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Volumn , Issue , 2011, Pages

Zinc metalloproteinases and amyloid beta-peptide metabolism: The positive side of proteolysis in Alzheimer's disease

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EID: 78349293078     PISSN: 20902247     EISSN: 20902255     Source Type: Journal    
DOI: 10.1155/2011/721463     Document Type: Review
Times cited : (31)

References (143)
  • 1
  • 2
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • Duyckaerts C., Delatour B., Potier M.-C., Classification and basic pathology of Alzheimer disease Acta Neuropathologica 2009 118 1 5 36
    • (2009) Acta Neuropathologica , vol.118 , Issue.1 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.-C.3
  • 4
    • 77951060145 scopus 로고    scopus 로고
    • Proteases and proteolysis in alzheimer disease: A multifactorial view on the disease process
    • de Strooper B., Proteases and proteolysis in alzheimer disease: a multifactorial view on the disease process Physiological Reviews 2010 90 2 465 494
    • (2010) Physiological Reviews , vol.90 , Issue.2 , pp. 465-494
    • De Strooper, B.1
  • 8
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D. J., Alzheimer's disease: genes, proteins, and therapy Physiological Reviews 2001 81 2 741 766
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 9
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of - Amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson M. P., Cellular actions of -amyloid precursor protein and its soluble and fibrillogenic derivatives Physiological Reviews 1997 77 4 1081 1132
    • (1997) Physiological Reviews , vol.77 , Issue.4 , pp. 1081-1132
    • Mattson, M.P.1
  • 11
    • 1442264828 scopus 로고    scopus 로고
    • Take fiveBACE and the -secretase quartet conduct Alzheimer's amyloid -peptide generation
    • Haass C., Take fiveBACE and the -secretase quartet conduct Alzheimer's amyloid -peptide generation EMBO Journal 2004 23 3 483 488
    • (2004) EMBO Journal , vol.23 , Issue.3 , pp. 483-488
    • Haass, C.1
  • 13
    • 0026045172 scopus 로고
    • Secretion of the /A4 amyloid precursor protein: Identification of a cleavage site in cultured mammalian cells
    • Wang R., Meschia J. F., Cotter R. J., Sisodia S. S., Secretion of the /A4 amyloid precursor protein: identification of a cleavage site in cultured mammalian cells Journal of Biological Chemistry 1991 266 25 16960 16964
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.25 , pp. 16960-16964
    • Wang, R.1    Meschia, J.F.2    Cotter, R.J.3    Sisodia, S.S.4
  • 14
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent -secretase competes with -secretase for cleavage of amyloid- precursor protein in the trans-Golgi network
    • Skovronsky D. M., Moore D. B., Milla M. E., Doms R. W., Lee V. M.-Y., Protein kinase C-dependent -secretase competes with -secretase for cleavage of amyloid- precursor protein in the trans-Golgi network Journal of Biological Chemistry 2000 275 4 2568 2575
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.4 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.-Y.5
  • 16
    • 2542519087 scopus 로고    scopus 로고
    • Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone
    • Caill I., Allinquant B., Dupont E., Bouillot C., Langer A., Mller U., Prochiantz A., Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone Development 2004 131 9 2173 2181
    • (2004) Development , vol.131 , Issue.9 , pp. 2173-2181
    • Caill, I.1    Allinquant, B.2    Dupont, E.3    Bouillot, C.4    Langer, A.5    Mller, U.6    Prochiantz, A.7
  • 18
    • 0024395366 scopus 로고
    • Secreted form of amyloid β protein precursor is involved in the growth regulation of fibroblasts
    • DOI 10.1016/0092-8674(89)90096-2
    • Saitoh T., Sundsmo M., Roch J.-M., Kimura N., Cole G., Schubert D., Oltersdorf T., Schenk D. B., Secreted form of amyloid protein precursor is involved in the growth regulation of fibroblasts Cell 1989 58 4 615 622 (Pubitemid 19210955)
    • (1989) Cell , vol.58 , Issue.4 , pp. 615-622
    • Saitoh, T.1    Sundsmo, M.2    Roch, J.-M.3    Kimura, N.4    Cole, G.5    Schubert, D.6    Oltersdorf, T.7    Schenk, D.B.8
  • 19
    • 0026663993 scopus 로고
    • The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth
