Inhibition of tau phosphorylation: a new therapeutic strategy for the treatment of Alzheimer’s disease and other neurodegenerative disorders

Bibliography

• DUYCKAERTS C, COLLE MA, HAUW JJ: A sketch of Alzheimer's disease histopathology. In: Alzheimer's disease, and related disorders. Etiology, pathogenesis and therapeutics. Iqbal K, Swaab DF, Winlad B, Wisniewski HM (Eds.), John Wiley and Sons, Sussex, UK (1999):137–152.
   Google Scholar
• •A detailed description of the AD histopathology
   Google Scholar
• FELICIAN O, SANDSON TA: The neurobiology andpharmacotherapy of Alzheimer's disease. J. Neuropsy-chiatly Clin. NeuroscL (1999) 11:19–31.
   PubMed Web of Science ®Google Scholar
• BRAAK H, BRAAK E, GRUNDKE-IQBAL I, IQBAL K:Occurrence of neuropil threads in the senile human brain and in Alzheimer's disease: a third location of paired helical filaments outside the neurofibrillary tangles and neuritic plaques. Neurosci. Lett. (1986) 65:351–355.
   PubMed Web of Science ®Google Scholar
• RUBEN GC, WANG JZ, GRUNDKE-IQBAL I, IQBAL K:Paired helical filaments have a wide range of widths with similar helical periods. In: Alzheimer's disease, and related disorders. Etiology, pathogenesis and therapeutics. Iqbal K, Swaab DF, Winlad B, Wisniewski HM (Eds.), John Wiley and Sons, Sussex, UK (1999):187–192.
   Google Scholar
• JOHNSON GVW, HARTIGAN JA: Tau protein in normaland Alzheimer's disease brain: an update. Alzheimer's Dis. Rev. (1998) 3:125–141.
   Google Scholar
• BRANDT R, EIDENMULLER J: The tau proteins inAlzheimer's disease. Mol. Biol. Alzheimer's Dis. (1998) 17–43.
   Google Scholar
• TOLNAY M, PROBST A: Tau protein pathology inAlzheimer's disease and related disorders. Neuropathol. Appl. Neurobiol (1999) 25:171–187.
   PubMedGoogle Scholar
• SPILLANTINI MG, GOEDERT M: Tau protein pathologyin neurodegenerative disease. Trends NeuroscL (1998) 21:428–433.
   PubMed Web of Science ®Google Scholar
• SAYAS CL, MORENO-FLORES MT, AVILA J, WANDOSELL F: The neurite retraction induced by lysophosphatidic acid increases Alzheimer's disease-like tau phospho-rylation. j Biol. Chem. (1999) 274:37046–37052.
   PubMed Web of Science ®Google Scholar
• LARNER AJ: Tau protein as a therapeutic target in Alzheimer's disease and other neurodegenerative disorders. Exp. Opin. Ther. Patents (1999) 9:1359–1370.
   Web of Science ®Google Scholar
• ••Describes the main features of tau protein considered as atherapeutic target.
   Google Scholar
• BUEE L, DELACOURTE A: Comparative biochemistry oftau in progressive supranuclear palsy, corticobasal degeneration, F11)P-17 and Pick's disease. Brain Pathol. (1999) 9:681–693.
   PubMed Web of Science ®Google Scholar
• REYNOLDS CH, BETTS JC, BALCKSTOCK WP, NEBREDAAR, ANDERTON BH: Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38 and glycogen synthase kinase 3-beta. J. Neurochem. (2000) 74:1587–1595.
   PubMed Web of Science ®Google Scholar
• HOLZER M, HOLZAPFEL HP, KROHN K, GERTZ HJ, ARENDT T: Alterations in content and phosphoryla-tion state of cytoskeletal proteins in the sciatic nerve during ageing and Alzheimer's disease. J. Neural. Transm. (1999) 106:743–755.
   PubMedGoogle Scholar
• IMAHORI K, UCHIDA T: Physiology and pathology oftau protein kinases in relation to Alzheimer's disease. Biochem. (1997) 121:179–188.
   Google Scholar
• IQBAL K, ALONSO A, GONG CX et al.: Tau phosphatases.Brain Microtubule Assoc. Proteins (1997) 95–111.
   Google Scholar
• CHENG LY, WANG JZ, GONG CX et al: Multiple forms ofphosphatase from human brain: isolation and partial characterization of Affi-Gel blue binding phosphatases. Neurochem. Res. (2000) 25:107–120.
   PubMedGoogle Scholar
• IQBAL K, ALONSO A, GONDAL JA et al.: Inhibition of neurofibrillary degeneration: a rational promising therapeutic target. In: Alzheimer's disease, and related disorders. Etiology, pathogenesis and therapeutics. Iqbal K, Swaab DF, Winlad B, Wisniewski HM (Eds.), John Wiley and Sons, Sussex, UK (1999):270–280.
