메뉴 건너뛰기




Volumn 15, Issue 2, 2012, Pages 189-197

Positive lysosomal modulation as a unique strategy to treat age-related protein accumulation diseases

Author keywords

[No Author keywords available]

Indexed keywords

ALOXISTATIN ACID; ALPHA SECRETASE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; BAFILOMYCIN A1; BETA SECRETASE; CATHEPSIN; CATHEPSIN B; CHLOROQUINE; DIAZOACETYL 2 AMINOHEXANOIC ACID METHYL ESTER; GLYCOSIDASE INHIBITOR; GLYCYLPHENYLALANYLGLYCINALDEHYDE SEMICARBAZONE; HUNTINGTIN; INSULINASE; ISOFAGOMINE; LEUPEPTIN; M 31850; MEMBRANE METALLOENDOPEPTIDASE; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PEPSTATIN; PHENYLALANYLALANYLDIAZOMETHYL KETONE; PROTEASOME; PROTEINASE INHIBITOR; RAB PROTEIN; SEMICARBAZONE DERIVATIVE; TAU PROTEIN; TUBULIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84860282240     PISSN: 15491684     EISSN: 15578577     Source Type: Journal    
DOI: 10.1089/rej.2011.1282     Document Type: Article
Times cited : (42)

References (52)
  • 1
    • 0015274335 scopus 로고
    • The effect of aging on lysosomal permeability in nerve cells of the central nervous system An enzyme histochemical study in rat
    • Brunk U, Brun A. The effect of aging on lysosomal permeability in nerve cells of the central nervous system. An enzyme histochemical study in rat. Histochemie 1972;30:315-324
    • (1972) Histochemie. , vol.30 , pp. 315-324
    • Brunk, U.1    Brun, A.2
  • 2
    • 0028321380 scopus 로고
    • Accumulation of autofluorescent yellow lipofuscin in rat tissues estimated by sodium dodecylsulfate extraction
    • Kikugawa K, Beppu M, Kato T, Yamaki S, Kasai H. Accumulation of autofluorescent yellow lipofuscin in rat tissues estimated by sodium dodecylsulfate extraction. Mech Ageing Dev 1994;74:135-148
    • (1994) Mech. Ageing. Dev. , vol.74 , pp. 135-148
    • Kikugawa, K.1    Beppu, M.2    Kato, T.3    Yamaki, S.4    Kasai, H.5
  • 5
    • 0036830228 scopus 로고    scopus 로고
    • The neuropathogenic contributions of lysosomal dysfunction
    • Bahr BA, Bendiske J. The neuropathogenic contributions of lysosomal dysfunction. J Neurochem 2002;83:481-489
    • (2002) J. Neurochem. , vol.83 , pp. 481-489
    • Bahr, B.A.1    Bendiske, J.2
  • 7
    • 0036293375 scopus 로고    scopus 로고
    • Intracellular deposition, microtubule destabilization, and transport failure: An ''early'' pathogenic cascade leading to synaptic decline
    • Bendiske J, Caba E, Brown QB, Bahr BA. Intracellular deposition, microtubule destabilization, and transport failure: An ''early'' pathogenic cascade leading to synaptic decline. J Neuropathol Exp Neurol 2002;61:640-650
    • (2002) J. Neuropathol Exp. Neurol. , vol.61 , pp. 640-650
    • Bendiske, J.1    Caba, E.2    Brown, Q.B.3    Bahr, B.A.4
  • 10
    • 5344272541 scopus 로고    scopus 로고
    • A focus on the synapse for neuroprotection in Alzheimer disease and other dementias
    • Coleman P, Federoff H, Kurlan R. A focus on the synapse for neuroprotection in Alzheimer disease and other dementias. Neurology 2004;63:1155-1162
    • (2004) Neurology. , vol.63 , pp. 1155-1162
    • Coleman, P.1    Federoff, H.2    Kurlan, R.3
  • 11
    • 0018824092 scopus 로고
    • Reduced dopaminergic binding during aging in the rodent striatum
    • Severson JA, Finch CE. Reduced dopaminergic binding during aging in the rodent striatum. Brain Res 1980;192:147-162
    • (1980) Brain. Res. , vol.192 , pp. 147-162
    • Severson, J.A.1    Finch, C.E.2
  • 12
    • 0027390458 scopus 로고
    • Quantitative synaptic alterations in the human neocortex during normal aging
    • Masliah E, Mallory M, Hansen L, DeTeresa R, Terry R. Quantitative synaptic alterations in the human neocortex during normal aging. Neurology 1993;43:192-197
    • (1993) Neurology. , vol.43 , pp. 192-197
    • Masliah, E.1    Mallory, M.2    Hansen, L.3    DeTeresa, R.4    Terry, R.5
  • 13
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ. Alzheimer's disease is a synaptic failure. Science 2002;298:789-791
