the decrease of the associating molecular chaperone αB-crystallin in unloaded soleus muscle atrophy without stretch
    • Sakurai T, Fujita Y, Ohto E, Oguro A, Atomi Y. The decrease of the cytoskeleton tubulin follows the decrease of the associating molecular chaperone αB-crystallin in unloaded soleus muscle atrophy without stretch. FASEB J. 2005;19:1199-1201.
    • (2005) FASEB J , vol.19 , pp. 1199-1201
    • Sakurai, T.1    Fujita, Y.2    Ohto, E.3    Oguro, A.4    Atomi, Y.5
  • 15
    • 0028924759 scopus 로고
    • Modulation of cellular thermo resistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • Lavoie JN, Lambert H, Hickey E, Weber LA, Landry J. Modulation of cellular thermo resistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol. 1995;15:505-516.
    • (1995) Mol Cell Biol , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 16
    • 0037064065 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation
    • Kamradt MC, Chen F, Sam S, Cryns VL. The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J Biol Chem. 2002;277:38731-38736.
    • (2002) J Biol Chem , vol.277 , pp. 38731-38736
    • Kamradt, M.C.1    Chen, F.2    Sam, S.3    Cryns, V.L.4
  • 17
    • 0037422859 scopus 로고    scopus 로고
    • Mimicking phosphorylation of alphaB-crystallin on serine-59 is necessary and sufficient to provide maximal protection of cardiac myocytes from apoptosis
    • Morrison LE, Hoover HE, Thuerauf DJ, Glembotski CC. Mimicking phosphorylation of alphaB-crystallin on serine-59 is necessary and sufficient to provide maximal protection of cardiac myocytes from apoptosis. Circ Res. 2003;92:203-211.
    • (2003) Circ Res , vol.92 , pp. 203-211
    • Morrison, L.E.1    Hoover, H.E.2    Thuerauf, D.J.3    Glembotski, C.C.4
  • 18
    • 0142186172 scopus 로고    scopus 로고
    • Aging and molecular chaperones
    • Soti C, Csermely P. Aging and molecular chaperones. Exp Gerontol. 2003;38:1037-1040.
    • (2003) Exp Gerontol , vol.38 , pp. 1037-1040
    • Soti, C.1    Csermely, P.2
  • 19
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • Stokoe D, Engel K, Campbell DG, Cohen P, Gaestel M. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 1992;313:307-313.
    • (1992) FEBS Lett , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3    Cohen, P.4    Gaestel, M.5
  • 20
    • 0029923193 scopus 로고    scopus 로고
    • Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase
    • McLaughlin MM, Kumar S, McDonnell PC, et al. Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase. J Biol Chem. 1996;271:8488-8492.
    • (1996) J Biol Chem , vol.271 , pp. 8488-8492
    • McLaughlin, M.M.1    Kumar, S.2    McDonnell, P.C.3
  • 21
    • 0032526694 scopus 로고    scopus 로고
    • PRAK, a novel protein kinase regulated by the p38 MAP kinase
    • New L, Jiang Y, Zhao M, et al. PRAK, a novel protein kinase regulated by the p38 MAP kinase. EMBO J. 1998;17:3372-3384.
    • (1998) EMBO J , vol.17 , pp. 3372-3384
    • New, L.1    Jiang, Y.2    Zhao, M.3
  • 23
    • 0032561079 scopus 로고    scopus 로고
    • Phosphorylation of alphaB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation
    • Kato K, Ito H, Kamei K, Inaguma Y, Iwamoto I, Saga S. Phosphorylation of alphaB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J Biol Chem. 1998;273:28346-28354.
    • (1998) J Biol Chem , vol.273 , pp. 28346-28354
    • Kato, K.1    Ito, H.2    Kamei, K.3    Inaguma, Y.4    Iwamoto, I.5    Saga, S.6
  • 24
    • 1442300779 scopus 로고    scopus 로고
    • Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions
    • Koh TJ, Escobedo J. Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions. Am J Physiol Cell Physiol. 2004;286:C713-C722.
    • (2004) Am J Physiol Cell Physiol , vol.286
    • Koh, T.J.1    Escobedo, J.2
  • 25
    • 0036239489 scopus 로고    scopus 로고
    • Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes
    • Ito H, Kamei K, Iwamoto I, et al. Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes. J Biochem (Tokyo). 2002;131:593-603.
    • (2002) J Biochem (Tokyo) , vol.131 , pp. 593-603
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3
  • 26
    • 0035146830 scopus 로고    scopus 로고
    • Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease
    • Kato K, Inaguma Y, Ito H, et al. Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease. J Neurochem. 2001;76:730-736.
