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Volumn 172, Issue 3, 2015, Pages 829-840

Tubulin acetylation promoting potency and absorption efficacy of deacetylase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

AKG 2; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE INHIBITOR; MICROTUBULE ASSOCIATED PROTEIN; SILENT INFORMATION REGULATOR PROTEIN 2; TRICHOSTATIN A; TUBULIN; TUBULIN POLYMERIZATION PROMOTING PROTEIN; UNCLASSIFIED DRUG; HISTONE DEACETYLASE; NERVE PROTEIN; P25 PROTEIN, HUMAN;

EID: 84920843368     PISSN: 00071188     EISSN: 14765381     Source Type: Journal    
DOI: 10.1111/bph.12946     Document Type: Article
Times cited : (17)

References (41)
  • 2
    • 0028948839 scopus 로고
    • A theoretical basis for a biopharmaceutic drug classification: The correlation of in vitro drug product dissolution and in vivo bioavailability
    • Amidon GL, Lennernäs H, Shah VP, Crison JR (1995). A theoretical basis for a biopharmaceutic drug classification: the correlation of in vitro drug product dissolution and in vivo bioavailability. Pharm Res 12: 413-420.
    • (1995) Pharm Res , vol.12 , pp. 413-420
    • Amidon, G.L.1    Lennernäs, H.2    Shah, V.P.3    Crison, J.R.4
  • 3
    • 71249151075 scopus 로고    scopus 로고
    • Role of the oligodendroglial cytoskeleton in differentiation and myelination
    • Bauer NG, Richter-Landsberg C, Ffrench-Constant C (2009). Role of the oligodendroglial cytoskeleton in differentiation and myelination. Glia 57: 1691-1705.
    • (2009) Glia , vol.57 , pp. 1691-1705
    • Bauer, N.G.1    Richter-Landsberg, C.2    Ffrench-Constant, C.3
  • 5
  • 6
    • 65249107203 scopus 로고    scopus 로고
    • Microtubule assembly, organization and dynamics in axons and dendrites
    • Conde C, Cáceres A (2009). Microtubule assembly, organization and dynamics in axons and dendrites. Nat Rev Neurosci 10: 319-332.
    • (2009) Nat Rev Neurosci , vol.10 , pp. 319-332
    • Conde, C.1    Cáceres, A.2
  • 7
    • 59349089711 scopus 로고    scopus 로고
    • Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin
    • Creppe C, Malinouskaya L, Volvert ML, Gillard M, Close P, Malaise O et al. (2009). Elongator controls the migration and differentiation of cortical neurons through acetylation of alpha-tubulin. Cell 136: 551-564.
    • (2009) Cell , vol.136 , pp. 551-564
    • Creppe, C.1    Malinouskaya, L.2    Volvert, M.L.3    Gillard, M.4    Close, P.5    Malaise, O.6
  • 8
    • 84855602576 scopus 로고    scopus 로고
    • Interplay between microtubule dynamics and intracellular organization
    • De Forges H, Bouissou A, Perez F (2012). Interplay between microtubule dynamics and intracellular organization. Int J Biochem Cell Biol 44: 266-274.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 266-274
    • De Forges, H.1    Bouissou, A.2    Perez, F.3
  • 9
    • 0014589701 scopus 로고
    • Drug absorption. I. An in situ rat gut technique yielding realistic absorption rates
    • Doluisio JT, Billups NF, Dittert LW, Sugita ET, Swintosky JV (1969). Drug absorption. I. An in situ rat gut technique yielding realistic absorption rates. J Pharm Sci 58: 1196-1200.
