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Volumn 8, Issue 9, 2017, Pages 14502-14515

KLK6 proteolysis is implicated in the turnover and uptake of extracellular alpha-synuclein species

Author keywords

Degradomics; In vitro substrates; KLK6; Metalloproteases; synuclein

Indexed keywords

ADAMTS PROTEIN; ADAMTS19 PROTEIN; ADENOVIRUS VECTOR; ALPHA SYNUCLEIN; ENZYME PRECURSOR; KALLIKREIN 6; PRO MATRIX METALLOPROTEINASE 2; RECOMBINANT ENZYME; RECOMBINANT KALLIKREIN 6; UNCLASSIFIED DRUG; KALLIKREIN; PROTEIN KINASE; PRSS18 PROTEIN, MOUSE;

EID: 85014082933     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.13264     Document Type: Article
Times cited : (36)

References (46)
  • 3
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol. 2010; 11:301-307.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 4
    • 84869109864 scopus 로고    scopus 로고
    • Pathological a-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk KC, Kehm V, Carroll J, Zhang B, O'Brien P, Trojanowski JQ, Lee VM. Pathological a-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science. 2012; 338:949-953.
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 7
    • 0036445596 scopus 로고    scopus 로고
    • Expression of MMP-2, MMP-9, and MMP-1 and their endogenous counterregulators TIMP-1 and TIMP-2 in postmortem brain tissue of Parkinson's disease
    • Lorenzl S, Albers DS, Narr S, Chirichigno J, Beal MF. Expression of MMP-2, MMP-9, and MMP-1 and their endogenous counterregulators TIMP-1 and TIMP-2 in postmortem brain tissue of Parkinson's disease. Exp Neurol. 2002; 178:13-20.
    • (2002) Exp Neurol , vol.178 , pp. 13-20
    • Lorenzl, S.1    Albers, D.S.2    Narr, S.3    Chirichigno, J.4    Beal, M.F.5
  • 9
    • 0034712918 scopus 로고    scopus 로고
    • 2000 Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation
    • Serpell LC, Berriman J, Jakes R, Goedert M, Crowther RA. 2000 Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc Natl Acad Sci USA. 2000; 97:4897-4902.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 10
    • 0031728689 scopus 로고    scopus 로고
    • 1998 Synthetic filaments assembled from C-terminally truncated alpha-synuclein
    • Crowther RA, Jakes R, Spillantini MG, Goedert M. 1998. Synthetic filaments assembled from C-terminally truncated alpha-synuclein. FEBS Lett. 1998; 436:309-312.
    • (1998) FEBS Lett , vol.436 , pp. 309-312
    • Crowther, R.A.1    Jakes, R.2    Spillantini, M.G.3    Goedert, M.4
  • 12
    • 0142154275 scopus 로고    scopus 로고
    • Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies
    • Iwata A, Maruyama M, Akagi T, Hashikawa T, Kanazawa I, Tsuji S, Nukina N. Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies. Hum Mol Genet. 2003; 12:2625-2635.
    • (2003) Hum Mol Genet , vol.12 , pp. 2625-2635
    • Iwata, A.1    Maruyama, M.2    Akagi, T.3    Hashikawa, T.4    Kanazawa, I.5    Tsuji, S.6    Nukina, N.7
  • 15
    • 0029844185 scopus 로고    scopus 로고
    • A novel protease homolog differentially expressed in breast and ovarian cancer
    • Anisowicz A, Sotiropoulou G, Stenman G, Mok SC, Sager R. A novel protease homolog differentially expressed in breast and ovarian cancer. Mol Med. 1996; 2:624-636.
    • (1996) Mol Med , vol.2 , pp. 624-636
    • Anisowicz, A.1    Sotiropoulou, G.2    Stenman, G.3    Mok, S.C.4    Sager, R.5
  • 16
    • 0030730261 scopus 로고    scopus 로고
    • Nervous systemspecific expression of a novel serine protease: regulation in the adult rat spinal cord by excitotoxic injury
    • Scarisbrick IA, Towner MD, Isackson PJ. Nervous systemspecific expression of a novel serine protease: regulation in the adult rat spinal cord by excitotoxic injury. J Neurosci 1997; 17:8156-8168.
    • (1997) J Neurosci , vol.17 , pp. 8156-8168
    • Scarisbrick, I.A.1    Towner, M.D.2    Isackson, P.J.3
  • 18
    • 33847151166 scopus 로고    scopus 로고