   Google Scholar
• ••A thorough review of the molecular basis of neurofibrillarydegeneration.
   Google Scholar
• SENGUPTA A, WU Q, GRUNDKE-IQBAL I, IQBAL K, SINGH TJ: Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5. Mol. Biochem. (1997) 167:99–105.
   Google Scholar
• IMAHORI K, UCHIDA T: Physiology and pathology of tau protein kinases in relation to Alzheimer's disease. Biochem. (1997) 121:179–188.
   Google Scholar
• ISHIGURO K, SHIRATSUCHI A, SATO S et al.: Glycogen synthase 3-beta is identical to tau protein kinase I generating several epitopes of paired helical filaments. FEBS Lett. (1993) 325:167–172.
   PubMed Web of Science ®Google Scholar
• ISHIGURO K, KOBAYASHI S, OMORI A et al: Identifiac-tion of the 23 kDa subunit of tau protein kinase II as a putative activator of cdk5 in bovine brain. FEBS Lett. (1994) 342:203–208.
   PubMedGoogle Scholar
• JICHA GA, WEAVER C, LANE E et al.: cAMP-dependent protein kinase phosphorylation on tau Alzheimer's disease. J NeuroscL (1999) 19:7486–7494.
   PubMed Web of Science ®Google Scholar
• SINGH TJ, GRUNDKE-IQBAL,WU QL et al: Protein kinase C and calcium/calmodulin-dependent protein kinase II phosphorylate three repeat and four repeat tau isoforms at different rates. Mol Cell Biochem. (1997) 167:141–148.
   Google Scholar
• WANG JZ, WU Q, SMITH A, GRUNDKE-IKQBAL I, IQBALK: Tau is phosphorylated by GSK-3 at several sites found in Alzheimer's disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kin ase FEBSS Lett. (1998) 436:28-34.
   Google Scholar
• RAGANO-CARACCIOLO M, WILLIAM K, MILLER MW, HANOVER JA: Nuclear glycogen and glycogen synthase kinase 3. Biochem. Biophys. Res. Commun. (1998) 249:422–427.
   PubMedGoogle Scholar
• LAU KF, MILLER CCJ, ANDERTON BH, SHAW PC: Expres-sion analysis of glycogen synthase kinase-3 in human tissues. j Pept. Res. (1999) 54:85–91.
   PubMedGoogle Scholar
• YOST C, FARR GH, PIERCE SB, FERKEY DM, CHEN MM, KIMELMAN D: GBP, an inhibitor of GSK-3, is implicated in Xenopus development and oncogenesis. Cell (1998) 93:1031–1041.
   PubMed Web of Science ®Google Scholar
• SUMMERS SA, KAO AW, KOHN AD et al.: The role ofglycogen synthase kinase 3 beta in insulin-stimulated glucose metabolism. J Biol. Chem. (1999) 274:17934–17940.
   PubMed Web of Science ®Google Scholar
• MARCUS EA, KINTNER C, HARRIS W: The role of GSK-3beta in regulating neuronal differentiation in Xenopus laevis. Mol. Cell. Neurosci. (1998) 12:269–280.
   PubMedGoogle Scholar
• MUNOZ-MONTANO JR, LIM F, MORENO FJ, AVILA J, DIAZ-NIDO J: Glycogen synthase kinase-3I3 regulates axonal outgrowth in cultured neurons. J. Alzheimer's Dis. (1999) 1:361–378.
   PubMedGoogle Scholar
• MAGGIRWAR SB, TONG N, RAMIREZ S, GELBARD HA, DEWHURST S: HIV-1 tat-mediated activation of GSK-3I3 contributes to tat-mediated neurotoxicity. J. Neurochem. (1999) 73:578–586.
   PubMed Web of Science ®Google Scholar
• BROWNLESS J, IRVING NG, BRION JP et al: Tau phospho-rylation in transgenic mice expressing glycogen synthase kinase-3I3 transgenes. NeuroReport (1997) 8:3251–3255.
   PubMedGoogle Scholar
• WANG JZ, WU Q, SMITH A, GRUNDKE-IQBAL I, IQBAL K: Tau is phosphorylated by GSK-3 at several sites found in Alzheimer's disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase. FEBS Lett. (1998) 436:28–34.
   PubMed Web of Science ®Google Scholar
• MORENO F, MUSIOZ-MONTANO JR, AVILA J: Glycogen synthase kinase 3 phosphorylation of different residues in the presence of different factors: analysis of tau protein. Mol. Cell. Biochem. (1996) 165 :47–54.
   PubMedGoogle Scholar
• UTTON MA, VANDECANDELAERE A, WAGNER U et al.: Phosphorylation of tau by glycogen synthase kinase-3I3 affects the ability of tau to promote microtu- bule self-assembly. Biochem. J (1997) 323:741–747.
