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Volumn 1790, Issue 3, 2009, Pages 188-197

Biochemical characterization of tau protein and its associated syndapin 1 and protein kinase Ce{open} for their functional regulation in rat brain

Author keywords

Casein kinase 1; Cholesterol 3 sulfate; Glycogen synthase kinase 3 ; Protein kinase Ce open ; Rat brain; Sulfatide; Syndapin 1; Tau protein

Indexed keywords

BRAIN PROTEIN; GLYCOGEN SYNTHASE KINASE 3BETA; ISOPROTEIN; PROTEIN KINASE C EPSILON; SYNDAPIN 1; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 60249089296     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.11.007     Document Type: Article
Times cited : (4)

References (39)
  • 1
    • 0029922250 scopus 로고    scopus 로고
    • Tau is enriched on dynamic microtubules in the distal region of growing axons
    • Black M.M., Slaughter T., Moshiach S., Obrocka M., and Fischer I. Tau is enriched on dynamic microtubules in the distal region of growing axons. J. Neurosci. 16 (1996) 3601-3619
    • (1996) J. Neurosci. , vol.16 , pp. 3601-3619
    • Black, M.M.1    Slaughter, T.2    Moshiach, S.3    Obrocka, M.4    Fischer, I.5
  • 2
    • 0038292060 scopus 로고    scopus 로고
    • Isoforms changes of tau protein during development in various species
    • Takuma H., Arawaka S., and Mori H. Isoforms changes of tau protein during development in various species. Brain Res. Dev. Brain Res. 142 (2003) 121-127
    • (2003) Brain Res. Dev. Brain Res. , vol.142 , pp. 121-127
    • Takuma, H.1    Arawaka, S.2    Mori, H.3
  • 3
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • Avila J., Lucas J.J., Perez M., and Hernandez F. Role of tau protein in both physiological and pathological conditions. Physiol. Rev. 84 (2004) 361-384
    • (2004) Physiol. Rev. , vol.84 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3    Hernandez, F.4
  • 6
    • 1942469505 scopus 로고    scopus 로고
    • Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules
    • Li G., Yin H., and Kuret J. Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules. J. Biol. Chem. 279 (2004) 15938-15945
    • (2004) J. Biol. Chem. , vol.279 , pp. 15938-15945
    • Li, G.1    Yin, H.2    Kuret, J.3
  • 9
    • 0036644988 scopus 로고    scopus 로고
    • Expression of the myelin and oligodendrocyte progenitor marker sulfatide in neurons and astrocytes of adult rat brain
    • Pernber Z., Molander-Melin M., Berthold C.H., Hansson E., and Fredman P. Expression of the myelin and oligodendrocyte progenitor marker sulfatide in neurons and astrocytes of adult rat brain. J. Neurosci. Res. 69 (2002) 86-93
    • (2002) J. Neurosci. Res. , vol.69 , pp. 86-93
    • Pernber, Z.1    Molander-Melin, M.2    Berthold, C.H.3    Hansson, E.4    Fredman, P.5
  • 11
    • 34548167106 scopus 로고    scopus 로고
    • Sulfatide storage in neurons causes hyperexcitability and axonal degeneration in a mouse model of metachromatic leukodystrophy
    • Eckhardt M., Hedayati K.K., Pitsch J., Lüllmann-Rauch R., Beck H., Fewou S.N., and Gieselmann V. Sulfatide storage in neurons causes hyperexcitability and axonal degeneration in a mouse model of metachromatic leukodystrophy. J. Neurosci. 27 (2007) 9009-9021
    • (2007) J. Neurosci. , vol.27 , pp. 9009-9021
    • Eckhardt, M.1    Hedayati, K.K.2    Pitsch, J.3    Lüllmann-Rauch, R.4    Beck, H.5    Fewou, S.N.6    Gieselmann, V.7
  • 12
    • 0026658286 scopus 로고
