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Volumn 92, Issue 4, 2007, Pages 364-370

Serotonin stimulates mouse skeletal muscle 6-phosphofructo-1-kinase through tyrosine-phosphorylation of the enzyme altering its intracellular localization

Author keywords

Glycolysis; Metabolism; Metabolom; Phosphofructokinase; Regulation

Indexed keywords

6 PHOSPHOFRUCTOKINASE; F ACTIN; GENISTEIN; INSULIN; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; SEROTONIN; SEROTONIN 2A RECEPTOR; TYROSINE; WORTMANNIN;

EID: 36148972876     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2007.07.010     Document Type: Article
Times cited : (52)

References (34)
  • 1
    • 0028945584 scopus 로고
    • Expression of a serotonin-gated ion channel in embryonic neural and nonneural tissues
    • Tecott L., Shtrom S., and Julius D. Expression of a serotonin-gated ion channel in embryonic neural and nonneural tissues. Mol. Cell. Neurosci. 6 (1995) 43-55
    • (1995) Mol. Cell. Neurosci. , vol.6 , pp. 43-55
    • Tecott, L.1    Shtrom, S.2    Julius, D.3
  • 2
    • 0028972605 scopus 로고
    • 5-Hydroxytryptamine stimulates glucose transport in cardiomyocytes via a monoamine oxidase-dependent reaction
    • Fischer Y., Thomas J., Kamp J., Jungling E., Rose H., Carepene C., and Kammermeier H. 5-Hydroxytryptamine stimulates glucose transport in cardiomyocytes via a monoamine oxidase-dependent reaction. Biochem. J. 311 (1995) 575-583
    • (1995) Biochem. J. , vol.311 , pp. 575-583
    • Fischer, Y.1    Thomas, J.2    Kamp, J.3    Jungling, E.4    Rose, H.5    Carepene, C.6    Kammermeier, H.7
  • 3
    • 0019321173 scopus 로고
    • Activation of rabbit muscle phosphofructokinase by F-actin and reconstituted thin filaments
    • Liou R.S., and Anderson S. Activation of rabbit muscle phosphofructokinase by F-actin and reconstituted thin filaments. Biochemistry 19 (1980) 2684-2688
    • (1980) Biochemistry , vol.19 , pp. 2684-2688
    • Liou, R.S.1    Anderson, S.2
  • 4
    • 33646045331 scopus 로고    scopus 로고
    • The 5-HT2A serotoninergic receptor is expressed in the MCF-7 human breast cancer cell line and reveals a mitogenic effect of serotonin
    • Sonier B., Arseneault M., Lavigne C., Ouellette R.J., and Vaillancourt C. The 5-HT2A serotoninergic receptor is expressed in the MCF-7 human breast cancer cell line and reveals a mitogenic effect of serotonin. Biochem. Biophys. Res. Commun. 343 (2006) 1053-1059
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , pp. 1053-1059
    • Sonier, B.1    Arseneault, M.2    Lavigne, C.3    Ouellette, R.J.4    Vaillancourt, C.5
  • 5
    • 20444424930 scopus 로고    scopus 로고
    • Expression of the 5-HT2A serotoninergic receptor in human placenta and choriocarcinoma cells: mitogenic implications of serotonin
    • Sonier B., Lavigne C., Arseneault M., Ouellette R., and Vaillancourt C. Expression of the 5-HT2A serotoninergic receptor in human placenta and choriocarcinoma cells: mitogenic implications of serotonin. Placenta 26 (2005) 484-490
    • (2005) Placenta , vol.26 , pp. 484-490
    • Sonier, B.1    Lavigne, C.2    Arseneault, M.3    Ouellette, R.4    Vaillancourt, C.5
  • 7
    • 0028897149 scopus 로고
    • 5-HT receptors: past, present and future
    • Peroutka S.J. 5-HT receptors: past, present and future. Trends Neurosci. 18 (1995) 68-69
    • (1995) Trends Neurosci. , vol.18 , pp. 68-69
    • Peroutka, S.J.1
  • 9
    • 0345556939 scopus 로고
    • A unique serotonin receptor in choroid plexus is linked to phosphatidylinositol turnover
    • Conn P.J., Sandersbush E., Hoffman B.J., and Hartig P.R. A unique serotonin receptor in choroid plexus is linked to phosphatidylinositol turnover. Proc. Natl. Acad. Sci. USA 83 (1986) 928-932
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 928-932
    • Conn, P.J.1    Sandersbush, E.2    Hoffman, B.J.3    Hartig, P.R.4
  • 11
    • 0033531943 scopus 로고    scopus 로고
    • Serotonin (5-hydroxytryptamine), a novel regulator of glucose transport in rat skeletal muscle
    • Hajduch E., Rencurel F., Balendran A., Batty I.H., Downes C.P., and Hundal H.S. Serotonin (5-hydroxytryptamine), a novel regulator of glucose transport in rat skeletal muscle. J. Biol. Chem. 274 (1999) 13563-13568
