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Volumn 371, Issue 3, 2003, Pages 857-866

Stimulation of glycogen synthesis by heat shock in L6 skeletal-muscle cells: Regulatory role of site-specific phosphorylation of glycogen-associated protein phosphatase 1

Author keywords

Cellular stress; Contraction; Glycogen synthase; Protein phosphatase 1

Indexed keywords

CELLS; HEAT TREATMENT; POLYSACCHARIDES; PROTEINS; SYNTHESIS (CHEMICAL);

EID: 0038583955     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021644     Document Type: Article
Times cited : (11)

References (48)
  • 3
    • 0023928214 scopus 로고
    • Phosphorylation of the glycogen-binding subunit of protein phosphatase-1G in response to adrenalin
    • MacKintosh, C., Campbell, D. G., Hiraga, A. and Cohen, P. (1988) Phosphorylation of the glycogen-binding subunit of protein phosphatase-1G in response to adrenalin. FEBS Lett. 234, 189-194
    • (1988) FEBS Lett. , vol.234 , pp. 189-194
    • MacKintosh, C.1    Campbell, D.G.2    Hiraga, A.3    Cohen, P.4
  • 4
    • 0025522071 scopus 로고
    • The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle
    • Dent, P., Lavoinne, A., Nakielny, S., Caudwell, F. B., Watt, P. and Cohen, P. (1990) The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle. Nature (London) 348, 302-308
    • (1990) Nature (London) , vol.348 , pp. 302-308
    • Dent, P.1    Lavoinne, A.2    Nakielny, S.3    Caudwell, F.B.4    Watt, P.5    Cohen, P.6
  • 6
    • 0034714239 scopus 로고    scopus 로고
    • Glycogen synthase association with the striated muscle glycogen-targeting subunit of protein phosphatase-1. Synthase activation involves scaffolding regulated by β-adrenergic signaling
    • Liu, J. and Brautigan, D. L. (2000) Glycogen synthase association with the striated muscle glycogen-targeting subunit of protein phosphatase-1. Synthase activation involves scaffolding regulated by β-adrenergic signaling. J. Biol. Chem. 275, 26074-26081
    • (2000) J. Biol. Chem. , vol.275 , pp. 26074-26081
    • Liu, J.1    Brautigan, D.L.2
  • 8
    • 0025093615 scopus 로고
    • Identification of three in vivo phosphorylation sites on the glycogen-binding subunit of protein phosphatase 1 from rabbit skeletal muscle, and their response to adrenaline
    • Dent, P., Campbell, D. G., Caudwell, F. B. and Cohen, P. (1990) Identification of three in vivo phosphorylation sites on the glycogen-binding subunit of protein phosphatase 1 from rabbit skeletal muscle, and their response to adrenaline. FEBS Lett. 259, 281-285
    • (1990) FEBS Lett. , vol.259 , pp. 281-285
    • Dent, P.1    Campbell, D.G.2    Caudwell, F.B.3    Cohen, P.4
  • 9
    • 0034493114 scopus 로고    scopus 로고
    • HSP72 gene expression progressively increases in human skeletal muscle during prolonged, exhaustive exercise
    • Febbraio, M. A. and Koukoulas, I. (2000) HSP72 gene expression progressively increases in human skeletal muscle during prolonged, exhaustive exercise. J Appl. Physiol. 89, 1055-1060
    • (2000) J Appl. Physiol. , vol.89 , pp. 1055-1060
    • Febbraio, M.A.1    Koukoulas, I.2
  • 10
    • 0023924166 scopus 로고
    • Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression
    • Mizzen, L. A. and Welsh, W. J. (1988) Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression. J. Cell Biol. 4, 1105-1116
    • (1988) J. Cell Biol. , vol.4 , pp. 1105-1116
    • Mizzen, L.A.1    Welsh, W.J.2
  • 11
    • 0026808914 scopus 로고
    • Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein
    • Terlecky, S. R., Chiang, H. L., Olson, T. S. and Dice, J. F. (1992) Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein. J. Biol. Chem. 267, 9202-9209
    • (1992) J. Biol. Chem. , vol.267 , pp. 9202-9209
