메뉴 건너뛰기




Volumn 853, Issue 2, 2000, Pages 344-351

Gelsolin inhibits the fibrillization of amyloid beta-protein, and also defibrillizes its preformed fibrils

Author keywords

Alzheimer's disease; Amyloid beta protein; Cerebrospinal fluid; Fibrillization; Gelsolin; Plasma

Indexed keywords

AMYLOID BETA PROTEIN; CONGO RED; GELSOLIN;

EID: 0033988752     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(99)02315-X     Document Type: Article
Times cited : (62)

References (31)
  • 2
    • 0031023320 scopus 로고    scopus 로고
    • Media from rhabdomyosarcoma and neuroblastoma cell cultures stimulate in vitro aggregation and fibrillization of amyloid beta-protein
    • Chauhan A., Chauhan V.P.S., Rubenstein R., Wegiel J., Wisniewski H.M. Media from rhabdomyosarcoma and neuroblastoma cell cultures stimulate in vitro aggregation and fibrillization of amyloid beta-protein. Neurochem. Res. 22:1997;227-232.
    • (1997) Neurochem. Res. , vol.22 , pp. 227-232
    • Chauhan, A.1    Chauhan, V.P.S.2    Rubenstein, R.3    Wegiel, J.4    Wisniewski, H.M.5
  • 3
    • 0030430289 scopus 로고    scopus 로고
    • Impact of normal and heat-inactivated serum on in vitro aggregation and fibrillization of synthetic amyloid beta-protein
    • Chauhan A., Chauhan V.P.S., Wegiel J., Wisniewski H.M. Impact of normal and heat-inactivated serum on in vitro aggregation and fibrillization of synthetic amyloid beta-protein. Alzheimer's Res. 2:1996;243-248.
    • (1996) Alzheimer's Res. , vol.2 , pp. 243-248
    • Chauhan, A.1    Chauhan, V.P.S.2    Wegiel, J.3    Wisniewski, H.M.4
  • 6
    • 0030807917 scopus 로고    scopus 로고
    • The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons
    • Furukawa K., Fu W., Li Y., Witke W., Kwiatkowski D.J., Mattson M.P. The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons. J. Neurosci. 17:1997;8178-8186.
    • (1997) J. Neurosci. , vol.17 , pp. 8178-8186
    • Furukawa, K.1    Fu, W.2    Li, Y.3    Witke, W.4    Kwiatkowski, D.J.5    Mattson, M.P.6
  • 7
    • 0027186334 scopus 로고
    • The cerebrospinal fluid soluble form of Alzheimer's amyloid β is complexed to SP-40, 40 (APO J), an inhibitor of the complement membrane-attack complex
    • Ghiso J., Matsubara E., Koudinov A., Wisniewski T., Frangione B. The cerebrospinal fluid soluble form of Alzheimer's amyloid β is complexed to SP-40, 40 (APO J), an inhibitor of the complement membrane-attack complex. Biochem. J. 293:1993;27-30.
    • (1993) Biochem. J. , vol.293 , pp. 27-30
    • Ghiso, J.1    Matsubara, E.2    Koudinov, A.3    Wisniewski, T.4    Frangione, B.5
  • 9
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20:1997;403-407.
    • (1997) Trends Neurosci. , vol.20 , pp. 403-407
    • Hardy, J.1
  • 10
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease
    • Hilbich C., Kisters-Woike B., Reed J., Masters C.L., Beyreuther K. Aggregation and secondary structure of synthetic amyloid beta A4 peptides of Alzheimer's disease. J. Mol. Biol. 218:1991;149-163.
    • (1991) J. Mol. Biol. , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 11
    • 0021801388 scopus 로고
    • Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking
    • Janney P.A., Chapannier C., Lind S.E., Zaner K.S., Stossel T.P., Yin H.L. Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking. Biochemistry. 24:1985;3714-3723.
    • (1985) Biochemistry , vol.24 , pp. 3714-3723
    • Janney, P.A.1    Chapannier, C.2    Lind, S.E.3    Zaner, K.S.4    Stossel, T.P.5    Yin, H.L.6
  • 12
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • Jarrett J.T., Lansbury P.T. Jr. Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry. 31:1992;12345-12352.
    • (1992) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury P.T., Jr.2
  • 14
    • 0028609448 scopus 로고
