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Volumn 27, Issue 8, 2004, Pages 850-856

Tissue transglutaminase is not involved in the aggregate formation of stably expressed α-synuclein in SH-SY5Y human neuroblastoma cells

Author keywords

A53T; Inclusion A30p; SH SY5Y human neuroblastoma; Tissue transglutaminase (tTG); Synuclein

Indexed keywords

ALPHA SYNUCLEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; NERVE PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; SNCA PROTEIN, HUMAN; SYNUCLEIN; TRANSGLUTAMINASE 2;

EID: 16644386736     PISSN: 02536269     EISSN: 02536269     Source Type: Journal    
DOI: 10.1007/BF02980178     Document Type: Article
Times cited : (6)

References (37)
  • 1
    • 4644336256 scopus 로고    scopus 로고
    • Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease
    • Andringa, G., Lam, K. Y., Chegary, M., Wang, X., Chase, T. N., and Bennett, M. C., Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease. FASEB J., 18, 932-934 (2004).
    • (2004) FASEB J. , vol.18 , pp. 932-934
    • Andringa, G.1    Lam, K.Y.2    Chegary, M.3    Wang, X.4    Chase, T.N.5    Bennett, M.C.6
  • 2
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway, K. A., Harper, J. D., and Lansbury, P. T., Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med., 4, 1318-1320 (1998).
    • (1998) Nat. Med. , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 3
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A., Lee, S. J., Rochet, J. C., Ding, T. T., Williamson, R. E., and Lansbury, P. T., Jr. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. U.S.A., 97, 571-576 (2000).
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury Jr., P.T.6
  • 4
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W. S., Jonas, A., Clayton, D. F., and George, J. M., Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem., 273, 9443-9449 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 5
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation
    • Folk, J. E., Mechanism and basis for specificity of transglutaminase- catalyzed epsilon-(gamma-glutamyl) lysine bond formation. Adv. Enzymol. Relat. Areas Mol. Biol., 54, 1-56 (1983).
    • (1983) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 6
    • 0035109738 scopus 로고    scopus 로고
    • Synucleinopathies: Clinical and pathological implications
    • Galvin, J. E., Lee, V. M., and Trojanowski, J. Q., Synucleinopathies: clinical and pathological implications. Arch. Neurol., 58, 186-190 (2001).
    • (2001) Arch. Neurol. , vol.58 , pp. 186-190
    • Galvin, J.E.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 7
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson, B. I., Uryu, K., Trojanowski, J. Q., and Lee, V. M., Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem., 274, 7619-7622 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 7619-7622
    • Giasson, B.I.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 8
    • 0027507667 scopus 로고
    • Human genetic diseases due to codon reiteration: Relationship to an evolutionary mechanism
    • Green, H., Human genetic diseases due to codon reiteration: relationship to an evolutionary mechanism [letter]. Cell, 74, 955-956 (1993).
    • (1993) Cell , vol.74 , pp. 955-956
    • Green, H.1
  • 9
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg, C. S., Birckbichler, P. J., and Rice, R. H., Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J., 5, 3071-3077 (1991).
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 10
    • 0028177277 scopus 로고
    • Cross-linking of beta-amyloid protein precursor catalyzed by tissue transglutaminase
    • Ho, G. J., Gregory, E. J., Smirnova, I. V., Zoubine, M. N., and Festoff, B. W., Cross-linking of beta-amyloid protein precursor catalyzed by tissue transglutaminase. FEBS Lett., 349, 151-154 (1994).
    • (1994) FEBS Lett. , vol.349 , pp. 151-154
    • Ho, G.J.1    Gregory, E.J.2    Smirnova, I.V.3    Zoubine, M.N.4    Festoff, B.W.5
  • 11
    • 0037452813 scopus 로고    scopus 로고
    • Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies
    • Junn, E., Ronchetti, R. D., Quezado, M. M., Kim, S. Y., and Mouradian, M. M., Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies. Proc. Natl Acad. Sci. U.S.A., 100, 2047-2052 (2003).
    • (2003) Proc. Natl Acad. Sci. U.S.A. , vol.100 , pp. 2047-2052