    • Terlecky, S.R.1    Chiang, H.L.2    Olson, T.S.3    Dice, J.F.4
  • 12
    • 0019164438 scopus 로고
    • Heat shock, deciliation and release from anoxia induce the synthesis of the same set of polypeptides in starved T. pyriformis
    • Guttman, S. D., Glover, C. V., Allis, C. D. and Gorovsky, M. A. (1980) Heat shock, deciliation and release from anoxia induce the synthesis of the same set of polypeptides in starved T. pyriformis. Cell (Cambridge, Mass.) 22, 299-307
    • (1980) Cell (Cambridge, Mass.) , vol.22 , pp. 299-307
    • Guttman, S.D.1    Glover, C.V.2    Allis, C.D.3    Gorovsky, M.A.4
  • 13
    • 0022398020 scopus 로고
    • Similar dose response of heat shock protein synthesis and intracellular pH change in yeast
    • Weitzel, G., Pilatus, U. and Rensing, L. (1985) Similar dose response of heat shock protein synthesis and intracellular pH change in yeast. Exp. Cell Res. 159, 252-256
    • (1985) Exp. Cell Res. , vol.159 , pp. 252-256
    • Weitzel, G.1    Pilatus, U.2    Rensing, L.3
  • 14
    • 0021075626 scopus 로고
    • The effects of glucose on protein synthesis and thermosensitivity in Chinese hamster ovary cells
    • Sciandra, J. J. and Subjeck, J. R. (1983) The effects of glucose on protein synthesis and thermosensitivity in Chinese hamster ovary cells. J. Biol. Chem. 258, 12091-12093
    • (1983) J. Biol. Chem. , vol.258 , pp. 12091-12093
    • Sciandra, J.J.1    Subjeck, J.R.2
  • 15
    • 0030727477 scopus 로고    scopus 로고
    • Oxidants differentially regulate the heat-shock response
    • Wallen, E. S., Buettner, G. R. and Moseley, P. L. (1997) Oxidants differentially regulate the heat-shock response. Int. J. Hyperthermia 13, 517-524
    • (1997) Int. J. Hyperthermia , vol.13 , pp. 517-524
    • Wallen, E.S.1    Buettner, G.R.2    Moseley, P.L.3
  • 17
    • 0029854076 scopus 로고    scopus 로고
    • Influence of elevated muscle temperature on metabolism during intense, dynamic exercise
    • Febbraio, M. A., Carey, M. F., Snow, R. J., Stathis, C. G. and Hargreaves, M. (1996) Influence of elevated muscle temperature on metabolism during intense, dynamic exercise. Am. J. Physiol. 271, R1251-R1255
    • (1996) Am. J. Physiol. , vol.271
    • Febbraio, M.A.1    Carey, M.F.2    Snow, R.J.3    Stathis, C.G.4    Hargreaves, M.5
  • 19
    • 0025913239 scopus 로고
    • HSP70 and other possible heat shock or oxidative stress proteins are induced in skeletal muscle, heart, and liver during exercise
    • Salo, D. C., Donovan, C. M. and Davies, K. J. (1991) HSP70 and other possible heat shock or oxidative stress proteins are induced in skeletal muscle, heart, and liver during exercise. Free Radical. Biol. Med. 11, 239-246
    • (1991) Free Radical. Biol. Med. , vol.11 , pp. 239-246
    • Salo, D.C.1    Donovan, C.M.2    Davies, K.J.3
  • 20
    • 0026007812 scopus 로고
    • Synthesis of 70K stress protein by human leukocytes: Effect of exercise in the heat
    • Ryan, A. J., Gisolfi, C. V. and Moseley, P. L. (1991) Synthesis of 70K stress protein by human leukocytes: effect of exercise in the heat. J. Appl. Physiol. 70, 466-471
    • (1991) J. Appl. Physiol. , vol.70 , pp. 466-471
    • Ryan, A.J.1    Gisolfi, C.V.2    Moseley, P.L.3
  • 21
    • 0036021808 scopus 로고    scopus 로고
    • Exercise-induced elevation of HSP70 is intensity dependent
    • Milne, K. J. and Noble, E. G. (2002) Exercise-induced elevation of HSP70 is intensity dependent. J. Appl. Physiol. 93, 561-568
    • (2002) J. Appl. Physiol. , vol.93 , pp. 561-568
    • Milne, K.J.1    Noble, E.G.2
  • 22
    • 0028835412 scopus 로고
    • HSP70 induction during exercise and heat stress in rats: Role of internal temperature
    • Skidmore, R., Gutierrez, J. A., Guerriero, Jr, V. and Kregel, K. C. (1995) HSP70 induction during exercise and heat stress in rats: role of internal temperature. Am. J. Physiol. 268, R92-R97