    • Milward E. A., Papadopoulos R., Fuller S. J., Moir R. D., Small D., Beyreuther K., Masters C. L., The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth Neuron 1992 9 1 129 137
    • (1992) Neuron , vol.9 , Issue.1 , pp. 129-137
    • Milward, E.A.1    Papadopoulos, R.2    Fuller, S.J.3    Moir, R.D.4    Small, D.5    Beyreuther, K.6    Masters, C.L.7
  • 20
    • 0029841562 scopus 로고    scopus 로고
    • Increased activity-regulating and neuroprotective efficacy of - Secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain
    • Furukawa K., Sopher B. L., Rydel R. E., Begley J. G., Pham D. G., Martin G. M., Fox M., Mattson M. P., Increased activity-regulating and neuroprotective efficacy of -secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain Journal of Neurochemistry 1996 67 5 1882 1896
    • (1996) Journal of Neurochemistry , vol.67 , Issue.5 , pp. 1882-1896
    • Furukawa, K.1    Sopher, B.L.2    Rydel, R.E.3    Begley, J.G.4    Pham, D.G.5    Martin, G.M.6    Fox, M.7    Mattson, M.P.8
  • 21
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the -amyloid precursor protein
    • Mattson M. P., Cheng B., Culwell A. R., Esch F. S., Lieberburg I., Rydel R. E., Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the -amyloid precursor protein Neuron 1993 10 2 243 254
    • (1993) Neuron , vol.10 , Issue.2 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 22
    • 0032533290 scopus 로고    scopus 로고
    • Novel domain-specific actions of amyloid precursor protein on developing synapses
    • Morimoto T., Novel domain-specific actions of amyloid precursor protein on developing synapses Journal of Neuroscience 1998 18 22 9386 9393
    • (1998) Journal of Neuroscience , vol.18 , Issue.22 , pp. 9386-9393
    • Morimoto, T.1
  • 24
    • 33745263255 scopus 로고    scopus 로고
    • Soluble amyloid precursor protein reduces neuronal injury and improves functional outcome following diffuse traumatic brain injury in rats
    • Thornton E., Vink R., Blumbergs P. C., van den Heuvel C., Soluble amyloid precursor protein reduces neuronal injury and improves functional outcome following diffuse traumatic brain injury in rats Brain Research 2006 1094 1 38 46
    • (2006) Brain Research , vol.1094 , Issue.1 , pp. 38-46
    • Thornton, E.1    Vink, R.2    Blumbergs, P.C.3    Van Den Heuvel, C.4
  • 26
    • 34447640166 scopus 로고    scopus 로고
    • The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice
    • Ring S., Weyer S., Kilian S. W., The secreted beta-amyloid precursor protein ectodomain APPs alpha is sufficient to rescue the anatomical, behavioral, and electrophysiological abnormalities of APP-deficient mice Journal of Neuroscience 2007 27 7817 7826
    • (2007) Journal of Neuroscience , vol.27 , pp. 7817-7826
    • Ring, S.1    Weyer, S.2    Kilian, S.W.3
  • 30
    • 0032502033 scopus 로고    scopus 로고
    • Alzheimer's amyloid precursor protein α-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: Similarities to the angiotensin converting enzyme secretase
    • DOI 10.1021/bi972034y
    • Parvathy S., Hussain I., Karran E. H., Turner A. J., Hooper N. M., Alzheimer's amyloid precursor protein -secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: similarities to the angiotensin converting enzyme secretase Biochemistry 1998 37 6 1680 1685 (Pubitemid 28093684)
    • (1998) Biochemistry , vol.37 , Issue.6 , pp. 1680-1685
    • Parvathy, S.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 31
    • 0033049442 scopus 로고    scopus 로고
    • Activity of -secretase as the common final effector of protein kinase C-dependent and -independent modulation of amyloid precursor protein metabolism
    • Racchi M., Solano D. C., Sironi M., Govoni S., Activity of -secretase as the common final effector of protein kinase C-dependent and -independent modulation of amyloid precursor protein metabolism Journal of Neurochemistry 1999 72 6 2464 2470
    • (1999) Journal of Neurochemistry , vol.72 , Issue.6 , pp. 2464-2470
    • Racchi, M.1    Solano, D.C.2    Sironi, M.3    Govoni, S.4
  • 34
    • 63649141727 scopus 로고    scopus 로고
    • The "A Disintegrin and Metalloprotease" (ADAM) family of sheddases: Physiological and cellular functions
    • Reiss K., Saftig P., The "A Disintegrin And Metalloprotease" (ADAM) family of sheddases: physiological and cellular functions Seminars in Cell and Developmental Biology 2009 20 2 126 137
    • (2009) Seminars in Cell and Developmental Biology , vol.20 , Issue.2 , pp. 126-137
