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Volumn 401, Issue 2, 2010, Pages 219-224

Trafficking of amyloid β-precursor protein products C83 and C99 on the endocytic pathway

Author keywords

Amyloid precursor protein; Detergent resistant membrane; Endosomes; Protease inhibitors; Secretases

Indexed keywords

AMYLOID PRECURSOR PROTEIN; AMYLOID PRECURSOR PROTEIN C83; AMYLOID PRECURSOR PROTEIN C99; GAMMA SECRETASE; GAMMA SECRETASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 77957804623     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.09.033     Document Type: Article
Times cited : (6)

References (32)
  • 1
    • 0036441486 scopus 로고    scopus 로고
    • A cell biological perspective on Alzheimer's disease
    • Annaert W., DeStrooper B. A cell biological perspective on Alzheimer's disease. Ann. Rev. Cell Dev. Biol. 2002, 18:25-51.
    • (2002) Ann. Rev. Cell Dev. Biol. , vol.18 , pp. 25-51
    • Annaert, W.1    DeStrooper, B.2
  • 2
    • 1442264828 scopus 로고    scopus 로고
    • Take five-BACE the γ-secretase quartet conduct Alzheimer's amyloid -peptide generation
    • Haass C. Take five-BACE the γ-secretase quartet conduct Alzheimer's amyloid -peptide generation. EMBO. J. 2004, 23:483-488.
    • (2004) EMBO. J. , vol.23 , pp. 483-488
    • Haass, C.1
  • 4
    • 8744225623 scopus 로고    scopus 로고
    • Proteolytic processing of amyloid-beta precursor protein by secretases does not require cell surface transport
    • Khvotchev M., Sudhof T.C. Proteolytic processing of amyloid-beta precursor protein by secretases does not require cell surface transport. J. Biol. Chem. 2004, 279:7101-47108.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7101-47108
    • Khvotchev, M.1    Sudhof, T.C.2
  • 5
    • 0345803941 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid beta-protein at the cell surface
    • Chyung J.H., Selkoe D.J. Inhibition of receptor-mediated endocytosis demonstrates generation of amyloid beta-protein at the cell surface. J. Biol. Chem. 2003, 278:51035-51043.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51035-51043
    • Chyung, J.H.1    Selkoe, D.J.2
  • 6
    • 33644862462 scopus 로고    scopus 로고
    • Amyloid precursor protein and notch intracellular domains are generated after transport of their precursors to the cell surface
    • C Kaether, S Schmitt, Willem M., Hass C. Amyloid precursor protein and notch intracellular domains are generated after transport of their precursors to the cell surface. Traffic 2006, 7:408-415.
    • (2006) Traffic , vol.7 , pp. 408-415
    • C, K.1    S, S.2    Willem, M.3    Hass, C.4
  • 7
    • 14244268498 scopus 로고    scopus 로고
    • Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage
    • Chyung J.H., Raper D.M., Selkoe D.J. Gamma-secretase exists on the plasma membrane as an intact complex that accepts substrates and effects intramembrane cleavage. J. Biol. Chem. 2005, 28:4383-4392.
    • (2005) J. Biol. Chem. , vol.28 , pp. 4383-4392
    • Chyung, J.H.1    Raper, D.M.2    Selkoe, D.J.3
  • 8
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta protein involves the endocytic pathway
    • Koo EH E.H., Squazzo SL S.L. Evidence that production and release of amyloid beta protein involves the endocytic pathway. J. Biol. Chem. 1994, 269:17386-17389.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17386-17389
    • Koo EH, E.H.1    Squazzo SL, S.L.2
  • 9
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments including Abeta42
    • Perez R.G., Soriano S., Hayes J.D., Ostaszewski B., Xia W., Selkoe D.J., Chen X., Stokin G.B. Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments including Abeta42. J. Biol. Chem. 1999, 274:18851-18856.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18851-18856
    • Perez, R.G.1    Soriano, S.2    Hayes, J.D.3    Ostaszewski, B.4    Xia, W.5    Selkoe, D.J.6    Chen, X.7    Stokin, G.B.8
  • 11
    • 0042733013 scopus 로고    scopus 로고