    • (1995) Am. J. Physiol. , vol.268
    • Skidmore, R.1    Gutierrez, J.A.2    Guerriero V., Jr.3    Kregel, K.C.4
  • 23
    • 0029781814 scopus 로고    scopus 로고
    • Blunting the rise in body temperature reduces muscle glycogenolysis during exercise in humans
    • Febbraio, M. A., Snow, R. J., Stathis, C. G., Hargreaves, M. and Carey, M. F. (1996) Blunting the rise in body temperature reduces muscle glycogenolysis during exercise in humans. Exp. Physiol. 81, 685-693
    • (1996) Exp. Physiol. , vol.81 , pp. 685-693
    • Febbraio, M.A.1    Snow, R.J.2    Stathis, C.G.3    Hargreaves, M.4    Carey, M.F.5
  • 24
    • 0027184670 scopus 로고
    • Purified mammalian HSP-70 kDa activates phosphoprotein phosphatases in vitro
    • Mivechi, N. F., Trainor, L. D. and Hahn, G. M. (1993) Purified mammalian HSP-70 kDa activates phosphoprotein phosphatases in vitro. Biochem. Biophys. Res. Commun. 192, 954-963
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 954-963
    • Mivechi, N.F.1    Trainor, L.D.2    Hahn, G.M.3
  • 26
    • 0036227062 scopus 로고    scopus 로고
    • Decreased expression of heat shock protein 72 in skeletal muscle of patients with type 2 diabetes correlates with insulin resistance
    • Kurucz, I., Morva, A., Vaag, A., Eriksson, K. F., Huang, X., Groop, L. and Koranyi, L. (2002) Decreased expression of heat shock protein 72 in skeletal muscle of patients with type 2 diabetes correlates with insulin resistance. Diabetes 51, 1102-1109
    • (2002) Diabetes , vol.51 , pp. 1102-1109
    • Kurucz, I.1    Morva, A.2    Vaag, A.3    Eriksson, K.F.4    Huang, X.5    Groop, L.6    Koranyi, L.7
  • 27
    • 0032541032 scopus 로고    scopus 로고
    • Transcriptional activity of heat shock factor 1 at 37 °C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases Cα and Cζ
    • Chu, B., Zhong, R., Soncin, F., Stevenson, M. A. and Calderwood, S. K. (1998) Transcriptional activity of heat shock factor 1 at 37 °C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases Cα and Cζ. J. Biol. Chem. 273, 18640-18646
    • (1998) J. Biol. Chem. , vol.273 , pp. 18640-18646
    • Chu, B.1    Zhong, R.2    Soncin, F.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 28
    • 0029846433 scopus 로고    scopus 로고
    • Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1
    • Chu, B., Soncin, F., Price, B. D., Stevenson, M. A. and Calderwood, S. K. (1996) Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1. J. Biol. Chem. 271, 30847-30857
    • (1996) J. Biol. Chem. , vol.271 , pp. 30847-30857
    • Chu, B.1    Soncin, F.2    Price, B.D.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 29
    • 0032938742 scopus 로고    scopus 로고
    • Glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription in Saccharomyces cerevisiae
    • Lin, J. T. and Lis, J. T. (1999) Glycogen synthase phosphatase interacts with heat shock factor to activate CUP1 gene transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 19, 3237-3245
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3237-3245
    • Lin, J.T.1    Lis, J.T.2
  • 30
    • 0031742046 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3β and extracellular signal-regulated kinase inactivate heat shock transcription factor 1 by facilitating the disappearance of transcriptionally active granules after heat shock
    • He, B., Meng, Y. H. and Mivechi, N. F. (1998) Glycogen synthase kinase 3β and extracellular signal-regulated kinase inactivate heat shock transcription factor 1 by facilitating the disappearance of transcriptionally active granules after heat shock. Mol. Cell. Biol. 18, 6624-6633
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6624-6633
    • He, B.1    Meng, Y.H.2    Mivechi, N.F.3