    • (1999) J. Biol. Chem. , vol.274 , pp. 13563-13568
    • Hajduch, E.1    Rencurel, F.2    Balendran, A.3    Batty, I.H.4    Downes, C.P.5    Hundal, H.S.6
  • 12
    • 0030902977 scopus 로고    scopus 로고
    • Identification and localization of a skeletal muscle serotonin 5-HT2A receptor coupled to the Jak/STAT pathway
    • Guillet-Deniau I., Burnol A.F., and Girard J. Identification and localization of a skeletal muscle serotonin 5-HT2A receptor coupled to the Jak/STAT pathway. J. Biol. Chem. 272 (1997) 14825-14829
    • (1997) J. Biol. Chem. , vol.272 , pp. 14825-14829
    • Guillet-Deniau, I.1    Burnol, A.F.2    Girard, J.3
  • 13
    • 0025189905 scopus 로고
    • The 5HT2 receptor defines a family of structurally distinct but functionally conserved serotonin receptors
    • Julius D., Huang K.M., Livelli T.J., Axel R., and Jessel T.M. The 5HT2 receptor defines a family of structurally distinct but functionally conserved serotonin receptors. Proc. Natl. Acad. Sci. USA 87 (1992) 928-932
    • (1992) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 928-932
    • Julius, D.1    Huang, K.M.2    Livelli, T.J.3    Axel, R.4    Jessel, T.M.5
  • 14
    • 0026815453 scopus 로고
    • 5-HT2 receptor mRNA is overexpressed in cultured rat aortic smooth muscle cells relative to normal aorta
    • Corson M.A., Alexander R.W., and Berk B.C. 5-HT2 receptor mRNA is overexpressed in cultured rat aortic smooth muscle cells relative to normal aorta. Am. J. Physiol. 262 (1992) C309-C313
    • (1992) Am. J. Physiol. , vol.262
    • Corson, M.A.1    Alexander, R.W.2    Berk, B.C.3
  • 15
    • 0028016331 scopus 로고
    • Primary structure of the human platelet serotonin 5-HT2A receptor: identify with frontal cortex serotonin 5-HT2A receptor
    • Cook E.H., Fletcher K.E., Wainwright M., Marks N., Yan S.Y., and Leventhal B.L. Primary structure of the human platelet serotonin 5-HT2A receptor: identify with frontal cortex serotonin 5-HT2A receptor. J. Neurochem. 63 (1994) 465-469
    • (1994) J. Neurochem. , vol.63 , pp. 465-469
    • Cook, E.H.1    Fletcher, K.E.2    Wainwright, M.3    Marks, N.4    Yan, S.Y.5    Leventhal, B.L.6
  • 16
    • 0031691803 scopus 로고    scopus 로고
    • Activation of membrane skeleton-bound phosphofructokinase in erythrocytes induced by serotonin
    • Assouline-Cohen M., Ben-Porat H., and Beitner R. Activation of membrane skeleton-bound phosphofructokinase in erythrocytes induced by serotonin. Mol. Genet. Metab. 63 (1998) 235-238
    • (1998) Mol. Genet. Metab. , vol.63 , pp. 235-238
    • Assouline-Cohen, M.1    Ben-Porat, H.2    Beitner, R.3
  • 17
    • 85047669951 scopus 로고
    • Allosteric regulatory properties of muscle phosphofructokinase
    • Kemp R.G., and Foe L.G. Allosteric regulatory properties of muscle phosphofructokinase. Mol. Cell. Biochem. 57 (1993) 147-154
    • (1993) Mol. Cell. Biochem. , vol.57 , pp. 147-154
    • Kemp, R.G.1    Foe, L.G.2
  • 18
    • 0030272292 scopus 로고    scopus 로고
    • Myofibril-bound muscle phosphofructokinase is less sensitive to inhibition by ATP than the free enzyme, but retains its sensitivity to stimulation by bisphosphorylated hexoses
    • Andrés V., Carreras J., and Cussó R. Myofibril-bound muscle phosphofructokinase is less sensitive to inhibition by ATP than the free enzyme, but retains its sensitivity to stimulation by bisphosphorylated hexoses. Int. J. Biochem. Cell Biol. 28 (1996) 1179-1184
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 1179-1184
    • Andrés, V.1    Carreras, J.2    Cussó, R.3
  • 19
    • 0022973976 scopus 로고
    • The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with F-actin
    • Luther M.A., and Lee J.C. The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with F-actin. J. Biol. Chem. 261 (1986) 1753-1759
    • (1986) J. Biol. Chem. , vol.261 , pp. 1753-1759
    • Luther, M.A.1    Lee, J.C.2
  • 20
    • 0022551530 scopus 로고
    • Factors affecting the activation of rabbit muscle phosphofructokinase by actin