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 14
    • 79957663035 scopus 로고    scopus 로고
    • Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy
    • Lee S, Sato Y, Nixon RA. Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy. J Neurosci 2011;31:7817-7830
    • (2011) J. Neurosci. , vol.31 , pp. 7817-7830
    • Lee, S.1    Sato, Y.2    Nixon, R.A.3
  • 15
    • 0032551528 scopus 로고    scopus 로고
    • Amyloid b protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein
    • Bahr BA, Hoffman KB, Yang AJ, Hess US, Glabe CG, Lynch G. Amyloid b protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein. J Comp Neurol 1998;397:139-147
    • (1998) J. Comp. Neurol. , vol.397 , pp. 139-147
    • Bahr, B.A.1    Hoffman, K.B.2    Yang, A.J.3    Hess, U.S.4    Glabe, C.G.5    Lynch, G.6
  • 16
    • 0036827031 scopus 로고    scopus 로고
    • Intraneuronal Alzheimer Ab42 accumulates in multivesicular bodies and is associated with synaptic pathology
    • Takahashi RH. Intraneuronal Alzheimer Ab42 accumulates in multivesicular bodies and is associated with synaptic pathology. Am J Pathol 2002;161:1869-1879
    • (2002) Am. J. Pathol. , vol.161 , pp. 1869-1879
    • Takahashi, R.H.1
  • 17
    • 0033025080 scopus 로고    scopus 로고
    • Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles
    • Callahan LM, Vaules WA, Coleman PD. Quantitative decrease in synaptophysin message expression and increase in cathepsin D message expression in Alzheimer disease neurons containing neurofibrillary tangles. J Neuropathol Exp Neurol 1999;58:275-287
    • (1999) J. Neuropathol Exp. Neurol. , vol.58 , pp. 275-287
    • Callahan, L.M.1    Vaules, W.A.2    Coleman, P.D.3
  • 18
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomallysosomal system
    • Cataldo AM, Barnett JL, Berman SA, Li J, Quarless S, Bursztajn S, Lippa C, Nixon RA. Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomallysosomal system. Neuron 1995;14:671-680
    • (1995) Neuron. , vol.14 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3    Li, J.4    Quarless, S.5    Bursztajn, S.6    Lippa, C.7    Nixon, R.A.8
  • 21
    • 70249092882 scopus 로고    scopus 로고
    • Lysosomal modulatory drugs for a broad strategy against protein accumulation disorders
    • Bahr BA. Lysosomal modulatory drugs for a broad strategy against protein accumulation disorders. Curr Alzheimer Res 2009;6:438-445
    • (2009) Curr. Alzheimer. Res. , vol.6 , pp. 438-445
    • Bahr, B.A.1
  • 22
    • 0032530266 scopus 로고    scopus 로고
    • Specific alterations in levels of mannose 6-phosphorylated glycoproteins in different neuronal ceroid lipofuscinoses
    • Sleat DE, Sohar I, Pullarkat PS, Lobel P, Pullarkat RK. Specific alterations in levels of mannose 6-phosphorylated glycoproteins in different neuronal ceroid lipofuscinoses. Biochem J 1998;334:547-551
    • (1998) Biochem J. , vol.334 , pp. 547-551
    • Sleat, D.E.1    Sohar, I.2    Pullarkat, P.S.3    Lobel, P.4    Pullarkat, R.K.5
  • 23
    • 0037989761 scopus 로고    scopus 로고
    • Lysosomal activation is a compensatory response against protein accumulation and associated synaptopathogenesis-an approach for slowing Alzheimer disease
    • Bendiske J, Bahr BA. Lysosomal activation is a compensatory response against protein accumulation and associated synaptopathogenesis-an approach for slowing Alzheimer disease? J Neuropathol Exp Neurol 2003;62:451-463
    • (2003) J. Neuropathol. Exp. Neurol. , vol.62 , pp. 451-463
    • Bendiske, J.1    Bahr, B.A.2
  • 24
    • 0035110055 scopus 로고    scopus 로고
    • Lysosomal membrane damage in soluble Ab-mediated cell death in Alzheimer's disease
    • Ditaranto K, Tekirian TL, Yang AJ. Lysosomal membrane damage in soluble Ab-mediated cell death in Alzheimer's disease. Neurobiol Dis 2001;8:19-31
    • (2001) Neurobiol. Dis. , vol.8 , pp. 19-31
    • Ditaranto, K.1    Tekirian, T.L.2    Yang, A.J.3
  • 26
    • 0028864852 scopus 로고
    • Long-term hippocampal slices: A model system for investigating synaptic mechanisms and pathologic processes