    • 4+ oligodendrocytes in postnatal rat cerebellum: analysis in unfixed tissue slices using anti-glycolipid antibodies
    • 4+ oligodendrocytes in postnatal rat cerebellum: analysis in unfixed tissue slices using anti-glycolipid antibodies. J. Neurosci. Res. 33 (1992) 338-353
    • (1992) J. Neurosci. Res. , vol.33 , pp. 338-353
    • Warrington, A.E.1    Pfeiffer, S.E.2
  • 13
    • 36448995805 scopus 로고    scopus 로고
    • Developmental changes of glycosphingolipids and expression of glycogenes in mouse brains
    • Ngamukote S., Yanagisawa M., Ariga T., Ando S., and Yu R.K. Developmental changes of glycosphingolipids and expression of glycogenes in mouse brains. J. Neurochem. 103 (2007) 2327-2341
    • (2007) J. Neurochem. , vol.103 , pp. 2327-2341
    • Ngamukote, S.1    Yanagisawa, M.2    Ariga, T.3    Ando, S.4    Yu, R.K.5
  • 14
    • 0142074270 scopus 로고    scopus 로고
    • Cholesterol sulfate in human physiology: what's it all about?
    • Strott C.A., and Higashi Y. Cholesterol sulfate in human physiology: what's it all about?. J. Lipid Res. 44 (2003) 1268-1278
    • (2003) J. Lipid Res. , vol.44 , pp. 1268-1278
    • Strott, C.A.1    Higashi, Y.2
  • 15
    • 84919585371 scopus 로고
    • X-linked ichthyosis due to steroid-sulphatase deficiency
    • Webster D., France J.T., Shapiro L.J., and Weiss R. X-linked ichthyosis due to steroid-sulphatase deficiency. Lancet 1 (1978) 70-72
    • (1978) Lancet , vol.1 , pp. 70-72
    • Webster, D.1    France, J.T.2    Shapiro, L.J.3    Weiss, R.4
  • 16
    • 38849101462 scopus 로고    scopus 로고
    • A novel consensus phosphorylation motif in sulfatide- and cholesterol-3-sulfate-binding protein substrates for CK1 in vitro
    • Kawakami F., Suzuki K., and Ohtsuki K. A novel consensus phosphorylation motif in sulfatide- and cholesterol-3-sulfate-binding protein substrates for CK1 in vitro. Biol. Pharm. Bull. 31 (2008) 193-200
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 193-200
    • Kawakami, F.1    Suzuki, K.2    Ohtsuki, K.3
  • 17
    • 40549107427 scopus 로고    scopus 로고
    • Biochemical characterization of phospholipids, sulfatide and heparin as potent stimulators for autophosphorylation of GSK-3β and the GSK-3β-mediated phosphorylation of myelin basic protein in vitro
    • Kawakami F., Yamaguchi A., Suzuki K., Yamamoto T., and Ohtsuki K. Biochemical characterization of phospholipids, sulfatide and heparin as potent stimulators for autophosphorylation of GSK-3β and the GSK-3β-mediated phosphorylation of myelin basic protein in vitro. J. Biochem. 143 (2008) 359-367
    • (2008) J. Biochem. , vol.143 , pp. 359-367
    • Kawakami, F.1    Yamaguchi, A.2    Suzuki, K.3    Yamamoto, T.4    Ohtsuki, K.5
  • 18
    • 33644897325 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a fibroblast growth factor-binding protein (FGF-BP) from the lactoferrin fraction of bovine milk
    • Kawakami A., Hirayama K., Kawakami F., Kawakami H., Fujihara M., and Ohtsuki K. Purification and biochemical characterization of a fibroblast growth factor-binding protein (FGF-BP) from the lactoferrin fraction of bovine milk. Biochim. Biophys. Acta 1760 (2006) 421-431
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 421-431
    • Kawakami, A.1    Hirayama, K.2    Kawakami, F.3    Kawakami, H.4    Fujihara, M.5    Ohtsuki, K.6
  • 19
    • 23844433938 scopus 로고    scopus 로고
