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Volumn 20, Issue 5, 2000, Pages 1657-1665

Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme

Author keywords

Alzheimer's disease; Amyloid protein degradation; Insulin degrading enzyme; Membrane proteins; Neurons; Oligomerization

Indexed keywords

AMYLOID BETA PROTEIN; CELL MEMBRANE PROTEIN; INSULINASE;

EID: 0034161516     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.20-05-01657.2000     Document Type: Article
Times cited : (449)

References (40)
  • 3
    • 0029811040 scopus 로고    scopus 로고
    • Association of insulin-degrading enzyme with a 70 kDa cytosolic protein in hepatoma cells
    • Authier F, Cameron PH, Taupin V (1996a) Association of insulin-degrading enzyme with a 70 kDa cytosolic protein in hepatoma cells. Biochem J 319:149-158.
    • (1996) Biochem J , vol.319 , pp. 149-158
    • Authier, F.1    Cameron, P.H.2    Taupin, V.3
  • 5
    • 0027410472 scopus 로고
    • The rat insulin-degrading enzyme. Molecular cloning and characterization of tissue-specific transcripts
    • Baumeister H, Muller D, Rehbein M, Richter D (1993) The rat insulin-degrading enzyme. Molecular cloning and characterization of tissue-specific transcripts. FEBS Lett 317:250-254.
    • (1993) FEBS Lett , vol.317 , pp. 250-254
    • Baumeister, H.1    Muller, D.2    Rehbein, M.3    Richter, D.4
  • 6
    • 0033605607 scopus 로고    scopus 로고
    • Insulin-degrading enzyme in the Alzheimer's disease brain: Prominent localization in neurons and senile plaques
    • Bernstein HG, Ansorge S, Riederer P, Reiser M, Frolich L, Bogerts B (1999) Insulin-degrading enzyme in the Alzheimer's disease brain: prominent localization in neurons and senile plaques. Neurosci Lett 263:161-164.
    • (1999) Neurosci Lett , vol.263 , pp. 161-164
    • Bernstein, H.G.1    Ansorge, S.2    Riederer, P.3    Reiser, M.4    Frolich, L.5    Bogerts, B.6
  • 7
    • 0031030053 scopus 로고    scopus 로고
    • Preferential absorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ1-42, in differentiated PC12
    • Burdick D, Kosmoski J, Knauer MF, Glabe CG (1997) Preferential absorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ1-42, in differentiated PC12. Brain Res 740:275-284.
    • (1997) Brain Res , vol.740 , pp. 275-284
    • Burdick, D.1    Kosmoski, J.2    Knauer, M.F.3    Glabe, C.G.4
  • 8
    • 0030787591 scopus 로고    scopus 로고
    • Insulin-degrading enzyme does not require peroxisomal localization for insulin degradation
    • Chesneau V, Perlman RK, Li W, Keller G-A, Rosner MR (1997) Insulin-degrading enzyme does not require peroxisomal localization for insulin degradation. Endocrinology 138:3444-3451.
    • (1997) Endocrinology , vol.138 , pp. 3444-3451
    • Chesneau, V.1    Perlman, R.K.2    Li, W.3    Keller, G.-A.4    Rosner, M.R.5
  • 10
    • 0031907459 scopus 로고    scopus 로고
    • Cerebrospinal fluid and plasma insulin levels in Alzheimer's disease: Relationship to severity of dementia and apolipoprotein E genotype
    • Craft S, Peskind E, Schwartz MW, Schellenberg GD, Raskind M, Porte Jr D (1998) Cerebrospinal fluid and plasma insulin levels in Alzheimer's disease: relationship to severity of dementia and apolipoprotein E genotype. Neurology 50:164-168.
    • (1998) Neurology , vol.50 , pp. 164-168
    • Craft, S.1    Peskind, E.2    Schwartz, M.W.3    Schellenberg, G.D.4    Raskind, M.5    Porte D., Jr.6
  • 11
    • 0018763489 scopus 로고
    • Insulin degradation by liver cell membranes
    • Duckworth WC (1979) Insulin degradation by liver cell membranes. Endocrinology 104:1758-1763.
    • (1979) Endocrinology , vol.104 , pp. 1758-1763
    • Duckworth, W.C.1
  • 12
    • 0024062933 scopus 로고
    • Insulin degradation: Mechanisms, products and significance
    • Duckworth WC (1988) Insulin degradation: mechanisms, products and significance. Endocr Rev 9:319-345.
    • (1988) Endocr Rev , vol.9 , pp. 319-345
    • Duckworth, W.C.1
  • 14
    • 0024525751 scopus 로고
    • An insulin epidermal growth factor-binding protein from Drosophila has insulin-degrading activity
    • Garcia JV, Stoppelli MP, Decker SJ, Rosner MR (1989) An insulin epidermal growth factor-binding protein from Drosophila has insulin-degrading activity. J Cell Biol 108:177-182.
