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Volumn 10, Issue 3, 2011, Pages 333-339

Prolyl oligopeptidase, inositol phosphate signalling and lithium sensitivity

Author keywords

Bipolar mood disorder; Dictyostelium; Inositol phosphate signalling; Lithium; Multiple inositol polyphosphate phosphatase; Prolyl oligopeptidase

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3; INOSITOL PHOSPHATE; LITHIUM; PROLYL ENDOPEPTIDASE;

EID: 79951696069     PISSN: 18715273     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152711794653779     Document Type: Review
Times cited : (17)

References (58)
  • 1
    • 0019127799 scopus 로고
    • The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain
    • Hallcher, L.M.; Sherman, W.R. The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. J. Biol. Chem., 1980, 255(22), 10896-10901.
    • (1980) J. Biol. Chem , vol.255 , Issue.22 , pp. 10896-10901
    • Hallcher, L.M.1    Sherman, W.R.2
  • 2
    • 67349159879 scopus 로고    scopus 로고
    • Inositol trisphosphate and calcium signaling mechanisms
    • Berridge, M.J. Inositol trisphosphate and calcium signaling mechanisms. Biochim. Biophys. Acta, 2009, 1793(6), 933-940.
    • (2009) Biochim. Biophys. Acta , vol.1793 , Issue.6 , pp. 933-940
    • Berridge, M.J.1
  • 3
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L.C. The phosphoinositide 3-kinase pathway. Science, 2002, 296, 1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 4
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo, G.; De Camilli, P. Phosphoinositides in cell regulation and membrane dynamics. Nature, 2006, 443, 651-657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    de Camilli, P.2
  • 5
    • 0023705726 scopus 로고
    • Properties of inositol polyphosphate 1 phosphatase
    • Inhorn, R.C.; Majerus, P.W. Properties of inositol polyphosphate 1 phosphatase. J. Biol. Chem., 1988, 263(28), 14559-14565.
    • (1988) J. Biol. Chem , vol.263 , Issue.28 , pp. 14559-14565
    • Inhorn, R.C.1    Majerus, P.W.2
  • 6
    • 12344329222 scopus 로고    scopus 로고
    • Lithium and bipolar mood disorder: The inositoldepletion hypothesis revisited. Mol
    • Harwood, A.J. Lithium and bipolar mood disorder: the inositoldepletion hypothesis revisited. Mol. Psychiatry, 2005, 10(1), 117-126.
    • (2005) Psychiatry , vol.10 , Issue.1 , pp. 117-126
    • Harwood, A.J.1
  • 7
    • 0034209028 scopus 로고    scopus 로고
    • The high affinity inositol transport system--implications for the pathophysiology and treatment of bipolar disorder
    • van Calker, D.; Belmaker, R.H. The high affinity inositol transport system--implications for the pathophysiology and treatment of bipolar disorder. Bipolar Disord., 2000, 2, 102-107.
    • (2000) Bipolar Disord , vol.2 , pp. 102-107
    • van Calker, D.1    Belmaker, R.H.2
  • 8
    • 0027512040 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor
    • Mikoshiba, K. Inositol 1,4,5-trisphosphate receptor. Trends Pharmacol. Sci., 1993, 14, 86-89.
    • (1993) Trends Pharmacol. Sci , vol.14 , pp. 86-89
    • Mikoshiba, K.1
  • 9
    • 0027359892 scopus 로고
    • Lithium increases accumulation of second messenger inositol 1,4,5-trisphosphate in brain cortex slices in species ranging from mouse to monkey
    • Hokin, L.E. Lithium increases accumulation of second messenger inositol 1,4,5-trisphosphate in brain cortex slices in species ranging from mouse to monkey. Adv. Enzyme Regul., 1993, 33, 299-312.
    • (1993) Adv. Enzyme Regul , vol.33 , pp. 299-312
    • Hokin, L.E.1
  • 10
    • 0032493304 scopus 로고    scopus 로고
    • Lithium acutely inhibits and chronically up-regulates and stabilizes glutamate uptake by presynaptic nerve endings in mouse cerebral cortex
    • Dixon, J.F.; Hokin, L.E. Lithium acutely inhibits and chronically up-regulates and stabilizes glutamate uptake by presynaptic nerve endings in mouse cerebral cortex. Proc. Natl. Acad. Sci. USA, 1998, 95(14), 8363-8368.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.14 , pp. 8363-8368
    • Dixon, J.F.1    Hokin, L.E.2
  • 11
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 and PIP3: Complex roles at the cell surface
    • Czech, M.P. PIP2 and PIP3: complex roles at the cell surface. Cell, 2000, 100(6), 603-606.