    • A combined dataset of human cerebrospinal fluid proteins identified by multi-dimensional chromatography and tandem mass spectrometry
    • Pan S, Zhu D, Quinn JF, Peskind ER, Montine TJ, Lin B, Goodlett DR, Taylor G, Eng J, Zhang J. A combined dataset of human cerebrospinal fluid proteins identified by multi-dimensional chromatography and tandem mass spectrometry. Proteomics. 2007; 7:469-473.
    • (2007) Proteomics , vol.7 , pp. 469-473
    • Pan, S.1    Zhu, D.2    Quinn, J.F.3    Peskind, E.R.4    Montine, T.J.5    Lin, B.6    Goodlett, D.R.7    Taylor, G.8    Eng, J.9    Zhang, J.10
  • 19
    • 13844310832 scopus 로고    scopus 로고
    • Proteomics analysis of prefractionated human lumbar cerebrospinal fluid
    • Yuan X, Desiderio DM. Proteomics analysis of prefractionated human lumbar cerebrospinal fluid. Proteomics. 2005; 5:541-550.
    • (2005) Proteomics , vol.5 , pp. 541-550
    • Yuan, X.1    Desiderio, D.M.2
  • 20
    • 84965084989 scopus 로고    scopus 로고
    • Accumulation of a-synuclein in dementia with Lewy bodies is associated with decline in the a-synuclein-degrading enzymes kallikrein-6 and calpain-1
    • Miners JS, Renfrew R, Swirski M, Love S. Accumulation of a-synuclein in dementia with Lewy bodies is associated with decline in the a-synuclein-degrading enzymes kallikrein-6 and calpain-1. Acta Neuropathol Commun. 2014; 2: 164.
    • (2014) Acta Neuropathol Commun , vol.2 , pp. 164
    • Miners, J.S.1    Renfrew, R.2    Swirski, M.3    Love, S.4
  • 21
    • 84871921645 scopus 로고    scopus 로고
    • Lentivirus mediated delivery of neurosin promotes clearance of wild-type alphasynuclein and reduces the pathology in the alpha-synuclein model of LBD
    • Spencer B, Michael S, Shen J, Kosberg K, Rockenstein E, Patrick C, Adame A, Masliah E. Lentivirus mediated delivery of neurosin promotes clearance of wild-type alphasynuclein and reduces the pathology in the alpha-synuclein model of LBD. Mol Ther. 2013; 21:31-41.
    • (2013) Mol Ther , vol.21 , pp. 31-41
    • Spencer, B.1    Michael, S.2    Shen, J.3    Kosberg, K.4    Rockenstein, E.5    Patrick, C.6    Adame, A.7    Masliah, E.8
  • 24
    • 0029031780 scopus 로고
    • Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate
    • Itoh Y, Binner S, Nagase H. Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate. Biochem J. 1995; 308:645-651.
    • (1995) Biochem J , vol.308 , pp. 645-651
    • Itoh, Y.1    Binner, S.2    Nagase, H.3
  • 25
    • 65549102934 scopus 로고    scopus 로고
    • Inducible over-expression of wild-type alpha-synuclein in human neuronal cells leads to caspase-dependent nonapoptotic death
    • Vekrellis K, Xilouri M, Emmanouilidou E, Stefanis L. Inducible over-expression of wild-type alpha-synuclein in human neuronal cells leads to caspase-dependent nonapoptotic death. J Neurochem. 2009; 109:1348-1362.
    • (2009) J Neurochem , vol.109 , pp. 1348-1362
    • Vekrellis, K.1    Xilouri, M.2    Emmanouilidou, E.3    Stefanis, L.4
  • 28
    • 12344258657 scopus 로고    scopus 로고
    • Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors
    • Snoek-van Beurden PA, Von den Hoff JW. Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors. Biotechniques. 2005; 38:73-83.
    • (2005) Biotechniques , vol.38 , pp. 73-83
    • Snoek-van Beurden, P.A.1    Von den Hoff, J.W.2
  • 29
    • 3242786608 scopus 로고    scopus 로고
    • Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation
    • Bayés A, Tsetsenis T, Ventura S, Vendrell J, Aviles FX, Sotiropoulou G. Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation. Biol Chem. 2009; 385:517-524.
    • (2009) Biol Chem , vol.385 , pp. 517-524
    • Bayés, A.1    Tsetsenis, T.2    Ventura, S.3    Vendrell, J.4    Aviles, F.X.5    Sotiropoulou, G.6
  • 30
    • 84892981176 scopus 로고    scopus 로고
    • Secretome and degradome profiling shows that kallikreinrelated peptidases 4, 5, 6, and 7 induce TGFβ-1 signaling in ovarian cancer cells