    • (1969) J Pharm Sci , vol.58 , pp. 1196-1200
    • Doluisio, J.T.1    Billups, N.F.2    Dittert, L.W.3    Sugita, E.T.4    Swintosky, J.V.5
  • 10
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai R, Komatsu Y, Nishino N, Khochbin S, Yoshida M, Horinouchi S (2001). Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc Natl Acad Sci U S A 98: 87-92.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 11
    • 0037047003 scopus 로고    scopus 로고
    • Brain-specific p25 protein binds to tubulin and microtubules and induces aberrant microtubule assemblies at substoichiometric concentrations
    • Hlavanda E, Kovács J, Oláh J, Orosz F, Medzihradszky KF, Ovádi J (2002). Brain-specific p25 protein binds to tubulin and microtubules and induces aberrant microtubule assemblies at substoichiometric concentrations. Biochemistry 41: 8657-8664.
    • (2002) Biochemistry , vol.41 , pp. 8657-8664
    • Hlavanda, E.1    Kovács, J.2    Oláh, J.3    Orosz, F.4    Medzihradszky, K.F.5    Ovádi, J.6
  • 12
    • 78649351587 scopus 로고    scopus 로고
    • Tubulin polymerization promoting protein (TPPP/p25) as a marker for oligodendroglial changes in multiple sclerosis
    • Höftberger R, Fink S, Aboul-Enein F, Botond G, Oláh J, Berki T et al. (2010). Tubulin polymerization promoting protein (TPPP/p25) as a marker for oligodendroglial changes in multiple sclerosis. Glia 58: 1847-1857.
    • (2010) Glia , vol.58 , pp. 1847-1857
    • Höftberger, R.1    Fink, S.2    Aboul-Enein, F.3    Botond, G.4    Oláh, J.5    Berki, T.6
  • 14
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • Janke C, Bulinski JC (2011). Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions. Nat Rev Mol Cell Biol 12: 773-786.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 16
    • 84857426309 scopus 로고    scopus 로고
    • Ciliary and flagellar structure and function - their regulations by posttranslational modifications of axonemal tubulin
    • Konno A, Setou M, Ikegami K (2012). Ciliary and flagellar structure and function - their regulations by posttranslational modifications of axonemal tubulin. Int Rev Cell Mol Biol 294: 133-170.
    • (2012) Int Rev Cell Mol Biol , vol.294 , pp. 133-170
    • Konno, A.1    Setou, M.2    Ikegami, K.3
  • 17
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR (2000). Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 10: 524-530.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 18
    • 5144231819 scopus 로고    scopus 로고
    • Natively unfolded tubulin polymerization promoting protein TPPP/p25 is a common marker of alpha-synucleinopathies
    • Kovács GG, László L, Kovács J, Jensen PH, Lindersson E, Botond G et al. (2004). Natively unfolded tubulin polymerization promoting protein TPPP/p25 is a common marker of alpha-synucleinopathies. Neurobiol Dis 17: 155-162.
    • (2004) Neurobiol Dis , vol.17 , pp. 155-162
    • Kovács, G.G.1    László, L.2    Kovács, J.3    Jensen, P.H.4    Lindersson, E.5    Botond, G.6
  • 19
    • 12344322940 scopus 로고    scopus 로고
    • Dynamic targeting of microtubules by TPPP/p25 affects cell survival
    • Lehotzky A, Tirián L, To{combining double acute accent}kési N, Lénárt P, Szabó B, Kovács J et al. (2004). Dynamic targeting of microtubules by TPPP/p25 affects cell survival. J Cell Sci 117 (Pt 25): 6249-6259.
    • (2004) J Cell Sci , vol.117 , pp. 6249-6259
    • Lehotzky, A.1    Tirián, L.2    Tokési, N.3    Lénárt, P.4    Szabó, B.5    Kovács, J.6
  • 20
    • 73149109270 scopus 로고    scopus 로고
    • Tubulin polymerization-promoting protein (TPPP/p25) is critical for oligodendrocyte differentiation
    • Lehotzky A, Lau P, To{combining double acute accent}kési N, Muja N, Hudson LD, Ovádi J (2010). Tubulin polymerization-promoting protein (TPPP/p25) is critical for oligodendrocyte differentiation. Glia 58: 157-168.
