메뉴 건너뛰기




Volumn 7, Issue 4, 2012, Pages

Somatostatin modulates insulin-degrading-enzyme metabolism: Implications for the regulation of microglia activity in AD

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; INSULINASE; OCTREOTIDE; SOMATOSTATIN; AMYLOID BETA PROTEIN[1-40]; GELATINASE B; PEPTIDE FRAGMENT;

EID: 84859241651     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0034376     Document Type: Article
Times cited : (39)

References (43)
  • 2
    • 0035997231 scopus 로고    scopus 로고
    • Biogenesis and metabolism of Alzheimer's disease Aß amyloid peptides
    • Evin G, Weidemann A, (2002) Biogenesis and metabolism of Alzheimer's disease Aß amyloid peptides. Peptides 23: 1285-1297.
    • (2002) Peptides , vol.23 , pp. 1285-1297
    • Evin, G.1    Weidemann, A.2
  • 4
    • 0029852887 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1-40)
    • Backstrom JR, Lim GP, Cullen MJ, Tökés ZA, (1996) Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1-40). J Neurosci 15: 7910-7919.
    • (1996) J Neurosci , vol.15 , pp. 7910-7919
    • Backstrom, J.R.1    Lim, G.P.2    Cullen, M.J.3    Tökés, Z.A.4
  • 5
    • 0000398342 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation
    • Qiu WQ, Walsh DM, Ye Z, Vekrellis K, Zhang J, (1998) Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. J Biol Chem 273: 32730-32738.
    • (1998) J Biol Chem , vol.273 , pp. 32730-32738
    • Qiu, W.Q.1    Walsh, D.M.2    Ye, Z.3    Vekrellis, K.4    Zhang, J.5
  • 6
    • 0035947207 scopus 로고    scopus 로고
    • Metabolic regulation of brain A. by neprilysin
    • Iwata N, Tsubuki S, Takaki T, (2001) Metabolic regulation of brain A. by neprilysin. Science 292: 1550-1552.
    • (2001) Science , vol.292 , pp. 1550-1552
    • Iwata, N.1    Tsubuki, S.2    Takaki, T.3
  • 8
    • 0031690490 scopus 로고    scopus 로고
    • Insulin degradation: progress and potential
    • Duckworth WC, Bennett RG, Hamel FG, (1998) Insulin degradation: progress and potential. Endocr Rev 19: 608-624.
    • (1998) Endocr Rev , vol.19 , pp. 608-624
    • Duckworth, W.C.1    Bennett, R.G.2    Hamel, F.G.3
  • 9
    • 0037219221 scopus 로고    scopus 로고
    • Reduced hippocampal insulin-degrading zenzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele
    • Cook DG, Leverenz JB, McMillan PJ, Kulstad JJ, Ericksen S, et al. (2003) Reduced hippocampal insulin-degrading zenzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele. Am J Pathol 162: 313-319.
    • (2003) Am J Pathol , vol.162 , pp. 313-319
    • Cook, D.G.1    Leverenz, J.B.2    McMillan, P.J.3    Kulstad, J.J.4    Ericksen, S.5
  • 10
    • 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, Frölich L, et al. (1999) Insulin degrading enzyme in the Alzheimer's disease brain: prominent localization in neurons and senile plaques. Neuroscience Letters 263: 161-164.
    • (1999) Neuroscience Letters , vol.263 , pp. 161-164
    • Bernstein, H.G.1    Ansorge, S.2    Riederer, P.3    Reiser, M.4    Frölich, L.5
  • 11
    • 0025119656 scopus 로고
    • Insulin-degrading enzyme: stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes
    • Affholter JA, Hsieh CL, Francke U, Roth RA, (1990) Insulin-degrading enzyme: stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes. Mol Endocrinol 8: 1125-1135.
    • (1990) Mol Endocrinol , vol.8 , pp. 1125-1135
    • Affholter, J.A.1    Hsieh, C.L.2    Francke, U.3    Roth, R.A.4
  • 12
    • 0025824601 scopus 로고
    • Localization of the gene encoding insulin-degrading-enzyme to human chromosome10, bands q23q25
    • Espinosa R, Lemons RS, Perlman RK, Kuo WL, Rosner MR, et al. (1991) Localization of the gene encoding insulin-degrading-enzyme to human chromosome10, bands q23q25. Cytog Cell Gen 57: 184-186.
    • (1991) Cytog Cell Gen , vol.57 , pp. 184-186
    • Espinosa, R.1    Lemons, R.S.2    Perlman, R.K.3    Kuo, W.L.4    Rosner, M.R.5
  • 13
    • 1642290835 scopus 로고    scopus 로고
    • Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid beta-protein
    • Farris W, Mansourian S, Leissring MA, Eckman EA, Bertram L, et al. (2004) Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid beta-protein. Am J Pathol 164: 1425-1434.
