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Volumn 395, Issue 1, 2014, Pages 109-118

Amyloid β peptide cleavage by kallikrein 7 attenuates fibril growth and rescues neurons from Aβ-mediated toxicity in vitro

Author keywords

Alzheimer disease; cation ; clearance; protease; substrate

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; INSULINASE; STRATUM CORNEUM CHYMOTRYPTIC ENZYME;

EID: 84890378967     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2013-0230     Document Type: Article
Times cited : (19)

References (52)
  • 1
    • 0034636749 scopus 로고    scopus 로고
    • Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR-1 or protein C
    • Arosio, D., Ayala, Y.M., and Di Cera, E. (2000). Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR-1 or protein C. Biochemistry 39, 8095-8101.
    • (2000) Biochemistry , vol.39 , pp. 8095-8101
    • Arosio, D.1    Ayala, Y.M.2    Di Cera, E.3
  • 2
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by A16-22, a seven-residue fragment of the Alzheimer's -amyloid peptide, and structural characterization by solid state NMR
    • Balbach, J.J., Ishii, Y., Antzutkin, O.N., Leapman, R.D., Rizzo, N.W., Dyda, F., Reed, J., and Tycko, R. (2000). Amyloid fibril formation by A16-22, a seven-residue fragment of the Alzheimer's -amyloid peptide, and structural characterization by solid state NMR. Biochemistry 39, 13748-13759.
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzutkin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5    Dyda, F.6    Reed, J.7    Tycko, R.8
  • 3
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Ab oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova, I., Karran, E., and De Strooper, B. (2012). The toxic Ab oligomer and Alzheimer's disease: An emperor in need of clothes. Nat. Neurosci. 15, 349-357.
    • (2012) Nat. Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 5
    • 33646726556 scopus 로고    scopus 로고
    • Protease specificity determination by using cellular libraries of peptide substrates (CLiPS
    • Boulware, K.T. and Daugherty, P.S. (2006). Protease specificity determination by using cellular libraries of peptide substrates (CLiPS). Proc. Natl. Acad. Sci. USA 103, 7583-7588.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7583-7588
    • Boulware, K.T.1    Daugherty, P.S.2
  • 6
    • 77953570947 scopus 로고    scopus 로고
    • Evolutionary optimization of peptide substrates for proteases that exhibit rapid hydrolysis kinetics
    • Boulware, K.T., Jabaiah, A., and Daugherty, P.S. (2010). Evolutionary optimization of peptide substrates for proteases that exhibit rapid hydrolysis kinetics. Biotechnol. Bioeng. 106, 339-346.
    • (2010) Biotechnol. Bioeng , vol.106 , pp. 339-346
    • Boulware, K.T.1    Jabaiah, A.2    Daugherty, P.S.3
  • 7
    • 2442428082 scopus 로고    scopus 로고
    • Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7
    • Caubet, C., Jonca, N., Brattsand, M., Guerrin, M., Bernard, D., Schmidt, R., Egelrud, T., Simon, M., and Serre, G. (2004). Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7. J. Invest. Dermatol. 122, 1235-1244.
    • (2004) J. Invest. Dermatol , vol.122 , pp. 1235-1244
    • Caubet, C.1    Jonca, N.2    Brattsand, M.3    Guerrin, M.4    Bernard, D.5    Schmidt, R.6    Egelrud, T.7    Simon, M.8    Serre, G.9
  • 10
    • 1242269946 scopus 로고    scopus 로고
    • Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia
    • Diamandis, E.P., Scorilas, A., Kishi, T., Blennow, K., Luo, L.-Y., Soosaipillai, A., Rademaker, A.W., and Sjogren, M. (2004). Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia. Clin. Biochem. 37, 230-237.
    • (2004) Clin. Biochem , vol.37 , pp. 230-237
    • Diamandis, E.P.1    Scorilas, A.2    Kishi, T.3    Blennow, K.4    Luo, L.-Y.5    Soosaipillai, A.6    Rademaker, A.W.7    Sjogren, M.8
  • 11
    • 77950818717 scopus 로고    scopus 로고
    • Kallikrein-related peptidase 7 promotes multicellular aggregation via the 51 integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma
    • Dong, Y., Tan, O.L., Loessner, D., Stephens, C., Walpole, C., Boyle, G.M., Parsons, P.G., and Clements, J.A. (2010). Kallikrein-related peptidase 7 promotes multicellular aggregation via the 51 integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma. Cancer Res. 70, 2624-2633.
    • (2010) Cancer Res , vol.70 , pp. 2624-2633
    • Dong, Y.1    Tan, O.L.2    Loessner, D.3    Stephens, C.4    Walpole, C.5    Boyle, G.M.6    Parsons, P.G.7    Clements, J.A.8
  • 12
    • 0037462769 scopus 로고    scopus 로고
    • Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme
    • Eckman, E.A., Watson, M., Marlow, L., Sambamurti, K., and Eckman, C.B. (2003). Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. J. Biol. Chem. 278, 2081-2084.
    • (2003) J. Biol. Chem , vol.278 , pp. 2081-2084
    • Eckman, E.A.1    Watson, M.2    Marlow, L.3    Sambamurti, K.4    Eckman, C.B.5
  • 16
    • 0033578302 scopus 로고    scopus 로고
    • Cation-interactions in structural biology
    • Gallivan, J.P. and Dougherty, D.A. (1999). Cation-interactions in structural biology. Proc. Natl. Acad. Sci. 96, 9459-9464.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 9459-9464
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 17
    • 0027956112 scopus 로고
    • Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase
    • Hansson, L., Stromqvist, M., Backman, A., Wallbrandt, P., Carlstein, A., and Egelrud, T. (1994). Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase. J. Biol. Chem. 269, 19420-19426.
    • (1994) J. Biol. Chem , vol.269 , pp. 19420-19426
    • Hansson, L.1    Stromqvist, M.2    Backman, A.3    Wallbrandt, P.4    Carlstein, A.5    Egelrud, T.6
  • 19
    • 34548182582 scopus 로고    scopus 로고
    • Structural model of human PSA: A target for prostate cancer therapy
    • Hassan, M.I., Kumar, V., Singh, T.P., and Yadav, S. (2007). Structural model of human PSA: A target for prostate cancer therapy. Chem. Biol. Drug Des. 70, 261-267.
    • (2007) Chem. Biol. Drug des , vol.70 , pp. 261-267
    • Hassan, M.I.1    Kumar, V.2    Singh, T.P.3    Yadav, S.4
  • 22
    • 79953064715 scopus 로고    scopus 로고
    • Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines
    • Jabaiah, A. and Daugherty, P.S. (2011). Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines. Chem. Biol. 18, 392-401.
    • (2011) Chem. Biol , vol.18 , pp. 392-401
    • Jabaiah, A.1    Daugherty, P.S.2
  • 23
    • 79955662958 scopus 로고    scopus 로고
    • Amyloid clearance as a treatment target against Alzheimer's disease
    • Kurz, A. and Perneczky, R. (2011). Amyloid clearance as a treatment target against Alzheimer's disease. J. Alzheimer's Dis. 24, 61-73.
    • (2011) J. Alzheimer's Dis , vol.24 , pp. 61-73
    • Kurz, A.1    Perneczky, R.2
  • 25
    • 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., and Selkoe, D.J. (2003). Enhanced proteolysis of -amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40, 1087-1093.
    • (2003) Neuron , vol.40 , 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
  • 26
    • 0029962944 scopus 로고    scopus 로고
    • Conservation and variability in the structures of serine proteinases of the chymotrypsin family
    • Lesk, A.M. and Fordham, W.D. (1996). Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J. Mol. Biol. 258, 501-537.
    • (1996) J. Mol. Biol , vol.258 , pp. 501-537
    • Lesk, A.M.1    Fordham, W.D.2
  • 28
    • 34948887671 scopus 로고    scopus 로고
    • A human-specific mutation leads to the origin of a novel splice form of neuropsin (KLK8), a gene involved in learning and memory
    • Lu, Z., Peng, J., and Su, B. (2007). A human-specific mutation leads to the origin of a novel splice form of neuropsin (KLK8), a gene involved in learning and memory. Hum. Mutat. 28, 978-984.
    • (2007) Hum. Mutat , vol.28 , pp. 978-984
    • Lu, Z.1    Peng, J.2    Su, B.3
  • 29
    • 50249143450 scopus 로고    scopus 로고
    • Amyloid -degrading cryptidases: Insulin degrading enzyme, presequence peptidase, and neprilysin