    • Bahr BA. Long-term hippocampal slices: A model system for investigating synaptic mechanisms and pathologic processes. J Neurosci Res 1995;42:294-305
    • (1995) J. Neurosci. Res. , vol.42 , pp. 294-305
    • Bahr, B.A.1
  • 27
    • 33644658460 scopus 로고    scopus 로고
    • Oxidative stress and lysosomes: CNSrelated consequences and implications for lysosomal enhancement strategies and induction of autophagy
    • Butler D, Bahr BA. Oxidative stress and lysosomes: CNSrelated consequences and implications for lysosomal enhancement strategies and induction of autophagy. Antioxid Redox Signal 2006;8:185-196
    • (2006) Antioxid. Redox. Signal. , vol.8 , pp. 185-196
    • Butler, D.1    Bahr, B.A.2
  • 30
    • 0028171520 scopus 로고
    • Induction of b-amyloid-containing polypeptides in hippocampus: Evidence for a concomitant loss of synaptic proteins and interactions with an excitotoxin
    • Bahr BA, Abai B, Gall CM, Vanderklish PW, Hoffman KB, Lynch G. Induction of b-amyloid-containing polypeptides in hippocampus: Evidence for a concomitant loss of synaptic proteins and interactions with an excitotoxin. Exp Neurol 1994;129:81-94
    • (1994) Exp. Neurol. , vol.129 , pp. 81-94
    • Bahr, B.A.1    Abai, B.2    Gall, C.M.3    Vanderklish, P.W.4    Hoffman, K.B.5    Lynch, G.6
  • 31
    • 77955604553 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal Ab42 uptake and lysosomal trafficking
    • Fuentealba RA, Liu Q, Zhang J, Kanekiyo T, Hu X, Lee JM, LaDu MJ, Bu G. Low-density lipoprotein receptor-related protein 1 (LRP1) mediates neuronal Ab42 uptake and lysosomal trafficking. PLoS One 2010;5:e11884
    • (2010) PLoS One. , vol.5
    • Fuentealba, R.A.1    Liu, Q.2    Zhang, J.3    Kanekiyo, T.4    Hu, X.5    Lee, J.M.6    LaDu, M.J.7    Bu, G.8
  • 33
    • 0025223273 scopus 로고
    • Inhibitor studies indicate that active cathepsin L is probably essential to its own processing in cultured fibroblasts
    • Salminen A, Gottesman MM. Inhibitor studies indicate that active cathepsin L is probably essential to its own processing in cultured fibroblasts. Biochem J 1990;272:39-44
    • (1990) Biochem. J. , vol.272 , pp. 39-44
    • Salminen, A.1    Gottesman, M.M.2
  • 35
    • 33847032037 scopus 로고    scopus 로고
    • High-throughput screening for human lysosomal b-NAcetyl hexosaminidase inhibitors acting as pharmacological chaperones
    • Tropak MB, Blanchard JE, Withers SG, Brown ED, Mahuran D. High-throughput screening for human lysosomal b-NAcetyl hexosaminidase inhibitors acting as pharmacological chaperones. Chem Biol 2007;14:153-164
    • (2007) Chem. Biol. , vol.14 , pp. 153-164
    • Tropak, M.B.1    Blanchard, J.E.2    Withers, S.G.3    Brown, E.D.4    Mahuran, D.5
  • 37
    • 0032931344 scopus 로고    scopus 로고
    • Lysosomal dysfunction results in lamina-specific meganeurite formation but not apoptosis in frontal cortex
    • Yong AP, Bednarski E, Gall CM, Lynch G, Ribak CE. Lysosomal dysfunction results in lamina-specific meganeurite formation but not apoptosis in frontal cortex. Exp Neurol 1999;157:150-160
    • (1999) Exp. Neurol. , vol.157 , pp. 150-160
    • Yong, A.P.1    Bednarski, E.2    Gall, C.M.3    Lynch, G.4    Ribak, C.E.5
  • 38
    • 42949101621 scopus 로고    scopus 로고
    • Gephyrin alterations due to protein accumulation stress are reduced by the lysosomal modulator Z-Phe
    • Ala-diazomethylketone
    • Ryzhikov S, Bahr BA. Gephyrin alterations due to protein accumulation stress are reduced by the lysosomal modulator Z-Phe-Ala-diazomethylketone. J Mol Neurosci 2008;34:131-139
    • (2008) J. Mol. Neurosci. , vol.34 , pp. 131-139
    • Ryzhikov, S.1    Bahr, B.A.2
  • 39
    • 38149082008 scopus 로고    scopus 로고
    • Increased expression and altered subunit composition of proteasomes induced by continuous proteasome inhibition establish apoptosis resistance and hyperproliferation of Burkitt lymphoma cells