   PubMedGoogle Scholar
• GOOLD RG, OWEN R, GORDON-WEEKS PR: 13 Phospho-rylation of microtubule-associated protein 1B regulates the stability of microtubules in growth cones. J Cell ScL (1999) 112:3373–3384.
   PubMedGoogle Scholar
• PEI JJ, BRAAK E, GRUNDKE-IQBAL I, IQBAL K, WINBLAD B, COWBURN RF: Distribution of active glycogen synthase kinase 3P (GSK-3I3) in brains staged for Alzheimer's disease neurofibrillary changes. J. Neuropathol. Exp. Neurol (1999) 58:1010–1019.
   PubMed Web of Science ®Google Scholar
• ANDO S, IKUHARA T, KAMATA T et al.: Role of thepyrrolidine ring of proline in determining the substrate specificity of cdc2 kinase or cdk5. j Biochem. (1997) 122:409–414.
   PubMedGoogle Scholar
• CHOU KC, WATENPAUGHT KD, HEIRIKSON RL: A modelof the complex between cyclin-dependent kinase 5 and the activation domain of neuronal cdk5 activator. Biochem. Biophys. Res. Commun. (1999) 259:420–428.
   PubMed Web of Science ®Google Scholar
• •A 3-dimensional model of CDK5/p35 dimer is proposed. Very interesting for the design of inhibitors of TPK II.
   Google Scholar
• PATRICK GN, ZHOU P, KWON YT, HOWLEY PM, TSAI LH: p35, the neuronal-specific activator of cyclin dependent kinase 5 (cdk5) is degradated by the ubiquitin-proteasome pathway. J Biol. Chem. (1998) 273:24057–24064.
   PubMed Web of Science ®Google Scholar
• GRAY N, DETIVAUD L, DOERING C, MEIJER L: ATP-siteddirected inhibitors of cyclin-dependent kinases. Curr. Med. Chem. (1999) 6:859–875.
   PubMed Web of Science ®Google Scholar
• PIGINO G, PAGLINI G, ULLOA L, AVILA J, CACERES A: Analysis of the expression, distribution and function of cyclin dependent kinase 5 (cdk5) in developing cerebellar macromolecules. J. Cell Sci. (1997) 110:257–270.
   PubMed Web of Science ®Google Scholar
• PAVIA J, DE CEBALLOS ML, DE LA CUESTA F: Alzheimer's disease: relationship between muscarinic cholinergic receptors, P-amyloid and tau proteins. Fundam. Clin. Pharmacol. (1998) 12:473–481.
   PubMedGoogle Scholar
• FERREIRA A, LU Q, ORECCHIO L, KOSIK KS: Selective phosphorylation of adult tau isoforms in mature hipp ocampal neurons exposed to fibrillar Ab. Mol. Cell NeuroscL (1997) 9:220–234.
   PubMedGoogle Scholar
• TAKASHISMA A, HONDA T, YASUTAKE K et al.: Activa-tion of tau protein kinase 1/glycogen synthase kinase-3b by amiloid b peptide (25-35) enhances phosphorylation of tau in hippocampal neurons. NeuroscL Res. (1998) 31:317–323.
   PubMedGoogle Scholar
• ALVAREZ G, MUSIOZ-MONTAN JR, SATRUSTEGUI J, AVILA J: Lithium protects cultured neurons against P-amyloid-induced neurodegeneration. FEBS Lett. (1999) 453:260–264.
   PubMed Web of Science ®Google Scholar
• ALVAREZ A, TORO R, CACERES A, MACCIONI RB: Inhibi-tion of tau phosphorylating protein kinase cdk5 prevents b-amyloid-induced neuronal death. FEBS Lett. (1999) 459:421–426.
   PubMedGoogle Scholar
• MANJI HK, MOORE GJ, CHEN G: lithium at 50: have the neuroprotective affects of this unique cation been overlooked? Biol. Psychiatry (1999) 46:929–940.
   Web of Science ®Google Scholar
• MCKEON-O'MALLEY C, SAUNDERS A, BUSH A, TANZI R: Potential therapeutic targets for Alzheimer's disease. Emerging Therapeutic Targets (1998) 2:157–179.
   Google Scholar
• EMMERLING MR, SPIEGEL K, HALL ED et al.: Emerging strategies for the treatment of Alzheimer's disease at the millennium. Emerging Drugs (1999) 4:35–86.
   Google Scholar
• RYVES WJ, FRYER L, DALE T, HARWOOD AJ: An assay for glycogen synthase kinase 3 (GSK-3) for use in crude cell extracts. Anal. Biochem. (1998) 264:124–127.
