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Volumn 288, Issue 50, 2013, Pages 35952-35960

Farnesyltransferase haplodeficiency reduces neuropathology and rescues cognitive function in a mouse model of Alzheimer disease

Author keywords

[No Author keywords available]

Indexed keywords

COGNITIVE FUNCTIONS; FARNESYLTRANSFERASE; GERANYLGERANYLATION; LEARNING AND MEMORY; NEUROINFLAMMATION; PRECURSOR PROTEINS; PRENYLTRANSFERASES; SYNAPTIC PLASTICITY;

EID: 84890351522     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.503904     Document Type: Article
Times cited : (36)

References (48)
  • 1
    • 84875354777 scopus 로고    scopus 로고
    • 2013 Alzheimer's disease facts and figures
    • and Alzheimer's Association
    • Thies, W., Bleiler, L., and Alzheimer's Association (2013) 2013 Alzheimer's disease facts and figures. Alzheimers Dement. 9, 208-245
    • (2013) Alzheimers Dement. , vol.9 , pp. 208-245
    • Thies, W.1    Bleiler, L.2
  • 2
    • 33646137779 scopus 로고    scopus 로고
    • Isoprenoids and Alzheimer's disease: A complex relationship
    • Cole, S. L., and Vassar, R. (2006) Isoprenoids and Alzheimer's disease: a complex relationship. Neurobiol. Dis. 22, 209-222
    • (2006) Neurobiol. Dis. , vol.22 , pp. 209-222
    • Cole, S.L.1    Vassar, R.2
  • 4
    • 84868146096 scopus 로고    scopus 로고
    • Isoprenoids and related pharmacological interventions: Potential application in Alzheimer's disease
    • Li, L., Zhang, W., Cheng, S., Cao, D., and Parent, M. (2012) Isoprenoids and related pharmacological interventions: potential application in Alzheimer's disease. Mol. Neurobiol. 46, 64-77
    • (2012) Mol. Neurobiol. , vol.46 , pp. 64-77
    • Li, L.1    Zhang, W.2    Cheng, S.3    Cao, D.4    Parent, M.5
  • 5
    • 33644748133 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I
    • Lane, K. T., and Beese, L. S. (2006) Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. J. Lipid Res. 47, 681-699
    • (2006) J. Lipid Res. , vol.47 , pp. 681-699
    • Lane, K.T.1    Beese, L.S.2
  • 6
    • 33644748150 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Geranylgeranylation of Rab GTPases
    • Leung, K. F., Baron, R., and Seabra, M. C. (2006) Thematic review series: lipid posttranslational modifications. geranylgeranylation of Rab GTPases. J. Lipid Res. 47, 467-475
    • (2006) J. Lipid Res. , vol.47 , pp. 467-475
    • Leung, K.F.1    Baron, R.2    Seabra, M.C.3
  • 7
    • 32044435884 scopus 로고    scopus 로고
    • Isoprenylated proteins
    • McTaggart, S. J. (2006) Isoprenylated proteins. Cell. Mol. Life Sci. 63, 255-267
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 255-267
    • McTaggart, S.J.1
  • 9
    • 21444445440 scopus 로고    scopus 로고
    • Statins cause intracellular accumulation of amyloid precursor protein, β-secretase-cleaved fragments, and amyloid β-peptide via an isoprenoid-dependent mechanism
    • Cole, S. L., Grudzien, A., Manhart, I. O., Kelly, B. L., Oakley, H., and Vassar, R. (2005) Statins cause intracellular accumulation of amyloid precursor protein, β-secretase-cleaved fragments, and amyloid β-peptide via an isoprenoid-dependent mechanism. J. Biol. Chem. 280, 18755-18770
    • (2005) J. Biol. Chem. , vol.280 , pp. 18755-18770
    • Cole, S.L.1    Grudzien, A.2    Manhart, I.O.3    Kelly, B.L.4    Oakley, H.5    Vassar, R.6
  • 10
    • 34848835187 scopus 로고    scopus 로고