    • (2010) Glia , vol.58 , pp. 157-168
    • Lehotzky, A.1    Lau, P.2    Tokési, N.3    Muja, N.4    Hudson, L.D.5    Ovádi, J.6
  • 21
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alpha-tubulin
    • Li W, Zhang B, Tang J, Cao Q, Wu Y, Wu C et al. (2007). Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alpha-tubulin. J Neurosci 27: 2606-2616.
    • (2007) J Neurosci , vol.27 , pp. 2606-2616
    • Li, W.1    Zhang, B.2    Tang, J.3    Cao, Q.4    Wu, Y.5    Wu, C.6
  • 22
    • 23944435458 scopus 로고    scopus 로고
    • PsN-Toolkit - A collection of computer intensive statistical methods for non-linear mixed effect modeling using NONMEM
    • Lindbom L, Pihlgren P, Jonsson EN (2005). PsN-Toolkit - a collection of computer intensive statistical methods for non-linear mixed effect modeling using NONMEM. Comput Methods Programs Biomed 79: 241-257.
    • (2005) Comput Methods Programs Biomed , vol.79 , pp. 241-257
    • Lindbom, L.1    Pihlgren, P.2    Jonsson, E.N.3
  • 23
    • 0026534003 scopus 로고
    • CG-4, a new bipotential glial cell line from rat brain, is capable of differentiating in vitro into either mature oligodendrocytes or type-2 astrocytes
    • Louis JC, Magal E, Muir D, Manthorpe M, Varon S (1992). CG-4, a new bipotential glial cell line from rat brain, is capable of differentiating in vitro into either mature oligodendrocytes or type-2 astrocytes. J Neurosci Res 31: 193-204.
    • (1992) J Neurosci Res , vol.31 , pp. 193-204
    • Louis, J.C.1    Magal, E.2    Muir, D.3    Manthorpe, M.4    Varon, S.5
  • 24
    • 77954331629 scopus 로고    scopus 로고
    • Guidelines for reporting experiments involving animals: The ARRIVE guidelines
    • McGrath J, Drummond G, McLachlan E, Kilkenny C, Wainwright C (2010). Guidelines for reporting experiments involving animals: the ARRIVE guidelines. Br J Pharmacol 160: 1573-1576.
    • (2010) Br J Pharmacol , vol.160 , pp. 1573-1576
    • McGrath, J.1    Drummond, G.2    McLachlan, E.3    Kilkenny, C.4    Wainwright, C.5
  • 25
    • 34547920351 scopus 로고    scopus 로고
    • Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin
    • Nahhas F, Dryden SC, Abrams J, Tainsky MA (2007). Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin. Mol Cell Biochem 303: 221-230.
    • (2007) Mol Cell Biochem , vol.303 , pp. 221-230
    • Nahhas, F.1    Dryden, S.C.2    Abrams, J.3    Tainsky, M.A.4
  • 26
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (2003). The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11: 437-444.
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 28
    • 80053209344 scopus 로고    scopus 로고
    • Interactions of pathological hallmark proteins: Tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein
    • Oláh J, Vincze O, Virók D, Simon D, Bozsó Z, To{combining double acute accent}kési N et al. (2011). Interactions of pathological hallmark proteins: tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein. J Biol Chem 286: 34088-34100.
    • (2011) J Biol Chem , vol.286 , pp. 34088-34100
    • Oláh, J.1    Vincze, O.2    Virók, D.3    Simon, D.4    Bozsó, Z.5    Et Al, T.D.A.A.N.6
  • 29
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease
    • Outeiro TF, Kontopoulos E, Altmann SM, Kufareva I, Strathearn KE, Amore AM et al. (2007). Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 317: 516-519.
    • (2007) Science , vol.317 , pp. 516-519
    • Outeiro, T.F.1    Kontopoulos, E.2    Altmann, S.M.3    Kufareva, I.4    Strathearn, K.E.5    Amore, A.M.6
  • 31
    • 84891791940 scopus 로고    scopus 로고
    • The IUPHAR/BPS Guide to PHARMACOLOGY: An expert-driven knowledge base of drug targets and their ligands
    • Database Issue
    • Pawson AJ, Sharman JL, Benson HE, Faccenda E, Alexander SP, Buneman OP et al.; NC-IUPHAR (2014). The IUPHAR/BPS Guide to PHARMACOLOGY: an expert-driven knowledge base of drug targets and their ligands. Nucl. Acids Res. 42 (Database Issue): D1098-1106.