   PubMedGoogle Scholar
• WELSH G, PATEL JC, PROUD CG: Peptide substrate suitable for assaying glycogen synthase kinase-3 in crude cell extracts. Anal. Biochem. (1997) 244:16–21.
   PubMedGoogle Scholar
• YANAG-ISAWA M, PLANEL E, ISHIGURO K, FUJITA SC: Starvation induces tau phosphorylation in mouse brain: implications for Alzheimer's disease. FEBS Lett. (1999) 46:329–333.
   Google Scholar
• AHLIJANIAN MK, BARREZUETA NX, WILLIAMS RD et al.: Hyperphosphorylated tau and neurofilament and cytoskeletal disruptions in mice overexpressing human p25, an activator of cdk5. Proc. Natl. Acad. ScL USA (2000) 97:2910–2915.
   PubMed Web of Science ®Google Scholar
• STAMBOLIC V, RUEL L, WOODGETT JR: lithium inhibits glycogen synthase kinase-3 activity and mimics Wingless signaling in intact cells. Curr. Biol. (1996) 6:1664–1668.
   PubMed Web of Science ®Google Scholar
• MUSIOZ-MONTANO JR, MORENO F, AVILA J, DIAZ-NIDO J: Lithium inhibits Alzheimer's disease-like tau protein phosphorylation in neurons. FEBS Lett. (1997) 411:183–188.
   PubMedGoogle Scholar
• LOVESTONE S, DAVIS DR, WEBSTER MT et al: lithiumreduces tau phosphorylation: effects in living cells and in neurons at therapeutic concentrations. Biol. Psychiatry (1999) 45:995–1003.
   PubMed Web of Science ®Google Scholar
• NORMAN TC, GRAY NS, KOH JT, SCHULTZ PG: A structure-based library approach to kinase inhibitors. J. Am. Chem. Soc. (1996) 118:7430–7431.
   Web of Science ®Google Scholar
• HERS I, TAVARE JM, DENTON RM: The protein kinase Cinhibitors bisindolylmaleimide I (GF 109203x) and IX (Ro 31-8220) are potent inhibitors of glycogen synthase kinase-3 activity. FEBS Lett. (1999) 460:433–436.
   PubMed Web of Science ®Google Scholar
• MEIJER L, THUNNISSEN AM, WHITE AW et al: Inhibitionof cyclin-dependent kinases, GSK-313 and CK1 by hymenialdisine, a marine sponge constituent. Chem. Biol. (2000) 7:51–63.
   PubMed Web of Science ®Google Scholar
• ZAHAREVITZ DW, GUSSIO R, LEOST M et al.: Discoveryand initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases. Cancer Res. (1999) 59:2566–2569
   PubMed Web of Science ®Google Scholar
• HOESSEL R, LECLERCQ S, ENDICOTT JA et al: In dirubin,the active constituent of a Chinese an tileukaemia medicine, inhibits cyclin -dep en den t kinases. Nature Cell Biol. (1999) 1:60–67.
   PubMed Web of Science ®Google Scholar
• GARCIA-ECHEVARRIA C, TRAXLER P, EVANS DB: ATP site-directed competitive and irreversible inhibitors of protein kinases. Med. Res. Rev. (2000) 20:28–57.
   PubMedGoogle Scholar
• ROSANIA GR, CHANG YT: Targeting hyperproliferativedisorders with cyclin dependent kinase inhibitors. Exp. Opin. Ther. Patents (2000) 10(2):215–230.
   Web of Science ®Google Scholar
• ISHIGURO K, HOSHI M, TAKASHIMA A: Involvement oftau protein kinase I/GSK-3 in Alzheimer's disease pathogenesis. Kinases Phosph. Lymph. Neur. Sig. (1997) 272–282.
   Google Scholar
• ISHIGURO K: Involvement of tau protein kinase inamyloid-13-in duced neurodegeneration. Rinsho Byori (1998) 46:1003–1007.
   PubMedGoogle Scholar
• ISHIGURO K, HOSHI M, TAKASHIMA A: An approach toAlzheimer's disease with TPK 1. Shinkei Kenkyu no Shinpo (1997) 41:866–871.
   Google Scholar
• IMAHORI K, HOSHI M: Tau protein kinase 1 /GSK-3b andacetylcholine metabolism. Dementia Jpn. (1997) 11:105–109.
   Google Scholar
• HERMANN M, GOLOMBOWSKI S, KRAUCHI K et al: IIISA-quantitation of phosphorylated tau protein in the Alzheimer's disease brain. Eur. Neurol. (1999) 42:205–210.
   PubMedGoogle Scholar
• GU M, WANG X, MU Y, FAN M: Development in theresearch of molecular mechanism of Alzheimer's disease. Chin. Sci. Bull. (1999) 44:1257–1264.
   Google Scholar