    • Malito, E., Hulse, R.E., and Tang, W.-J. (2008). Amyloid -degrading cryptidases: Insulin degrading enzyme, presequence peptidase, and neprilysin. Cell. Mol. Life Sci. 65, 2574-2585.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 2574-2585
    • Malito, E.1    Hulse, R.E.2    Tang, W.-J.3
  • 33
    • 0028301445 scopus 로고
    • Amino/aromatic interactions in proteins: Is the evidence stacked against hydrogen bonding
    • Mitchell, J.B.O., Nandi, C.L., McDonald, I.K., Thornton, J.M., and Price, S.L. (1994). Amino/aromatic interactions in proteins: Is the evidence stacked against hydrogen bonding J. Mol. Biol. 239, 315-331.
    • (1994) J. Mol. Biol , vol.239 , pp. 315-331
    • Mitchell, J.B.O.1    Nandi, C.L.2    McDonald, I.K.3    Thornton, J.M.4    Price, S.L.5
  • 34
    • 0037931536 scopus 로고    scopus 로고
    • Differential degradation of amyloid genetic variants associated with hereditary dementia or stroke by insulin-degrading enzyme
    • Morelli, L., Llovera, R., Gonzalez, S.A., Affranchino, J.L., Prelli, F., Frangione, B., Ghiso, J., and Castano, E.M. (2003). Differential degradation of amyloid genetic variants associated with hereditary dementia or stroke by insulin-degrading enzyme. J. Biol. Chem. 278, 23221-23226.
    • (2003) J. Biol. Chem , vol.278 , pp. 23221-23226
    • Morelli, L.1    Llovera, R.2    Gonzalez, S.A.3    Affranchino, J.L.4    Prelli, F.5    Frangione, B.6    Ghiso, J.7    Castano, E.M.8
  • 35
    • 84655160768 scopus 로고    scopus 로고
    • Are amyloid-degrading enzymes viable therapeutic targets in Alzheimer's disease
    • Nalivaeva, N.N., Beckett, C., Belyaev, N.D., and Turner, A.J. (2012). Are amyloid-degrading enzymes viable therapeutic targets in Alzheimer's disease J. Neurochem. 120, 167-185.
    • (2012) J. Neurochem , vol.120 , pp. 167-185
    • Nalivaeva, N.N.1    Beckett, C.2    Belyaev, N.D.3    Turner, A.J.4
  • 36
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen, A.W. and Daugherty, P.S. (2005). Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 23, 355-360.
    • (2005) Nat. Biotechnol , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 37
    • 77950924188 scopus 로고    scopus 로고
    • Mechanisms of enzymatic degradation of amyloid microfibrils generating nanofilaments and nanospheres related to cytotoxicity
    • Numata, K. and Kaplan, D.L. (2010). Mechanisms of enzymatic degradation of amyloid microfibrils generating nanofilaments and nanospheres related to cytotoxicity. Biochemistry 49, 3254-3260.
    • (2010) Biochemistry , vol.49 , pp. 3254-3260
    • Numata, K.1    Kaplan, D.L.2
  • 38
    • 46249126804 scopus 로고    scopus 로고
    • Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression
    • Psyrri, A., Kountourakis, P., Scorilas, A., Markakis, S., Camp, R., Kowalski, D., Diamandis, E.P., and Dimopoulos, M.A. (2008). Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression. Ann. Oncol. 19, 1271-1277.
    • (2008) Ann. Oncol , vol.19 , pp. 1271-1277
    • Psyrri, A.1    Kountourakis, P.2    Scorilas, A.3    Markakis, S.4    Camp, R.5    Kowalski, D.6    Diamandis, E.P.7    Dimopoulos, M.A.8
  • 39
    • 41149167016 scopus 로고    scopus 로고
    • The extracellular matrix protein fibronectin is a substrate for kallikrein 7
    • Ramani, V.C. and Haun, R.S. (2008). The extracellular matrix protein fibronectin is a substrate for kallikrein 7. Biochem. Biophys. Res. Commun. 369, 1169-1173.
    • (2008) Biochem. Biophys. Res. Commun , vol.369 , pp. 1169-1173
    • Ramani, V.C.1    Haun, R.S.2
  • 40
    • 79959335983 scopus 로고    scopus 로고
    • Proteolytic action of kallikrein-related peptidase 7 produces unique active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains
    • Ramani, V.C., Kaushal, G.P., and Haun, R.S. (2011). Proteolytic action of kallikrein-related peptidase 7 produces unique active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains. Biochim. Biophys. Acta Mol. Cell Res. 1813, 1525-1531.
    • (2011) Biochim. Biophys. Acta Mol. Cell Res , vol.1813 , pp. 1525-1531
