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Volumn 287, Issue 3 56-3, 2004, Pages

Coordinate downregulation of CaM kinase II and phospholamban accompanies contractile phenotype transition in the hyperthyroid rabbit soleus

Author keywords

Calcium ion adenosinetriphosphatase; Calmodulin kinase II; Phospholamban; Sarcoplasmic reticulum

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ISOPROTEIN; LEVOTHYROXINE; PROTEIN KINASE (CALCIUM,CALMODULIN) II; THYROID HORMONE;

EID: 4143143037     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.00352.2003     Document Type: Article
Times cited : (5)

References (60)
  • 1
    • 0025814646 scopus 로고
    • Effect of thyroid hormone on the expression of mRNA encoding sarcoplasmic reticulum proteins
    • Arai M, Otsy K, MacLennan DH, Alpert NR, and Periasamy M. Effect of thyroid hormone on the expression of mRNA encoding sarcoplasmic reticulum proteins. Circ Res 69: 266-276, 1991.
    • (1991) Circ Res , vol.69 , pp. 266-276
    • Arai, M.1    Otsy, K.2    MacLennan, D.H.3    Alpert, N.R.4    Periasamy, M.5
  • 2
    • 0034686045 scopus 로고    scopus 로고
    • 2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP
    • 2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP. J Biol Chem 275: 15034-15038, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 15034-15038
    • Asahi, M.1    Mckenna, E.2    Kurzydlowski, K.3    Tada, M.4    MacLennan, D.H.5
  • 3
    • 0032185669 scopus 로고    scopus 로고
    • αKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle
    • Bayer KU, Harbers K, and Schulman H. αKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle. EMBO J 17: 5598-5605, 1998.
    • (1998) EMBO J , vol.17 , pp. 5598-5605
    • Bayer, K.U.1    Harbers, K.2    Schulman, H.3
  • 4
    • 0028917370 scopus 로고
    • The multifunctional calcium/calmodulin-dependent protein kinase: From form to function
    • Braun AP and Schulman H. The multifunctional calcium/calmodulin-dependent protein kinase: from form to function. Annu Rev Physiol 57: 417-445, 1995.
    • (1995) Annu Rev Physiol , vol.57 , pp. 417-445
    • Braun, A.P.1    Schulman, H.2
  • 6
    • 0040136263 scopus 로고
    • Single fiber analysis of type IIA myosin heavy chain distribution in hyper-and hypothyroid soleus
    • Caiozzo VJ, Swoap S, Tao M, Menzel D, and Baldwin KM. Single fiber analysis of type IIA myosin heavy chain distribution in hyper-and hypothyroid soleus. Am J Physiol Cell Physiol 265: C842-C850, 1993.
    • (1993) Am J Physiol Cell Physiol , vol.265
    • Caiozzo, V.J.1    Swoap, S.2    Tao, M.3    Menzel, D.4    Baldwin, K.M.5
  • 9
    • 0034627188 scopus 로고    scopus 로고
    • Phosphorylation of anchoring protein by calmodulin protein kinase associated to the sarcoplasmic reticulum of rabbit fast-twitch muscle
    • Damiani E, Sacchetto R, and Margreth A. Phosphorylation of anchoring protein by calmodulin protein kinase associated to the sarcoplasmic reticulum of rabbit fast-twitch muscle. Biochem Biophys Res Commun 279: 181-189, 2000.
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 181-189
    • Damiani, E.1    Sacchetto, R.2    Margreth, A.3
  • 10
    • 0025017166 scopus 로고
    • The rate of tetanic relaxation is correlated with the density of calcium ATPase in the terminal cisternae of thyrotoxic skeletal muscle
    • Dulhunty AF. The rate of tetanic relaxation is correlated with the density of calcium ATPase in the terminal cisternae of thyrotoxic skeletal muscle. Pflügers Arch 415: 433-439, 1990.
    • (1990) Pflügers Arch , vol.415 , pp. 433-439
    • Dulhunty, A.F.1
  • 11
    • 0024201809 scopus 로고
    • A computer program for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato A. A computer program for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands. Methods Enzymol 157: 378-417, 1988.