    • Reiss, K.1    Saftig, P.2
  • 35
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
    • Anders A., Gilbert S., Garten W., Postina R., Fahrenholz F., Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases The FASEB Journal 2001 15 10 1837 1839
    • (2001) The FASEB Journal , vol.15 , Issue.10 , pp. 1837-1839
    • Anders, A.1    Gilbert, S.2    Garten, W.3    Postina, R.4    Fahrenholz, F.5
  • 36
    • 0035964879 scopus 로고    scopus 로고
    • Activation of ADAM 12 protease by copper
    • Loechel F., Wewer U. M., Activation of ADAM 12 protease by copper FEBS Letters 2001 506 1 65 68
    • (2001) FEBS Letters , vol.506 , Issue.1 , pp. 65-68
    • Loechel, F.1    Wewer, U.M.2
  • 38
    • 0035089318 scopus 로고    scopus 로고
    • Constitutive alpha-secretase cleavage of the beta-amyloid precursor protein in the furin-deficient LoVo cell line: Involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10
    • Lopez-Perez E., Zhang Y., Frank S. J., Creemers J., Seidah N., Checler F., Constitutive alpha-secretase cleavage of the beta-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10 Journal of Neurochemistry 2001 76 1532 1539
    • (2001) Journal of Neurochemistry , vol.76 , pp. 1532-1539
    • Lopez-Perez, E.1    Zhang, Y.2    Frank, S.J.3    Creemers, J.4    Seidah, N.5    Checler, F.6
  • 40
    • 0034074860 scopus 로고    scopus 로고
    • ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the v 3 integrin through an RGD-independent mechanism
    • Cal S., Freije J. M. P., Lpez J. M., Takada Y., Lpez-Otn C., ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the v 3 integrin through an RGD-independent mechanism Molecular Biology of the Cell 2000 11 4 1457 1469
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.4 , pp. 1457-1469
    • Cal, S.1    Freije, J.M.P.2    Lpez, J.M.3    Takada, Y.4    Lpez-Otn, C.5
  • 41
    • 0037189557 scopus 로고    scopus 로고
    • ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin
    • Gaultier A., Cousin H., Darribre T., Alfandari D., ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin Journal of Biological Chemistry 2002 277 26 23336 23344
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23336-23344
    • Gaultier, A.1    Cousin, H.2    Darribre, T.3    Alfandari, D.4
  • 45
    • 0033230156 scopus 로고    scopus 로고
    • Disintegrin-like/cysteine-rich region of ADAM 12 is an active cell adhesion domain
    • Zolkiewska A., Disintegrin-like/cysteine-rich region of ADAM 12 is an active cell adhesion domain Experimental Cell Research 1999 252 2 423 431
    • (1999) Experimental Cell Research , vol.252 , Issue.2 , pp. 423-431
    • Zolkiewska, A.1
  • 47
    • 0024818172 scopus 로고
    • A novel metalloproteinase associated with brain myelin membranes. Isolation and characterization
    • Chantry A., Gregson N. A., Glynn P., A novel metalloproteinase associated with brain myelin membranes. Isolation and characterization Journal of Biological Chemistry 1989 264 36 21603 21607
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.36 , pp. 21603-21607
    • Chantry, A.1    Gregson, N.A.2    Glynn, P.3
  • 48
    • 0026742152 scopus 로고
    • Degradation of myelin basic protein by a membrane-associated metalloprotease: Neural distribution of the enzyme
    • Chantry A., Gregson N., Glynn P., Degradation of myelin basic protein by a membrane-associated metalloprotease: neural distribution of the enzyme Neurochemical Research 1992 17 9 861 868
    • (1992) Neurochemical Research , vol.17 , Issue.9 , pp. 861-868
    • Chantry, A.1    Gregson, N.2    Glynn, P.3
  • 50
  • 51
    • 0031573918 scopus 로고    scopus 로고
    • Assignment of a disintegrin and metalloproteinase domain 10 (Adam10) gene to mouse chromosome 9
    • Yamazaki K., Mizui Y., Sagane K., Tanaka I., Assignment of a disintegrin and metalloproteinase domain 10 (Adam10) gene to mouse chromosome 9 Genomics 1997 46 3 528 529
    • (1997) Genomics , vol.46 , Issue.3 , pp. 528-529
    • Yamazaki, K.1    Mizui, Y.2    Sagane, K.3    Tanaka, I.4
  • 52
    • 0030664460 scopus 로고    scopus 로고
    • Radiation hybrid mapping of human ADAM10 gene to chromosome 15
    • Yamazaki K., Mizui Y., Tanaka I., Radiation hybrid mapping of human ADAM10 gene to chromosome 15 Genomics 1997 45 2 457 459
    • (1997) Genomics , vol.45 , Issue.2 , pp. 457-459
