메뉴 건너뛰기




Volumn , Issue , 2012, Pages

Caspase-6 does not contribute to the proteolysis of mutant huntingtin in the HdhQ150 Knock-in mouse model of Huntington's disease

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 6; HUNTINGTIN;

EID: 84867459264     PISSN: None     EISSN: 21573999     Source Type: Journal    
DOI: 10.1371/4fd085bfc9973     Document Type: Article
Times cited : (19)

References (27)
  • 1
    • 3242692878 scopus 로고    scopus 로고
    • The Polyglutamine Diseases
    • In: Bates GP, Harper PS, Jones AL, editors, 3rd ed. Oxford: Oxford University Press
    • Bates GP, Benn C (2002) The Polyglutamine Diseases. In: Bates GP, Harper PS, Jones AL, editors. Huntington's Disease. 3rd ed. Oxford: Oxford University Press. pp. 429-472.
    • (2002) Huntington's Disease , pp. 429-472
    • Bates, G.P.1    Benn, C.2
  • 2
    • 8844220536 scopus 로고    scopus 로고
    • Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series
    • Landles C, Bates GP (2004) Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series. EMBO Rep 5: 958-963.
    • (2004) EMBO Rep , vol.5 , pp. 958-963
    • Landles, C.1    Bates, G.P.2
  • 3
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • Harjes P, Wanker EE (2003) The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem Sci 28: 425-433.
    • (2003) Trends Biochem Sci , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 5
    • 33847684865 scopus 로고    scopus 로고
    • The Hdh(Q150/Q150) knock-in mouse model of HD and the R6/2 exon 1 model develop comparable and widespread molecular phenotypes
    • Woodman B, Butler R, Landles C, Lupton MK, Tse J, et al. (2007) The Hdh(Q150/Q150) knock-in mouse model of HD and the R6/2 exon 1 model develop comparable and widespread molecular phenotypes. Brain Res Bull 72: 83-97.
    • (2007) Brain Res Bull , vol.72 , pp. 83-97
    • Woodman, B.1    Butler, R.2    Landles, C.3    Lupton, M.K.4    Tse, J.5
  • 6
    • 77950584656 scopus 로고    scopus 로고
    • Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease
    • Landles C, Sathasivam K, Weiss A, Woodman B, Moffitt H, et al. (2010) Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease. J Biol Chem 285: 8808-8823.
    • (2010) J Biol Chem , vol.285 , pp. 8808-8823
    • Landles, C.1    Sathasivam, K.2    Weiss, A.3    Woodman, B.4    Moffitt, H.5
  • 7
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, et al. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277: 1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5
  • 8
    • 0036671821 scopus 로고    scopus 로고
    • Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions
    • Lunkes A, Lindenberg KS, Ben-Haiem L, Weber C, Devys D, et al. (2002) Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol Cell 10: 259-269.
    • (2002) Mol Cell , vol.10 , pp. 259-269
    • Lunkes, A.1    Lindenberg, K.S.2    Ben-Haiem, L.3    Weber, C.4    Devys, D.5
  • 9
    • 37549065909 scopus 로고    scopus 로고
    • N-terminal proteolysis of fulllength mutant huntingtin in an inducible PC12 cell model of Huntington's disease
    • Ratovitski T, Nakamura M, D'Ambola J, Chighladze E, Liang Y, et al. (2007) N-terminal proteolysis of fulllength mutant huntingtin in an inducible PC12 cell model of Huntington's disease. Cell Cycle 6: 2970-2981.
    • (2007) Cell Cycle , vol.6 , pp. 2970-2981
    • Ratovitski, T.1    Nakamura, M.2    D'Ambola, J.3    Chighladze, E.4    Liang, Y.5
  • 10
    • 67449094981 scopus 로고    scopus 로고
    • Mutant huntingtin N-terminal fragments of specific size mediate aggregation and toxicity in neuronal cells
    • Ratovitski T, Gucek M, Jiang H, Chighladze E, Waldron E, et al. (2009) Mutant huntingtin N-terminal fragments of specific size mediate aggregation and toxicity in neuronal cells. J Biol Chem 284: 10855-10867.
    • (2009) J Biol Chem , vol.284 , pp. 10855-10867
    • Ratovitski, T.1    Gucek, M.2    Jiang, H.3    Chighladze, E.4    Waldron, E.5
  • 11
    • 0037107151 scopus 로고    scopus 로고
    • Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease
    • Wellington CL, Ellerby LM, Gutekunst CA, Rogers D, Warby S, et al. (2002) Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease. J Neurosci 22: 7862-7872.
    • (2002) J Neurosci , vol.22 , pp. 7862-7872
    • Wellington, C.L.1    Ellerby, L.M.2    Gutekunst, C.A.3    Rogers, D.4    Warby, S.5
  • 12
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
    • Kim YJ, Yi Y, Sapp E, Wang Y, Cuiffo B, et al. (2001) Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc Natl Acad Sci U S A 98: 12784-12789.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    Sapp, E.3    Wang, Y.4    Cuiffo, B.5
  • 13
    • 2442631459 scopus 로고    scopus 로고
    • Inhibition of calpain cleavage of huntingtin reduces toxicity: Accumulation of calpain/caspase fragments in the nucleus
    • Gafni J, Hermel E, Young JE, Wellington CL, Hayden MR, et al. (2004) Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J Biol Chem 279: 20211-20220.
    • (2004) J Biol Chem , vol.279 , pp. 20211-20220
    • Gafni, J.1    Hermel, E.2    Young, J.E.3    Wellington, C.L.4    Hayden, M.R.5
  • 14
    • 77955500335 scopus 로고    scopus 로고
    • Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease
    • Miller JP, Holcomb J, Al-Ramahi I, de Haro M, Gafni J, et al. (2010) Matrix metalloproteinases are modifiers of huntingtin proteolysis and toxicity in Huntington's disease. Neuron 67: 199-212.
    • (2010) Neuron , vol.67 , pp. 199-212
    • Miller, J.P.1    Holcomb, J.2    Al-Ramahi, I.3    de Haro, M.4    Gafni, J.5
  • 15
    • 33646121970 scopus 로고    scopus 로고
    • Lysosomal proteases are involved in generation of N-terminal huntingtin fragments
    • Kim YJ, Sapp E, Cuiffo BG, Sobin L, Yoder J, et al. (2006) Lysosomal proteases are involved in generation of N-terminal huntingtin fragments. Neurobiol Dis 22: 346-356.
    • (2006) Neurobiol Dis , vol.22 , pp. 346-356
    • Kim, Y.J.1    Sapp, E.2    Cuiffo, B.G.3    Sobin, L.4    Yoder, J.5
  • 16
    • 34147179928 scopus 로고    scopus 로고
    • Characterization of huntingtin pathologic fragments in human Huntington disease, transgenic mice, and cell models
    • Schilling G, Klevytska A, Tebbenkamp AT, Juenemann K, Cooper J, et al. (2007) Characterization of huntingtin pathologic fragments in human Huntington disease, transgenic mice, and cell models. J Neuropathol Exp Neurol 66: 313-320.
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 313-320
    • Schilling, G.1    Klevytska, A.2    Tebbenkamp, A.T.3    Juenemann, K.4    Cooper, J.5
  • 17
    • 0036451321 scopus 로고    scopus 로고
    • Polyglutamine repeat length-dependent proteolysis of huntingtin
    • Sun B, Fan W, Balciunas A, Cooper JK, Bitan G, et al. (2002) Polyglutamine repeat length-dependent proteolysis of huntingtin. Neurobiol Dis 11: 111-122.
    • (2002) Neurobiol Dis , vol.11 , pp. 111-122
    • Sun, B.1    Fan, W.2    Balciunas, A.3    Cooper, J.K.4    Bitan, G.5
  • 18
    • 30744439549 scopus 로고    scopus 로고
    • Progressive phenotype and nuclear accumulation of an amino-terminal cleavage fragment in a transgenic mouse model with inducible expression of full-length mutant huntingtin
    • Tanaka Y, Igarashi S, Nakamura M, Gafni J, Torcassi C, et al. (2006) Progressive phenotype and nuclear accumulation of an amino-terminal cleavage fragment in a transgenic mouse model with inducible expression of full-length mutant huntingtin. Neurobiol Dis 21: 381-391.
    • (2006) Neurobiol Dis , vol.21 , pp. 381-391
    • Tanaka, Y.1    Igarashi, S.2    Nakamura, M.3    Gafni, J.4    Torcassi, C.5
  • 19
    • 84855921378 scopus 로고    scopus 로고
    • Transgenic mouse model expressing the caspase 6 fragment of mutant huntingtin
    • Waldron-Roby E, Ratovitski T, Wang X, Jiang M, Watkin E, et al. (2012) Transgenic mouse model expressing the caspase 6 fragment of mutant huntingtin. J Neurosci 32: 183-193.
    • (2012) J Neurosci , vol.32 , pp. 183-193
