메뉴 건너뛰기




Volumn 217, Issue 2-3, 1996, Pages 117-120

1-Antichymotrypsin interaction with Aβ(1-42) does not inhibit fibril formation but attenuates the peptide toxicity

Author keywords

Amyloid; Fibril formation; Neurotoxicity; 1 Antichymotrypsin

Indexed keywords

ALPHA 1 ANTITRYPSIN; AMYLOID BETA PROTEIN; ALPHA 1 ANTICHYMOTRYPSIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); COLORING AGENT; NEUROTOXIN; PEPTIDE FRAGMENT; SERINE PROTEINASE INHIBITOR; TETRAZOLIUM; THIAZOLE DERIVATIVE; THIAZOLYL BLUE;

EID: 0030592330     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/0304-3940(96)13082-2     Document Type: Article
Times cited : (23)

References (22)
  • 1
    • 0023838532 scopus 로고
    • Immunochemical identification of serine protease inhibitor α1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease
    • [1] Abraham, C.R., Selkoe, D.J. and Potter, H., Immunochemical identification of serine protease inhibitor α1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease, Cell, 52 (1988) 487-501.
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.R.1    Selkoe, D.J.2    Potter, H.3
  • 2
    • 0029969354 scopus 로고    scopus 로고
    • Glutamine synthetase-induced enhancement of Aβ(1-40) neurotoxicity accompanied by abrogation of fibril formation and amyloid β-peptide fragmentation
    • [2] Aksenov, M.Y., Aksenova, M.V., Butterfield, D.A., Hensley, K., Vigo-Pelfrey, C. and Carney, J.M., Glutamine synthetase-induced enhancement of Aβ(1-40) neurotoxicity accompanied by abrogation of fibril formation and amyloid β-peptide fragmentation, J. Neurochem., 66 (1996) 2050-2056.
    • (1996) J. Neurochem. , vol.66 , pp. 2050-2056
    • Aksenov, M.Y.1    Aksenova, M.V.2    Butterfield, D.A.3    Hensley, K.4    Vigo-Pelfrey, C.5    Carney, J.M.6
  • 3
    • 0029661902 scopus 로고    scopus 로고
    • α1-Antichymotrypsin interaction with Aβ(1-40) inhibits fibril formation but does not affect the peptide toxicity
    • [3] Aksenova, M.V., Aksenov, M.Y., Butterfield, D.A. and Carney, J.M., α1-Antichymotrypsin interaction with Aβ(1-40) inhibits fibril formation but does not affect the peptide toxicity, Neurosci. Lett., 411 (1996) 45-48.
    • (1996) Neurosci. Lett. , vol.411 , pp. 45-48
    • Aksenova, M.V.1    Aksenov, M.Y.2    Butterfield, D.A.3    Carney, J.M.4
  • 4
    • 0028986408 scopus 로고
    • Fibrillogenesis in Alzheimer's disease of amyloid β peptides and apolipoprotein E
    • [4] Castaño, E.M., Prelli, F., Wisniewski, T., Golabek, A., Kumar, R.A. and Frangione, B., Fibrillogenesis in Alzheimer's disease of amyloid β peptides and apolipoprotein E, Biochem, J., 306 (1995) 599-604.
    • (1995) Biochem, J. , vol.306 , pp. 599-604
    • Castaño, E.M.1    Prelli, F.2    Wisniewski, T.3    Golabek, A.4    Kumar, R.A.5    Frangione, B.6
  • 5
    • 0028889206 scopus 로고
    • Expression of the Alzheimer amyloid-promoting factor antichymotrypsin is induced in human astrocytes by IL-1
    • [5] Das, S. and Potter, H., Expression of the Alzheimer amyloid-promoting factor antichymotrypsin is induced in human astrocytes by IL-1, Neuron, 14 (1995) 447-456.
    • (1995) Neuron , vol.14 , pp. 447-456
    • Das, S.1    Potter, H.2
  • 6
    • 0028986858 scopus 로고
    • Alpha 1-antichymotrypsin regulates beta-amyloid peptide fibril formation
    • [6] Eriksson, S., Janciauskiene, S. and Lannfelt, L., Alpha 1-antichymotrypsin regulates beta-amyloid peptide fibril formation, Proc. Natl. Acad. Sci. USA, 92 (1995) 2313-2317.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2313-2317
    • Eriksson, S.1    Janciauskiene, S.2    Lannfelt, L.3
  • 7
    • 0027322517 scopus 로고
    • α-Antichymotrypsin binding to Alzheimer Aβ peptides is sequence specific and induces fibril disaggregation in vitro
    • [7] Fraser, P.E., Nguyen, J.T., McLachlan, D.R., Abraham, C.R. and Kirschner, D.R., α-Antichymotrypsin binding to Alzheimer Aβ peptides is sequence specific and induces fibril disaggregation in vitro, J. Neurochem., 61 (1993) 298-305.
    • (1993) J. Neurochem. , vol.61 , pp. 298-305
    • Fraser, P.E.1    Nguyen, J.T.2    McLachlan, D.R.3    Abraham, C.R.4    Kirschner, D.R.5
  • 8
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's amyloid beta-peptide (1-40) in cultured hippocampal neurons