    • Yamazaki, K.1    Mizui, Y.2    Tanaka, I.3
  • 53
    • 24644483112 scopus 로고    scopus 로고
    • Genomic structure and functional characterization of the human ADAM10 promoter
    • Prinzen C., Mller U., Endres K., Fahrenholz F., Postina R., Genomic structure and functional characterization of the human ADAM10 promoter FASEB Journal 2005 19 11 1522 1524
    • (2005) FASEB Journal , vol.19 , Issue.11 , pp. 1522-1524
    • Prinzen, C.1    Mller, U.2    Endres, K.3    Fahrenholz, F.4    Postina, R.5
  • 54
    • 67649359888 scopus 로고    scopus 로고
    • Up-regulation of the -secretase ADAM10 by retinoic acid receptors and acitretin
    • Tippmann F., Hundt J., Schneider A., Endres K., Fahrenholz F., Up-regulation of the -secretase ADAM10 by retinoic acid receptors and acitretin FASEB Journal 2009 23 6 1643 1654
    • (2009) FASEB Journal , vol.23 , Issue.6 , pp. 1643-1654
    • Tippmann, F.1    Hundt, J.2    Schneider, A.3    Endres, K.4    Fahrenholz, F.5
  • 55
    • 77955046461 scopus 로고    scopus 로고
    • SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10
    • Donmez G., Wang D., Cohen D. E., Guarente L., SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10 Cell 2010 142 320 332
    • (2010) Cell , vol.142 , pp. 320-332
    • Donmez, G.1    Wang, D.2    Cohen, D.E.3    Guarente, L.4
  • 68
    • 63649105591 scopus 로고    scopus 로고
    • The good, the bad and the ugly substrates for ADAM10 and ADAM17 in brain pathology, inflammation and cancer
    • Pruessmeyer J., Ludwig A., The good, the bad and the ugly substrates for ADAM10 and ADAM17 in brain pathology, inflammation and cancer Seminars in Cell and Developmental Biology 2009 20 2 164 174
    • (2009) Seminars in Cell and Developmental Biology , vol.20 , Issue.2 , pp. 164-174
    • Pruessmeyer, J.1    Ludwig, A.2
  • 70
    • 0032544723 scopus 로고    scopus 로고
    • Pro-tumor necrosis factor- processing activity is tightly controlled by a component that does not affect Notch processing
    • Merlos-Surez A., Fernndez-Larrea J., Reddy P., Baselga J., Arribas J., Pro-tumor necrosis factor- processing activity is tightly controlled by a component that does not affect Notch processing Journal of Biological Chemistry 1998 273 38 24955 24962
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.38 , pp. 24955-24962
    • Merlos-Surez, A.1    Fernndez-Larrea, J.2    Reddy, P.3    Baselga, J.4    Arribas, J.5
  • 71
    • 18744364692 scopus 로고    scopus 로고
    • Effect of tumor necrosis factor- converting enzyme (TACE) and metalloprotease inhibitor on amyloid precursor protein metabolism in human neurons
    • Blacker M., Noe M. C., Carty T. J., Goodyer C. G., LeBlanc A. C., Effect of tumor necrosis factor- converting enzyme (TACE) and metalloprotease inhibitor on amyloid precursor protein metabolism in human neurons Journal of Neurochemistry 2002 83 6 1349 1357
    • (2002) Journal of Neurochemistry , vol.83 , Issue.6 , pp. 1349-1357
    • Blacker, M.1    Noe, M.C.2    Carty, T.J.3    Goodyer, C.G.4    Leblanc, A.C.5
  • 72
    • 77956392552 scopus 로고    scopus 로고
    • ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons
    • Kuhn P. H., Wang H., Dislich B., ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons EMBO Journal 2010 29 17 3020 3032
    • (2010) EMBO Journal , vol.29 , Issue.17 , pp. 3020-3032
    • Kuhn, P.H.1    Wang, H.2    Dislich, B.3
  • 73
    • 0035424693 scopus 로고    scopus 로고
    • Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor- converting enzyme
    • Slack B. E., Ma L. K., Seah C. C., Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor- converting enzyme Biochemical Journal 2001 357 3 787 794
    • (2001) Biochemical Journal , vol.357 , Issue.3 , pp. 787-794
    • Slack, B.E.1    Ma, L.K.2    Seah, C.C.3
  • 74
    • 34547893833 scopus 로고    scopus 로고
    • Enhancement of -secretase cleavage of amyloid precursor protein by a metalloendopeptidase nardilysin
    • Hiraoka Y., Ohno M., Yoshida K., Okawa K., Tomimoto H., Kita T., Nishi E., Enhancement of -secretase cleavage of amyloid precursor protein by a metalloendopeptidase nardilysin Journal of Neurochemistry 2007 102 5 1595 1605
    • (2007) Journal of Neurochemistry , vol.102 , Issue.5 , pp. 1595-1605
    • Hiraoka, Y.1    Ohno, M.2    Yoshida, K.3    Okawa, K.4    Tomimoto, H.5    Kita, T.6    Nishi, E.7
  • 78
    • 0030049705 scopus 로고    scopus 로고
    • MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains
    • DOI 10.1083/jcb.132.4.717
    • Weskamp G., Krtzschmar J., Reid M. S., Blobel C. P., MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains Journal of Cell Biology 1996 132 4 717 726 (Pubitemid 26069249)
    • (1996) Journal of Cell Biology , vol.132 , Issue.4 , pp. 717-726
    • Weskamp, G.1    Kratzschmar, J.2    Reid, M.S.3    Blobel, C.P.4
  • 82
    • 78449288804 scopus 로고    scopus 로고
    • Promoter polymorphisms which regulate ADAM9 transcription are protective against sporadic Alzheimer's disease
    • In press
    • Cong L., Jia J., Promoter polymorphisms which regulate ADAM9 transcription are protective against sporadic Alzheimer's disease. Neurobiology of Aging. In press
    • Neurobiology of Aging
    • Cong, L.1    Jia, J.2
  • 83
    • 28844433559 scopus 로고    scopus 로고
    • The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity
    • Ciss M. A., Sunyach C., Lefranc-Jullien S., Postina R., Vincent B., Checler F., The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity Journal of Biological Chemistry 2005 280 49 40624 40631
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40624-40631
    • Ciss, M.A.1    Sunyach, C.2    Lefranc-Jullien, S.3    Postina, R.4    Vincent, B.5    Checler, F.6
  • 84
    • 70349295148 scopus 로고    scopus 로고
    • Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein
    • Harris B., Pereira I., Parkin E., Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein Brain Research 2009 1296 203 215
    • (2009) Brain Research , vol.1296 , pp. 203-215
    • Harris, B.1    Pereira, I.2    Parkin, E.3
  • 89
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper N. M., Families of zinc metalloproteases FEBS Letters 1994 354 1 1 6
    • (1994) FEBS Letters , vol.354 , Issue.1 , pp. 1-6
    • Hooper, N.M.1
  • 91
    • 50249143450 scopus 로고    scopus 로고
    • Amyloid -degrading cryptidases: Insulin degrading enzyme, presequence peptidase, and neprilysin
    • Malito E., Hulse R. E., Tang W.-J., Amyloid -degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin Cellular and Molecular Life Sciences 2008 65 16 2574 2585
    • (2008) Cellular and Molecular Life Sciences , vol.65 , Issue.16 , pp. 2574-2585
    • Malito, E.1    Hulse, R.E.2    Tang, W.-J.3
  • 92
    • 70449564488 scopus 로고    scopus 로고
    • Insulin-degrading enzyme: Structure-function relationship and its possible roles in health and disease
    • Fernndez-Gamba A., Leal M. C., Morelli L., Castao E. M., Insulin-degrading enzyme: structure-function relationship and its possible roles in health and disease Current Pharmaceutical Design 2009 15 31 3644 3655
    • (2009) Current Pharmaceutical Design , vol.15 , Issue.31 , pp. 3644-3655
    • Fernndez-Gamba, A.1    Leal, M.C.2    Morelli, L.3    Castao, E.M.4
  • 96
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of -amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring M. A., Farris W., Chang A. Y., Walsh D. M., Wu X., Sun X., Frosch M. P., Selkoe D. J., Enhanced proteolysis of -amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death Neuron 2003 40 6 1087 1093
    • (2003) Neuron , vol.40 , Issue.6 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 98
    • 35848951410 scopus 로고    scopus 로고
    • Insulysin cleaves the APP cytoplasmic fragment at multiple sites
    • Venugopal C., Pappolla M. A., Sambamurti K., Insulysin cleaves the APP cytoplasmic fragment at multiple sites Neurochemical Research 2007 32 12 2225 2234
    • (2007) Neurochemical Research , vol.32 , Issue.12 , pp. 2225-2234
    • Venugopal, C.1    Pappolla, M.A.2    Sambamurti, K.3
  • 99
    • 0033605607 scopus 로고    scopus 로고
    • Insulin-degrading enzyme in the Alzheimer's disease brain: Prominent localization in neurons and senile plaques
    • Bernstein H.-G., Ansorge S., Riederer P., Reiser M., Frlich L., Bogerts B., Insulin-degrading enzyme in the Alzheimer's disease brain: prominent localization in neurons and senile plaques Neuroscience Letters 1999 263 2-3 161 164
    • (1999) Neuroscience Letters , vol.263 , Issue.23 , pp. 161-164
    • Bernstein, H.-G.1    Ansorge, S.2    Riederer, P.3    Reiser, M.4    Frlich, L.5    Bogerts, B.6
  • 100
    • 11244276934 scopus 로고    scopus 로고