    • Biochemical characterization of an effective substrate and potent activators of CK2 copurified with Bowman-Birk-type proteinase inhibitor from soybean seeds in vitro
    • Katano T., Kamata Y., Ueno T., Furuya T., Nakamura T., and Ohtsuki K. Biochemical characterization of an effective substrate and potent activators of CK2 copurified with Bowman-Birk-type proteinase inhibitor from soybean seeds in vitro. Biochim. Biophys. Acta 1725 (2005) 47-56
    • (2005) Biochim. Biophys. Acta , vol.1725 , pp. 47-56
    • Katano, T.1    Kamata, Y.2    Ueno, T.3    Furuya, T.4    Nakamura, T.5    Ohtsuki, K.6
  • 20
  • 22
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258 (1992) 607-614
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 23
    • 0026609681 scopus 로고
    • Isolation and characterization of the e{open} subspecies of protein kinase C from rat brain
    • Koide H., Ogita K., Kikkawa U., and Nishizuka Y. Isolation and characterization of the e{open} subspecies of protein kinase C from rat brain. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 1149-1153
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 1149-1153
    • Koide, H.1    Ogita, K.2    Kikkawa, U.3    Nishizuka, Y.4
  • 24
    • 0028216874 scopus 로고
    • The protein kinase C family for neuronal signaling
    • Tanaka C., and Nishizuka C.Y. The protein kinase C family for neuronal signaling. Annu. Rev. Neurosci. 17 (1994) 551-567
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 551-567
    • Tanaka, C.1    Nishizuka, C.Y.2
  • 25
    • 33846528583 scopus 로고    scopus 로고
    • PKC signaling deficits: a mechanistic hypothesis for the origins of Alzheimer's disease
    • Alkon D.L., Sun M.K., and Nelson T.J. PKC signaling deficits: a mechanistic hypothesis for the origins of Alzheimer's disease. Trends Pharmacol. Sci. 28 (2007) 51-60
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 51-60
    • Alkon, D.L.1    Sun, M.K.2    Nelson, T.J.3
  • 27
    • 0346434153 scopus 로고    scopus 로고
    • Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory
    • Liu S.J., Zhang A.H., Li H.L., Wang Q., Deng H.M., Netzer W.J., Xu H., and Wang J.Z. Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory. J. Neurochem. 87 (2003) 1333-1344
    • (2003) J. Neurochem. , vol.87 , pp. 1333-1344
    • Liu, S.J.1    Zhang, A.H.2    Li, H.L.3    Wang, Q.4    Deng, H.M.5    Netzer, W.J.6    Xu, H.7    Wang, J.Z.8
  • 28
    • 0034815845 scopus 로고    scopus 로고
    • Biochemical characterization of cholesterol-3-sulfate as the sole effector for the phosphorylation of HMG1 by casein kinase I in vitro
    • Okano M., Kano S., Munakata H., and Ohtsuki K. Biochemical characterization of cholesterol-3-sulfate as the sole effector for the phosphorylation of HMG1 by casein kinase I in vitro. Biochem. Biophys. Res. Commun. 281 (2001) 1325-1330
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 1325-1330
    • Okano, M.1    Kano, S.2    Munakata, H.3    Ohtsuki, K.4
  • 29
    • 16544386244 scopus 로고    scopus 로고
    • The effects of cholesterol-3-sulfate (CH-3S) on the phosphorylation of human C3a (hC3a) in vitro and on the ability of hC3a to induce vascular permeability in rats
    • Kawakami F., Ito M., Matsuda Y., Hayashi I., and Ohtsuki K. The effects of cholesterol-3-sulfate (CH-3S) on the phosphorylation of human C3a (hC3a) in vitro and on the ability of hC3a to induce vascular permeability in rats. Biol. Pharm. Bull. 27 (2004) 282-287
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 282-287