    • (2001) J Neurochem , vol.76 , pp. 730-736
    • Kato, K.1    Inaguma, Y.2    Ito, H.3
  • 27
    • 0043133793 scopus 로고    scopus 로고
    • HSP27 is a ubiquitin-binding protein involved in I-kappaB alpha proteasomal degradation
    • Parcellier A, Schmitt E, Gurbuxani S, et al. HSP27 is a ubiquitin-binding protein involved in I-kappaB alpha proteasomal degradation. Mol Cell Biol. 2003;23:5790-5802.
    • (2003) Mol Cell Biol , vol.23 , pp. 5790-5802
    • Parcellier, A.1    Schmitt, E.2    Gurbuxani, S.3
  • 28
    • 0037648469 scopus 로고    scopus 로고
    • The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination
    • den Engelsman J, Keijsers V, de Jong WW, Boelens WC. The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination. J Biol Chem. 2003;278:4699-4704.
    • (2003) J Biol Chem , vol.278 , pp. 4699-4704
    • den Engelsman, J.1    Keijsers, V.2    de Jong, W.W.3    Boelens, W.C.4
  • 30
    • 0032562574 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells
    • Gredinger E, Gerber AN, Tamir Y, Tapscott SJ, Bengal E. Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells. J Biol Chem. 1998;273:10436-10444.
    • (1998) J Biol Chem , vol.273 , pp. 10436-10444
    • Gredinger, E.1    Gerber, A.N.2    Tamir, Y.3    Tapscott, S.J.4    Bengal, E.5
  • 31
    • 0842304360 scopus 로고    scopus 로고
    • Constitutive activation of MAPK cascade in acute quadriplegic myopathy
    • Di Giovanni S, Molon A, Broccolini A, et al. Constitutive activation of MAPK cascade in acute quadriplegic myopathy. Ann Neurol. 2004;55:195-206.
    • (2004) Ann Neurol , vol.55 , pp. 195-206
    • Di Giovanni, S.1    Molon, A.2    Broccolini, A.3
  • 32
    • 0142093519 scopus 로고    scopus 로고
    • Aberrant p38 mitogen-activated protein kinase signalling in skeletal muscle from Type 2 diabetic patients
    • Koistinen HA, Chibalin AV, Zierath JR. Aberrant p38 mitogen-activated protein kinase signalling in skeletal muscle from Type 2 diabetic patients. Diabetologia. 2003;46:1324-1328.
    • (2003) Diabetologia , vol.46 , pp. 1324-1328
    • Koistinen, H.A.1    Chibalin, A.V.2    Zierath, J.R.3
  • 33
    • 2342439076 scopus 로고    scopus 로고
    • AlphaB-crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly
    • Fujita Y, Ohto E, Katayama E, Atomi Y. AlphaB-crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly. J Cell Sci. 2004;117:1719-1726.
    • (2004) J Cell Sci , vol.117 , pp. 1719-1726
    • Fujita, Y.1    Ohto, E.2    Katayama, E.3    Atomi, Y.4
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA. 1979;76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0033977056 scopus 로고    scopus 로고
    • The stress kit: A new method based on competitive reverse transcriptase-polymerase chain reaction to quantify the expression of human alphaB-crystallin, Hsp27, and Hsp60
    • Bajramovic JJ, Geutskens SB, Bsibsi M, et al. The stress kit: a new method based on competitive reverse transcriptase-polymerase chain reaction to quantify the expression of human alphaB-crystallin, Hsp27, and Hsp60. Cell Stress Chaperones. 2000;5:30-35.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 30-35
    • Bajramovic, J.J.1    Geutskens, S.B.2    Bsibsi, M.3
  • 38
    • 34447553165 scopus 로고
    • The contractile apparatus and cytoskeleton
    • Frederiken DW, Cunningham LW, eds, New York: Academic Press;
    • Knight P, Trinick JA. The contractile apparatus and cytoskeleton. In: Frederiken DW, Cunningham LW, eds. Methods in Enzymology. New York: Academic Press; 1985:9-12.
    • (1985) Methods in Enzymology , pp. 9-12
    • Knight, P.1    Trinick, J.A.2
  • 39
    • 0034767173 scopus 로고    scopus 로고
    • Age-related changes in protein oxidation and proteolysis in mammalian cells
    • Grune T, Shringarpure R, Sitte N, Davies K. Age-related changes in protein oxidation and proteolysis in mammalian cells. J Gerontol Biol Sci. 2001;56A:B459-B467.