    • Rab5-stimulated up-regulation of the endocytic pathway increases intracellular beta-cleaved amyloid precursor protein carboxyl-terminal fragment levels and Abeta production
    • Grbovic O.M., Mathews P.M., Jiang Y., Schmidt S.D., Dinakar Y., Summers-Terio N.B., Ceresa B.P., Nixon R.A., Cataldo A A. Rab5-stimulated up-regulation of the endocytic pathway increases intracellular beta-cleaved amyloid precursor protein carboxyl-terminal fragment levels and Abeta production. J. Biol. Chem. 2003, 278:31261-31268.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31261-31268
    • Grbovic, O.M.1    Mathews, P.M.2    Jiang, Y.3    Schmidt, S.D.4    Dinakar, Y.5    Summers-Terio, N.B.6    Ceresa, B.P.7    Nixon, R.A.8    Cataldo A, A.9
  • 13
    • 4344689871 scopus 로고    scopus 로고
    • Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for beta-amyloid peptide over-production and localization in Alzheimer's disease
    • Yu Y.H., Kuman A., Peterhoff C., Shapiro L., Kulnane L., Uchiyama Y., Lamb B.T., Cuervo A.M., Nixon RA R.A. Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for beta-amyloid peptide over-production and localization in Alzheimer's disease. Int. J. Biochem. Cell Biol. 2004, 36:2531-2540.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2531-2540
    • Yu, Y.H.1    Kuman, A.2    Peterhoff, C.3    Shapiro, L.4    Kulnane, L.5    Uchiyama, Y.6    Lamb, B.T.7    Cuervo, A.M.8    Nixon RA, R.A.9
  • 14
    • 33749042749 scopus 로고    scopus 로고
    • Sorting through the cell biology of Azlheimer's disease: intracellular pathways to pathogenesis
    • Small S.A., Gandy S S. Sorting through the cell biology of Azlheimer's disease: intracellular pathways to pathogenesis. Neuron 2006, 52:15-31.
    • (2006) Neuron , vol.52 , pp. 15-31
    • Small, S.A.1    Gandy S, S.2
  • 15
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking processing and function
    • Thinakaran G., Koo E. Amyloid precursor protein trafficking processing and function. J. Biol. Chem. 2008, 283:29615-29619.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.2
  • 16
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R., Keller P., Haass C., Thiele C., Simons K. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J. Cell Biol. 2005, 160:113-123.
    • (2005) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 18
    • 0347318065 scopus 로고    scopus 로고
    • Cholesterol and the biology of Alzheimer's disease
    • Wolozin Cholesterol and the biology of Alzheimer's disease. Neuron 2004, 41:7-10.
    • (2004) Neuron , vol.41 , pp. 7-10
    • Wolozin1
  • 21
    • 14844317284 scopus 로고    scopus 로고
    • The regulation of beta-secretase by cholesterol and statins in Alzheimer's disease
    • Sidera C., Parsons R., Austen B. The regulation of beta-secretase by cholesterol and statins in Alzheimer's disease. J. Neurol. Sci. 2005, 229:269-273.
    • (2005) J. Neurol. Sci. , vol.229 , pp. 269-273
    • Sidera, C.1    Parsons, R.2    Austen, B.3
  • 22
    • 33645299023 scopus 로고    scopus 로고
    • The involvement of lipid rafts in Alzheimer's disease
    • Cordy J.M., Hooper N.M., Turner A.J. The involvement of lipid rafts in Alzheimer's disease. Mol. Membr. Biol. 2006, 23:111-122.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 111-122
    • Cordy, J.M.1    Hooper, N.M.2    Turner, A.J.3
  • 23
    • 0025602328 scopus 로고
    • Compartmentation and turnover of the low density lipoprotein receptor in skin fibroblasts
    • Hare J.F. Compartmentation and turnover of the low density lipoprotein receptor in skin fibroblasts. J. Biol. Chem. 1990, 265:21758-21763.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21758-21763
    • Hare, J.F.1
  • 24
    • 0025949276 scopus 로고
    • Mechanisms of plasma membrane protein degradation: recycling proteiens are degraded more rapidly than those confined to the cell surface
    • Hare J.F., Taylor K. Mechanisms of plasma membrane protein degradation: recycling proteiens are degraded more rapidly than those confined to the cell surface. Proc. Natl. Acad. Sci USA. 1991, 88:5902-5906.
