메뉴 건너뛰기




Volumn 116, Issue 16, 2003, Pages 3339-3346

Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes

Author keywords

Alzheimer's disease; Amyloid precursor protein; Amyloid peptide; BACE; Co localization; Endocytosis; Fluorescence resonance energy transfer

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; MUTANT PROTEIN;

EID: 0042887148     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00643     Document Type: Review
Times cited : (240)

References (32)
  • 1
    • 0029764358 scopus 로고    scopus 로고
    • Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: Fluorescent-labeled protein kinase C beta I
    • Bastiaens, P. I. and Jovin, T. M. (1996). Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: fluorescent-labeled protein kinase C beta I. Proc. Natl. Acad. Sci. USA 93, 8407-8412.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8407-8412
    • Bastiaens, P.I.1    Jovin, T.M.2
  • 3
    • 0030739716 scopus 로고    scopus 로고
    • Novel beta-secretase cleavage of beta-amyloid precursor protein in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Chyung, A. S., Greenberg, B. D., Cook, D. G., Doms, R. W. and Lee, V. M. (1997). Novel beta-secretase cleavage of beta-amyloid precursor protein in the endoplasmic reticulum/intermediate compartment of NT2N cells. J. Cell Biol. 138, 671-680.
    • (1997) J. Cell Biol. , vol.138 , pp. 671-680
    • Chyung, A.S.1    Greenberg, B.D.2    Cook, D.G.3    Doms, R.W.4    Lee, V.M.5
  • 4
    • 0028924248 scopus 로고
    • Generation of amyloid beta protein from its precursor is sequence specific
    • Citron, M., Teplow, D. B. and Selkoe, D. J. (1995). Generation of amyloid beta protein from its precursor is sequence specific. Neuron 14, 661-670.
    • (1995) Neuron , vol.14 , pp. 661-670
    • Citron, M.1    Teplow, D.B.2    Selkoe, D.J.3
  • 5
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook, D. G., Forman, M. S., Sung, J. C., Leight, S., Kolson, D. L., Iwatsubo, T, Lee, V. M.-Y. and Doms, R. W. (1997). Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat. Med. 3, 1021-1023.
    • (1997) Nat. Med. , vol.3 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5    Iwatsubo, T.6    Lee, V.M.-Y.7    Doms, R.W.8
  • 6
    • 0034049944 scopus 로고    scopus 로고
    • Proteolytic processing and cell biological functions of the amyloid precursor protein
    • De Strooper, B. and Annaert, W. (2000). Proteolytic processing and cell biological functions of the amyloid precursor protein. J. Cell Sci. 113, 1857-1870.
    • (2000) J. Cell Sci. , vol.113 , pp. 1857-1870
    • De Strooper, B.1    Annaert, W.2
  • 8
    • 0036718272 scopus 로고    scopus 로고
    • Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease
    • Fukumoto, H., Cheung, B. S., Hyman, B. T. and Irizarry, M. C. (2002). Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease. Arch. Neurol. 59, 1381-1389.
    • (2002) Arch. Neurol. , vol.59 , pp. 1381-1389
    • Fukumoto, H.1    Cheung, B.S.2    Hyman, B.T.3    Irizarry, M.C.4
  • 9
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway
    • Haass, C., Lemere, C. A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L. and Selkoe, D. J. (1995). The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Nat. Med. 1, 1291-1296.
    • (1995) Nat. Med. , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3    Citron, M.4    Seubert, P.5    Schenk, D.6    Lannfelt, L.7    Selkoe, D.J.8
  • 11
    • 0036260892 scopus 로고    scopus 로고
    • Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease
    • Holsinger, R. M., McLean, C. A., Beyreuther, K., Masters, C. L. and Evin, G. (2002). Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease. Ann. Neurol. 51, 783-786.
    • (2002) Ann. Neurol. , vol.51 , pp. 783-786
    • Holsinger, R.M.1    McLean, C.A.2    Beyreuther, K.3    Masters, C.L.4    Evin, G.5
  • 12
