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Volumn 33, Issue 6, 2012, Pages 1125.e9-1125.e18

Calpastatin modulates APP processing in the brains of β-amyloid depositing but not wild-type mice

Author keywords

Alzheimer's disease; APP; A ; Calpain; Calpastatin

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CALPAIN; CALPASTATIN; MITOGEN ACTIVATED PROTEIN KINASE; TAU PROTEIN;

EID: 84859502846     PISSN: 01974580     EISSN: 15581497     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2011.11.023     Document Type: Article
Times cited : (13)

References (50)
  • 2
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division
    • Arthur J.S., Elce J.S., Hegadorn C., Williams K., Greer P.A. Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol. Cell. Biol 2000, 20:4474-4481.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 3
    • 0035008875 scopus 로고    scopus 로고
    • Disruption of the mouse μ-calpain gene reveals an essential role in platelet function
    • Azam M., Andrabi S.S., Sahr K.E., Kamath L., Kuliopulos A., Chishti A.H. Disruption of the mouse μ-calpain gene reveals an essential role in platelet function. Mol. Cell. Biol 2001, 21:2213-2220.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 2213-2220
    • Azam, M.1    Andrabi, S.S.2    Sahr, K.E.3    Kamath, L.4    Kuliopulos, A.5    Chishti, A.H.6
  • 5
    • 33644897573 scopus 로고    scopus 로고
    • Calpain inhibition: a therapeutic strategy targeting multiple disease states
    • Carragher N.O. Calpain inhibition: a therapeutic strategy targeting multiple disease states. Curr. Pharm. Des 2006, 12:615-638.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 615-638
    • Carragher, N.O.1
  • 6
    • 70349570600 scopus 로고    scopus 로고
    • Aberrant phosphorylation in the pathogenesis of Alzheimer's disease
    • Chung S.H. Aberrant phosphorylation in the pathogenesis of Alzheimer's disease. BMB Rep 2009, 42:467-474.
    • (2009) BMB Rep , vol.42 , pp. 467-474
    • Chung, S.H.1
  • 7
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: structure, function, and regulation
    • Croall D.E., DeMartino G.N. Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol. Rev 1991, 71:813-847.
    • (1991) Physiol. Rev , vol.71 , pp. 813-847
    • Croall, D.E.1    DeMartino, G.N.2
  • 8
    • 33644853371 scopus 로고    scopus 로고
    • Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid β-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3
    • Fifre A., Sponne I., Koziel V., Kriem B., Yen Potin F.T., Bihain B.E., Olivier J.L., Oster T., Pillot T. Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid β-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3. J. Biol. Chem 2006, 281:229-240.
    • (2006) J. Biol. Chem , vol.281 , pp. 229-240
    • Fifre, A.1    Sponne, I.2    Koziel, V.3    Kriem, B.4    Yen Potin, F.T.5    Bihain, B.E.6    Olivier, J.L.7    Oster, T.8    Pillot, T.9
  • 10
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ42 fibrils
    • Götz J., Chen F., van Dorpe J., Nitsch R.M. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Aβ42 fibrils. Science 2001, 293:1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Götz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 11
    • 26844515806 scopus 로고    scopus 로고
    • Lack of phenotype for LTP and fear conditioning learning in calpain 1 knock-out mice
    • Grammer M., Kuchay S., Chishti A., Baudry M. Lack of phenotype for LTP and fear conditioning learning in calpain 1 knock-out mice. Neurobiol. Learn. Mem 2005, 84:222-227.
    • (2005) Neurobiol. Learn. Mem , vol.84 , pp. 222-227
    • Grammer, M.1    Kuchay, S.2    Chishti, A.3    Baudry, M.4
  • 12
    • 0030836467 scopus 로고    scopus 로고
    • Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease
    • Grynspan F., Griffin W.R., Cataldo A., Katayama S., Nixon R.A. Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease. Brain Res 1997, 763:145-158.
    • (1997) Brain Res , vol.763 , pp. 145-158
    • Grynspan, F.1    Griffin, W.R.2    Cataldo, A.3    Katayama, S.4    Nixon, R.A.5
  • 13
    • 17644393902 scopus 로고    scopus 로고
    • Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors
    • Higuchi M., Tomioka M., Takano J., Shirotani K., Iwata N., Masumoto H., Maki M., Itohara S., Saido T.C. Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors. J. Biol. Chem 2005, 280:15229-15237.
    • (2005) J. Biol. Chem , vol.280 , pp. 15229-15237
    • Higuchi, M.1    Tomioka, M.2    Takano, J.3    Shirotani, K.4    Iwata, N.5    Masumoto, H.6    Maki, M.7    Itohara, S.8    Saido, T.C.9
  • 14
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • Huang Y., Wang K.K. The calpain family and human disease. Trends Mol. Med 2001, 7:355-362.
    • (2001) Trends Mol. Med , vol.7 , pp. 355-362
    • Huang, Y.1    Wang, K.K.2
  • 16
    • 0029905596 scopus 로고    scopus 로고
    • The carboxyl termini of β-amyloid peptides 1-40 and 1-42 are generated by distinct γ-secretase activities
    • Klafki H., Abramowski D., Swoboda R., Paganetti P.A., Staufenbiel M. The carboxyl termini of β-amyloid peptides 1-40 and 1-42 are generated by distinct γ-secretase activities. J. Biol. Chem 1996, 271:28655-28659.
    • (1996) J. Biol. Chem , vol.271 , pp. 28655-28659
    • Klafki, H.1    Abramowski, D.2    Swoboda, R.3    Paganetti, P.A.4    Staufenbiel, M.5
  • 17
    • 0037112117 scopus 로고    scopus 로고
    • Activation of calpain in cultured neurons overexpressing Alzheimer amyloid precursor protein
    • Kuwako K., Nishimura I., Uetsuki T., Saido T.C., Yoshikawa K. Activation of calpain in cultured neurons overexpressing Alzheimer amyloid precursor protein. Brain Res. Mol. Brain Res 2002, 107:166-175.
    • (2002) Brain Res. Mol. Brain Res , vol.107 , pp. 166-175
    • Kuwako, K.1    Nishimura, I.2    Uetsuki, T.3    Saido, T.C.4    Yoshikawa, K.5
  • 20
    • 77956258994 scopus 로고    scopus 로고
    • Calpain activation promotes BACE1 expression, amyloid precursor protein processing, and amyloid plaque formation in a transgenic mouse model of Alzheimer disease
    • Liang B., Duan B.Y., Zhou X.P., Gong J.X., Luo Z.G. Calpain activation promotes BACE1 expression, amyloid precursor protein processing, and amyloid plaque formation in a transgenic mouse model of Alzheimer disease. J. Biol. Chem 2010, 285:27737-27744.
    • (2010) J. Biol. Chem , vol.285 , pp. 27737-27744
    • Liang, B.1    Duan, B.Y.2    Zhou, X.P.3    Gong, J.X.4    Luo, Z.G.5
  • 21
    • 27844553889 scopus 로고    scopus 로고
    • Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain
    • Liu F., Grundke-Iqbal I., Iqbal K., Oda Y., Tomizawa K., Gong C.X. Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain. J. Biol. Chem 2005, 280:37755-37762.
    • (2005) J. Biol. Chem , vol.280 , pp. 37755-37762
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Oda, Y.4    Tomizawa, K.5    Gong, C.X.6
  • 24
    • 0037184127 scopus 로고    scopus 로고
    • Calpain activity regulates the cell surface distribution of amyloid precursor protein: inhibition of calpains enhances endosomal generation of β-cleaved C-terminal APP fragments
    • Mathews P.M., Jiang Y., Schmidt S.D., Grbovic O.M., Mercken M., Nixon R.A. Calpain activity regulates the cell surface distribution of amyloid precursor protein: inhibition of calpains enhances endosomal generation of β-cleaved C-terminal APP fragments. J. Biol. Chem 2002, 277:36415-36424.
    • (2002) J. Biol. Chem , vol.277 , pp. 36415-36424
    • Mathews, P.M.1    Jiang, Y.2    Schmidt, S.D.3    Grbovic, O.M.4    Mercken, M.5    Nixon, R.A.6