    • Kuo K.J., Malencik D.A., Liou R.S., and Anderson S.R. Factors affecting the activation of rabbit muscle phosphofructokinase by actin. Biochemistry 25 (1986) 1278-1286
    • (1986) Biochemistry , vol.25 , pp. 1278-1286
    • Kuo, K.J.1    Malencik, D.A.2    Liou, R.S.3    Anderson, S.R.4
  • 21
    • 0037388501 scopus 로고    scopus 로고
    • Epinephrine modulates cellular distribution of muscle phosphofructokinase
    • Alves G.G., and Sola-Penna M. Epinephrine modulates cellular distribution of muscle phosphofructokinase. Mol. Genet. Metab. 78 (2003) 302-306
    • (2003) Mol. Genet. Metab. , vol.78 , pp. 302-306
    • Alves, G.G.1    Sola-Penna, M.2
  • 22
    • 4644249046 scopus 로고    scopus 로고
    • Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle
    • Silva A.P., Alves G.G., Araujo A.H., and Sola-Penna M. Effects of insulin and actin on phosphofructokinase activity and cellular distribution in skeletal muscle. An. Acad. Bras. Cienc. 76 (2004) 541-548
    • (2004) An. Acad. Bras. Cienc. , vol.76 , pp. 541-548
    • Silva, A.P.1    Alves, G.G.2    Araujo, A.H.3    Sola-Penna, M.4
  • 23
    • 27644553063 scopus 로고    scopus 로고
    • Calcium influx: a possible role for insulin modulation of intracellular distribution and activity of 6-phosphofructo-1-kinase in human erythrocytes
    • Zancan P., and Sola-Penna M. Calcium influx: a possible role for insulin modulation of intracellular distribution and activity of 6-phosphofructo-1-kinase in human erythrocytes. Mol. Genet. Metab. 86 (2005) 392-400
    • (2005) Mol. Genet. Metab. , vol.86 , pp. 392-400
    • Zancan, P.1    Sola-Penna, M.2
  • 24
    • 27644585878 scopus 로고    scopus 로고
    • Regulation of human erythrocyte metabolism by insul
    • cellular distribution of 6-phosphofructo-1-kinase and its implication for red blood cell function
    • Zancan P., and Sola-Penna M. Regulation of human erythrocyte metabolism by insul. cellular distribution of 6-phosphofructo-1-kinase and its implication for red blood cell function. Mol. Genet. Metab. 86 (2005) 401-411
    • (2005) Mol. Genet. Metab. , vol.86 , pp. 401-411
    • Zancan, P.1    Sola-Penna, M.2
  • 25
    • 36148940296 scopus 로고    scopus 로고
    • 32P]-nucleoside triphosphate, with high specific activity, in: C.M. Morel (ed.) Genes and Antigenes of Parasites, A Laboratory Manual. Fundação Oswaldo Cruz, Rio de Janeiro, Brasil, 1983, pp. 146-157.
  • 26
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0026761109 scopus 로고
    • 5-Hydroxytryptamine receptors
    • Zifa E., and Fillion G. 5-Hydroxytryptamine receptors. Pharmacol. Rev. 44 (1992) 401-458
    • (1992) Pharmacol. Rev. , vol.44 , pp. 401-458
    • Zifa, E.1    Fillion, G.2
  • 31
    • 0030932901 scopus 로고    scopus 로고
    • Regulation of rabbit muscle phosphofructokinase by phosphorylation
    • Cai C.Z., Callaci T.P., Luther M.A., and Lee J.C. Regulation of rabbit muscle phosphofructokinase by phosphorylation. Biophys. Chem. 64 (1997) 199-209
    • (1997) Biophys. Chem. , vol.64 , pp. 199-209
    • Cai, C.Z.1    Callaci, T.P.2    Luther, M.A.3    Lee, J.C.4
  • 32
    • 0041888303 scopus 로고    scopus 로고
    • Cellular distribution of phosphofructokinase activity and implications to metabolic regulation in human breast cancer
    • El-Bacha T., de Freitas M.S., and Sola-Penna M. Cellular distribution of phosphofructokinase activity and implications to metabolic regulation in human breast cancer. Mol. Genet. Metab. 79 (2003) 294-299
    • (2003) Mol. Genet. Metab. , vol.79 , pp. 294-299
    • El-Bacha, T.1    de Freitas, M.S.2    Sola-Penna, M.3
  • 33
    • 34047160935 scopus 로고    scopus 로고
    • Clotrimazole inhibits and modulates heterologous association of the key glycolytic enzyme 6-phosphofructo-1-kinase
    • Zancan P., Rosas A.O., Marcondes M.C., Marinho-Carvalho M.M., and Sola-Penna M. Clotrimazole inhibits and modulates heterologous association of the key glycolytic enzyme 6-phosphofructo-1-kinase. Biochem. Pharmacol. 73 (2007) 1520-1527
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 1520-1527
    • Zancan, P.1    Rosas, A.O.2    Marcondes, M.C.3    Marinho-Carvalho, M.M.4    Sola-Penna, M.5


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