    • 0037013209 scopus 로고    scopus 로고
    • β-secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain
    • Huse, J. T., Liu, K., Pijak, D. S., Carlin, D., Lee, V. M.-Y. and Doms, R. W. (2002). β-secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain. J. Biol. Chem. 277, 16278-16284.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16278-16284
    • Huse, J.T.1    Liu, K.2    Pijak, D.S.3    Carlin, D.4    Lee, V.M.-Y.5    Doms, R.W.6
  • 13
    • 0035503797 scopus 로고    scopus 로고
    • Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: Role of the intracellular adapter protein Fe65
    • Kinoshita, A., Whelan, C. M., Smith, C. J., Mikhailenko, I., Rebeck, G. W., Strickland, D. K. and Hyman, B. T. (2001). Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: role of the intracellular adapter protein Fe65. J. Neurosci. 21, 8354-8361.
    • (2001) J. Neurosci. , vol.21 , pp. 8354-8361
    • Kinoshita, A.1    Whelan, C.M.2    Smith, C.J.3    Mikhailenko, I.4    Rebeck, G.W.5    Strickland, D.K.6    Hyman, B.T.7
  • 14
    • 0035923502 scopus 로고    scopus 로고
    • Alzheimer's beta-secretase, beta-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase
    • Kitazume, S., Tachida, Y., Oka, R., Shirotani, K., Saido, T. C. and Hashimoto, Y. (2001). Alzheimer's beta-secretase, beta-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase. Proc. Natl. Acad. Sci. USA 98, 13554-13559.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13554-13559
    • Kitazume, S.1    Tachida, Y.2    Oka, R.3    Shirotani, K.4    Saido, T.C.5    Hashimoto, Y.6
  • 15
    • 0032851485 scopus 로고    scopus 로고
    • Demonstration by fluorescence resonance energy transfer of a close association between activated MAP kinase and neurofibrillary tangle: Implications for MAP kinase activation in Alzheimer's disease
    • Knowles, R. B., Chin, J., Ruff, C. T. and Hyman, B. T. (1999). Demonstration by fluorescence resonance energy transfer of a close association between activated MAP kinase and neurofibrillary tangle: implications for MAP kinase activation in Alzheimer's disease. J. Neuropathol. Exp. Neurol. 58, 1090-1098.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 1090-1098
    • Knowles, R.B.1    Chin, J.2    Ruff, C.T.3    Hyman, B.T.4
  • 16
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo, E. H. and Squazzo, S. L. (1994). Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 269, 21162-21166.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21162-21166
    • Koo, E.H.1    Squazzo, S.L.2
  • 17
    • 0027484116 scopus 로고
    • The Alzheimer beta-amyloid protein precursor/protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells
    • Kuentzel, S. L., Ali, S. M., Altman, R. A., Greenberg, B. D. and Raub, T. J. (1993). The Alzheimer beta-amyloid protein precursor/protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells. Biochem. J. 295, 367-378.
    • (1993) Biochem. J. , vol.295 , pp. 367-378
    • Kuentzel, S.L.1    Ali, S.M.2    Altman, R.A.3    Greenberg, B.D.4    Raub, T.J.5
  • 18
    • 0034708767 scopus 로고    scopus 로고
    • Membrane association and protein conformation of a-Synuclein in intact neurons
    • McLean, P. J., Kawamata, H., Ribich, S. and Hyman, B. T. (2000). Membrane association and protein conformation of a-Synuclein in intact neurons. J. Biol. Chem. 275, 8812-8816.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8812-8816
    • McLean, P.J.1    Kawamata, H.2    Ribich, S.3    Hyman, B.T.4
  • 19
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identified new signals for b-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Aβ42
    • Perez, R. G., Soriano, S., Hayes, J. D., Ostaszewski, B., Xia, W., Selkow, D. J., Chen, X., Stokin, G. B. and Koo, E. H. (1999). Mutagenesis identified new signals for b-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Aβ42. J. Biol. Chem. 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    Selkow, D.J.6    Chen, X.7    Stokin, G.B.8    Koo, E.H.9