    • (1988) Methods Enzymol , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 13
    • 0028918056 scopus 로고
    • Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from cardiac muscle
    • Hain J, Onoue H, Mayreitner M, Fleischer S, and Schindler H. Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from cardiac muscle. J Biol Chem 270: 2074-2081, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 2074-2081
    • Hain, J.1    Onoue, H.2    Mayreitner, M.3    Fleischer, S.4    Schindler, H.5
  • 14
    • 0028080919 scopus 로고
    • 2+/calmodulin-dependent protein kinase: Characterization of optimal conditions for calcium pump phosphorylation
    • 2+/ calmodulin-dependent protein kinase: characterization of optimal conditions for calcium pump phosphorylation. J Biol Chem 269: 31198-31206, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 31198-31206
    • Hawkins, C.1    Xu, A.2    Narayanan, N.3
  • 15
    • 0021952893 scopus 로고
    • Firing patterns of motor units in normal rats
    • Henning R and Lomo T. Firing patterns of motor units in normal rats. Nature 214: 164-166, 1985.
    • (1985) Nature , vol.214 , pp. 164-166
    • Henning, R.1    Lomo, T.2
  • 16
    • 0026115122 scopus 로고
    • Myogenic regulation of mammalian skeletal muscle fibres
    • Hoh JF. Myogenic regulation of mammalian skeletal muscle fibres. News Physiol Sci 6: 1-6, 1991.
    • (1991) News Physiol Sci , vol.6 , pp. 1-6
    • Hoh, J.F.1
  • 17
    • 0001830748 scopus 로고
    • Three hierarchies in skeletal muscle fiber classification: Allotype, isotype and phenotype
    • edited by Kedes L and Stockdale FE. New York: Liss
    • Hoh JF, Hughes S, Hugh H, and Pozgai I. Three hierarchies in skeletal muscle fiber classification: allotype, isotype and phenotype. In: Cellular and Molecular Biology of Muscle Development, edited by Kedes L and Stockdale FE. New York: Liss, 1989, p. 15-26.
    • (1989) Cellular and Molecular Biology of Muscle Development , pp. 15-26
    • Hoh, J.F.1    Hughes, S.2    Hugh, H.3    Pozgai, I.4
  • 19
    • 0022616134 scopus 로고
    • All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner
    • Izumo S, Nadal-Ginard B, and Mahdavi V. All members of the MHC multigene family respond to thyroid hormone in a highly tissue-specific manner. Science 231: 597-600, 1986.
    • (1986) Science , vol.231 , pp. 597-600
    • Izumo, S.1    Nadal-Ginard, B.2    Mahdavi, V.3
  • 20
    • 0027329145 scopus 로고
    • Age-related alterations in the phosphorylation of sarcoplasmic reticulum and myofibrillar proteins and diminished contractile response to isoproterenol in intact rat ventricle
    • Jiang MT, Moffat MP, and Narayanan N. Age-related alterations in the phosphorylation of sarcoplasmic reticulum and myofibrillar proteins and diminished contractile response to isoproterenol in intact rat ventricle. Circ Res 72: 102-111, 1993.
    • (1993) Circ Res , vol.72 , pp. 102-111
    • Jiang, M.T.1    Moffat, M.P.2    Narayanan, N.3
  • 21
    • 33750869255 scopus 로고    scopus 로고
    • Defibrillation depresses heart sarcoplasmic reticulum calcium pump: A mechanism of postshock dysfunction
    • Jones DL and Narayanan N. Defibrillation depresses heart sarcoplasmic reticulum calcium pump: a mechanism of postshock dysfunction. Am J Physiol Heart Circ Physiol 274: H98-H105, 1998.
    • (1998) Am J Physiol Heart Circ Physiol , vol.274
    • Jones, D.L.1    Narayanan, N.2
  • 22
    • 0003388947 scopus 로고
    • 2+-ATPase of cardiac sarcoplasmic reticulum cross reacts with slow type I but not fast type II canine skeletal muscle fibers: An immunohistochemical and immunocytochemical study
    • 2+-ATPase of cardiac sarcoplasmic reticulum cross reacts with slow type I but not fast type II canine skeletal muscle fibers: an immunohistochemical and immunocytochemical study. Cell Motil Cytoskeleton 9: 166-174, 1988.