    • (2004) Am J Pathol , vol.164 , pp. 1425-1434
    • Farris, W.1    Mansourian, S.2    Leissring, M.A.3    Eckman, E.A.4    Bertram, L.5
  • 14
    • 1842765688 scopus 로고    scopus 로고
    • Genetic variants in a haplotype block spanning IDE are significantly associated with plasma Abeta42 levels and risk for Alzhimer disease
    • Ertekin-Taner N, Allen M, Fadale D, Scanlin L, Younkin L, et al. (2004) Genetic variants in a haplotype block spanning IDE are significantly associated with plasma Abeta42 levels and risk for Alzhimer disease. Hum Mutat 23: 334-342.
    • (2004) Hum Mutat , vol.23 , pp. 334-342
    • Ertekin-Taner, N.1    Allen, M.2    Fadale, D.3    Scanlin, L.4    Younkin, L.5
  • 15
    • 21444432879 scopus 로고    scopus 로고
    • Mutation screening of a haplotypes block around the insulin degrading enzyme gene and association with Alzheimer's disease
    • Feuk L, McCarthy S, Andersson B, Prince JA, Brookes AJ, (2005) Mutation screening of a haplotypes block around the insulin degrading enzyme gene and association with Alzheimer's disease. Am J Med Genet B Neuropsychiatr Genet 136: 69-71.
    • (2005) Am J Med Genet B Neuropsychiatr Genet , vol.136 , pp. 69-71
    • Feuk, L.1    McCarthy, S.2    Andersson, B.3    Prince, J.A.4    Brookes, A.J.5
  • 16
    • 34447556836 scopus 로고    scopus 로고
    • Positive association between risk for late-onset Alzheimer disease and genetic variation in IDE
    • Björk BF, Katzov H, Kehoe P, Fratiglioni L, Winblad B, et al. (2007) Positive association between risk for late-onset Alzheimer disease and genetic variation in IDE. Neurobiol Aging 28: 1374-1380.
    • (2007) Neurobiol Aging , vol.28 , pp. 1374-1380
    • Björk, B.F.1    Katzov, H.2    Kehoe, P.3    Fratiglioni, L.4    Winblad, B.5
  • 17
    • 58549093250 scopus 로고    scopus 로고
    • Somatostatin: a novel substrate and a modulator of insulin-degrading enzyme activity
    • Ciaccio C, Tundo GR, Grasso G, Spoto G, Marasco D, et al. (2009) Somatostatin: a novel substrate and a modulator of insulin-degrading enzyme activity. J Mol Biol 385: 1556-1567.
    • (2009) J Mol Biol , vol.385 , pp. 1556-1567
    • Ciaccio, C.1    Tundo, G.R.2    Grasso, G.3    Spoto, G.4    Marasco, D.5
  • 18
  • 19
    • 0035747677 scopus 로고    scopus 로고
    • Processing of neuropeptide Y, galanin, and somatostatin in the cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia
    • Nilsson CL, Brinkmalm A, Minthon L, Blennow K, Ekman R, (2001) Processing of neuropeptide Y, galanin, and somatostatin in the cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia. Peptides 22: 2105-2112.
    • (2001) Peptides , vol.22 , pp. 2105-2112
    • Nilsson, C.L.1    Brinkmalm, A.2    Minthon, L.3    Blennow, K.4    Ekman, R.5
  • 20
    • 34548835206 scopus 로고    scopus 로고
    • An update on somatostatin receptor signaling in native systems and new insights on their pathophysiology
    • Cervia D, Bagnoli P, (2007) An update on somatostatin receptor signaling in native systems and new insights on their pathophysiology. Pharmacol Ther 116: 322-341.
    • (2007) Pharmacol Ther , vol.116 , pp. 322-341
    • Cervia, D.1    Bagnoli, P.2
  • 21
    • 0032890435 scopus 로고    scopus 로고
    • A novel role for receptor associated protein in somatostatin modulation: implications for Alzheimer's disease
    • Van Uden E, Veinbergs I, Mallory M, Orlando R, Masliah E, (1999) A novel role for receptor associated protein in somatostatin modulation: implications for Alzheimer's disease. Neuroscience 88: 687-700.
    • (1999) Neuroscience , vol.88 , pp. 687-700
    • Van Uden, E.1    Veinbergs, I.2    Mallory, M.3    Orlando, R.4    Masliah, E.5
  • 22
    • 17644425569 scopus 로고    scopus 로고
    • Somatostatin regulates brain amyloid peptide A.42 through modulation of proteolytic degradation
    • Saito T, Iwata N, Tsubuki S, Takaki T, Takano J, (2005) Somatostatin regulates brain amyloid peptide A.42 through modulation of proteolytic degradation. Nat Medicine 11: 434-439.
