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Volumn 364, Issue 1, 2007, Pages 19-29

Identification of inhibitors using a cell-based assay for monitoring Golgi-resident protease activity

Author keywords

Alkaline phosphatase; Alzheimer's; BACE; Furin; NSAIDs; Prohormone convertase; SEAP; TGN

Indexed keywords

DIAGNOSIS; DRUG PRODUCTS; MAMMALS; MUTAGENS; NEURODEGENERATIVE DISEASES;

EID: 33947695615     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.01.013     Document Type: Article
Times cited : (33)

References (53)
  • 1
    • 0029927422 scopus 로고    scopus 로고
    • The role of proteases during apoptosis
    • Patel T., Gores G.J., and Kaufmann S.H. The role of proteases during apoptosis. FASEB J. 10 (1996) 587-597
    • (1996) FASEB J. , vol.10 , pp. 587-597
    • Patel, T.1    Gores, G.J.2    Kaufmann, S.H.3
  • 2
    • 0344389027 scopus 로고    scopus 로고
    • Caspases: The proteases of the apoptotic pathway
    • Nunez G., Benedict M.A., Hu Y., and Inohara N. Caspases: The proteases of the apoptotic pathway. Oncogene 17 (1998) 3237-3245
    • (1998) Oncogene , vol.17 , pp. 3237-3245
    • Nunez, G.1    Benedict, M.A.2    Hu, Y.3    Inohara, N.4
  • 3
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • Gordon V.M., Klimpel K.R., Arora N., Henderson M.A., and Leppla S.H. Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect. Immunol. 63 (1995) 82-87
    • (1995) Infect. Immunol. , vol.63 , pp. 82-87
    • Gordon, V.M.1    Klimpel, K.R.2    Arora, N.3    Henderson, M.A.4    Leppla, S.H.5
  • 4
    • 0038461962 scopus 로고    scopus 로고
    • Curbing activation: Proprotein convertases in homeostasis and pathology
    • Taylor N.A., Van de Ven W.J., and Creemers J.W. Curbing activation: Proprotein convertases in homeostasis and pathology. FASEB J. 17 (2003) 1215-1227
    • (2003) FASEB J. , vol.17 , pp. 1215-1227
    • Taylor, N.A.1    Van de Ven, W.J.2    Creemers, J.W.3
  • 5
    • 0038056180 scopus 로고    scopus 로고
    • Proteases in blood clotting
    • Walsh P.N., and Ahmad S.S. Proteases in blood clotting. Essays Biochem. 38 (2002) 95-111
    • (2002) Essays Biochem. , vol.38 , pp. 95-111
    • Walsh, P.N.1    Ahmad, S.S.2
  • 6
    • 0005292810 scopus 로고
    • Role of proteolytic enzymes in biological regulation (a review)
    • Neurath H., and Walsh K.A. Role of proteolytic enzymes in biological regulation (a review). Proc. Natl. Acad. Sci. USA 73 (1976) 3825-3832
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3825-3832
    • Neurath, H.1    Walsh, K.A.2
  • 7
    • 33645299092 scopus 로고    scopus 로고
    • Caspases at the crossroads of immune-cell life and death
    • Siegel R.M. Caspases at the crossroads of immune-cell life and death. Nat. Rev. Immunol. 6 (2006) 308-317
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 308-317
    • Siegel, R.M.1
  • 8
    • 0021272399 scopus 로고
    • Golgi/Granule processing of peptide hormone and neuropeptide precursors: A minireview
    • Steiner D.F., Docherty K., and Carroll R. Golgi/Granule processing of peptide hormone and neuropeptide precursors: A minireview. J. Cell. Biochem. 24 (1984) 121-130
    • (1984) J. Cell. Biochem. , vol.24 , pp. 121-130
    • Steiner, D.F.1    Docherty, K.2    Carroll, R.3
  • 9
    • 0023636948 scopus 로고
    • Proteolytic enzymes in the post-translational processing of polypeptide hormone precursors
    • Gluschankof P., and Cohen P. Proteolytic enzymes in the post-translational processing of polypeptide hormone precursors. Neurochem. Res. 12 (1987) 951-958
    • (1987) Neurochem. Res. , vol.12 , pp. 951-958
    • Gluschankof, P.1    Cohen, P.2
  • 10
    • 0033059994 scopus 로고    scopus 로고
    • Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis
    • Molloy S.S., Anderson E.D., Jean F., and Thomas G. Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis. Trends Cell. Biol. 9 (1999) 28-35
    • (1999) Trends Cell. Biol. , vol.9 , pp. 28-35
    • Molloy, S.S.1    Anderson, E.D.2    Jean, F.3    Thomas, G.4