    • (1988) Cell Motil Cytoskeleton , vol.9 , pp. 166-174
    • Jorgensen, A.O.1    Arnold, W.2    Pepper, D.R.3    Kahl, S.D.4    Mandel, F.5    Campbell, K.P.6
  • 24
    • 0026776493 scopus 로고
    • The nature of heterophilic antibodies and their role in immunoassay interference
    • Levinson SS. The nature of heterophilic antibodies and their role in immunoassay interference. J Clin Immunoassay 15: 108-115, 1992.
    • (1992) J Clin Immunoassay , vol.15 , pp. 108-115
    • Levinson, S.S.1
  • 25
    • 0030995776 scopus 로고    scopus 로고
    • Contractility and myosin isoform compositions of skeletal muscles and muscle cells from rats treated with thyroid hormone for 0, 4, and 8 weeks
    • Li X and Larsson L. Contractility and myosin isoform compositions of skeletal muscles and muscle cells from rats treated with thyroid hormone for 0, 4, and 8 weeks. J Muscle Res Cell Motil 18: 335-344, 1997.
    • (1997) J Muscle Res Cell Motil , vol.18 , pp. 335-344
    • Li, X.1    Larsson, L.2
  • 28
    • 0026691835 scopus 로고
    • Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps
    • Lytton J, Westlin M, Burk SE, Shull GE, and MacLennan DH. Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps. J Biol Chem 267: 14483-14489, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 14483-14489
    • Lytton, J.1    Westlin, M.2    Burk, S.E.3    Shull, G.E.4    MacLennan, D.H.5
  • 30
    • 0026754524 scopus 로고
    • The time course of thyroid-hormone-induced changes in the isotonic and isometric properties of rat soleus muscle
    • Montgomery A. The time course of thyroid-hormone-induced changes in the isotonic and isometric properties of rat soleus muscle. Pflügers Arch 421: 350-356, 1992.
    • (1992) Pflügers Arch , vol.421 , pp. 350-356
    • Montgomery, A.1
  • 32
    • 0019804241 scopus 로고
    • Differential alterations in ATP-supported calcium transport activities of sarcoplasmic reticulum and sarcolemma of aging myocardium
    • Narayanan N. Differential alterations in ATP-supported calcium transport activities of sarcoplasmic reticulum and sarcolemma of aging myocardium. Biochim Biophys Acta 678: 442-459, 1981.
    • (1981) Biochim Biophys Acta , vol.678 , pp. 442-459
    • Narayanan, N.1
  • 33
    • 0029862517 scopus 로고    scopus 로고
    • Effects of aging on sarcoplasmic reticulum function and contraction duration in skeletal muscles of the rat
    • Narayanan N, Jones DL, Xu A, and Yu JC. Effects of aging on sarcoplasmic reticulum function and contraction duration in skeletal muscles of the rat. Am J Physiol Cell Physiol 271: C1032-C1040, 1996.
    • (1996) Am J Physiol Cell Physiol , vol.271
    • Narayanan, N.1    Jones, D.L.2    Xu, A.3    Yu, J.C.4
  • 34
    • 0025941177 scopus 로고
    • Inhibitory and stimulatory effects of fluoride on the calcium pump of cardiac sarcoplasmic reticulum
    • Narayanan N, Su N, and Bedard P. Inhibitory and stimulatory effects of fluoride on the calcium pump of cardiac sarcoplasmic reticulum. Biochim Biophys Acta 1070: 83-91, 1991.
    • (1991) Biochim Biophys Acta , vol.1070 , pp. 83-91
    • Narayanan, N.1    Su, N.2    Bedard, P.3
  • 35
    • 4143139621 scopus 로고    scopus 로고
    • Unique calmodulin control of the sarcoplasmic reticulum calcium pump cycle and relaxation in heart muscle
    • Narayanan N and Xu A. Unique calmodulin control of the sarcoplasmic reticulum calcium pump cycle and relaxation in heart muscle (Abstract). J Mol Cell Cardiol 34: A20, 2002.