    • Ramani, V.C.1    Kaushal, G.P.2    Haun, R.S.3
  • 41
    • 79957996565 scopus 로고    scopus 로고
    • Amyloid -mediated cell death of cultured hippocampal neurons reveals extensive tau fragmentation without increased full-length tau phosphorylation
    • Reifert, J., Hartung-Cranston, D., and Feinstein, S.C. (2011). Amyloid -mediated cell death of cultured hippocampal neurons reveals extensive tau fragmentation without increased full-length tau phosphorylation. J. Biol. Chem. 286, 20797-20811.
    • (2011) J. Biol. Chem , vol.286 , pp. 20797-20811
    • Reifert, J.1    Hartung-Cranston, D.2    Feinstein, S.C.3
  • 42
    • 0021125414 scopus 로고
    • Synaptic release of excitatory amino acid neurotransmitter mediates anoxic neuronal death
    • Rothman, S. (1984). Synaptic release of excitatory amino acid neurotransmitter mediates anoxic neuronal death. J. Neurosci. 4, 1884-1891.
    • (1984) J. Neurosci , vol.4 , pp. 1884-1891
    • Rothman, S.1
  • 44
    • 34547634419 scopus 로고    scopus 로고
    • Distribution of 15 human kallikreins in tissues and biological fluids
    • Shaw, J.L.V. and Diamandis, E.P. (2007). Distribution of 15 human kallikreins in tissues and biological fluids. Clin. Chem. 53, 1423-1432.
    • (2007) Clin. Chem , vol.53 , pp. 1423-1432
    • Shaw, J.L.V.1    Diamandis, E.P.2
  • 45
    • 0029058938 scopus 로고
    • Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme
    • Skytt, A., Stromqvist, M., and Egelrud, T. (1995). Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme. Biochem. Biophys. Res. Commun. 211, 586-589.
    • (1995) Biochem. Biophys. Res. Commun , vol.211 , pp. 586-589
    • Skytt, A.1    Stromqvist, M.2    Egelrud, T.3
  • 46
    • 57449117668 scopus 로고    scopus 로고
    • Long-term neprilysin gene transfer is associated with reduced levels of intracellular Ab and behavioral improvement in APP transgenic mice
    • Spencer, B., Marr, R.A., Rockenstein, E., Crews, L., Adame, A., Potkar, R., Patrick, C., Gage, F.H., Verma, I.M., and Masliah, E. (2008). Long-term neprilysin gene transfer is associated with reduced levels of intracellular Ab and behavioral improvement in APP transgenic mice. BMC Neurosci. 9, 109.
    • (2008) BMC Neurosci , vol.9 , pp. 109
    • Spencer, B.1    Marr, R.A.2    Rockenstein, E.3    Crews, L.4    Adame, A.5    Potkar, R.6    Patrick, C.7    Gage, F.H.8    Verma, I.M.9    Masliah, E.10
  • 50
    • 0036669881 scopus 로고    scopus 로고
    • Amyloid-beta oligomers: Their production, toxicity and therapeutic inhibition
    • Walsh, D., Klyubin, I., Fadeeva, J., Rowan, M., and Selkoe, D. (2002). Amyloid-beta oligomers: Their production, toxicity and therapeutic inhibition. Biochem. Soc. Trans. 30, 552-557.
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 552-557
    • Walsh, D.1    Klyubin, I.2    Fadeeva, J.3    Rowan, M.4    Selkoe, D.5
  • 51
    • 84876919211 scopus 로고    scopus 로고
    • Engineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial libraries
    • Yi, L., Gebhard, M.C., Li, Q., Taft, J.M., Georgiou, G., and Iverson, B.L. (2013). Engineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial libraries. Proc. Natl. Acad. Sci. USA 110, 7229-7234.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 7229-7234
    • Yi, L.1    Gebhard, M.C.2    Li, Q.3    Taft, J.M.4    Georgiou, G.5    Iverson, B.L.6
  • 52
    • 33751112725 scopus 로고    scopus 로고
    • Matrix metalloproteinases expressed by astrocytes mediate extracellular amyloid-peptide catabolism
    • Yin, K.J., Cirrito, J.R., Yan, P., Hu, X., Xiao, Q., Pan, X., Bateman, R., Song, H., Hsu, F.F., and Turk, J. (2006). Matrix metalloproteinases expressed by astrocytes mediate extracellular amyloid-peptide catabolism. J. Neurosci. 26, 10939-10948.
    • (2006) J. Neurosci , vol.26 , pp. 10939-10948
    • Yin, K.J.1    Cirrito, J.R.2    Yan, P.3    Hu, X.4    Xiao, Q.5    Pan, X.6    Bateman, R.7    Song, H.8    Hsu, F.F.9    Turk, J.10


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