    • (1991) Proc. Natl. Acad. Sci USA. , vol.88 , pp. 5902-5906
    • Hare, J.F.1    Taylor, K.2
  • 25
    • 77957766350 scopus 로고
    • Surface exposed proteins of 3T3-L1 adipocytes: identification of phosphorylated insulin-translocated and recycling proteins
    • Hare J.F., Taylor K. Surface exposed proteins of 3T3-L1 adipocytes: identification of phosphorylated insulin-translocated and recycling proteins. Arch. Biochem. Biophys. 1992, 451:79-90.
    • (1992) Arch. Biochem. Biophys. , vol.451 , pp. 79-90
    • Hare, J.F.1    Taylor, K.2
  • 26
    • 0034805489 scopus 로고    scopus 로고
    • Protease inhibitors divert amyloid precursor protein to the secretory pathway
    • Hare J.F. Protease inhibitors divert amyloid precursor protein to the secretory pathway. Biochem. Biophys. Res. Commun. 2001, 281:1298-1303.
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 1298-1303
    • Hare, J.F.1
  • 27
    • 34548496491 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein promotes amyloid precursor protein trafficking to lipid rafts in the endocytic pathway
    • Yoon I.S., Chen E., Busse R., Repetto E., Lakshmana M.K., Koo E.H., Kang D.E. Low-density lipoprotein receptor-related protein promotes amyloid precursor protein trafficking to lipid rafts in the endocytic pathway. FASEB J. 2007, 21:742-2752.
    • (2007) FASEB J. , vol.21 , pp. 742-2752
    • Yoon, I.S.1    Chen, E.2    Busse, R.3    Repetto, E.4    Lakshmana, M.K.5    Koo, E.H.6    Kang, D.E.7
  • 28
    • 0035830911 scopus 로고    scopus 로고
    • MG132, blocks maturation of the amyloid precursor protein Swedish mutant preventing cleavage by β-secretase
    • Steinhilb M.L., Turner R.S., Gaunt JR J.R., inhibitor The protease MG132, blocks maturation of the amyloid precursor protein Swedish mutant preventing cleavage by β-secretase. J. Biol. Chem. 2001, 276:4476-4484.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4476-4484
    • Steinhilb, M.L.1    Turner, R.S.2    Gaunt JR, J.R.3    inhibitor, T.P.4
  • 29
    • 33845655221 scopus 로고    scopus 로고
    • Presenilin/gamma-secretase activity regulates protein clearance from the endocytic recycling compartment
    • Zhang M., Haapasalo A., Kim D.Y., Ingano L.A., Pettingell W.H., Kovacs D.M. Presenilin/gamma-secretase activity regulates protein clearance from the endocytic recycling compartment. FASEB J. 2006, 20:1176-1178.
    • (2006) FASEB J. , vol.20 , pp. 1176-1178
    • Zhang, M.1    Haapasalo, A.2    Kim, D.Y.3    Ingano, L.A.4    Pettingell, W.H.5    Kovacs, D.M.6
  • 30
    • 0035830844 scopus 로고    scopus 로고
    • Accumulation and aggregation of amyloid β-protein in late endosomes of Niemann-Pick type C cells
    • Yamazaki T., Chang T., Haass C., Ihara Y Y. Accumulation and aggregation of amyloid β-protein in late endosomes of Niemann-Pick type C cells. J. Biol. Chem. 2001, 276:4454-4460.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4454-4460
    • Yamazaki, T.1    Chang, T.2    Haass, C.3    Ihara Y, Y.4
  • 31
    • 33845655221 scopus 로고    scopus 로고
    • Presenilin/gamma-secretase activity regulates protein clearance from the endocytic recycling compartment
    • Zhang M., Haapasalo A., Kim D.Y., Ingano L.A., Pettigell W.H., Kovacs D.M. Presenilin/gamma-secretase activity regulates protein clearance from the endocytic recycling compartment. FASEB J. 2006, 20:1176-1178.
    • (2006) FASEB J. , vol.20 , pp. 1176-1178
    • Zhang, M.1    Haapasalo, A.2    Kim, D.Y.3    Ingano, L.A.4    Pettigell, W.H.5    Kovacs, D.M.6
  • 32
    • 33645299023 scopus 로고    scopus 로고
    • The involvement of lipid rafts in Alzheimer's disease
    • Cordy J., Hooper N.M., Turner A.J. The involvement of lipid rafts in Alzheimer's disease. Mol. Membr. Biol. 2006, 23:111-122.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 111-122
    • Cordy, J.1    Hooper, N.M.2    Turner, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.