    • Fuchs D, Berges C, Opelz G, Daniel V, Naujokat C. Increased expression and altered subunit composition of proteasomes induced by continuous proteasome inhibition establish apoptosis resistance and hyperproliferation of Burkitt lymphoma cells. J Cell Biochem 2008;103:270-283
    • (2008) J. Cell. Biochem. , vol.103 , pp. 270-283
    • Fuchs, D.1    Berges, C.2    Opelz, G.3    Daniel, V.4    Naujokat, C.5
  • 40
    • 29144497497 scopus 로고    scopus 로고
    • Dysfunction and activation of the lysosomal system: Implications for and against Alzheimer's disease
    • Welsh EM (ed) Nova Science Publishers, Hauppauge, NY
    • Bahr BA. Dysfunction and activation of the lysosomal system: Implications for and against Alzheimer's disease. In: Welsh EM (ed). Focus on Alzheimer's Disease Research. Nova Science Publishers, Hauppauge, NY, 2003, pp 115- 150
    • (2003) Focus on Alzheimer's Disease Research , pp. 115-150
    • Bahr, B.A.1
  • 42
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of asynuclein oligomeric intermediates via the lysosomal degradation pathway
    • Lee HJ, Khoshaghideh F, Patel S, Lee SJ. Clearance of asynuclein oligomeric intermediates via the lysosomal degradation pathway. J Neurosci 2004;24:1888-1896
    • (2004) J. Neurosci. , vol.24 , pp. 1888-1896
    • Lee, H.J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.J.4
  • 44
    • 33745862719 scopus 로고    scopus 로고
    • Potential compensatory responses through autophagic/lysosomal pathways in neurodegenerative diseases
    • Butler D, Nixon RA, Bahr BA. Potential compensatory responses through autophagic/lysosomal pathways in neurodegenerative diseases. Autophagy 2006;2:234-237
    • (2006) Autophagy. , vol.2 , pp. 234-237
    • Butler, D.1    Nixon, R.A.2    Bahr, B.A.3
  • 46
    • 33947315806 scopus 로고    scopus 로고
    • When an inhibitor promotes activity
    • Bouvier M. When an inhibitor promotes activity. Chem Biol 2007;14:241-242
    • (2007) Chem. Biol. , vol.14 , pp. 241-242
    • Bouvier, M.1
  • 48
    • 80054118121 scopus 로고    scopus 로고
    • Submicromolar Ab42 reduces hippocampal glutamate receptors and presynaptic markers in an aggregation-dependent manner
    • Wisniewski ML, Hwang J, Bahr BA. Submicromolar Ab42 reduces hippocampal glutamate receptors and presynaptic markers in an aggregation-dependent manner. Biochim Biophys Acta 2011 1812:1664-1674
    • (2011) Biochim. Biophys. Acta. , vol.1812 , pp. 1664-1674
    • Wisniewski, M.L.1    Hwang, J.2    Bahr, B.A.3
  • 50
    • 0031882943 scopus 로고    scopus 로고
    • Age-related phosphorylation and fragmentation events influence the distribution profiles of distinct tau isoforms in mouse brain
    • Bahr BA, Vicente JS. Age-related phosphorylation and fragmentation events influence the distribution profiles of distinct tau isoforms in mouse brain. J Neuropathol Exp Neurol 1998;57:111-121
    • (1998) J. Neuropathol Exp. Neurol. , vol.57 , pp. 111-121
    • Bahr, B.A.1    Vicente, J.S.2
  • 51
    • 33947519211 scopus 로고    scopus 로고
    • Microtubule-stabilizing agent prevents protein accumulation- induced loss of synaptic markers
    • Butler D, Bendiske J, Michaelis ML, Karanian DA, Bahr BA. Microtubule-stabilizing agent prevents protein accumulation- induced loss of synaptic markers. Eur J Pharmacol 2007;562:20-27
    • (2007) Eur. J. Pharmacol , vol.562 , pp. 20-27
    • Butler, D.1    Bendiske, J.2    Michaelis, M.L.3    Karanian, D.A.4    Bahr, B.A.5
  • 52
    • 0024238264 scopus 로고
    • Inhibition of early but not late proteolytic processing events leads to the missorting and oversecretion of precursor forms of lysosomal enzymes in Dictyostelium discoideum
    • Richardson JM, Woychik NA, Ebert DL, Cardelli JA. Inhibition of early but not late proteolytic processing events leads to the missorting and oversecretion of precursor forms of lysosomal enzymes in Dictyostelium discoideum. J Cell Biol 1988;107:2097-2107
    • (1988) J. Cell Biol. , vol.107 , pp. 2097-2107
    • Richardson, J.M.1    Woychik, N.A.2    Ebert, D.L.3    Cardelli, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.