    • Kawakami, F.1    Ito, M.2    Matsuda, Y.3    Hayashi, I.4    Ohtsuki, K.5
  • 30
    • 0029888525 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II phosphorylates tau at Ser-262 but only partially inhibits its binding to microtubules
    • Singh T.J., Wang J.Z., Novak M., Kontzekova E., Grundke-Iqbal I., and Iqbal K. Calcium/calmodulin-dependent protein kinase II phosphorylates tau at Ser-262 but only partially inhibits its binding to microtubules. FEBS Lett. 387 (1996) 145-148
    • (1996) FEBS Lett. , vol.387 , pp. 145-148
    • Singh, T.J.1    Wang, J.Z.2    Novak, M.3    Kontzekova, E.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 31
    • 0026625670 scopus 로고
    • Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain
    • Correas I., Díaz-Nido J., and Avila J. Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain. J. Biol. Chem. 267 (1992) 15721-15728
    • (1992) J. Biol. Chem. , vol.267 , pp. 15721-15728
    • Correas, I.1    Díaz-Nido, J.2    Avila, J.3
  • 32
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions
    • Feng S., Chen J.K., Yu H., Simon J.A., and Schreiber S.L. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266 (1994) 1241-1247
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 33
    • 0022967090 scopus 로고
    • Microheterogeneity of microtubule-associated tau proteins is due to differences in phosphorylation
    • Butler M., and Shelanski M.L. Microheterogeneity of microtubule-associated tau proteins is due to differences in phosphorylation. J. Neurochem. 47 (1986) 1517-1522
    • (1986) J. Neurochem. , vol.47 , pp. 1517-1522
    • Butler, M.1    Shelanski, M.L.2
  • 35
    • 46749151737 scopus 로고    scopus 로고
    • Tau isoform expression and regulation in human cortical neurons
    • Deshpande A., Win K.M., and Busciglio J. Tau isoform expression and regulation in human cortical neurons. FASEB J. 22 (2008) 2357-2367
    • (2008) FASEB J. , vol.22 , pp. 2357-2367
    • Deshpande, A.1    Win, K.M.2    Busciglio, J.3
  • 37
    • 33847770454 scopus 로고    scopus 로고
    • Cross-talk between IGF-1 and estradiol in the brain: focus on neuroprotection
    • Garcia-Segura L.M., Sanz A., and Mendez P. Cross-talk between IGF-1 and estradiol in the brain: focus on neuroprotection. Neuroendocrinology 84 (2006) 275-279
    • (2006) Neuroendocrinology , vol.84 , pp. 275-279
    • Garcia-Segura, L.M.1    Sanz, A.2    Mendez, P.3
  • 38
    • 0034685703 scopus 로고    scopus 로고
    • Casein kinase 1 delta mRNA is upregulated in Alzheimer disease brain
    • Yasojima K., Kuret J., DeMaggio A.J., McGeer E., and McGeer P.L. Casein kinase 1 delta mRNA is upregulated in Alzheimer disease brain. Brain Res. 865 (2000) 116-120
    • (2000) Brain Res. , vol.865 , pp. 116-120
    • Yasojima, K.1    Kuret, J.2    DeMaggio, A.J.3    McGeer, E.4    McGeer, P.L.5
  • 39
    • 33646234697 scopus 로고    scopus 로고
    • Casein kinase-1 isoforms differentially associate with neurofibrillary and granulovacuolar degeneration lesions
    • Kannanayakal T.J., Tao H., Vandre D.D., and Kuret J. Casein kinase-1 isoforms differentially associate with neurofibrillary and granulovacuolar degeneration lesions. Acta Neuropathol. 111 (2006) 413-421
    • (2006) Acta Neuropathol. , vol.111 , pp. 413-421
    • Kannanayakal, T.J.1    Tao, H.2    Vandre, D.D.3    Kuret, J.4


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