    • Junn, E.1    Ronchetti, R.D.2    Quezado, M.M.3    Kim, S.Y.4    Mouradian, M.M.5
  • 12
    • 0034008852 scopus 로고    scopus 로고
    • Enhanced vulnerability to oxidative stress by alpha-synuclein mutations and C-terminal truncation
    • Kanda, S., Bishop, J. F., Eglitis, M. A., Yang, Y., and Mouradian, M. M., Enhanced vulnerability to oxidative stress by alphasynuclein mutations and C-terminal truncation. Neuroscience, 97, 279-284 (2000).
    • (2000) Neuroscience , vol.97 , pp. 279-284
    • Kanda, S.1    Bishop, J.F.2    Eglitis, M.A.3    Yang, Y.4    Mouradian, M.M.5
  • 13
    • 0033594894 scopus 로고    scopus 로고
    • Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei
    • Karpuj, M. V., Garren, H., Slunt, H., Price, D. L., Gusella, J., Becher, M. W., and Steinman, L., Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei. Proc. Natl. Acad. Sci. U.S.A., 96, 7388-7393 (1999).
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7388-7393
    • Karpuj, M.V.1    Garren, H.2    Slunt, H.3    Price, D.L.4    Gusella, J.5    Becher, M.W.6    Steinman, L.7
  • 14
    • 0033773403 scopus 로고    scopus 로고
    • Sensitization of neuronal cells to oxidative stress with mutated human alpha-synuclein
    • Ko, L., Mehta, N. D., Farrer, M., Easson, C., Hussey, J., Yen, S., Hardy, J., and Yen, S. H., Sensitization of neuronal cells to oxidative stress with mutated human alpha-synuclein. J. Neurochem., 75, 2546-2554 (2000).
    • (2000) J. Neurochem. , vol.75 , pp. 2546-2554
    • Ko, L.1    Mehta, N.D.2    Farrer, M.3    Easson, C.4    Hussey, J.5    Yen, S.6    Hardy, J.7    Yen, S.H.8
  • 17
    • 0031890194 scopus 로고    scopus 로고
    • Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP
    • Lai, T. S., Slaughter, T. F., Peoples, K. A., Hettasch, J. M., and Greenberg, C. S., Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP. J. Biol. Chem., 273, 1776-1781 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 1776-1781
    • Lai, T.S.1    Slaughter, T.F.2    Peoples, K.A.3    Hettasch, J.M.4    Greenberg, C.S.5
  • 18
    • 0032742674 scopus 로고    scopus 로고
    • Tissue transglutaminase is increased in Huntington's disease brain
    • Lesort, M., Chun, W., Johnson, G. V., and Ferrante, R. J., Tissue transglutaminase is increased in Huntington's disease brain. J. Neurochem., 73, 2018-2027 (1999).
    • (1999) J. Neurochem. , vol.73 , pp. 2018-2027
    • Lesort, M.1    Chun, W.2    Johnson, G.V.3    Ferrante, R.J.4
  • 20
    • 0036884733 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: Dopamine, vesicles and alpha-synuclein
    • Lotharius, J. and Brundin, P., Pathogenesis of Parkinson's disease: dopamine, vesicles and alpha-synuclein. Nat. Rev. Neurosci., 3, 932-942 (2002).
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 932-942
    • Lotharius, J.1    Brundin, P.2
  • 21
    • 0022627398 scopus 로고
    • Transglutaminase and the neuronal cytoskeleton in Alzheimer's disease
    • Miller, C. C. and Anderton, B. H., Transglutaminase and the neuronal cytoskeleton in Alzheimer's disease. J. Neurochem., 46, 1912-1922 (1986).
    • (1986) J. Neurochem. , vol.46 , pp. 1912-1922
    • Miller, C.C.1    Anderton, B.H.2
  • 22
    • 0029096258 scopus 로고
    • Transglutaminase cross-linking of the tau protein
    • Miller, M. L. and Johnson, G. V., Transglutaminase cross-linking of the tau protein. J. Neurochem., 65, 1760-1770 (1995).
    • (1995) J. Neurochem. , vol.65 , pp. 1760-1770
    • Miller, M.L.1    Johnson, G.V.2
  • 24
    • 0032936755 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Olanow, C. W. and Tatton, W. G., Etiology and pathogenesis of Parkinson's disease. Annu. Rev. Neurosci., 22, 123-144 (1999).
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 123-144
    • Olanow, C.W.1    Tatton, W.G.2
  • 25
    • 0034663039 scopus 로고    scopus 로고
    • The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity
    • Ostrerova-Golts, N., Petrucelli, L., Hardy, J., Lee, J. M., Farer, M., and Wolozin, B., The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity. J. Neurosci., 20, 6048-6054 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 6048-6054
    • Ostrerova-Golts, N.1    Petrucelli, L.2    Hardy, J.3    Lee, J.M.4    Farer, M.5    Wolozin, B.6
  • 26
    • 0032472212 scopus 로고    scopus 로고