    • (1989) J Cell Biol , vol.108 , pp. 177-182
    • Garcia, J.V.1    Stoppelli, M.P.2    Decker, S.J.3    Rosner, M.R.4
  • 16
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ (1992) Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 357:500-503.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 19
    • 0026728215 scopus 로고
    • Secretion of peptides and proteins lacking hydrophobic signal sequences: The role of adenosine triphosphate-driven membrane translocators
    • Kuchler K, Thorner J (1992) Secretion of peptides and proteins lacking hydrophobic signal sequences: the role of adenosine triphosphate-driven membrane translocators. Endocr Rev 13:499-514.
    • (1992) Endocr Rev , vol.13 , pp. 499-514
    • Kuchler, K.1    Thorner, J.2
  • 20
    • 0027964969 scopus 로고
    • Inducible expression and cellular localization of insulin-degrading enzyme in a stably transfected cell line
    • Kuo W-L, Gehm BD, Rosner MR, Li W, Keller G (1994) Inducible expression and cellular localization of insulin-degrading enzyme in a stably transfected cell line. J Biol Chem 269:22599-22606.
    • (1994) J Biol Chem , vol.269 , pp. 22599-22606
    • Kuo, W.-L.1    Gehm, B.D.2    Rosner, M.R.3    Li, W.4    Keller, G.5
  • 21
    • 0028176821 scopus 로고
    • Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • Kurochkin IV, Goto S (1994) Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett 345:33-37.
    • (1994) FEBS Lett , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 22
    • 0029804989 scopus 로고    scopus 로고
    • Degradation of Alzheimer's beta-amyloid protein by human cathepsin D
    • McDermott JR, Gibson AM (1996) Degradation of Alzheimer's beta-amyloid protein by human cathepsin D. NeuroReport 7:2163-2166.
    • (1996) NeuroReport , vol.7 , pp. 2163-2166
    • McDermott, J.R.1    Gibson, A.M.2
  • 23
    • 0030902635 scopus 로고    scopus 로고
    • Degradation of Alzheimer's beta-amyloid protein by serine protease activity in brain microvessels
    • McDermott JR, Gibson AM (1997) Degradation of Alzheimer's beta-amyloid protein by serine protease activity in brain microvessels. Neurosci Res Commun 20:93-102.
    • (1997) Neurosci Res Commun , vol.20 , pp. 93-102
    • McDermott, J.R.1    Gibson, A.M.2
  • 24
    • 0021333892 scopus 로고
    • Partial purification and characterization of insulin protease and its intracellular inhibitor from rat liver
    • McKenzie RA, Burghen GA (1984) Partial purification and characterization of insulin protease and its intracellular inhibitor from rat liver. Arch Biochem Biophys 229:604-611.
    • (1984) Arch Biochem Biophys , vol.229 , pp. 604-611
    • McKenzie, R.A.1    Burghen, G.A.2
  • 25
    • 0031890884 scopus 로고    scopus 로고
    • Proteolytic degradation of Alzheimer's disease amyloid β-peptide by a metalloproteinase from microglia cells
    • Mentlein R, Ludwig R, Martensen I (1998) Proteolytic degradation of Alzheimer's disease amyloid β-peptide by a metalloproteinase from microglia cells. J Neurochem 70:721-726.
    • (1998) J Neurochem , vol.70 , pp. 721-726
    • Mentlein, R.1    Ludwig, R.2    Martensen, I.3
  • 26
    • 0033605325 scopus 로고    scopus 로고
    • Internalization and resistance to degradation of Alzheimer's Aβ 1-42 at nanomolar concentrations in THP-1 human monocytic cell line
    • Morelli L, Giambartolomei GH, Prat MI, Castano EM (1999) Internalization and resistance to degradation of Alzheimer's Aβ 1-42 at nanomolar concentrations in THP-1 human monocytic cell line. Neu-rosci Lett 262:5-8.
    • (1999) Neu-rosci Lett , vol.262 , pp. 5-8
    • Morelli, L.1    Giambartolomei, G.H.2    Prat, M.I.3    Castano, E.M.4
  • 27
    • 0026527618 scopus 로고
    • Affinity purification of insulin-degrading enzyme and its endogenous inhibitor from rat liver
    • Ogawa W, Shii K, Yonezawa K, Baba S, Yokono K (1992) Affinity purification of insulin-degrading enzyme and its endogenous inhibitor from rat liver. J Biol Chem 267:1310-1316.
    • (1992) J Biol Chem , vol.267 , pp. 1310-1316
    • Ogawa, W.1    Shii, K.2    Yonezawa, K.3    Baba, S.4    Yokono, K.5
  • 28
    • 0028587344 scopus 로고