    • Statins reduce amyloid-β production through inhibition of protein isoprenylation
    • Ostrowski, S. M., Wilkinson, B. L., Golde, T. E., and Landreth, G. (2007) Statins reduce amyloid-β production through inhibition of protein isoprenylation. J. Biol. Chem. 282, 26832-26844
    • (2007) J. Biol. Chem. , vol.282 , pp. 26832-26844
    • Ostrowski, S.M.1    Wilkinson, B.L.2    Golde, T.E.3    Landreth, G.4
  • 11
    • 38049173483 scopus 로고    scopus 로고
    • Geranylgeranyl pyrophosphate stimulates γ-secretase to increase the generation of Aβ and APP-CTFγ
    • Zhou, Y., Suram, A., Venugopal, C., Prakasam, A., Lin, S., Su, Y., Li, B., Paul, S. M., and Sambamurti, K. (2008) Geranylgeranyl pyrophosphate stimulates γ-secretase to increase the generation of Aβ and APP-CTFγ. FASEB J. 22, 47-54
    • (2008) FASEB J. , vol.22 , pp. 47-54
    • Zhou, Y.1    Suram, A.2    Venugopal, C.3    Prakasam, A.4    Lin, S.5    Su, Y.6    Li, B.7    Paul, S.M.8    Sambamurti, K.9
  • 14
    • 65849255721 scopus 로고    scopus 로고
    • Rac1 inhibition negatively regulates transcriptional activity of the amyloid precursor protein gene
    • Wang, P. L., Niidome, T., Akaike, A., Kihara, T., and Sugimoto, H. (2009) Rac1 inhibition negatively regulates transcriptional activity of the amyloid precursor protein gene. J. Neurosci. Res. 87, 2105-2114
    • (2009) J. Neurosci. Res. , vol.87 , pp. 2105-2114
    • Wang, P.L.1    Niidome, T.2    Akaike, A.3    Kihara, T.4    Sugimoto, H.5
  • 15
    • 45449087037 scopus 로고    scopus 로고
    • Rac1 changes the substrate specificity of γ-secretase between amyloid precursor protein and Notch1
    • Boo, J. H., Sohn, J. H., Kim, J. E., Song, H., and Mook-Jung, I. (2008) Rac1 changes the substrate specificity of γ-secretase between amyloid precursor protein and Notch1. Biochem. Biophys. Res. Commun. 372, 913-917
    • (2008) Biochem. Biophys. Res. Commun. , vol.372 , pp. 913-917
    • Boo, J.H.1    Sohn, J.H.2    Kim, J.E.3    Song, H.4    Mook-Jung, I.5
  • 17
    • 67649781671 scopus 로고    scopus 로고
    • Regulation of the brain isoprenoids farnesyl- and geranylgeranylpyrophosphate is altered in male Alzheimer patients
    • Eckert, G. P., Hooff, G. P., Strandjord, D. M., Igbavboa, U., Volmer, D. A., Müller, W. E., and Wood, W. G. (2009) Regulation of the brain isoprenoids farnesyl- and geranylgeranylpyrophosphate is altered in male Alzheimer patients. Neurobiol. Dis. 35, 251-257
    • (2009) Neurobiol. Dis. , vol.35 , pp. 251-257
    • Eckert, G.P.1    Hooff, G.P.2    Strandjord, D.M.3    Igbavboa, U.4    Volmer, D.A.5    Müller, W.E.6    Wood, W.G.7
  • 18
    • 12144261198 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors attenuate β-amyloid-induced microglial inflammatory responses
    • Cordle, A., and Landreth, G. (2005) 3-Hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors attenuate β-amyloid-induced microglial inflammatory responses. J. Neurosci. 25, 299-307
    • (2005) J. Neurosci. , vol.25 , pp. 299-307
    • Cordle, A.1    Landreth, G.2
  • 22
    • 78049425264 scopus 로고    scopus 로고
    • p120 catenin/αN-catenin are molecular targets in the neuroprotection and neuronal plasticity mediated by atorvastatin after focal cerebral ischemia
    • Céspedes-Rubio, A., Jurado, F. W., and Cardona-Gómez, G. P. (2010) p120 catenin/αN-catenin are molecular targets in the neuroprotection and neuronal plasticity mediated by atorvastatin after focal cerebral ischemia. J. Neurosci. Res. 88, 3621-3634