    • Shahinian H, Loessner D, Biniossek ML, Kizhakkedathu JN, Clements JA, Magdolen V, Schilling O. Secretome and degradome profiling shows that kallikreinrelated peptidases 4, 5, 6, and 7 induce TGFβ-1 signaling in ovarian cancer cells. Mol Oncol. 2014; 8:68-82.
    • (2014) Mol Oncol , vol.8 , pp. 68-82
    • Shahinian, H.1    Loessner, D.2    Biniossek, M.L.3    Kizhakkedathu, J.N.4    Clements, J.A.5    Magdolen, V.6    Schilling, O.7
  • 34
    • 70450231593 scopus 로고    scopus 로고
    • Functional roles of human kallikrein-related peptidases
    • Sotiropoulou G, Pampalakis G, Diamandis EP. Functional roles of human kallikrein-related peptidases. J Biol Chem. 2009; 284:32989-32994.
    • (2009) J Biol Chem , vol.284 , pp. 32989-32994
    • Sotiropoulou, G.1    Pampalakis, G.2    Diamandis, E.P.3
  • 35
    • 0037025309 scopus 로고    scopus 로고
    • 2002. Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system
    • Bernett MJ1, Blaber SI, Scarisbrick IA, Dhanarajan P, Thompson SM, Blaber M. 2002. Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system. J Biol Chem. 2002; 277:24562-24570.
    • (2002) J Biol Chem , vol.277 , pp. 24562-24570
    • Bernett, M.J.1    Blaber, S.I.2    Scarisbrick, I.A.3    Dhanarajan, P.4    Thompson, S.M.5    Blaber, M.6
  • 38
    • 51549106105 scopus 로고    scopus 로고
    • Cathepsin D is the main lysosomal enzyme involved in the degradation of a-synuclein and generation of its C-terminally truncated species
    • Sevlever D, Jiang P, Yen SH. Cathepsin D is the main lysosomal enzyme involved in the degradation of a-synuclein and generation of its C-terminally truncated species. Biochemistry. 2008; 47:9678-9687.
    • (2008) Biochemistry , vol.47 , pp. 9678-9687
    • Sevlever, D.1    Jiang, P.2    Yen, S.H.3
  • 39
    • 40049105086 scopus 로고    scopus 로고
    • Identification and analysis of mammalian KLK6 orthologue genes for prediction of physiological substrates
    • Pampalakis G, Arampatzidou M, Amoutzias G, Kossida S, Sotiropoulou G. Identification and analysis of mammalian KLK6 orthologue genes for prediction of physiological substrates. Comput Biol Chem. 2008; 32:111-121.
    • (2008) Comput Biol Chem , vol.32 , pp. 111-121
    • Pampalakis, G.1    Arampatzidou, M.2    Amoutzias, G.3    Kossida, S.4    Sotiropoulou, G.5
  • 42
    • 84942327159 scopus 로고    scopus 로고
    • 2015. A brain-targeted, modified neurosin (kallikrein-6) reduces a-synuclein accumulation in a mouse model of multiple system atrophy
    • Spencer B, Valera E, Rockenstein E, Trejo-Morales M, Adame A, Masliah E. 2015. A brain-targeted, modified neurosin (kallikrein-6) reduces a-synuclein accumulation in a mouse model of multiple system atrophy. Mol Neurodegener. 2015; 10: 48.
    • (2015) Mol Neurodegener , vol.10 , pp. 48
    • Spencer, B.1    Valera, E.2    Rockenstein, E.3    Trejo-Morales, M.4    Adame, A.5    Masliah, E.6
  • 43
    • 84885422046 scopus 로고    scopus 로고
    • Kallikrein 6 signals through PAR1 and PAR2 to promote neuron injury and exacerbate glutamate neurotoxicity
    • Yoon H1, Radulovic M, Wu J, Blaber SI, Blaber M, Fehlings MG, Scarisbrick IA. Kallikrein 6 signals through PAR1 and PAR2 to promote neuron injury and exacerbate glutamate neurotoxicity. J Neurochem. 2013; 127:283-98.
    • (2013) J Neurochem , vol.127 , pp. 283-298
    • Yoon, H.1    Radulovic, M.2    Wu, J.3    Blaber, S.I.4    Blaber, M.5    Fehlings, M.G.6    Scarisbrick, I.A.7
  • 45
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • Vogiatzi T, Xilouri M, Vekrellis K, Stefanis L. Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J Biol Chem. 2008; 283:23542-23556.
    • (2008) J Biol Chem , vol.283 , pp. 23542-23556
    • Vogiatzi, T.1    Xilouri, M.2    Vekrellis, K.3    Stefanis, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.