  • 26
    • 70349614359 scopus 로고    scopus 로고
    • In vivo turnover of tau and APP metabolites in the brains of wild-type and Tg2576 mice: greater stability of sAPP in the β-amyloid depositing mice
    • Morales-Corraliza J., Mazzella M.J., Berger J.D., Diaz N.S., Choi J.H., Levy E., Matsuoka Y., Planel E., Mathews P.M. In vivo turnover of tau and APP metabolites in the brains of wild-type and Tg2576 mice: greater stability of sAPP in the β-amyloid depositing mice. PLoS One 2009, 4:e7134.
    • (2009) PLoS One , vol.4
    • Morales-Corraliza, J.1    Mazzella, M.J.2    Berger, J.D.3    Diaz, N.S.4    Choi, J.H.5    Levy, E.6    Matsuoka, Y.7    Planel, E.8    Mathews, P.M.9
  • 28
    • 0141762744 scopus 로고    scopus 로고
    • The calpains in aging and aging-related diseases
    • Nixon R.A. The calpains in aging and aging-related diseases. Ageing Res. Rev 2003, 2:407-418.
    • (2003) Ageing Res. Rev , vol.2 , pp. 407-418
    • Nixon, R.A.1
  • 29
    • 0034304390 scopus 로고    scopus 로고
    • The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: a review
    • Nixon R.A., Cataldo A.M., Mathews P.M. The endosomal-lysosomal system of neurons in Alzheimer's disease pathogenesis: a review. Neurochem. Res 2000, 25:1161-1172.
    • (2000) Neurochem. Res , vol.25 , pp. 1161-1172
    • Nixon, R.A.1    Cataldo, A.M.2    Mathews, P.M.3
  • 30
    • 0034800876 scopus 로고    scopus 로고
    • Accumulation of non-erythroid αII-spectrin and calpain-cleaved αII-spectrin breakdown products in cerebrospinal fluid after traumatic brain injury in rats
    • Pike B.R., Flint J., Dutta S., Johnson E., Wang K.K., Hayes R.L. Accumulation of non-erythroid αII-spectrin and calpain-cleaved αII-spectrin breakdown products in cerebrospinal fluid after traumatic brain injury in rats. J. Neurochem 2001, 78:1297-1306.
    • (2001) J. Neurochem , vol.78 , pp. 1297-1306
    • Pike, B.R.1    Flint, J.2    Dutta, S.3    Johnson, E.4    Wang, K.K.5    Hayes, R.L.6
  • 34
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration
    • Saito K., Elce J.S., Hamos J.E., Nixon R.A. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:2628-2632.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 35
    • 22844438739 scopus 로고    scopus 로고
    • Tissue processing prior to protein analysis and β-amyloid quantitation
    • Schmidt S.D., Jiang Y., Nixon R.A., Mathews P.M. Tissue processing prior to protein analysis and β-amyloid quantitation. Methods Mol. Biol 2005, 299:267-278.
    • (2005) Methods Mol. Biol , vol.299 , pp. 267-278
    • Schmidt, S.D.1    Jiang, Y.2    Nixon, R.A.3    Mathews, P.M.4
  • 36
    • 22844438408 scopus 로고    scopus 로고
    • ELISA method for measurement of β-amyloid levels
    • Schmidt S.D., Nixon R.A., Mathews P.M. ELISA method for measurement of β-amyloid levels. Methods Mol. Biol 2005, 299:279-297.
    • (2005) Methods Mol. Biol , vol.299 , pp. 279-297
    • Schmidt, S.D.1    Nixon, R.A.2    Mathews, P.M.3
  • 37
    • 0024020782 scopus 로고
    • Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo
    • Siman R., Noszek J.C. Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo. Neuron 1988, 1:279-287.
    • (1988) Neuron , vol.1 , pp. 279-287
    • Siman, R.1    Noszek, J.C.2
  • 38
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H., Ishiura S., Suzuki K. Structure and physiological function of calpains. Biochem. J 1997, 328:721-732.
    • (1997) Biochem. J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 40
    • 18144407551 scopus 로고    scopus 로고
    • Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice
    • Takano J., Tomioka M., Tsubuki S., Higuchi M., Iwata N., Itohara S., Maki M., Saido T.C. Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice. J. Biol. Chem 2005, 280:16175-16184.