    • (2010) J. Neurosci. Res. , vol.88 , pp. 3621-3634
    • Céspedes-Rubio, A.1    Jurado, F.W.2    Cardona-Gómez, G.P.3
  • 23
    • 84864382406 scopus 로고    scopus 로고
    • Pitavastatin decreases κ levels via the inactivation of Rho/ROCK
    • Hamano, T., Yen, S. H., Gendron, T., Ko, L. W., and Kuriyama, M. (2012) Pitavastatin decreases κ levels via the inactivation of Rho/ROCK. Neurobiol. Aging 33, 2306-2320
    • (2012) Neurobiol. Aging , vol.33 , pp. 2306-2320
    • Hamano, T.1    Yen, S.H.2    Gendron, T.3    Ko, L.W.4    Kuriyama, M.5
  • 24
    • 77951887071 scopus 로고    scopus 로고
    • Simvastatin enhances hippocampal long-term potentiation in C57BL/6 mice
    • Mans, R. A., Chowdhury, N., Cao, D., McMahon, L. L., and Li, L. (2010) Simvastatin enhances hippocampal long-term potentiation in C57BL/6 mice. Neuroscience 166, 435-444
    • (2010) Neuroscience , vol.166 , pp. 435-444
    • Mans, R.A.1    Chowdhury, N.2    Cao, D.3    McMahon, L.L.4    Li, L.5
  • 25
    • 84856228305 scopus 로고    scopus 로고
    • Simvastatin-mediated enhancement of long-term potentiation is driven by farnesyl-pyrophosphate depletion and inhibition of farnesylation
    • Mans, R. A., McMahon, L. L., and Li, L. (2012) Simvastatin-mediated enhancement of long-term potentiation is driven by farnesyl-pyrophosphate depletion and inhibition of farnesylation. Neuroscience 202, 1-9
    • (2012) Neuroscience , vol.202 , pp. 1-9
    • Mans, R.A.1    McMahon, L.L.2    Li, L.3
  • 26
    • 33846048569 scopus 로고    scopus 로고
    • Simvastatin enhances learning and memory independent of amyloid load in mice
    • Li, L., Cao, D., Kim, H., Lester, R., and Fukuchi, K. (2006) Simvastatin enhances learning and memory independent of amyloid load in mice. Ann. Neurol. 60, 729-739
    • (2006) Ann. Neurol. , vol.60 , pp. 729-739
    • Li, L.1    Cao, D.2    Kim, H.3    Lester, R.4    Fukuchi, K.5
  • 27
    • 78049309392 scopus 로고    scopus 로고
    • Small G protein signaling in neuronal plasticity and memory formation: The specific role of ras family proteins
    • Ye, X., and Carew, T. J. (2010) Small G protein signaling in neuronal plasticity and memory formation: the specific role of ras family proteins. Neuron 68, 340-361
    • (2010) Neuron , vol.68 , pp. 340-361
    • Ye, X.1    Carew, T.J.2
  • 29
    • 0037106353 scopus 로고    scopus 로고
    • Implication of the small GTPase Rac1 in the generation of reactive oxygen species in response to β-amyloid in C6 astroglioma cells
    • Lee, M., You, H. J., Cho, S. H., Woo, C. H., Yoo, M. H., Joe, E. H., and Kim, J. H. (2002) Implication of the small GTPase Rac1 in the generation of reactive oxygen species in response to β-amyloid in C6 astroglioma cells. Biochem. J. 366, 937-943
    • (2002) Biochem. J. , vol.366 , pp. 937-943
    • Lee, M.1    You, H.J.2    Cho, S.H.3    Woo, C.H.4    Yoo, M.H.5    Joe, E.H.6    Kim, J.H.7
  • 32
    • 37549035051 scopus 로고    scopus 로고
    • Intake of sucrose-sweetened water induces insulin resistance and exacerbates memory deficits and amyloidosis in a transgenic mouse model of Alzheimer disease
    • Cao, D., Lu, H., Lewis, T. L., and Li, L. (2007) Intake of sucrose-sweetened water induces insulin resistance and exacerbates memory deficits and amyloidosis in a transgenic mouse model of Alzheimer disease. J. Biol. Chem. 282, 36275-36282