  • 31
    • 0015105955 scopus 로고
    • Tissue temperatures and whole-animal oxygen consumption after exercise
    • Brooks, G. A., Hittelman, K. J., Faulkner, J. A. and Beyer, R. E. (1971) Tissue temperatures and whole-animal oxygen consumption after exercise. Am. J. Physiol. 221, 427-431
    • (1971) Am. J. Physiol. , vol.221 , pp. 427-431
    • Brooks, G.A.1    Hittelman, K.J.2    Faulkner, J.A.3    Beyer, R.E.4
  • 32
    • 0015043804 scopus 로고
    • Temperature, skeletal muscle mitochondrial functions, and oxygen debt
    • Brooks, G. A., Hittelman, K. J., Faulkner, J. A. and Beyer, R. E. (1971) Temperature, skeletal muscle mitochondrial functions, and oxygen debt. Am. J. Physiol. 220, 1053-1059
    • (1971) Am. J. Physiol. , vol.220 , pp. 1053-1059
    • Brooks, G.A.1    Hittelman, K.J.2    Faulkner, J.A.3    Beyer, R.E.4
  • 33
    • 0031010897 scopus 로고    scopus 로고
    • The effect of modulating the glycogen-associated regulatory subunit of protein phosphatase-1 on insulin action in rat skeletal muscle cells
    • Ragolia, L. and Begum, N. (1997) The effect of modulating the glycogen-associated regulatory subunit of protein phosphatase-1 on insulin action in rat skeletal muscle cells. Endocrinology 138, 2398-2404
    • (1997) Endocrinology , vol.138 , pp. 2398-2404
    • Ragolia, L.1    Begum, N.2
  • 34
    • 0033304957 scopus 로고    scopus 로고
    • Effect of an Aspg905Tyr mutation of the glycogen-associated regulatory subunit of protein phosphatase-1 on the regulation of glycogen synthesis by insulin and cyclic adenosine 3′,5′-monophosphate agonists
    • Ragolia, L., Duddy, N. and Begum, N. (1999) Effect of an Aspg905Tyr mutation of the glycogen-associated regulatory subunit of protein phosphatase-1 on the regulation of glycogen synthesis by insulin and cyclic adenosine 3′,5′-monophosphate agonists. Mol. Endocrinol. 13, 1773-1783
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1773-1783
    • Ragolia, L.1    Duddy, N.2    Begum, N.3
  • 36
    • 0028279506 scopus 로고
    • Regulation of protein phosphalase 1 and 2A activities by insulin during myogenesis in rat skeletal muscle cells in culture
    • Srinivasan, M. and Begum, N. (1994) Regulation of protein phosphalase 1 and 2A activities by insulin during myogenesis in rat skeletal muscle cells in culture. J. Biol. Chem. 269, 12514-12520
    • (1994) J. Biol. Chem. , vol.269 , pp. 12514-12520
    • Srinivasan, M.1    Begum, N.2
  • 37
    • 0031953590 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 1 and 2A activities by insulin during myogenesis in rat skeletal muscle cells in culture
    • Ragolia, L. and Begum, N. (1998) Regulation of protein phosphatase 1 and 2A activities by insulin during myogenesis in rat skeletal muscle cells in culture. Mol. Cell. Biochem. 182, 49-58
    • (1998) Mol. Cell. Biochem. , vol.182 , pp. 49-58
    • Ragolia, L.1    Begum, N.2
  • 38
    • 0034875525 scopus 로고    scopus 로고
    • Selected contribution: Insulin utilizes NO/cGMP pathway to activate myosin phosphatase via Rho inhibition in vascular smooth muscle
    • Sandu, O. A., Ito, M. and Begum, N. (2001) Selected contribution: insulin utilizes NO/cGMP pathway to activate myosin phosphatase via Rho inhibition in vascular smooth muscle. J. Appl. Physiol. 91, 1475-1482
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1475-1482
    • Sandu, O.A.1    Ito, M.2    Begum, N.3
  • 40
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) 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) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 0035013151 scopus 로고    scopus 로고
    • Activation of arrestin: Requirement of phosphorylation as the negative charge on residues in synthetic peptides from the carboxyl-terminal region of rhodopsin