    • (2014) Nucl. Acids Res. , vol.42 , pp. D1098-D1106
    • Pawson, A.J.1    Sharman, J.L.2    Benson, H.E.3    Faccenda, E.4    Alexander, S.P.5    Buneman, O.P.6    NC-IUPHAR7
  • 32
    • 34250183465 scopus 로고    scopus 로고
    • TPPP/p25 in brain tumours: Expression in non-neoplastic oligodendrocytes but not in oligodendroglioma cells
    • Preusser M, Lehotzky A, Budka H, Ovádi J, Kovács GG (2007). TPPP/p25 in brain tumours: expression in non-neoplastic oligodendrocytes but not in oligodendroglioma cells. Acta Neuropathol 113: 213-215.
    • (2007) Acta Neuropathol , vol.113 , pp. 213-215
    • Preusser, M.1    Lehotzky, A.2    Budka, H.3    Ovádi, J.4    Kovács, G.G.5
  • 36
    • 0027393390 scopus 로고
    • A brain-specific protein p25 is localized and associated with oligodendrocytes, neuropil, and fiber-like structures of the CA3 hippocampal region in the rat brain
    • Takahashi M, Tomizawa K, Fujita SC, Sato K, Uchida T, Imahori K (1993). A brain-specific protein p25 is localized and associated with oligodendrocytes, neuropil, and fiber-like structures of the CA3 hippocampal region in the rat brain. J Neurochem 60: 228-235.
    • (1993) J Neurochem , vol.60 , pp. 228-235
    • Takahashi, M.1    Tomizawa, K.2    Fujita, S.C.3    Sato, K.4    Uchida, T.5    Imahori, K.6
  • 37
    • 40049093522 scopus 로고    scopus 로고
    • SIRT2, tubulin deacetylation, and oligodendroglia differentiation
    • Tang BL, Chua CE (2008). SIRT2, tubulin deacetylation, and oligodendroglia differentiation. Cell Motil Cytoskeleton 65: 179-182.
    • (2008) Cell Motil Cytoskeleton , vol.65 , pp. 179-182
    • Tang, B.L.1    Chua, C.E.2
  • 38
    • 77952930296 scopus 로고    scopus 로고
    • TPPP/p25 promotes tubulin acetylation by inhibiting histone deacetylase 6
    • To{combining double acute accent}kési N, Lehotzky A, Horváth I, Szabó B, Oláh J, Lau P et al. (2010). TPPP/p25 promotes tubulin acetylation by inhibiting histone deacetylase 6. J Biol Chem 285: 17896-17906.
    • (2010) J Biol Chem , vol.285 , pp. 17896-17906
    • Tokési, N.1    Lehotzky, A.2    Horváth, I.3    Szabó, B.4    Oláh, J.5    Lau, P.6
  • 39
  • 40
    • 33749371515 scopus 로고    scopus 로고
    • An oligodendrocyte-specific zinc-finger transcription regulator cooperates with Olig2 to promote oligodendrocyte differentiation
    • Wang SZ, Dulin J, Wu H, Hurlock E, Lee SE, Jansson K et al. (2006). An oligodendrocyte-specific zinc-finger transcription regulator cooperates with Olig2 to promote oligodendrocyte differentiation. Development 133: 3389-3398.
    • (2006) Development , vol.133 , pp. 3389-3398
    • Wang, S.Z.1    Dulin, J.2    Wu, H.3    Hurlock, E.4    Lee, S.E.5    Jansson, K.6
  • 41
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang WM, Yao YL, Sun JM, Davie JR, Seto E (1997). Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J Biol Chem 272: 28001-28007.
    • (1997) J Biol Chem , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5


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