    • (2007) J. Biol. Chem. , vol.282 , pp. 36275-36282
    • Cao, D.1    Lu, H.2    Lewis, T.L.3    Li, L.4
  • 33
    • 78449255602 scopus 로고    scopus 로고
    • Overexpression of human apolipoprotein A-I preserves cognitive function and attenuates neuroinflammation and cerebral amyloid angiopathy in a mouse model of Alzheimer disease
    • Lewis, T. L., Cao, D., Lu, H., Mans, R. A., Su, Y. R., Jungbauer, L., Linton, M. F., Fazio, S., LaDu, M. J., and Li, L. (2010) Overexpression of human apolipoprotein A-I preserves cognitive function and attenuates neuroinflammation and cerebral amyloid angiopathy in a mouse model of Alzheimer disease. J. Biol. Chem. 285, 36958-36968
    • (2010) J. Biol. Chem. , vol.285 , pp. 36958-36968
    • Lewis, T.L.1    Cao, D.2    Lu, H.3    Mans, R.A.4    Su, Y.R.5    Jungbauer, L.6    Linton, M.F.7    Fazio, S.8    LaDu, M.J.9    Li, L.10
  • 34
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice
    • Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L., and LaFerla, F. M. (2005) Intraneuronal Aβ causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice. Neuron 45, 675-688
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    LaFerla, F.M.5
  • 35
    • 84863504256 scopus 로고    scopus 로고
    • Apolipoprotein E and apolipoprotein E receptors: Normal biology and roles in Alzheimer disease
    • Holtzman, D. M., Herz, J., and Bu, G. (2012) Apolipoprotein E and apolipoprotein E receptors: normal biology and roles in Alzheimer disease. Cold Spring Harb. Perspect. Med. 2, a006312
    • (2012) Cold Spring Harb. Perspect. Med. , vol.2
    • Holtzman, D.M.1    Herz, J.2    Bu, G.3
  • 36
    • 0035950225 scopus 로고    scopus 로고
    • Clearing the brain's amyloid cobwebs
    • Selkoe, D. J. (2001) Clearing the brain's amyloid cobwebs. Neuron 32, 177-180
    • (2001) Neuron , vol.32 , pp. 177-180
    • Selkoe, D.J.1
  • 37
    • 78549284024 scopus 로고    scopus 로고
    • Statins promote the degradation of extracellular amyloid β-peptide by microglia via stimulation of exosome-associated insulin-degrading enzyme (IDE) secretion
    • Tamboli, I. Y., Barth, E., Christian, L., Siepmann, M., Kumar, S., Singh, S., Tolksdorf, K., Heneka, M. T., Lütjohann, D., Wunderlich, P., and Walter, J. (2010) Statins promote the degradation of extracellular amyloid β-peptide by microglia via stimulation of exosome-associated insulin-degrading enzyme (IDE) secretion. J. Biol. Chem. 285, 37405-37414
    • (2010) J. Biol. Chem. , vol.285 , pp. 37405-37414
    • Tamboli, I.Y.1    Barth, E.2    Christian, L.3    Siepmann, M.4    Kumar, S.5    Singh, S.6    Tolksdorf, K.7    Heneka, M.T.8    Lütjohann, D.9    Wunderlich, P.10    Walter, J.11
  • 38
    • 33846260506 scopus 로고    scopus 로고
    • Targeting and localized signalling by small GTPases
    • ten Klooster, J. P., and Hordijk, P. L. (2007) Targeting and localized signalling by small GTPases. Biol. Cell 99, 1-12
    • (2007) Biol. Cell , vol.99 , pp. 1-12
    • Ten Klooster, J.P.1    Hordijk, P.L.2
  • 39
    • 18344394166 scopus 로고    scopus 로고
    • Post-prenylation-processing enzymes as new targets in oncogenesis
    • Winter-Vann, A. M., and Casey, P. J. (2005) Post-prenylation-processing enzymes as new targets in oncogenesis. Nat. Rev. Cancer 5, 405-412
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 405-412
    • Winter-Vann, A.M.1    Casey, P.J.2
  • 40
    • 0037137175 scopus 로고    scopus 로고