    • Waldron-Roby, E.1    Ratovitski, T.2    Wang, X.3    Jiang, M.4    Watkin, E.5
  • 20
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham RK, Deng Y, Slow EJ, Haigh B, Bissada N, et al. (2006) Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 125: 1179-1191.
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3    Haigh, B.4    Bissada, N.5
  • 21
    • 77649297870 scopus 로고    scopus 로고
    • Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease
    • Sathasivam K, Lane A, Legleiter J, Warley A, Woodman B, et al. (2010) Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease. Hum Mol Genet 19: 65-78.
    • (2010) Hum Mol Genet , vol.19 , pp. 65-78
    • Sathasivam, K.1    Lane, A.2    Legleiter, J.3    Warley, A.4    Woodman, B.5
  • 22
    • 84859244583 scopus 로고    scopus 로고
    • Rescue from excitotoxicity and axonal degeneration accompanied by age-dependent behavioral and neuroanatomical alterations in caspase-6-deficient mice
    • Uribe V, Wong BK, Graham RK, Cusack CL, Skotte NH, et al. (2012) Rescue from excitotoxicity and axonal degeneration accompanied by age-dependent behavioral and neuroanatomical alterations in caspase-6-deficient mice. Hum Mol Genet 21: 1954-1967.
    • (2012) Hum Mol Genet , vol.21 , pp. 1954-1967
    • Uribe, V.1    Wong, B.K.2    Graham, R.K.3    Cusack, C.L.4    Skotte, N.H.5
  • 23
    • 0035502934 scopus 로고    scopus 로고
    • New anti-huntingtin monoclonal antibodies: Implications for huntingtin conformation and its binding proteins
    • Ko J, Ou S, Patterson PH (2001) New anti-huntingtin monoclonal antibodies: implications for huntingtin conformation and its binding proteins. Brain Res Bull 56: 319-329.
    • (2001) Brain Res Bull , vol.56 , pp. 319-329
    • Ko, J.1    Ou, S.2    Patterson, P.H.3
  • 24
    • 70349103737 scopus 로고    scopus 로고
    • Single-step detection of mutant huntingtin in animal and human tissues: A bioassay for Huntington's disease
    • Weiss A, Abramowski D, Bibel M, Bodner R, Chopra V, et al. (2009) Single-step detection of mutant huntingtin in animal and human tissues: a bioassay for Huntington's disease. Anal Biochem 395: 8-15.
    • (2009) Anal Biochem , vol.395 , pp. 8-15
    • Weiss, A.1    Abramowski, D.2    Bibel, M.3    Bodner, R.4    Chopra, V.5
  • 25
    • 79551567075 scopus 로고    scopus 로고
    • Microtiter plate quantification of mutant and wild-type huntingtin normalized to cell count
    • Weiss A, Grueninger S, Abramowski D, Giorgio FP, Lopatin MM, et al. (2011) Microtiter plate quantification of mutant and wild-type huntingtin normalized to cell count. Anal Biochem 410: 304-306.
    • (2011) Anal Biochem , vol.410 , pp. 304-306
    • Weiss, A.1    Grueninger, S.2    Abramowski, D.3    Giorgio, F.P.4    Lopatin, M.M.5
  • 26
    • 0035504960 scopus 로고    scopus 로고
    • Centrosome disorganization in fibroblast cultures derived from R6/2 Huntington's disease (HD) transgenic mice and HD patients
    • Sathasivam K, Woodman B, Mahal A, Bertaux F, Wanker EE, et al. (2001) Centrosome disorganization in fibroblast cultures derived from R6/2 Huntington's disease (HD) transgenic mice and HD patients. Hum Mol Genet 10: 2425-2435.
    • (2001) Hum Mol Genet , vol.10 , pp. 2425-2435
    • Sathasivam, K.1    Woodman, B.2    Mahal, A.3    Bertaux, F.4    Wanker, E.E.5
  • 27
    • 84861630493 scopus 로고    scopus 로고
    • Caspase-6 Activity in a BACHD Mouse Modulates Steady-State Levels of Mutant Huntingtin Protein But Is Not Necessary for Production of a 586 Amino Acid Proteolytic Fragment
    • Gafni J, Papanikolaou T, Degiacomo F, Holcomb J, Chen S, et al. (2012) Caspase-6 Activity in a BACHD Mouse Modulates Steady-State Levels of Mutant Huntingtin Protein But Is Not Necessary for Production of a 586 Amino Acid Proteolytic Fragment. J Neurosci 32: 7454-7465.
    • (2012) J Neurosci , vol.32 , pp. 7454-7465
    • Gafni, J.1    Papanikolaou, T.2    Degiacomo, F.3    Holcomb, J.4    Chen, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.