    • (2000) Cell , vol.100 , Issue.6 , pp. 603-606
    • Czech, M.P.1
  • 12
    • 0033073905 scopus 로고    scopus 로고
    • Identification of protein kinase B (PKB) as a phosphatidylinositol 3,4,5-trisphosphate binding protein in Dictyostelium discoideum
    • Tanaka, K.; Adachi, H.; Konishi, H.; Iwamatsu, A.; Ohkawa, K.; Shirai, T.; Nagata, S.; Kikkawa, U.; Fukui, Y. Identification of protein kinase B (PKB) as a phosphatidylinositol 3,4,5-trisphosphate binding protein in Dictyostelium discoideum. Biosci. Biotechnol. Biochem., 1999, 63(2), 368-372.
    • (1999) Biosci. Biotechnol. Biochem , vol.63 , Issue.2 , pp. 368-372
    • Tanaka, K.1    Adachi, H.2    Konishi, H.3    Iwamatsu, A.4    Ohkawa, K.5    Shirai, T.6    Nagata, S.7    Kikkawa, U.8    Fukui, Y.9
  • 13
    • 0036550053 scopus 로고    scopus 로고
    • 3'-phosphoinositide-dependent kinase-1 (PDK-1) in PI 3-kinase signaling
    • Storz, P.; Toker, A. 3'-phosphoinositide-dependent kinase-1 (PDK-1) in PI 3-kinase signaling. Front. Biosci., 2002, 7, d886-d902.
    • (2002) Front. Biosci , vol.7
    • Storz, P.1    Toker, A.2
  • 16
    • 34247361650 scopus 로고    scopus 로고
    • Chemotaxis in the absence of PIP3 gradients
    • Hoeller, O.; Kay, R.R. Chemotaxis in the absence of PIP3 gradients. Curr. Biol., 2007, 17, 813-817.
    • (2007) Curr. Biol , vol.17 , pp. 813-817
    • Hoeller, O.1    Kay, R.R.2
  • 17
    • 34247372469 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinases in chemotaxis in Dictyostelium
    • Takeda, K.; Sasaki, A.T.; Ha, H.; Seung, H.A.; Firtel, R.A. Role of phosphatidylinositol 3-kinases in chemotaxis in Dictyostelium. J. Biol. Chem., 2007, 282(16), 11874-11884.
    • (2007) J. Biol. Chem , vol.282 , Issue.16 , pp. 11874-11884
    • Takeda, K.1    Sasaki, A.T.2    Ha, H.3    Seung, H.A.4    Firtel, R.A.5
  • 18
    • 65649100104 scopus 로고    scopus 로고
    • Unique and overlapping functions of GSK-3 isoforms in cell differentiation and proliferation and cardiovascular development
    • Force, T.; Woodgett, J.R. Unique and overlapping functions of GSK-3 isoforms in cell differentiation and proliferation and cardiovascular development. J. Biol. Chem., 2009, 284(15), 9643-9647.
    • (2009) J. Biol. Chem , vol.284 , Issue.15 , pp. 9643-9647
    • Force, T.1    Woodgett, J.R.2
  • 19
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • Klein, P.S.; Melton, D.A. A molecular mechanism for the effect of lithium on development. Proc. Natl. Acad. Sci. USA, 1996, 93(16), 8455-8459.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.16 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 20
    • 0034805180 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 by competition for magnesium
    • Ryves, W.J.; Harwood, A.J. Lithium inhibits glycogen synthase kinase-3 by competition for magnesium. Biochem. Biophys. Res. Commun., 2001, 280, 720-725.
    • (2001) Biochem. Biophys. Res. Commun , vol.280 , pp. 720-725
    • Ryves, W.J.1    Harwood, A.J.2
  • 21
    • 0036295233 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 inhibition by lithium and beryllium suggests the presence of two magnesium binding sites
    • Ryves, W.J.; Dajani, R.; Pearl, L.; Harwood, A.J. Glycogen synthase kinase-3 inhibition by lithium and beryllium suggests the presence of two magnesium binding sites. Biochem. Biophys. Res. Commun., 2002, 290, 967-972.