    • (2002) J Mol Cell Cardiol , vol.34
    • Narayanan, N.1    Xu, A.2
  • 36
    • 0019508979 scopus 로고
    • Effect of hyperthyroidism on the contractile and histochemical properties of fast and slow twitch skeletal muscle in the rat
    • Nicol CJ and Bruce DS. Effect of hyperthyroidism on the contractile and histochemical properties of fast and slow twitch skeletal muscle in the rat. Pflügers Arch 390: 73-79, 1981.
    • (1981) Pflügers Arch , vol.390 , pp. 73-79
    • Nicol, C.J.1    Bruce, D.S.2
  • 37
    • 0029666260 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent phosphorylation or by interaction with phospholamban
    • 2+/calmodulin-dependent phosphorylation or by interaction with phospholamban. J Biol Chem 271: 14206-14213, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 14206-14213
    • Odermatt, A.1    Kurzydlowski, K.2    MacLennan, D.H.3
  • 38
    • 33750888567 scopus 로고    scopus 로고
    • Modification of ischemia-reperfusion-induced changes in cardiac sarcoplasmic reticulum by preconditioning
    • Osada M, Netticadan T, Tamura K, and Dhalla NS. Modification of ischemia-reperfusion-induced changes in cardiac sarcoplasmic reticulum by preconditioning. Am J Physiol Heart Circ Physiol 274: H2025-H2034, 1998.
    • (1998) Am J Physiol Heart Circ Physiol , vol.274
    • Osada, M.1    Netticadan, T.2    Tamura, K.3    Dhalla, N.S.4
  • 39
    • 0026506792 scopus 로고
    • Altered gene expression in fast-twitch muscle induced by chronic low-frequency stimulation
    • Pette D and Dusterhoft S. Altered gene expression in fast-twitch muscle induced by chronic low-frequency stimulation. Am J Physiol Regul Integr Camp Physiol 262: R333-R338, 1992.
    • (1992) Am J Physiol Regul Integr Camp Physiol , vol.262
    • Pette, D.1    Dusterhoft, S.2
  • 40
    • 0026450106 scopus 로고
    • Adaptation of mammalian skeletal muscle fibres to chronic electrical stimulation
    • Pette D and Vrbova G. Adaptation of mammalian skeletal muscle fibres to chronic electrical stimulation. Rev Physiol Biochem Pharmacol 120: 115-202, 1992.
    • (1992) Rev Physiol Biochem Pharmacol , vol.120 , pp. 115-202
    • Pette, D.1    Vrbova, G.2
  • 42
    • 0034702973 scopus 로고    scopus 로고
    • 2+-ATPase slow-twitch isoform and of β calmodulin-dependent protein kinase in phospholamban-deficient sarcoplasmic reticulum of rabbit masseter muscle
    • 2+-ATPase slow-twitch isoform and of β calmodulin-dependent protein kinase in phospholamban-deficient sarcoplasmic reticulum of rabbit masseter muscle. FEBS Lett 481: 255-260, 2000.
    • (2000) FEBS Lett , vol.481 , pp. 255-260
    • Sacchetto, R.1    Damiani, E.2    Pallanca, A.3    Margreth, A.4
  • 43
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • Simmerman HK and Jones LR. Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol Rev 78: 921-947, 1998.
    • (1998) Physiol Rev , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 45
    • 0022724973 scopus 로고
    • Effects of the thyroid status on the sarcoplasmic reticulum in slow skeletal muscle of the rat
    • Simonides WS and van Hardeveld C. Effects of the thyroid status on the sarcoplasmic reticulum in slow skeletal muscle of the rat. Cell Calcium 7: 147-160, 1986.