    • (2005) Nat Medicine , vol.11 , pp. 434-439
    • Saito, T.1    Iwata, N.2    Tsubuki, S.3    Takaki, T.4    Takano, J.5
  • 23
    • 0032737079 scopus 로고    scopus 로고
    • Enhancement of memory in Alzheimer disease with insulin and somatostatin, but not glucose
    • Craft S, Asthana S, Newcomer JW, Wilkinson CW, Matos IT, et al. (1999) Enhancement of memory in Alzheimer disease with insulin and somatostatin, but not glucose. Arch Gen Psych 56: 1135-1140.
    • (1999) Arch Gen Psych , vol.56 , pp. 1135-1140
    • Craft, S.1    Asthana, S.2    Newcomer, J.W.3    Wilkinson, C.W.4    Matos, I.T.5
  • 24
    • 75149132487 scopus 로고    scopus 로고
    • Effects of insulin and octreotide on memory and growth hormone in Alzheimer's disease
    • Watson GS, Baker LD, Cholerton BA, Rhoads KW, Merriam GR, et al. (2009) Effects of insulin and octreotide on memory and growth hormone in Alzheimer's disease. J Alzheimers Dis 18: 595-602.
    • (2009) J Alzheimers Dis , vol.18 , pp. 595-602
    • Watson, G.S.1    Baker, L.D.2    Cholerton, B.A.3    Rhoads, K.W.4    Merriam, G.R.5
  • 25
    • 1642514618 scopus 로고    scopus 로고
    • The potential of activation of somatostatinergic neurotransmission with FK960 in Alzheimer's disease
    • Doggrell SA, (2004) The potential of activation of somatostatinergic neurotransmission with FK960 in Alzheimer's disease. Expert Opin Investig Drugs 13: 69-72.
    • (2004) Expert Opin Investig Drugs , vol.13 , pp. 69-72
    • Doggrell, S.A.1
  • 26
    • 28544441888 scopus 로고    scopus 로고
    • FK962, a novel enhancer of somatostatin release, exerts cognitive-enhancing actions in rats
    • Tokita K, Inoue T, Yamazaki S, Wang F, Yamaji T, et al. (2005) FK962, a novel enhancer of somatostatin release, exerts cognitive-enhancing actions in rats. Eur J Pharmacol 527: 111-120.
    • (2005) Eur J Pharmacol , vol.527 , pp. 111-120
    • Tokita, K.1    Inoue, T.2    Yamazaki, S.3    Wang, F.4    Yamaji, T.5
  • 27
    • 30344479822 scopus 로고    scopus 로고
    • Pharmacological strategies for the prevention of Alzheimer's disease
    • Doraiswamy PM, Xiong GL, (2006) Pharmacological strategies for the prevention of Alzheimer's disease. Expert Opin Pharmacother 7: 1-10.
    • (2006) Expert Opin Pharmacother , vol.7 , pp. 1-10
    • Doraiswamy, P.M.1    Xiong, G.L.2
  • 28
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation,secondary pathology, and premature death
    • Leissring MA, Farris W, Chang AY, Walsh DM, Wu X, et al. (2003) Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation,secondary pathology, and premature death. Neuron 40: 1087-1093.
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5
  • 29
    • 33747680357 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 degrades amyloid-beta fibrils in vitro and compact plaques in situ
    • Yan P, Hu X, Song H, Yin K, Bateman RJ, (2006) Matrix metalloproteinase-9 degrades amyloid-beta fibrils in vitro and compact plaques in situ. J Biol Chem 281: 24566-24574.
    • (2006) J Biol Chem , vol.281 , pp. 24566-24574
    • Yan, P.1    Hu, X.2    Song, H.3    Yin, K.4    Bateman, R.J.5
  • 30
    • 0032189250 scopus 로고    scopus 로고
    • Receptors and effects of the inhibitory neuropeptide somatostatin in microglial cells
    • Feindt J, Schmidt A, Mentlein R, (1998) Receptors and effects of the inhibitory neuropeptide somatostatin in microglial cells. Brain Res Mol Brain Res 60: 228-233.
    • (1998) Brain Res Mol Brain Res , vol.60 , pp. 228-233
    • Feindt, J.1    Schmidt, A.2    Mentlein, R.3
  • 32
    • 0030037586 scopus 로고    scopus 로고
    • Beta-amyloid peptide secretion by a microglial cell line is induced by beta-amyloid-(25-35) and lipopolysaccharide
    • Bitting L, Naidu A, Cordell B, Murphy GM, (1996) Beta-amyloid peptide secretion by a microglial cell line is induced by beta-amyloid-(25-35) and lipopolysaccharide. J Biol Chem 5: 16084-16089.