    • McDowell, J. H., Robinson, P. R., Miller, R. L., Brannock, M. T., Arendt, A., Smith, W. C. and Hargrave, P. A. (2001) Activation of arrestin: requirement of phosphorylation as the negative charge on residues in synthetic peptides from the carboxyl-terminal region of rhodopsin. Invest. Ophthalmol. Vis. Sci. 42, 1439-1443
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 1439-1443
    • McDowell, J.H.1    Robinson, P.R.2    Miller, R.L.3    Brannock, M.T.4    Arendt, A.5    Smith, W.C.6    Hargrave, P.A.7
  • 42
    • 0028959518 scopus 로고
    • Effects of mild heat shock on glycogenesis and its regulation by insulin in cultured fetal hepatocytes
    • Zachayus, J. L. and Plas, C. (1995) Effects of mild heat shock on glycogenesis and its regulation by insulin in cultured fetal hepatocytes. J. Cell. Physiol. 162, 330-340
    • (1995) J. Cell. Physiol. , vol.162 , pp. 330-340
    • Zachayus, J.L.1    Plas, C.2
  • 43
    • 0036710280 scopus 로고    scopus 로고
    • IRS proteins and the common path to diabetes
    • White, M. F. (2002) IRS proteins and the common path to diabetes. Am. J. Physiol. Endocrinol. Metab. 283, E413-E422
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.283
    • White, M.F.1
  • 44
    • 0035986087 scopus 로고    scopus 로고
    • Invited Review: Effect of acute exercise on insulin signalling and action in humans
    • Wojtaszewski, J. F., Nielsen, J. N. and Richter, E. A. (2002) Invited Review: effect of acute exercise on insulin signalling and action in humans. J. Appl. Physiol. 93, 384-392
    • (2002) J. Appl. Physiol. , vol.93 , pp. 384-392
    • Wojtaszewski, J.F.1    Nielsen, J.N.2    Richter, E.A.3
  • 45
    • 0033958102 scopus 로고    scopus 로고
    • Phosphorylation of the skeletal muscle glycogen-targeting subunit of protein phosphatase 1 in response to adrenaline in vivo
    • Walker, K. S., Watt, P. W. and Cohen, P. (2000) Phosphorylation of the skeletal muscle glycogen-targeting subunit of protein phosphatase 1 in response to adrenaline in vivo. FEBS Lett. 466, 121-124
    • (2000) FEBS Lett. , vol.466 , pp. 121-124
    • Walker, K.S.1    Watt, P.W.2    Cohen, P.3
  • 46
    • 0033845411 scopus 로고    scopus 로고
    • Effect of okadaic acid, a protein phosphatase inhibitor, on heat stress-induced HSP72 synthesis and thermotolerance
    • Joyeux, M., Arnaud, C., Richard, M. J., Yellon, D. M., Demenge, P. and Ribuot, C. (2000) Effect of okadaic acid, a protein phosphatase inhibitor, on heat stress-induced HSP72 synthesis and thermotolerance. Cardiovasc. Drugs Ther. 14, 441-446
    • (2000) Cardiovasc. Drugs Ther. , vol.14 , pp. 441-446
    • Joyeux, M.1    Arnaud, C.2    Richard, M.J.3    Yellon, D.M.4    Demenge, P.5    Ribuot, C.6
  • 47
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato, S., Fugita, N. and Tsuruo, T. (2000) Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl. Acad. Sci. U.S.A. 97, 10832-10837
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 10832-10837
    • Sato, S.1    Fugita, N.2    Tsuruo, T.3
  • 48
    • 0037044763 scopus 로고    scopus 로고
    • Acute activation of de novo sphingolipid biosynthesis upon heat shock causes an accumulation of ceramide and subsequent dephosphorylation of SR proteins
    • Jenkins, G. M., Cowart, L. A., Signorelli, P., Pettus, B. J., Chalfant, C. E. and Hannun, Y. (2002) Acute activation of de novo sphingolipid biosynthesis upon heat shock causes an accumulation of ceramide and subsequent dephosphorylation of SR proteins. J. Biol. Chem. 277, 42572-42578
    • (2002) J. Biol. Chem. , vol.277 , pp. 42572-42578
    • Jenkins, G.M.1    Cowart, L.A.2    Signorelli, P.3    Pettus, B.J.4    Chalfant, C.E.5    Hannun, Y.6


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