    • Insulin-degrading enzyme in brain microvessels: Proteolysis of amyloid vasculotropic variants and reduced activity in cerebral amyloid angiopathy
    • Morelli L., Llovera R. E., Mathov I., Lue L.-F., Frangione B., Ghiso J., Castao E. M., Insulin-degrading enzyme in brain microvessels: proteolysis of amyloid vasculotropic variants and reduced activity in cerebral amyloid angiopathy Journal of Biological Chemistry 2004 279 53 56004 56013
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 56004-56013
    • Morelli, L.1    Llovera, R.E.2    Mathov, I.3    Lue, L.-F.4    Frangione, B.5    Ghiso, J.6    Castao, E.M.7
  • 101
    • 34247100646 scopus 로고    scopus 로고
    • Insulin degrading enzyme activity selectively decreases in the hippocampal formation of cases at high risk to develop Alzheimer's disease
    • Zhao Z., Xiang Z., Haroutunian V., Buxbaum J. D., Stetka B., Pasinetti G. M., Insulin degrading enzyme activity selectively decreases in the hippocampal formation of cases at high risk to develop Alzheimer's disease Neurobiology of Aging 2007 28 6 824 830
    • (2007) Neurobiology of Aging , vol.28 , Issue.6 , pp. 824-830
    • Zhao, Z.1    Xiang, Z.2    Haroutunian, V.3    Buxbaum, J.D.4    Stetka, B.5    Pasinetti, G.M.6
  • 104
    • 0027475050 scopus 로고
    • Neutral endopeptidase 24.11: Structure, inhibition, and experimental and clinical pharmacology
    • Roques B. P., Noble F., Dauge V., Fournie-Zaluski M.-C., Beaumont A., Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology Pharmacological Reviews 1993 45 1 87 146
    • (1993) Pharmacological Reviews , vol.45 , Issue.1 , pp. 87-146
    • Roques, B.P.1    Noble, F.2    Dauge, V.3    Fournie-Zaluski, M.-C.4    Beaumont, A.5
  • 105
    • 0029061685 scopus 로고
    • Neutral endopeptidase can hydrolyze -amyloid(1-40) but shows no effect on -amyloid precursor protein metabolism
    • Howell S., Nalbantoglu J., Crine P., Neutral endopeptidase can hydrolyze -amyloid(1-40) but shows no effect on -amyloid precursor protein metabolism Peptides 1995 16 4 647 652
    • (1995) Peptides , vol.16 , Issue.4 , pp. 647-652
    • Howell, S.1    Nalbantoglu, J.2    Crine, P.3
  • 109
    • 0035369189 scopus 로고    scopus 로고
    • Immunohistochemical localization of neprilysin in the human cerebral cortex: Inverse association with vulnerability to amyloid -protein (A ) deposition
    • Akiyama H., Kondo H., Ikeda K., Kato M., McGeer P. L., Immunohistochemical localization of neprilysin in the human cerebral cortex: inverse association with vulnerability to amyloid -protein (A ) deposition Brain Research 2001 902 2 277 281
    • (2001) Brain Research , vol.902 , Issue.2 , pp. 277-281
    • Akiyama, H.1    Kondo, H.2    Ikeda, K.3    Kato, M.4    McGeer, P.L.5
  • 110
    • 0035846826 scopus 로고    scopus 로고
    • Reduced neprilysin in high plaque areas of Alzheimer brain: A possible relationship to deficient degradation of -amyloid peptide
    • Yasojima K., Akiyama H., McGeer E. G., McGeer P. L., Reduced neprilysin in high plaque areas of Alzheimer brain: a possible relationship to deficient degradation of -amyloid peptide Neuroscience Letters 2001 297 2 97 100
    • (2001) Neuroscience Letters , vol.297 , Issue.2 , pp. 97-100
    • Yasojima, K.1    Akiyama, H.2    McGeer, E.G.3    McGeer, P.L.4
  • 111
    • 37549012213 scopus 로고    scopus 로고
    • Age-dependent decline of neprilysin in Alzheimer's disease and normal brain: Inverse correlation with A levels
    • Hellstrm-Lindahl E., Ravid R., Nordberg A., Age-dependent decline of neprilysin in Alzheimer's disease and normal brain: inverse correlation with A levels Neurobiology of Aging 2008 29 2 210 221
    • (2008) Neurobiology of Aging , vol.29 , Issue.2 , pp. 210-221
    • Hellstrm-Lindahl, E.1    Ravid, R.2    Nordberg, A.3
  • 115
    • 77955659816 scopus 로고    scopus 로고
    • Endothelin-Biology and disease
    • Khimji A. -K., Rockey D. C., Endothelin-Biology and disease Cellular Signalling 2010 22 11 1615 1625
    • (2010) Cellular Signalling , vol.22 , Issue.11 , pp. 1615-1625
    • Khimji, A.-K.1    Rockey, D.C.2
  • 116
    • 0027960431 scopus 로고
    • Molecular characterization of human and bovine endothelin converting enzyme (ECE-1)
    • Schmidt M., Molecular characterization of human and bovine endothelin converting enzyme (ECE-1) FEBS Letters 1994 356 2-3 238 243
    • (1994) FEBS Letters , vol.356 , Issue.23 , pp. 238-243
    • Schmidt, M.1