    • Isoprenoids influence expression of Ras and Ras-related proteins
    • Holstein, S. A., Wohlford-Lenane, C. L., and Hohl, R. J. (2002) Isoprenoids influence expression of Ras and Ras-related proteins. Biochemistry 41, 13698-13704
    • (2002) Biochemistry , vol.41 , pp. 13698-13704
    • Holstein, S.A.1    Wohlford-Lenane, C.L.2    Hohl, R.J.3
  • 41
    • 9144236957 scopus 로고    scopus 로고
    • Inhibition of geranylgeranylation mediates the effects of 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase inhibitors on microglia
    • Bi, X., Baudry, M., Liu, J., Yao, Y., Fu, L., Brucher, F., and Lynch, G. (2004) Inhibition of geranylgeranylation mediates the effects of 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase inhibitors on microglia. J. Biol. Chem. 279, 48238-48245
    • (2004) J. Biol. Chem. , vol.279 , pp. 48238-48245
    • Bi, X.1    Baudry, M.2    Liu, J.3    Yao, Y.4    Fu, L.5    Brucher, F.6    Lynch, G.7
  • 43
    • 0038267569 scopus 로고    scopus 로고
    • H-Ras modulates N-methyl-D-aspartate receptor function via inhibition of Src tyrosine kinase activity
    • Thornton, C., Yaka, R., Dinh, S., and Ron, D. (2003) H-Ras modulates N-methyl-D-aspartate receptor function via inhibition of Src tyrosine kinase activity. J. Biol. Chem. 278, 23823-23829
    • (2003) J. Biol. Chem. , vol.278 , pp. 23823-23829
    • Thornton, C.1    Yaka, R.2    Dinh, S.3    Ron, D.4
  • 44
    • 0034175488 scopus 로고    scopus 로고
    • Regulation of long-term potentiation by H-Ras through NMDA receptor phosphorylation
    • Manabe, T., Aiba, A., Yamada, A., Ichise, T., Sakagami, H., Kondo, H., and Katsuki, M. (2000) Regulation of long-term potentiation by H-Ras through NMDA receptor phosphorylation. J. Neurosci. 20, 2504-2511
    • (2000) J. Neurosci. , vol.20 , pp. 2504-2511
    • Manabe, T.1    Aiba, A.2    Yamada, A.3    Ichise, T.4    Sakagami, H.5    Kondo, H.6    Katsuki, M.7
  • 45
    • 27644517404 scopus 로고    scopus 로고
    • The HMG-CoA reductase inhibitor lovastatin reverses the learning and attention deficits in a mouse model of neurofibromatosis type 1
    • Li, W., Cui, Y., Kushner, S. A., Brown, R. A., Jentsch, J. D., Frankland, P. W., Cannon, T. D., and Silva, A. J. (2005) The HMG-CoA reductase inhibitor lovastatin reverses the learning and attention deficits in a mouse model of neurofibromatosis type 1. Curr. Biol. 15, 1961-1967
    • (2005) Curr. Biol. , vol.15 , pp. 1961-1967
    • Li, W.1    Cui, Y.2    Kushner, S.A.3    Brown, R.A.4    Jentsch, J.D.5    Frankland, P.W.6    Cannon, T.D.7    Silva, A.J.8
  • 46
    • 79955789504 scopus 로고    scopus 로고
    • Control of synapse development and plasticity by Rho GTPase regulatory proteins
    • Tolias, K. F., Duman, J. G., and Um, K. (2011) Control of synapse development and plasticity by Rho GTPase regulatory proteins. Prog. Neurobiol. 94, 133-148
    • (2011) Prog. Neurobiol. , vol.94 , pp. 133-148
    • Tolias, K.F.1    Duman, J.G.2    Um, K.3
  • 48
    • 4644370323 scopus 로고    scopus 로고
    • Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity
    • Reid, T. S., Terry, K. L., Casey, P. J., and Beese, L. S. (2004) Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J. Mol. Biol. 343, 417-433
    • (2004) J. Mol. Biol. , vol.343 , pp. 417-433
    • Reid, T.S.1    Terry, K.L.2    Casey, P.J.3    Beese, L.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.