    • (2002) Biochem. Biophys. Res. Commun , vol.290 , pp. 967-972
    • Ryves, W.J.1    Dajani, R.2    Pearl, L.3    Harwood, A.J.4
  • 24
    • 0033587742 scopus 로고    scopus 로고
    • Lithium activates the serine/threonine kinase Akt-1 and suppresses glutamate-induced inhibition of Akt-1 activity in neurons
    • USA
    • Chalecka-Franaszek, E.; Chuang, D.M. Lithium activates the serine/threonine kinase Akt-1 and suppresses glutamate-induced inhibition of Akt-1 activity in neurons. Proc. Natl. Acad. Sci. USA, 1999, 96, 8745-8750.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 8745-8750
    • Chalecka-Franaszek, E.1    Chuang, D.M.2
  • 25
    • 0042357237 scopus 로고    scopus 로고
    • Inhibitory phosphorylation of glycogen synthase kinase-3 (GSK-3) in response to lithium: Evidence for autoregulation of GSK-3
    • Zhang, F.; Phiel, C.J.; Spece, L.; Gurvich, N.; Klein, P.S. Inhibitory phosphorylation of glycogen synthase kinase-3 (GSK-3) in response to lithium: evidence for autoregulation of GSK-3. J. Biol. Chem., 2003, 278, 33067-33077.
    • (2003) J. Biol. Chem , vol.278 , pp. 33067-33077
    • Zhang, F.1    Phiel, C.J.2    Spece, L.3    Gurvich, N.4    Klein, P.S.5
  • 26
    • 27844479156 scopus 로고    scopus 로고
    • A positive feedback loop between glycogen synthase kinase 3beta and protein phosphatase 1 after stimulation of NR2B NMDA receptors in forebrain neurons
    • Szatmari, E.; Habas, A.; Yang, P.; Zheng, J.J.; Hagg, T.; Hetman, M. A positive feedback loop between glycogen synthase kinase 3beta and protein phosphatase 1 after stimulation of NR2B NMDA receptors in forebrain neurons. J. Biol. Chem., 2005, 280, 37526-37535.
    • (2005) J. Biol. Chem , vol.280 , pp. 37526-37535
    • Szatmari, E.1    Habas, A.2    Yang, P.3    Zheng, J.J.4    Hagg, T.5    Hetman, M.6
  • 27
    • 0033577733 scopus 로고    scopus 로고
    • Loss of a prolyl oligopeptidase confers resistance to lithium by elevation of inositol (1,4,5) trisphosphate
    • Williams, R.S.; Eames, M.; Ryves, W.J.; Viggars, J.; Harwood, A.J. Loss of a prolyl oligopeptidase confers resistance to lithium by elevation of inositol (1,4,5) trisphosphate. EMBO J., 1999, 18(10), 2734-2745.
    • (1999) EMBO J , vol.18 , Issue.10 , pp. 2734-2745
    • Williams, R.S.1    Eames, M.2    Ryves, W.J.3    Viggars, J.4    Harwood, A.J.5
  • 28
    • 0028870305 scopus 로고
    • Glycogen synthase kinase 3 regulates cell fate in Dictyostelium
    • Harwood, A.J.; Plyte, S.E.; Woodgett, J.; Strutt, H.; Kay, R.R. Glycogen synthase kinase 3 regulates cell fate in Dictyostelium. Cell, 1995, 80(1), 139-148.
    • (1995) Cell , vol.80 , Issue.1 , pp. 139-148
    • Harwood, A.J.1    Plyte, S.E.2    Woodgett, J.3    Strutt, H.4    Kay, R.R.5
  • 31
    • 0028297009 scopus 로고
    • Role of phospholipase C in Dictyostelium formation of inositol 1,4,5-trisphosphate and normal development in cells lacking phospholipase C activity
    • Drayer, A.L.; Van der Kaay, J.; Mayr, G.W.; Van Haastert, P.J.M. Role of phospholipase C in Dictyostelium formation of inositol 1,4,5-trisphosphate and normal development in cells lacking phospholipase C activity. EMBO J., 1994, 13, 1601-1609.
    • (1994) EMBO J , vol.13 , pp. 1601-1609
    • Drayer, A.L.1    van der Kaay, J.2    Mayr, G.W.3    van Haastert, P.J.M.4
  • 32
    • 0034282769 scopus 로고    scopus 로고
    • + signalling is not required for chemotaxis in Dictyostelium
    • + signalling is not required for chemotaxis in Dictyostelium. EMBO J., 2000, 19(17), 4846-4854.