    • [8] Harris, M.E., Hensley, K., Butterfield, D.A., Leedle, R.A. and Carney, J.M., Direct evidence of oxidative injury produced by the Alzheimer's amyloid beta-peptide (1-40) in cultured hippocampal neurons, Exp. Neural., 131 (1995) 193-202.
    • (1995) Exp. Neural. , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 9
    • 0028990941 scopus 로고
    • APOE 4-associated Alzheimer's disease risk is modified by alpha 1-antichymortypsin polymorphism
    • [9] Kamboh, M.I., Sanghera, D.K., Ferrell, R.E. and DeKosky, S.T., APOE 4-associated Alzheimer's disease risk is modified by alpha 1-antichymortypsin polymorphism, Nature Genet., 10 (1995) 486-488.
    • (1995) Nature Genet. , vol.10 , pp. 486-488
    • Kamboh, M.I.1    Sanghera, D.K.2    Ferrell, R.E.3    DeKosky, S.T.4
  • 10
    • 0028174697 scopus 로고
    • Effect of α-antichymotrypsin on the toxicity of β-amyloid fragment 25-40 in rat primary cultured neurons
    • [10] Kobayashi, T., Abe, K., Saito, H. and Nishiyama, N., Effect of α-antichymotrypsin on the toxicity of β-amyloid fragment 25-40 in rat primary cultured neurons, Neurosci. Lett., 172 (1994) 147-150.
    • (1994) Neurosci. Lett. , vol.172 , pp. 147-150
    • Kobayashi, T.1    Abe, K.2    Saito, H.3    Nishiyama, N.4
  • 11
    • 0027288860 scopus 로고
    • Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neunte outgrowth
    • [11] Koo, E.H., Park, L. and Selkoe, D.J., Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neunte outgrowth, Proc. Natl. Acad. Sci. USA, 90 (1993) 4748-4752.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4748-4752
    • Koo, E.H.1    Park, L.2    Selkoe, D.J.3
  • 12
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo Red
    • [12] Lorenzo, A. and Yankner, B.A., β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo Red, Proc. Natl. Acad. Sci. USA, 91 (1994) 12243-12247.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 13
    • 0028173205 scopus 로고
    • Amyloid-associated proteins α-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
    • [13] Ma, J., Yee, A., Brewer, H.B., Das, S. and Potter, H., Amyloid-associated proteins α-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments, Nature, 372 (1994) 92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer, H.B.3    Das, S.4    Potter, H.5
  • 15
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • [15] Pike, C.J., Burdick, D., Walencewicz, A.J., Glabe, C.G. and Cotman, C.W., Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state, J. Neurosci., 13 (1993) 1676-1687.
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 16
    • 0011961815 scopus 로고
    • Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of beta-amyloid in rat PC12 cells
    • [16] Pollack, S.J., Sadler, I.I., Hawtin, S.R., Tailor, V.J. and Shearman, M.S., Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of beta-amyloid in rat PC12 cells, Brain Res., 671 (1995) 282-292.
    • (1995) Brain Res. , vol.671 , pp. 282-292
    • Pollack, S.J.1    Sadler, I.I.2    Hawtin, S.R.3    Tailor, V.J.4    Shearman, M.S.5
  • 17
    • 0028723818 scopus 로고
    • The involvement of amyloid-associated proteins in the formation of β-protein filaments in Alzheimer's disease
    • [17] Potter, H., Ma, J., Das, S. and Kayyali, U., The involvement of amyloid-associated proteins in the formation of β-protein filaments in Alzheimer's disease, Prog. Clin. Biol. Res., 390 (1994) 57-71.
    • (1994) Prog. Clin. Biol. Res. , vol.390 , pp. 57-71
    • Potter, H.1    Ma, J.2    Das, S.3    Kayyali, U.4
  • 19
    • 0029040824 scopus 로고
    • The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides
    • [19] Shearman, M.S., Hawtin, S.R. and Tailor, V.J., The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by β-amyloid peptides, J. Neurochem., 65 (1995) 218-227.
    • (1995) J. Neurochem. , vol.65 , pp. 218-227
    • Shearman, M.S.1    Hawtin, S.R.2    Tailor, V.J.3
  • 22
    • 0029670992 scopus 로고    scopus 로고
    • Deposits of Aβ fibrils are not toxic to cortical and hippocampal neurons in vitro
    • [22] Wujek, J.R., Dority, M.D., Frederickson, R.C.A. and Branden, K.R., Deposits of Aβ fibrils are not toxic to cortical and hippocampal neurons in vitro, Neurobiol. Aging, 17 (1996) 107-113.
    • (1996) Neurobiol. Aging , vol.17 , pp. 107-113
    • Wujek, J.R.1    Dority, M.D.2    Frederickson, R.C.A.3    Branden, K.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.