  • 117
    • 0029585975 scopus 로고
    • Organization of the gene encoding the human endothelin-converting enzyme (ECE-1)
    • Valdenaire O., Rohrbacher E., Mattei M.-G., Organization of the gene encoding the human endothelin-converting enzyme (ECE-1) Journal of Biological Chemistry 1995 270 50 29794 29798
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.50 , pp. 29794-29798
    • Valdenaire, O.1    Rohrbacher, E.2    Mattei, M.-G.3
  • 118
    • 0035816707 scopus 로고    scopus 로고
    • Degradation of the Alzheimer's amyloid peptide by endothelin-converting enzyme
    • Eckman E. A., Reed D. K., Eckman C. B., Degradation of the Alzheimer's amyloid peptide by endothelin-converting enzyme Journal of Biological Chemistry 2001 276 27 24540 24548
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.27 , pp. 24540-24548
    • Eckman, E.A.1    Reed, D.K.2    Eckman, C.B.3
  • 119
    • 0037462769 scopus 로고    scopus 로고
    • Alzheimer's disease -amyloid peptide is increased in mice deficient in endothelin-converting enzyme
    • Eckman E. A., Watson M., Marlow L., Sambamurti K., Eckman C. B., Alzheimer's disease -amyloid peptide is increased in mice deficient in endothelin-converting enzyme Journal of Biological Chemistry 2003 278 4 2081 2084
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2081-2084
    • Eckman, E.A.1    Watson, M.2    Marlow, L.3    Sambamurti, K.4    Eckman, C.B.5
  • 121
    • 77249149910 scopus 로고    scopus 로고
    • Endothelin-converting enzyme-1 promoter polymorphisms and susceptibility to sporadic late-onset Alzheimer's disease in a Chinese population
    • Jin Z., Luxiang C., Huadong Z., Yanjiang W., Zhiqiang X., Hongyuan C., Lihua H., Xu Y., Endothelin-converting enzyme-1 promoter polymorphisms and susceptibility to sporadic late-onset Alzheimer's disease in a Chinese population Disease Markers 2009 27 5 211 215
    • (2009) Disease Markers , vol.27 , Issue.5 , pp. 211-215
    • Jin, Z.1    Luxiang, C.2    Huadong, Z.3    Yanjiang, W.4    Zhiqiang, X.5    Hongyuan, C.6    Lihua, H.7    Xu, Y.8
  • 122
    • 67649984550 scopus 로고    scopus 로고
    • Endothelin-converting enzyme-2 is increased in Alzheimer's disease and up-regulated by A β
    • Palmer J. C., Baig S., Kehoe P. G., Love S., Endothelin-converting enzyme-2 is increased in Alzheimer's disease and up-regulated by A American Journal of Pathology 2009 175 1 262 270
    • (2009) American Journal of Pathology , vol.175 , Issue.1 , pp. 262-270
    • Palmer, J.C.1    Baig, S.2    Kehoe, P.G.3    Love, S.4
  • 125
    • 0014214810 scopus 로고
    • Second kininase in human blood plasma
    • Yang H. Y. T., Erds E. G., Second kininase in human blood plasma Nature 1967 215 5108 1402 1403
    • (1967) Nature , vol.215 , Issue.5108 , pp. 1402-1403
    • Yang, H.Y.T.1    Erds, E.G.2
  • 126
    • 0015051857 scopus 로고
    • Characterization of a dipeptide hydrolase (kininase II: Angiotensin i converting enzyme)
    • Yang H. Y., Erds E. G., Levin Y., Characterization of a dipeptide hydrolase (kininase II: angiotensin I converting enzyme) Journal of Pharmacology and Experimental Therapeutics 1971 177 1 291 300
    • (1971) Journal of Pharmacology and Experimental Therapeutics , vol.177 , Issue.1 , pp. 291-300
    • Yang, H.Y.1    Erds, E.G.2    Levin, Y.3
  • 127
    • 0028863980 scopus 로고
    • Recent advances in knowledge of the structure and function of the angiotensin i converting enzyme
    • Corvol P., Michaud A., Soubrier F., Williams T. A., Recent advances in knowledge of the structure and function of the angiotensin I converting enzyme Journal of Hypertension, Supplement 1995 13 3 S3 S10
    • (1995) Journal of Hypertension, Supplement , vol.13 , Issue.3
    • Corvol, P.1    Michaud, A.2    Soubrier, F.3    Williams, T.A.4
  • 128
    • 0024347759 scopus 로고
    • Angiotensin-converting enzyme: New concepts concerning its biological role
    • Ehlers M. R. W., Riordan J. F., Angiotensin-converting enzyme: new concepts concerning its biological role Biochemistry 1989 28 13 5311 5318
    • (1989) Biochemistry , vol.28 , Issue.13 , pp. 5311-5318
    • Ehlers, M.R.W.1    Riordan, J.F.2
  • 129
    • 0025284828 scopus 로고
    • Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene
    • Howard T. E., Shai S.-Y., Langford K. G., Martin B. M., Bernstein K. E., Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene Molecular and Cellular Biology 1990 10 8 4294 4302