    • (2000) EMBO J , vol.19 , Issue.17 , pp. 4846-4854
    • Traynor, D.1    Milne, J.L.2    Insall, R.H.3    Kay, R.R.4
  • 33
    • 0029618911 scopus 로고
    • A novel, phospholipase C-independent pathway of inositol 1, 4,5-trisphosphate formation in Dictyostelium and rat liver
    • Van Dijken, P.; De Haas, J.R.; Craxton, A.; Erneux, C.; Shears, S.B.; Van Haastert, P.J.M. A novel, phospholipase C-independent pathway of inositol 1, 4,5-trisphosphate formation in Dictyostelium and rat liver. J. Biol. Chem., 1995, 270, 29724-29731.
    • (1995) J. Biol. Chem , vol.270 , pp. 29724-29731
    • Van Dijken, P.1    De Haas, J.R.2    Craxton, A.3    Erneux, C.4    Shears, S.B.5    Van Haastert, P.J.M.6
  • 34
    • 0030684148 scopus 로고    scopus 로고
    • Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase
    • Craxton, A.; Caffrey, J.J.; Burkhart, W.; Safrany, S.T.; Shears, S.B. Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase. Biochem. J., 1997, 328, 75-81.
    • (1997) Biochem. J , vol.328 , pp. 75-81
    • Craxton, A.1    Caffrey, J.J.2    Burkhart, W.3    Safrany, S.T.4    Shears, S.B.5
  • 36
    • 43149103174 scopus 로고    scopus 로고
    • Dephosphorylation of 2, 3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt
    • Cho, J.; King, J.S.; Qian, X.; Harwood, A.J.; Shears, S.B. Dephosphorylation of 2, 3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt. Proc. Natl. Acad. Sci. USA, 2008, 105, 5998-6003.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5998-6003
    • Cho, J.1    King, J.S.2    Qian, X.3    Harwood, A.J.4    Shears, S.B.5
  • 37
    • 0014360315 scopus 로고
    • The interaction of hemoglobin and its subunits with 2, 3-diphosphoglycerate
    • USA
    • Benesch, R.; Benesch, R.E.; Enoki, Y. The interaction of hemoglobin and its subunits with 2, 3-diphosphoglycerate. Proc. Natl. Acad. Sci. USA, 1968, 61, 1102-1106.
    • (1968) Proc. Natl. Acad. Sci , vol.61 , pp. 1102-1106
    • Benesch, R.1    Benesch, R.E.2    Enoki, Y.3
  • 38
    • 0014250343 scopus 로고
    • Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin
    • USA
    • Benesch, R.; Benesch, R.E.; Yu, C.I. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proc. Natl. Acad. Sci. USA, 1968, 59, 526-532.
    • (1968) Proc. Natl. Acad. Sci , vol.59 , pp. 526-532
    • Benesch, R.1    Benesch, R.E.2    Yu, C.I.3
  • 39
    • 0028946336 scopus 로고
    • Structure and mechanism of inositol monophosphatase
    • Atack, J.R.; Broughton, H.B.; Pollack, S.J. Structure and mechanism of inositol monophosphatase. FEBS Lett., 1995, 361, 1-7.
    • (1995) FEBS Lett , vol.361 , pp. 1-7
    • Atack, J.R.1    Broughton, H.B.2    Pollack, S.J.3
  • 40
    • 0037414868 scopus 로고    scopus 로고
    • Regulation of chromatin remodeling by inositol polyphosphates
    • Steger, D.J.; Haswell, E.S.; Miller, A.L.; Wente, S.R.; O'Shea, E.K. Regulation of chromatin remodeling by inositol polyphosphates. Science, 2003, 299, 114-116.
    • (2003) Science , vol.299 , pp. 114-116
    • Steger, D.J.1    Haswell, E.S.2    Miller, A.L.3    Wente, S.R.4    O'Shea, E.K.5
  • 41
    • 34548859800 scopus 로고    scopus 로고
    • Inositol pentakisphosphate mediates Wnt/beta-catenin signaling
    • Gao, Y.; Wang, H.Y. Inositol pentakisphosphate mediates Wnt/beta-catenin signaling. J. Biol. Chem., 2007, 282, 26490-26502.
    • (2007) J. Biol. Chem , vol.282 , pp. 26490-26502
    • Gao, Y.1    Wang, H.Y.2
  • 42
    • 0037414839 scopus 로고    scopus 로고
    • Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates
    • Shen, X.; Xiao, H.; Ranallo, R.; Wu, W.H.; Wu, C. Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates. Science, 2003, 299, 112-114.