  • 11
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban P.A., and Irminger J.C. Sorting and processing of secretory proteins. Biochem. J. 299 (1994) 1-18
    • (1994) Biochem. J. , vol.299 , pp. 1-18
    • Halban, P.A.1    Irminger, J.C.2
  • 12
    • 0035200832 scopus 로고    scopus 로고
    • Carboxypeptidases from A to Z: Implications in embryonic development and Wnt binding
    • Reznik S.E., and Fricker L.D. Carboxypeptidases from A to Z: Implications in embryonic development and Wnt binding. Cell. Mol. Life Sci. 58 (2001) 1790-1804
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1790-1804
    • Reznik, S.E.1    Fricker, L.D.2
  • 13
    • 0037038816 scopus 로고    scopus 로고
    • β-Secretase (BACE) as a drug target for Alzheimer's disease
    • Vassar R. β-Secretase (BACE) as a drug target for Alzheimer's disease. Adv. Drug Deliv. Rev. 54 (2002) 1589-1602
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 1589-1602
    • Vassar, R.1
  • 14
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • Nakayama K. Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327 (1997) 625-635
    • (1997) Biochem. J. , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 16
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas G. Furin at the cutting edge: From protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell. Biol. 3 (2002) 753-766
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 753-766
    • Thomas, G.1
  • 17
    • 27644521904 scopus 로고    scopus 로고
    • Proprotein convertases: "Master switches" in the regulation of tumor growth and progression
    • Bassi D.E., Fu J., Lopez de Cicco R., and Klein-Szanto A.J. Proprotein convertases: "Master switches" in the regulation of tumor growth and progression. Mol. Carcinog. 44 (2005) 151-161
    • (2005) Mol. Carcinog. , vol.44 , pp. 151-161
    • Bassi, D.E.1    Fu, J.2    Lopez de Cicco, R.3    Klein-Szanto, A.J.4
  • 18
    • 0035253151 scopus 로고    scopus 로고
    • Implication of the proprotein convertases furin, PC5, and PC7 in the cleavage of surface glycoproteins of Hong Kong, ebola, and respiratory syncytial viruses: A comparative analysis with fluorogenic peptides
    • Basak A., Zhong M., Munzer J.S., Chretien M., and Seidah N.G. Implication of the proprotein convertases furin, PC5, and PC7 in the cleavage of surface glycoproteins of Hong Kong, ebola, and respiratory syncytial viruses: A comparative analysis with fluorogenic peptides. Biochem. J. 353 (2001) 537-545
    • (2001) Biochem. J. , vol.353 , pp. 537-545
    • Basak, A.1    Zhong, M.2    Munzer, J.S.3    Chretien, M.4    Seidah, N.G.5
  • 19
    • 0034634728 scopus 로고    scopus 로고
    • Maturation of HIV envelope glycoprotein precursors by cellular endoproteases
    • Moulard M., and Decroly E. Maturation of HIV envelope glycoprotein precursors by cellular endoproteases. Biochim. Biophys. Acta 1469 (2000) 121-132
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 121-132
    • Moulard, M.1    Decroly, E.2
  • 21
    • 0036828769 scopus 로고    scopus 로고
    • Alzheimer's disease: Treatments in discovery and development
    • Citron M. Alzheimer's disease: Treatments in discovery and development. Nat. Neurosci. 5 Suppl. (2002) 1055-1057
    • (2002) Nat. Neurosci. , vol.5 , Issue.SUPPL , pp. 1055-1057
    • Citron, M.1
  • 22
    • 0034662929 scopus 로고    scopus 로고
    • BACE2, a β-secretase homolog, cleaves at the β site and within the amyloid- β region of the amyloid-β precursor protein
    • Farzan M., Schnitzler C.E., Vasilieva N., Leung D., and Choe H. BACE2, a β-secretase homolog, cleaves at the β site and within the amyloid- β region of the amyloid-β precursor protein. Proc. Natl. Acad. Sci. USA 97 (2000) 9712-9717
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9712-9717
    • Farzan, M.1    Schnitzler, C.E.2    Vasilieva, N.3    Leung, D.4    Choe, H.5
  • 26
    • 33947640887 scopus 로고