    • (1996) J Biol Chem , vol.5 , pp. 16084-16089
    • Bitting, L.1    Naidu, A.2    Cordell, B.3    Murphy, G.M.4
  • 33
    • 51149120624 scopus 로고    scopus 로고
    • Microglial dysfunction and defective ß-amyloid clearance pathways in aging Alzheimer's disease mice
    • Hickman S, Allison EK, Khoury E, (2008) Microglial dysfunction and defective ß-amyloid clearance pathways in aging Alzheimer's disease mice. J Neurosc 13: 8354-8360.
    • (2008) J Neurosc , vol.13 , pp. 8354-8360
    • Hickman, S.1    Allison, E.K.2    Khoury, E.3
  • 34
    • 0019313317 scopus 로고
    • Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissues
    • McCarty MC, De Vellis J, (1980) Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissues. J Cell Biol 85: 890-902.
    • (1980) J Cell Biol , vol.85 , pp. 890-902
    • McCarty, M.C.1    De Vellis, J.2
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0019755779 scopus 로고
    • Somatostatin half-life: a case report on one healthy volunteer and a three month follow up
    • Bethge N, Diel F, Rösick M, Holz J, (1981) Somatostatin half-life: a case report on one healthy volunteer and a three month follow up. Horm Metabl Res 13: 709-710.
    • (1981) Horm Metabl Res , vol.13 , pp. 709-710
    • Bethge, N.1    Diel, F.2    Rösick, M.3    Holz, J.4
  • 37
    • 0028826393 scopus 로고
    • Expression of somatostatin receptor subtypes in cultured astrocytes and gliomas
    • Feindt J, Becker I, Blömer U, Hugo HH, Mehdorn HM, et al. (1995) Expression of somatostatin receptor subtypes in cultured astrocytes and gliomas. J Neurochem 5: 1997-2005.
    • (1995) J Neurochem , vol.5 , pp. 1997-2005
    • Feindt, J.1    Becker, I.2    Blömer, U.3    Hugo, H.H.4    Mehdorn, H.M.5
  • 38
    • 10944228564 scopus 로고    scopus 로고
    • Insulin-degrading enzyme as a downstream target of insulin receptor signaling cascade: implications for Alzheimer's disease intervention
    • Zhao L, Teter B, Morihara T, Lim GP, Ambegaokar SS, (2004) Insulin-degrading enzyme as a downstream target of insulin receptor signaling cascade: implications for Alzheimer's disease intervention. J Neurosci 8: 11120-11126.
    • (2004) J Neurosci , vol.8 , pp. 11120-11126
    • Zhao, L.1    Teter, B.2    Morihara, T.3    Lim, G.P.4    Ambegaokar, S.S.5
  • 39
    • 33646089457 scopus 로고    scopus 로고
    • Gene expression changes by amyloid beta peptide-stimulated human postmortem brain microglia identify activation of multiple inflammatory processes
    • Walker D, Link J, Lue L, Dalsing-Hernandez JE, Boyes BE, (2006) Gene expression changes by amyloid beta peptide-stimulated human postmortem brain microglia identify activation of multiple inflammatory processes. J Leukoc Biol 3: 596-610.
    • (2006) J Leukoc Biol , vol.3 , pp. 596-610
    • Walker, D.1    Link, J.2    Lue, L.3    Dalsing-Hernandez, J.E.4    Boyes, B.E.5
  • 42
    • 0020363575 scopus 로고
    • SMS 201-995: a very potent and selective octapeptide analogue of somatostatin with prolonged action
    • Bauer W, Briner U, Doepfner W, Haller R, Huguenin R, et al. (1982) SMS 201-995: a very potent and selective octapeptide analogue of somatostatin with prolonged action. Life Sci 31: 1133-1140.
    • (1982) Life Sci , vol.31 , pp. 1133-1140
    • Bauer, W.1    Briner, U.2    Doepfner, W.3    Haller, R.4    Huguenin, R.5
  • 43
    • 36749017492 scopus 로고    scopus 로고
    • Manipulation of microglial activation as a therapeutic strategy in Alzheimer's disease
    • Shie FS, Woltjer RL, (2007) Manipulation of microglial activation as a therapeutic strategy in Alzheimer's disease. Curr Med Chem 14: 2865-2871.
    • (2007) Curr Med Chem , vol.14 , pp. 2865-2871
    • Shie, F.S.1    Woltjer, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.