    • (1986) Cell Calcium , vol.7 , pp. 147-160
    • Simonides, W.S.1    Van Hardeveld, C.2
  • 48
    • 0026450768 scopus 로고
    • Myogenic cell lineages
    • Stockdale FE. Myogenic cell lineages. Dev Biol 154: 284-298, 1992.
    • (1992) Dev Biol , vol.154 , pp. 284-298
    • Stockdale, F.E.1
  • 49
    • 0022857821 scopus 로고
    • Stimulation of bovine cardiac sarcoplasmic reticulum calcium pump and blocking of phospholamban phosphorylation and dephosphorylation by a phospholamaban monoclonal antibody
    • Suzuki T and Wang JH. Stimulation of bovine cardiac sarcoplasmic reticulum calcium pump and blocking of phospholamban phosphorylation and dephosphorylation by a phospholamaban monoclonal antibody. J Biol Chem 261: 7018-7023, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 7018-7023
    • Suzuki, T.1    Wang, J.H.2
  • 50
    • 0020015867 scopus 로고
    • Phosphorylation of sarcoplasmic reticulum and sarcolemma
    • Tada M and Katz AM. Phosphorylation of sarcoplasmic reticulum and sarcolemma. Annu Rev Physiol 44: 401-423, 1982.
    • (1982) Annu Rev Physiol , vol.44 , pp. 401-423
    • Tada, M.1    Katz, A.M.2
  • 51
    • 0026537505 scopus 로고
    • Changes in myosin heavy-chain isoform synthesis of chronically stimulated rat fast-twitch muscle
    • Termin A and Pette D. Changes in myosin heavy-chain isoform synthesis of chronically stimulated rat fast-twitch muscle. Eur J Biochem 204: 569-573, 1992.
    • (1992) Eur J Biochem , vol.204 , pp. 569-573
    • Termin, A.1    Pette, D.2
  • 52
    • 0024455621 scopus 로고
    • Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs
    • Tobimatsy T and Fujisawa H. Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs. J Biol Chem 264: 17907-17912, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 17907-17912
    • Tobimatsy, T.1    Fujisawa, H.2
  • 56
    • 0032416120 scopus 로고    scopus 로고
    • 2+-cycling proteins and their phosphorylation in rat myocardium
    • 2+-cycling proteins and their phosphorylation in rat myocardium. Am J Physiol Heart Circ Physiol 275: H2087-H2094, 1998.
    • (1998) Am J Physiol Heart Circ Physiol , vol.275
    • Xu, A.1    Narayanan, N.2
  • 57
    • 0033614301 scopus 로고    scopus 로고
    • 2+-pumping in native cardiac sarcoplasmic reticulum
    • 2+-pumping in native cardiac sarcoplasmic reticulum. Biochem Biophys Res Commun 258: 66-72, 1999.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 66-72
    • Xu, A.1    Narayanan, N.2
  • 58
    • 0034635438 scopus 로고    scopus 로고
    • Reversible inhibition of the calcium-pumping ATPase in native cardiac sarcoplasmic reticulum by a calmodulin-binding peptide. Evidence for calmodulin-dependent regulation of the V(max) of calcium transport
    • Xu A and Narayanan N. Reversible inhibition of the calcium-pumping ATPase in native cardiac sarcoplasmic reticulum by a calmodulin-binding peptide. Evidence for calmodulin-dependent regulation of the V(max) of calcium transport. J Biol Chem 275: 4407-4416, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 4407-4416
    • Xu, A.1    Narayanan, N.2
  • 60
    • 0842264958 scopus 로고    scopus 로고
    • Different time course of changes in sarcoplasmic reticulum and myosin isoforms in rat soleus muscle at early stage of hyperthyroidism
    • Yamada T, Inashima S, Matsunaga S, Nara I, Kajihara H, and Wada M. Different time course of changes in sarcoplasmic reticulum and myosin isoforms in rat soleus muscle at early stage of hyperthyroidism. Acta Physiol Scand 180: 79-87, 2004.
    • (2004) Acta Physiol Scand , vol.180 , pp. 79-87
    • Yamada, T.1    Inashima, S.2    Matsunaga, S.3    Nara, I.4    Kajihara, H.5    Wada, M.6


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