    • (1990) Molecular and Cellular Biology , vol.10 , Issue.8 , pp. 4294-4302
    • Howard, T.E.1    Shai, S.-Y.2    Langford, K.G.3    Martin, B.M.4    Bernstein, K.E.5
  • 130
    • 0035930538 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme degrades Alzheimer amyloid -peptide (A ); Retards A aggregation, deposition, fibril formation; And inhibits cytotoxicity
    • Hu J., Igarashi A., Kamata M., Nakagawa H., Angiotensin-converting enzyme degrades Alzheimer amyloid -peptide (A ); retards A aggregation, deposition, fibril formation; and inhibits cytotoxicity Journal of Biological Chemistry 2001 276 51 47863 47868
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.51 , pp. 47863-47868
    • Hu, J.1    Igarashi, A.2    Kamata, M.3    Nakagawa, H.4
  • 132
    • 34547871652 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme converts amyloid beta-protein 1-42 (Abeta(1-42)) to Abeta(1-40), and its inhibition enhances brain Abeta deposition
    • Zou K., Yamaguchi H., Akatsu H., Angiotensin-converting enzyme converts amyloid beta-protein 1-42 (Abeta(1-42)) to Abeta(1-40), and its inhibition enhances brain Abeta deposition Journal of Neuroscience 2007 27 8628 8635
    • (2007) Journal of Neuroscience , vol.27 , pp. 8628-8635
    • Zou, K.1    Yamaguchi, H.2    Akatsu, H.3
  • 133
    • 77956178798 scopus 로고    scopus 로고
    • Effect of a centrally active angiotensin-converting enzyme inhibitor, perindopril, on cognitive performance in a mouse model of Alzheimer's disease
    • Yamada K., Uchida S., Takahashi S., Takayama M., Nagata Y., Suzuki N., Shirakura S., Kanda T., Effect of a centrally active angiotensin-converting enzyme inhibitor, perindopril, on cognitive performance in a mouse model of Alzheimer's disease Brain Research 2010 1352 176 186
    • (2010) Brain Research , vol.1352 , pp. 176-186
    • Yamada, K.1    Uchida, S.2    Takahashi, S.3    Takayama, M.4    Nagata, Y.5    Suzuki, N.6    Shirakura, S.7    Kanda, T.8
  • 134
    • 33947245344 scopus 로고    scopus 로고
    • Effects of prolonged angiotensin-converting enzyme inhibitor treatment on amyloid -protein metabolism in mouse models of Alzheimer disease
    • Hemming M. L., Selkoe D. J., Farris W., Effects of prolonged angiotensin-converting enzyme inhibitor treatment on amyloid -protein metabolism in mouse models of Alzheimer disease Neurobiology of Disease 2007 26 1 273 281
    • (2007) Neurobiology of Disease , vol.26 , Issue.1 , pp. 273-281
    • Hemming, M.L.1    Selkoe, D.J.2    Farris, W.3
  • 135
    • 70249088004 scopus 로고    scopus 로고
    • Effects of angiotensin II receptor blockers on dementia
    • Mogi M., Horiuchi M., Effects of angiotensin II receptor blockers on dementia Hypertension Research 2009 32 9 738 740
    • (2009) Hypertension Research , vol.32 , Issue.9 , pp. 738-740
    • Mogi, M.1    Horiuchi, M.2
  • 136
    • 58249126857 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their multiple roles in neurodegenerative diseases
    • Rosenberg G. A., Matrix metalloproteinases and their multiple roles in neurodegenerative diseases The Lancet Neurology 2009 8 2 205 216
    • (2009) The Lancet Neurology , vol.8 , Issue.2 , pp. 205-216
    • Rosenberg, G.A.1
  • 139
    • 0032900361 scopus 로고    scopus 로고
    • Activated isoforms of MMP-2 are induced in U87 human glioma cells in response to -amyloid peptide
    • Deb S., Zhang J. W., Gottschall P. E., Activated isoforms of MMP-2 are induced in U87 human glioma cells in response to -amyloid peptide Journal of Neuroscience Research 1999 55 1 44 53
    • (1999) Journal of Neuroscience Research , vol.55 , Issue.1 , pp. 44-53
    • Deb, S.1    Zhang, J.W.2    Gottschall, P.E.3
  • 140
  • 141
    • 0041835847 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and spontaneous hemorrhage in an animal model of cerebral amyloid angiopathy
    • Lee J.-M., Yin K.-J., Hsin I., Chen S., Fryer J. D., Holtzman D. M., Hsu C. Y., Xu J., Matrix metalloproteinase-9 and spontaneous hemorrhage in an animal model of cerebral amyloid angiopathy Annals of Neurology 2003 54 3 379 382
    • (2003) Annals of Neurology , vol.54 , Issue.3 , pp. 379-382
    • Lee, J.-M.1    Yin, K.-J.2    Hsin, I.3    Chen, S.4    Fryer, J.D.5    Holtzman, D.M.6    Hsu, C.Y.7    Xu, J.8


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