    • (2005) J. Biol. Chem , vol.280 , pp. 16175-16184
    • Takano, J.1    Tomioka, M.2    Tsubuki, S.3    Higuchi, M.4    Iwata, N.5    Itohara, S.6    Maki, M.7    Saido, T.C.8
  • 41
    • 77950569777 scopus 로고    scopus 로고
    • Iowa variant of familial Alzheimer's disease: accumulation of posttranslationally modified AβD23N in parenchymal and cerebrovascular amyloid deposits
    • Tomidokoro Y., Rostagno A., Neubert T.A., Lu Y., Rebeck G.W., Frangione B., Greenberg S.M., Ghiso J. Iowa variant of familial Alzheimer's disease: accumulation of posttranslationally modified AβD23N in parenchymal and cerebrovascular amyloid deposits. Am. J. Pathol 2010, 176:1841-1854.
    • (2010) Am. J. Pathol , vol.176 , pp. 1841-1854
    • Tomidokoro, Y.1    Rostagno, A.2    Neubert, T.A.3    Lu, Y.4    Rebeck, G.W.5    Frangione, B.6    Greenberg, S.M.7    Ghiso, J.8
  • 43
    • 34848835458 scopus 로고    scopus 로고
    • Calpastatin levels affect calpain activation and calpain proteolytic activity in APP transgenic mouse model of Alzheimer's disease
    • Vaisid T., Kosower N.S., Katzav A., Chapman J., Barnoy S. Calpastatin levels affect calpain activation and calpain proteolytic activity in APP transgenic mouse model of Alzheimer's disease. Neurochem. Int 2007, 51:391-397.
    • (2007) Neurochem. Int , vol.51 , pp. 391-397
    • Vaisid, T.1    Kosower, N.S.2    Katzav, A.3    Chapman, J.4    Barnoy, S.5
  • 45
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: can you tell the difference?
    • Wang K.K. Calpain and caspase: can you tell the difference?. Trends Neurosci 2000, 23:20-26.
    • (2000) Trends Neurosci , vol.23 , pp. 20-26
    • Wang, K.K.1
  • 47
    • 34250861485 scopus 로고    scopus 로고
    • Calpain- and caspase-mediated αII-spectrin and tau proteolysis in rat cerebrocortical neuronal cultures after ecstasy or methamphetamine exposure
    • Warren M.W., Zheng W., Kobeissy F.H., Cheng Liu M., Hayes R.L., Gold M.S., Larner S.F., Wang K.K. Calpain- and caspase-mediated αII-spectrin and tau proteolysis in rat cerebrocortical neuronal cultures after ecstasy or methamphetamine exposure. Int. J. Neuropsychopharmacol 2007, 10:479-489.
    • (2007) Int. J. Neuropsychopharmacol , vol.10 , pp. 479-489
    • Warren, M.W.1    Zheng, W.2    Kobeissy, F.H.3    Cheng Liu, M.4    Hayes, R.L.5    Gold, M.S.6    Larner, S.F.7    Wang, K.K.8
  • 48
    • 0030853452 scopus 로고    scopus 로고
    • Specific increase in β-amyloid-protein 42 secretion ratio by calpain inhibition
    • Yamazaki T., Haass C., Saido T.C., Omura S., Ihara Y. Specific increase in β-amyloid-protein 42 secretion ratio by calpain inhibition. Biochemistry 1997, 36:8377-8383.
    • (1997) Biochemistry , vol.36 , pp. 8377-8383
    • Yamazaki, T.1    Haass, C.2    Saido, T.C.3    Omura, S.4    Ihara, Y.5
  • 49
    • 20344386015 scopus 로고    scopus 로고
    • Calpains and disease
    • Zatz M., Starling A. Calpains and disease. N Engl J. Med 2005, 352:2413-2423.
    • (2005) N Engl J. Med , vol.352 , pp. 2413-2423
    • Zatz, M.1    Starling, A.2
  • 50
    • 0033605588 scopus 로고    scopus 로고
    • Calpain inhibitor I increases β-amyloid peptide production by inhibiting the degradation of the substrate of γ-secretase. Evidence that substrate availability limits β-amyloid peptide production
    • Zhang L., Song L., Parker E.M. Calpain inhibitor I increases β-amyloid peptide production by inhibiting the degradation of the substrate of γ-secretase. Evidence that substrate availability limits β-amyloid peptide production. J. Biol. Chem 1999, 274:8966-8972.
    • (1999) J. Biol. Chem , vol.274 , pp. 8966-8972
    • Zhang, L.1    Song, L.2    Parker, E.M.3


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