    • Quantitative detection of specific gene regulation with the Great EscAPe secreted alkaline phosphatase (SEAP) genetic reporter system
    • Yang T., Kondepudi A., Adams M., Kitts P., and Kain S. Quantitative detection of specific gene regulation with the Great EscAPe secreted alkaline phosphatase (SEAP) genetic reporter system. CLONTECHniques 9 (1994) 1-4
    • (1994) CLONTECHniques , vol.9 , pp. 1-4
    • Yang, T.1    Kondepudi, A.2    Adams, M.3    Kitts, P.4    Kain, S.5
  • 27
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang J.H., Chung T.D., and Oldenburg K.R. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 4 (1999) 67-73
    • (1999) J. Biomol. Screen. , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 28
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei D., and Weiss S.J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375 (1995) 244-247
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 30
    • 0033585434 scopus 로고    scopus 로고
    • Toward an enzyme/prodrug strategy for cancer gene therapy: Endogenous activation of carboxypeptidase A mutants by the PACE/furin family of propeptidases
    • Hamstra D.A., and Rehemtulla A. Toward an enzyme/prodrug strategy for cancer gene therapy: Endogenous activation of carboxypeptidase A mutants by the PACE/furin family of propeptidases. Hum. Gene Ther. 10 (1999) 235-248
    • (1999) Hum. Gene Ther. , vol.10 , pp. 235-248
    • Hamstra, D.A.1    Rehemtulla, A.2
  • 31
    • 0026720791 scopus 로고
    • Preferred sequence requirements for cleavage of pro-von Willebrand factor by propeptide-processing enzymes
    • Rehemtulla A., and Kaufman R.J. Preferred sequence requirements for cleavage of pro-von Willebrand factor by propeptide-processing enzymes. Blood 79 (1992) 2349-2355
    • (1992) Blood , vol.79 , pp. 2349-2355
    • Rehemtulla, A.1    Kaufman, R.J.2
  • 32
    • 0029917887 scopus 로고    scopus 로고
    • Anti-inflammatory drugs in the fight against Alzheimer's disease
    • McGeer P.L., and McGeer E.G. Anti-inflammatory drugs in the fight against Alzheimer's disease. Ann. N.Y. Acad. Sci. 777 (1996) 213-220
    • (1996) Ann. N.Y. Acad. Sci. , vol.777 , pp. 213-220
    • McGeer, P.L.1    McGeer, E.G.2
  • 33
    • 0030897133 scopus 로고    scopus 로고
    • Risk of Alzheimer's disease and duration of NSAID use
    • Stewart W.F., Kawas C., Corrada M., and Metter E.J. Risk of Alzheimer's disease and duration of NSAID use. Neurology 48 (1997) 626-632
    • (1997) Neurology , vol.48 , pp. 626-632
    • Stewart, W.F.1    Kawas, C.2    Corrada, M.3    Metter, E.J.4
  • 34
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions
    • Seidah N.G., Chretien M., and Day R. The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions. Biochimie 76 (1994) 197-209
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 35
    • 0030807070 scopus 로고    scopus 로고
    • A role for PACE4 in the proteolytic activation of anthrax toxin protective antigen
    • Gordon V.M., Rehemtulla A., and Leppla S.H. A role for PACE4 in the proteolytic activation of anthrax toxin protective antigen. Infect. Immunol. 65 (1997) 3370-3375
    • (1997) Infect. Immunol. , vol.65 , pp. 3370-3375
    • Gordon, V.M.1    Rehemtulla, A.2    Leppla, S.H.3
  • 36
    • 0029916795 scopus 로고    scopus 로고
    • cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases
    • Seidah N.G., Hamelin J., Mamarbachi M., Dong W., Tardos H., Mbikay M., Chretien M., and Day R. cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases. Proc. Natl. Acad. Sci. USA 93 (1996) 3388-3393
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3388-3393
    • Seidah, N.G.1    Hamelin, J.2    Mamarbachi, M.3    Dong, W.4    Tardos, H.5    Mbikay, M.6    Chretien, M.7    Day, R.8
  • 40
    • 0028801453 scopus 로고
    • Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediated by the human endoprotease furin
    • Vey M., Schafer W., Reis B., Ohuchi R., Britt W., Garten W., Klenk H.D., and Radsak K. Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediated by the human endoprotease furin. Virology 206 (1995) 746-749