    • The soluble form of Alzheimer's amyloid beta-protein is complexed to high-density lipoprotein 3 and very high density lipoprotein in normal human plasma
    • Koudinov A., Matsubara E., Frangione B., Ghiso J. The soluble form of Alzheimer's amyloid beta-protein is complexed to high-density lipoprotein 3 and very high density lipoprotein in normal human plasma. Biochem. Biophys. Res. Commun. 205:1994;1164-1171.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1164-1171
    • Koudinov, A.1    Matsubara, E.2    Frangione, B.3    Ghiso, J.4
  • 16
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation
    • Lorenzo A., Yankner B.A. β-Amyloid neurotoxicity requires fibril formation. Proc. Natl. Acad. Sci. U.S.A. 91:1994;12243-12247.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 17
    • 0028173205 scopus 로고
    • Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments
    • Ma J., Yee A., Brewer H.B. Jr., Das S., Potter H. Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature. 372:1994;92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer H.B., Jr.3    Das, S.4    Potter, H.5
  • 18
    • 0028003287 scopus 로고
    • Quantification of serum and cerebrospinal fluid gelsolin in familial amyloidosis, Finnish type (AGel), Amyloid
    • Paunio T., Kiuru S., Karonen S.-L., Palo J., Peltonen L. Quantification of serum and cerebrospinal fluid gelsolin in familial amyloidosis, Finnish type (AGel), Amyloid. Int. J. Exp. Clin. Invest. 1:1994;80-89.
    • (1994) Int. J. Exp. Clin. Invest. , vol.1 , pp. 80-89
    • Paunio, T.1    Kiuru, S.2    Karonen, S.-L.3    Palo, J.4    Peltonen, L.5
  • 22
    • 0343732584 scopus 로고
    • Actin-membrane interactions in eukaryotic mammalian cells
    • in: J.F. Hoffman, G. Giebisch (Eds.) Academic Press, NY
    • T.P. Stossel, Actin-membrane interactions in eukaryotic mammalian cells, in: J.F. Hoffman, G. Giebisch (Eds.), Current Topics in Membranes and Transport, Vol. 36, Academic Press, NY, 1990, pp. 97-107.
    • (1990) Current Topics in Membranes and Transport , vol.36 , pp. 97-107
    • Stossel, T.P.1
  • 25
    • 0028219293 scopus 로고
    • Localization and characterization of gelsolin in nervous tissues: Gelsolin is specifically enriched in myelin-forming cells
    • Tanaka J., Sobue K. Localization and characterization of gelsolin in nervous tissues: gelsolin is specifically enriched in myelin-forming cells. J. Neurosci. 14:1994;1038-1052.
    • (1994) J. Neurosci. , vol.14 , pp. 1038-1052
    • Tanaka, J.1    Sobue, K.2
  • 26
    • 0027379395 scopus 로고
    • Characterization of β-amyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey C., Lee D., Keim P., Lieberburg I., Schenk D.B. Characterization of β-amyloid peptide from human cerebrospinal fluid. J. Neurochem. 61:1993;1965-1968.
    • (1993) J. Neurochem. , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 27
    • 0030604656 scopus 로고    scopus 로고
    • Promotion of synthetic amyloid β-peptide fibrillization by cell culture media and abolishment of fibrillization by serum
    • Wegiel J., Chauhan A., Wisniewski H.M., Nowakowski J., Wang K.C., Levine H. Promotion of synthetic amyloid β-peptide fibrillization by cell culture media and abolishment of fibrillization by serum. Neurosci. Lett. 211:1996;151-154.
    • (1996) Neurosci. Lett. , vol.211 , pp. 151-154
    • Wegiel, J.1    Chauhan, A.2    Wisniewski, H.M.3    Nowakowski, J.4    Wang, K.C.5    Levine, H.6
  • 28
  • 30
  • 31
    • 0028945660 scopus 로고
    • Evidence that Aβ 42 is the real culprit in Alzheimer's disease
    • Younkin S.G. Evidence that Aβ 42 is the real culprit in Alzheimer's disease. Ann. Neurol. 37:1995;287-288.
    • (1995) Ann. Neurol. , vol.37 , pp. 287-288
    • Younkin, S.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.