  • 20
    • 0029989591 scopus 로고    scopus 로고
    • Enhanced release of amyloid beta-protein from codon 670/671 'Swedish' mutant beta-amyloid precursor protein occurs in both secretory and endocytic pathways
    • Perez, R. G., Squazzo, S. L. and Koo, E. H. (1996). Enhanced release of amyloid beta-protein from codon 670/671 'Swedish' mutant beta-amyloid precursor protein occurs in both secretory and endocytic pathways. J. Biol. Chem. 271, 9100-9107.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9100-9107
    • Perez, R.G.1    Squazzo, S.L.2    Koo, E.H.3
  • 21
  • 22
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of the beta-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe, D. J. (1998). The cell biology of the beta-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8, 447-453.
    • (1998) Trends Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 25
    • 0036326442 scopus 로고    scopus 로고
    • ELISA analysis of β-secretase cleavage of the Swedish amyloid precursor protein in the secretory and endocytic pathways
    • Steinhilb, M. S., Turner, R. S. and Gaut, J. R. (2002). ELISA analysis of β-secretase cleavage of the Swedish amyloid precursor protein in the secretory and endocytic pathways. J. Neurochem. 80, 1019-1028.
    • (2002) J. Neurochem. , vol.80 , pp. 1019-1028
    • Steinhilb, M.S.1    Turner, R.S.2    Gaut, J.R.3
  • 26
    • 0029942495 scopus 로고    scopus 로고
    • Metabolism of the 'Swedish' amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the 'beta-secretase' site occurs in the Golgi apparatus
    • Thinenkaran, G., Teplow, D. B., Siman, R., Greenberg, B. and Sisodia, S. S. (1996). Metabolism of the 'Swedish' amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the 'beta-secretase' site occurs in the Golgi apparatus. J. Biol. Chem. 271, 9390-9397.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9390-9397
    • Thinenkaran, G.1    Teplow, D.B.2    Siman, R.3    Greenberg, B.4    Sisodia, S.S.5
  • 27
    • 0034629292 scopus 로고    scopus 로고
    • Modulation of beta-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP). Evidence that LRP contributes to the pathogenesis of Alzheimer's disease
    • Ulery, P. G., Beers, J., Mikhailenko, I., Tanzi, R. E., Rebeck, G. W., Hyman, B. T. and Strickland, D. K. (2000). Modulation of beta-amyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP). Evidence that LRP contributes to the pathogenesis of Alzheimer's disease. J. Biol. Chem. 275, 7410-7415.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7410-7415
    • Ulery, P.G.1    Beers, J.2    Mikhailenko, I.3    Tanzi, R.E.4    Rebeck, G.W.5    Hyman, B.T.6    Strickland, D.K.7
  • 29
    • 0029934134 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization
    • Yamazaki, T., Koo, E. H. and Selkoe, D. J. (1996). Trafficking of cell-surface amyloid beta-protein precursor. II. Endocytosis, recycling and lysosomal targeting detected by immunolocalization. J. Cell Sci. 109, 999-1008.
    • (1996) J. Cell Sci. , vol.109 , pp. 999-1008
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 31
    • 0035965275 scopus 로고    scopus 로고
    • The transmembrane domain of the Alzheimer's beta-secretase (BACE1) determines its late Golgi localization and access to beta-amyloid precursor protein (APP) substrate
    • Yan, R., Han, P., Miao, H., Greengard, P. and Xu, H. (2001). The transmembrane domain of the Alzheimer's beta-secretase (BACE1) determines its late Golgi localization and access to beta-amyloid precursor protein (APP) substrate. J. Biol. Chem. 276, 36788-36796.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36788-36796
    • Yan, R.1    Han, P.2    Miao, H.3    Greengard, P.4    Xu, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.