    • (1995) Virology , vol.206 , pp. 746-749
    • Vey, M.1    Schafer, W.2    Reis, B.3    Ohuchi, R.4    Britt, W.5    Garten, W.6    Klenk, H.D.7    Radsak, K.8
  • 41
    • 4344670926 scopus 로고    scopus 로고
    • Furin inhibition by compounds of copper and zinc
    • Podsiadlo P., Komiyama T., Fuller R.S., and Blum O. Furin inhibition by compounds of copper and zinc. J. Biol. Chem. 279 (2004) 36219-36227
    • (2004) J. Biol. Chem. , vol.279 , pp. 36219-36227
    • Podsiadlo, P.1    Komiyama, T.2    Fuller, R.S.3    Blum, O.4
  • 43
    • 0036861132 scopus 로고    scopus 로고
    • Emerging Alzheimer's disease therapies: Inhibition of β-secretase
    • Citron M. Emerging Alzheimer's disease therapies: Inhibition of β-secretase. Neurobiol. Aging 23 (2002) 1017-1022
    • (2002) Neurobiol. Aging , vol.23 , pp. 1017-1022
    • Citron, M.1
  • 44
    • 0037010298 scopus 로고    scopus 로고
    • β-Secretase as a target for the treatment of Alzheimer's disease
    • Citron M. β-Secretase as a target for the treatment of Alzheimer's disease. J. Neurosci. Res. 70 (2002) 373-379
    • (2002) J. Neurosci. Res. , vol.70 , pp. 373-379
    • Citron, M.1
  • 45
    • 0031003233 scopus 로고    scopus 로고
    • The Alzheimer family of diseases: Many etiologies, one pathogenesis?
    • Hardy J. The Alzheimer family of diseases: Many etiologies, one pathogenesis?. Proc. Natl. Acad. Sci. USA 94 (1997) 2095-2097
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2095-2097
    • Hardy, J.1
  • 46
    • 33846059508 scopus 로고    scopus 로고
    • NSAIDs and Alzheimer disease: Epidemiological, animal model, and clinical studies
    • McGeer P.L., and McGeer E.G. NSAIDs and Alzheimer disease: Epidemiological, animal model, and clinical studies. Neurobiol. Aging (2006)
    • (2006) Neurobiol. Aging
    • McGeer, P.L.1    McGeer, E.G.2
  • 47
    • 0035369189 scopus 로고    scopus 로고
    • Immunohistochemical localization of neprilysin in the human cerebral cortex: Inverse association with vulnerability to amyloid-β protein (Aβ) deposition
    • Akiyama H., Kondo H., Ikeda K., Kato M., and McGeer P.L. Immunohistochemical localization of neprilysin in the human cerebral cortex: Inverse association with vulnerability to amyloid-β protein (Aβ) deposition. Brain Res. 902 (2001) 277-281
    • (2001) Brain Res. , vol.902 , pp. 277-281
    • Akiyama, H.1    Kondo, H.2    Ikeda, K.3    Kato, M.4    McGeer, P.L.5
  • 48
    • 0031900411 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drug use and Alzheimer-type pathology in aging
    • Mackenzie I.R., and Munoz D.G. Nonsteroidal anti-inflammatory drug use and Alzheimer-type pathology in aging. Neurology 50 (1998) 986-990
    • (1998) Neurology , vol.50 , pp. 986-990
    • Mackenzie, I.R.1    Munoz, D.G.2
  • 51
    • 0042090064 scopus 로고    scopus 로고
    • Early neuropathological Alzheimer's changes in aged individuals are accompanied by decreased cerebrospinal fluid melatonin levels
    • Zhou J.N., Liu R.Y., Kamphorst W., Hofman M.A., and Swaab D.F. Early neuropathological Alzheimer's changes in aged individuals are accompanied by decreased cerebrospinal fluid melatonin levels. J. Pineal Res. 35 (2003) 125-130
    • (2003) J. Pineal Res. , vol.35 , pp. 125-130
    • Zhou, J.N.1    Liu, R.Y.2    Kamphorst, W.3    Hofman, M.A.4    Swaab, D.F.5
  • 52
    • 0034666289 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-( ligands reduce neuronal inducible nitric oxide synthase expression and cell death in vivo
    • Heneka M.T., Klockgether T., and Feinstein D.L. Peroxisome proliferator-activated receptor-( ligands reduce neuronal inducible nitric oxide synthase expression and cell death in vivo. J. Neurosci. 20 (2000) 6862-6867
    • (2000) J. Neurosci. , vol.20 , pp. 6862-6867
    • Heneka, M.T.1    Klockgether, T.2    Feinstein, D.L.3


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