    • Self-oligomerization of NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer's disease amyloid, observed in the presence of a C-terminal A beta fragment (residues 25-35)
    • Paik, S. R., Lee, J. H., Kim, D. H., Chang, C. S., and Kim, Y. S., Self-oligomerization of NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer's disease amyloid, observed in the presence of a C-terminal A beta fragment (residues 25-35). FEBS Lett., 421, 73-76 (1998).
    • (1998) FEBS Lett. , vol.421 , pp. 73-76
    • Paik, S.R.1    Lee, J.H.2    Kim, D.H.3    Chang, C.S.4    Kim, Y.S.5
  • 29
    • 0000831917 scopus 로고
    • Brain transglutaminase: In vitro crosslinking of human neurofilament proteins into insoluble polymers
    • Selkoe, D. J., Abraham, C., and Ihara, Y., Brain transglutaminase: in vitro crosslinking of human neurofilament proteins into insoluble polymers. Proc. Natl. Acad. Sci. U.S.A., 79, 6070-6074 (1982).
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 6070-6074
    • Selkoe, D.J.1    Abraham, C.2    Ihara, Y.3
  • 30
    • 0037104723 scopus 로고    scopus 로고
    • An in vitro model of Parkinson's disease: Linking mitochondrial impairment to altered alpha-synuclein metabolism and oxidative damage
    • Sherer, T. B., Betarbet, R., Stout, A. K., Lund, S., Baptista, M., Panov, A. V., Cookson, M. R., and Greenamyre, J. T., An in vitro model of Parkinson's disease: linking mitochondrial impairment to altered alpha-synuclein metabolism and oxidative damage. J. Neurosci., 22, 7006-7015 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 7006-7015
    • Sherer, T.B.1    Betarbet, R.2    Stout, A.K.3    Lund, S.4    Baptista, M.5    Panov, A.V.6    Cookson, M.R.7    Greenamyre, J.T.8
  • 31
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease
    • Volles, M. J. and Lansbury, P. T., Jr., Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry, 42, 7871-7878 (2003).
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 32
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., and Lansbury, P. T., Jr., NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry, 35, 13709-13715 (1996).
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr., P.T.5
  • 33
    • 0033538541 scopus 로고    scopus 로고
    • Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease
    • Wood, S. J., Wypych, J., Steavenson, S., Louis, J. C., Citron, M., and Biere, A. L., Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J. Biol. Chem., 274, 19509-19512 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6
  • 34
    • 0032490652 scopus 로고    scopus 로고
    • The interrelationship between selective tau phosphorylation and microtubule association
    • Xie, H., Litersky, J. M., Hartigan, J. A., Jope, R. S., and Johnson, G. V., The interrelationship between selective tau phosphorylation and microtubule association. Brain Res., 798, 173-183 (1998).
    • (1998) Brain Res. , vol.798 , pp. 173-183
    • Xie, H.1    Litersky, J.M.2    Hartigan, J.A.3    Jope, R.S.4    Johnson, G.V.5
  • 35
    • 0031866960 scopus 로고    scopus 로고
    • Tissue transglutaminase is an in situ substrate of calpain: Regulation of activity
    • Zhang, J., Guttmann, R. P., and Johnson, G. V., Tissue transglutaminase is an in situ substrate of calpain: regulation of activity. J. Neurochem., 71, 240-247 (1998a).
    • (1998) J. Neurochem. , vol.71 , pp. 240-247
    • Zhang, J.1    Guttmann, R.P.2    Johnson, G.V.3
  • 36
    • 0031893826 scopus 로고    scopus 로고
    • Modulation of the in situ activity of tissue transglutaminase by calcium and GTP
    • Zhang, J., Lesort, M., Guttmann, R. P., and Johnson, G. V., Modulation of the in situ activity of tissue transglutaminase by calcium and GTP. J. Biol. Chem., 273, 2288-2295 (1998b).
    • (1998) J. Biol. Chem. , vol.273 , pp. 2288-2295
    • Zhang, J.1    Lesort, M.2    Guttmann, R.P.3    Johnson, G.V.4
  • 37
    • 0037451830 scopus 로고    scopus 로고
    • Modulation of cell death by alpha-synuclein is stimulus-dependent in mammalian cells
    • Zourlidou, A., Payne Smith, M. D., and Latchman, D. S., Modulation of cell death by alpha-synuclein is stimulus-dependent in mammalian cells. Neurosci. Lett., 340, 234-238 (2003).
    • (2003) Neurosci. Lett. , vol.340 , pp. 234-238
    • Zourlidou, A.1    Payne Smith, M.D.2    Latchman, D.S.3


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