    • Identification of zinc ligands of the insulin-degrading enzyme
    • Perlman RK, Rosner MR (1994) Identification of zinc ligands of the insulin-degrading enzyme. J Biol Chem 269:33140-33145.
    • (1994) J Biol Chem , vol.269 , pp. 33140-33145
    • Perlman, R.K.1    Rosner, M.R.2
  • 29
    • 0027454093 scopus 로고
    • Functional analysis of conserved residues in the active site of insulin-degrading enzyme
    • Perlman RK, Gehm BD, Kuo WL, Rosner MR (1993) Functional analysis of conserved residues in the active site of insulin-degrading enzyme. J Biol Chem 268:21538-21544.
    • (1993) J Biol Chem , vol.268 , pp. 21538-21544
    • Perlman, R.K.1    Gehm, B.D.2    Kuo, W.L.3    Rosner, M.R.4
  • 31
    • 0032539975 scopus 로고    scopus 로고
    • Oligomerization of endogenous and synthetic amyloid ß-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red
    • Podlisny MB, Walsh DM, Amarante P, Ostaszewski BL, Stimson ER, Maggio JE, Teplow DB, Selkoe DJ (1998) Oligomerization of endogenous and synthetic amyloid ß-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 37:3602-3611.
    • (1998) Biochemistry , vol.37 , pp. 3602-3611
    • Podlisny, M.B.1    Walsh, D.M.2    Amarante, P.3    Ostaszewski, B.L.4    Stimson, E.R.5    Maggio, J.E.6    Teplow, D.B.7    Selkoe, D.J.8
  • 32
    • 1842367306 scopus 로고    scopus 로고
    • Degradation of amyloid β-protein by a metalloprotease secreted by microglia and other neural and non-neural cells
    • Qiu WQ, Ye Z, Kholodenko D, Seubert P, Selkoe DJ (1997) Degradation of amyloid β-protein by a metalloprotease secreted by microglia and other neural and non-neural cells. J Biol Chem 272:6641-6646.
    • (1997) J Biol Chem , vol.272 , pp. 6641-6646
    • Qiu, W.Q.1    Ye, Z.2    Kholodenko, D.3    Seubert, P.4    Selkoe, D.J.5
  • 34
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of beta-amyloid precursor protein and prescnilin in Alzheimer's disease
    • Selkoe DJ (1998) The cell biology of beta-amyloid precursor protein and prescnilin in Alzheimer's disease. Trends Cell Biol 8:447-453.
    • (1998) Trends Cell Biol , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 35
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimcr's disease
    • Selkoe DJ (1999) Translating cell biology into therapeutic advances in Alzheimcr's disease. Nature 399:A23-A31.
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 36
    • 0031550507 scopus 로고    scopus 로고
    • Overexpression of insulin degrading enzyme: Cellular localization and effects on insulin signaling
    • Seta KA, Roth RA (1997) Overexpression of insulin degrading enzyme: cellular localization and effects on insulin signaling. Biochem Biophys Res Commun 231:167-171.
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 167-171
    • Seta, K.A.1    Roth, R.A.2
  • 37
    • 0022271537 scopus 로고
    • Covalent linkage of 1251-insulin to a cytosolic insulin-degrading enzyme
    • Shii K, Baba S, Yokono K, Roth RA (1985) Covalent linkage of 1251-insulin to a cytosolic insulin-degrading enzyme. J Biol Chem 260:6503-6506.
    • (1985) J Biol Chem , vol.260 , pp. 6503-6506
    • Shii, K.1    Baba, S.2    Yokono, K.3    Roth, R.A.4
  • 39
    • 0033603328 scopus 로고    scopus 로고
    • Metalloendopeptidase EC 3.4.24.15 is necessary for Alzheimer's amyloid-β peptide degradation
    • Yamin R, Malgeri EG, Sloane JA, McGraw WT, Abraham CR (1999) Metalloendopeptidase EC 3.4.24.15 is necessary for Alzheimer's amyloid-β peptide degradation. J Biol Chem 274:18777-18784.
    • (1999) J Biol Chem , vol.274 , pp. 18777-18784
    • Yamin, R.1    Malgeri, E.G.2    Sloane, J.A.3    McGraw, W.T.4    Abraham, C.R.5
  • 40
    • 0020201977 scopus 로고
    • Identification of insulin-degrading enzyme on the surface of cultured human lymphocytes, rat hepatoma cells, and primary cultures of rat hepatocytes
    • Yokono K, Roth RA, Baba S (1982) Identification of insulin-degrading enzyme on the surface of cultured human lymphocytes, rat hepatoma cells, and primary cultures of rat hepatocytes. Endocrinology 111:1102-1108.
    • (1982) Endocrinology , vol.111 , pp. 1102-1108
    • Yokono, K.1    Roth, R.A.2    Baba, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.