    • (2003) Science , vol.299 , pp. 112-114
    • Shen, X.1    Xiao, H.2    Ranallo, R.3    Wu, W.H.4    Wu, C.5
  • 43
    • 41549120972 scopus 로고    scopus 로고
    • Cellular and subcellular distribution of rat brain prolyl oligopeptidase and its association with specific neuronal neurotransmitters
    • Myohanen, T.T.; Venalainen, J.I.; Garcia-Horsman, J.A.; Piltonen, M.; Mannisto, P.T. Cellular and subcellular distribution of rat brain prolyl oligopeptidase and its association with specific neuronal neurotransmitters. J. Comp. Neurol., 2008, 507, 1694-1708.
    • (2008) J. Comp. Neurol , vol.507 , pp. 1694-1708
    • Myohanen, T.T.1    Venalainen, J.I.2    Garcia-Horsman, J.A.3    Piltonen, M.4    Mannisto, P.T.5
  • 45
    • 43949142408 scopus 로고    scopus 로고
    • Spatial association of prolyl oligopeptidase, inositol 1,4,5-triphosphate type 1 receptor, substance P and its neurokinin-1 receptor in the rat brain: An immunohistochemical colocalization study
    • Myohanen, T.T.; Venalainen, J.I.; Garcia-Horsman, J.A.; Mannisto, P.T. Spatial association of prolyl oligopeptidase, inositol 1,4,5-triphosphate type 1 receptor, substance P and its neurokinin-1 receptor in the rat brain: an immunohistochemical colocalization study. Neuroscience, 2008, 153, 1177-1189.
    • (2008) Neuroscience , vol.153 , pp. 1177-1189
    • Myohanen, T.T.1    Venalainen, J.I.2    Garcia-Horsman, J.A.3    Mannisto, P.T.4
  • 47
    • 0037118050 scopus 로고    scopus 로고
    • A common mechanism of action for three mood stabilizing drugs
    • Williams, R.S.; Cheng, L.; Mudge, A.W.; Harwood, A.J. A common mechanism of action for three mood stabilizing drugs. Nature, 2002, 417, 292-295.
    • (2002) Nature , vol.417 , pp. 292-295
    • Williams, R.S.1    Cheng, L.2    Mudge, A.W.3    Harwood, A.J.4
  • 50
    • 0028217535 scopus 로고
    • Lower serum prolyl endopeptidase enzyme activity in major depression: Further evidence that peptidases play a role in the pathophysiology of depression. Biol
    • Maes, M.; Goossens, F.; Scharpe, S.; Meltzer, H.Y.; D'Hondt, P.; Cosyns, P. Lower serum prolyl endopeptidase enzyme activity in major depression: further evidence that peptidases play a role in the pathophysiology of depression. Biol. Psychiatry, 1994, 35, 545-552.
    • (1994) Psychiatry , vol.35 , pp. 545-552
    • Maes, M.1    Goossens, F.2    Scharpe, S.3    Meltzer, H.Y.4    D'Hondt, P.5    Cosyns, P.6
  • 51
    • 0028802506 scopus 로고
    • Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: Effects of antidepressants, mood stabilizers, and antipsychotic drugs
    • Maes, M.; Goossens, F.; Scharpe, S.; Calabrese, J.; Desnyder, R.; Meltzer, H.Y. Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: effects of antidepressants, mood stabilizers, and antipsychotic drugs. Psychiatry Res., 1995, 58, 217-225.
    • (1995) Psychiatry Res , vol.58 , pp. 217-225
    • Maes, M.1    Goossens, F.2    Scharpe, S.3    Calabrese, J.4    Desnyder, R.5    Meltzer, H.Y.6
  • 55
    • 0000685667 scopus 로고    scopus 로고
    • A human myo-inositol monophosphatase gene (IMPA2) localized in a putative susceptibility region for bipolar disorder on chromosome 18p11.2: Genomic structure and polymorphism screening in manic-depressive patients
    • Sjoholt, G.; Gulbrandsen, A.K.; Lovlie, R.; Berle, J.O.; Molven, A.; Steen, V.M. A human myo-inositol monophosphatase gene (IMPA2) localized in a putative susceptibility region for bipolar disorder on chromosome 18p11.2: genomic structure and polymorphism screening in manic-depressive patients. Mol. Psychiatry, 2000, 5, 172-180.
    • (2000) Mol. Psychiatry , vol.5 , pp. 172-180
    • Sjoholt, G.1    Gulbrandsen, A.K.2    Lovlie, R.3    Berle, J.O.4    Molven, A.5    Steen, V.M.6


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