    • (2001) J Gerontol Biol Sci , vol.56 A
    • Grune, T.1    Shringarpure, R.2    Sitte, N.3    Davies, K.4
  • 40
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells
    • Welch WJ, Feramisco JR. Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells. J Biol Chem. 1984;259:4501-4513.
    • (1984) J Biol Chem , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 41
    • 16344363800 scopus 로고    scopus 로고
    • Altered proteasome structure, function, and oxidation in aged muscle
    • Ferrington DA, Husom AD, Thompson LV. Altered proteasome structure, function, and oxidation in aged muscle. FASEB J. 2005;19:644-646.
    • (2005) FASEB J , vol.19 , pp. 644-646
    • Ferrington, D.A.1    Husom, A.D.2    Thompson, L.V.3
  • 42
    • 4544333872 scopus 로고    scopus 로고
    • The proteasome inhibitor, MG132, promotes the reprogramming of translation in C2C12 myoblasts and facilitates the association of Hsp25 with the eIF4F complex
    • Cowan JL, Morley SJ. The proteasome inhibitor, MG132, promotes the reprogramming of translation in C2C12 myoblasts and facilitates the association of Hsp25 with the eIF4F complex. Eur J Biochem. 2004;271:3596-3611.
    • (2004) Eur J Biochem , vol.271 , pp. 3596-3611
    • Cowan, J.L.1    Morley, S.J.2
  • 43
    • 10044254417 scopus 로고    scopus 로고
    • Overexpression of wild-type heat shock protein 27 and a nonphosphorylatable heat shock protein 27 mutant protects against ischemia/reperfusion injury in a transgenic mouse model
    • Hollander JM, Martin JL, Belke DD, et al. Overexpression of wild-type heat shock protein 27 and a nonphosphorylatable heat shock protein 27 mutant protects against ischemia/reperfusion injury in a transgenic mouse model. Circulation. 2004;110:3544-3552.
    • (2004) Circulation , vol.110 , pp. 3544-3552
    • Hollander, J.M.1    Martin, J.L.2    Belke, D.D.3
  • 44
    • 0029903175 scopus 로고    scopus 로고
    • Coordinate activation of lysosomal, Ca 2+-activated and ATP-ubiquitin dependent proteinases in the unweighted rat soleus muscle
    • Taillandier D, Aurousseau E, Meynial-Denis D, et al. Coordinate activation of lysosomal, Ca 2+-activated and ATP-ubiquitin dependent proteinases in the unweighted rat soleus muscle. Biochem J. 1996;316:65-72.
    • (1996) Biochem J , vol.316 , pp. 65-72
    • Taillandier, D.1    Aurousseau, E.2    Meynial-Denis, D.3
  • 45
    • 21244492006 scopus 로고    scopus 로고
    • Hsp27-2D-gel electrophoresis is a diagnostic tool to differentiate primary desminopathies from myofibrillar myopathies
    • Clemen CS, Fischer D, Roth U, et al. Hsp27-2D-gel electrophoresis is a diagnostic tool to differentiate primary desminopathies from myofibrillar myopathies. FEBS Lett. 2005;579:3777-3782.
    • (2005) FEBS Lett , vol.579 , pp. 3777-3782
    • Clemen, C.S.1    Fischer, D.2    Roth, U.3
  • 46
    • 0035893961 scopus 로고    scopus 로고
    • The actin cytoskeleton response to oxidants: From small heat shock protein phosphorylation to changes in the redox state of actin itself
    • Dalle-Donne I, Rossi R, Milzani A, Di Simplicio P, Colombo R. The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself. Free Radic Biol Med. 2001;31:1624-1632.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1624-1632
    • Dalle-Donne, I.1    Rossi, R.2    Milzani, A.3    Di Simplicio, P.4    Colombo, R.5
  • 47
    • 18144384775 scopus 로고    scopus 로고
    • Essential role for mitogen-activated protein (MAP) kinase phosphatase-1 in stress-responsive MAP kinase and cell survival signaling
    • Wu JJ, Bennett AM. Essential role for mitogen-activated protein (MAP) kinase phosphatase-1 in stress-responsive MAP kinase and cell survival signaling. J Biol Chem. 2005;280:16461-16466.
    • (2005) J Biol Chem , vol.280 , pp. 16461-16466
    • Wu, J.J.1    Bennett, A.M.2
  • 49
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson GL, Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science. 2002;298:1911-1912.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 50
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature. 2000;408:239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2


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