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Volumn 11, Issue 4, 2005, Pages 434-439

Somatostatin regulates brain amyloid β peptide Aβ42 through modulation of proteolytic degradation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; MEMBRANE METALLOENDOPEPTIDASE; NEUROPEPTIDE; SOMATOSTATIN; SOMATOSTATIN RECEPTOR;

EID: 17644425569     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm1206     Document Type: Article
Times cited : (320)

References (29)
  • 1
    • 0031041781 scopus 로고    scopus 로고
    • Somatostatin and brain-derived neurotrophic factor mRNA expression in the primate brain: Decreased levels of mRNA during aging
    • Hayashi, M., Yamashita, A. & Shimizu, K. Somatostatin and brain-derived neurotrophic factor mRNA expression in the primate brain: decreased levels of mRNA during aging. Brain Res. 749, 283-289 (1997).
    • (1997) Brain Res. , vol.749 , pp. 283-289
    • Hayashi, M.1    Yamashita, A.2    Shimizu, K.3
  • 2
    • 3042631024 scopus 로고    scopus 로고
    • Gene regulation and DNA damage in the ageing human brain
    • Lu, T. et al. Gene regulation and DNA damage in the ageing human brain. Nature 429, 883-891 (2004).
    • (2004) Nature , vol.429 , pp. 883-891
    • Lu, T.1
  • 3
    • 0019256571 scopus 로고
    • Reduced somatostatin-like immunoreactivity in cerebral cortex from cases of Alzheimer's disease and Alzheimer senile dementia
    • Davies, P., Katzman, R. & Terry, R.D. Reduced somatostatin-like immunoreactivity in cerebral cortex from cases of Alzheimer's disease and Alzheimer senile dementia. Nature 288, 279-280 (1980).
    • (1980) Nature , vol.288 , pp. 279-280
    • Davies, P.1    Katzman, R.2    Terry, R.D.3
  • 4
    • 0036934833 scopus 로고    scopus 로고
    • Interstitial cells subjacent to the entorhinal region expressing somatostatin-28 immunoreactivity are susceptible to development of Alzheimer's disease-related cytoskeletal changes
    • van de Nes, J.A.P., Sandmann-Keil, D. & Braak, H. Interstitial cells subjacent to the entorhinal region expressing somatostatin-28 immunoreactivity are susceptible to development of Alzheimer's disease-related cytoskeletal changes. Acta Neuropathol. 104, 351-356 (2002).
    • (2002) Acta Neuropathol. , vol.104 , pp. 351-356
    • Van De Nes, J.A.P.1    Sandmann-Keil, D.2    Braak, H.3
  • 5
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. & Selkoe, D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356 (2002).
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 6
    • 0033621739 scopus 로고    scopus 로고
    • 1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
    • 2000
    • 1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition. Nat. Med. 6, 143-151 (2000).
    • (2000) Nat. Med. , vol.6 , pp. 143-151
    • Iwata, N.1
  • 7
    • 0035947207 scopus 로고    scopus 로고
    • Metabolic regulation of brain Aβ by neprilysin
    • Iwata, N. et al. Metabolic regulation of brain Aβ by neprilysin. Science 292, 1550-1552 (2001).
    • (2001) Science , vol.292 , pp. 1550-1552
    • Iwata, N.1
  • 8
    • 0037010286 scopus 로고    scopus 로고
    • Region-specific reduction of Aβ-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging
    • Iwata, N., Takaki, Y., Fukami, S., Tsubuki, S. & Saido, T.C. Region-specific reduction of Aβ-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging. J. Neurosci. Res. 70, 493-500 (2002).
    • (2002) J. Neurosci. Res. , vol.70 , pp. 493-500
    • Iwata, N.1    Takaki, Y.2    Fukami, S.3    Tsubuki, S.4    Saido, T.C.5
  • 9
    • 0035846826 scopus 로고    scopus 로고
    • Reduced neprilysin in high plaque areas of Alzheimer brain: A possible relationship to deficient degradation of β-amyloid peptide
    • Yasojima, K., Akiyama, H., McGeer, E.G. & McGeer, P.L. Reduced neprilysin in high plaque areas of Alzheimer brain: a possible relationship to deficient degradation of β-amyloid peptide. Neurosci. Lett. 297, 97-100 (2001).
    • (2001) Neurosci. Lett. , vol.297 , pp. 97-100
    • Yasojima, K.1    Akiyama, H.2    McGeer, E.G.3    McGeer, P.L.4
  • 10
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring, M.A. et al. Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40, 1087-1093 (2003).
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1
  • 11
    • 9144266913 scopus 로고    scopus 로고
    • Presynaptic localization of neprilysin contributes to efficient clearance of amyloid-β peptide in mouse brain
    • Iwata, N. et al. Presynaptic localization of neprilysin contributes to efficient clearance of amyloid-β peptide in mouse brain. J. Neurosci. 24, 991-998 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 991-998
    • Iwata, N.1
  • 12
    • 0032402711 scopus 로고    scopus 로고
    • Morphine preconditioning attenuates neutrophil activation in rat models of myocardial infarction
    • Wang, T.-L., Chang, H., Hung, C.-R. & Tseng, Y.-Z. Morphine preconditioning attenuates neutrophil activation in rat models of myocardial infarction. Cardiovasc. Res. 40, 557-563 (1998).
    • (1998) Cardiovasc. Res. , vol.40 , pp. 557-563
    • Wang, T.-L.1    Chang, H.2    Hung, C.-R.3    Tseng, Y.-Z.4
  • 13
    • 0035525740 scopus 로고    scopus 로고
    • Negative feedback on the effect of stem cell factor on hematopoiesis is partly mediated through neutral endopeptidase activity on substance P: A combined functional and proteomic study
    • Joshi, D.D. et al. Negative feedback on the effect of stem cell factor on hematopoiesis is partly mediated through neutral endopeptidase activity on substance P: a combined functional and proteomic study. Blood 98, 2697-2706 (2001).
    • (2001) Blood , vol.98 , pp. 2697-2706
    • Joshi, D.D.1
  • 14
    • 3142721151 scopus 로고    scopus 로고
    • Effects of neprilysin chimeric proteins targeted to subcellular compartments on amyloid β peptide clearance in primary neurons
    • Hama, E., Shirotani, K., Iwata, N. & Saido, T.C. Effects of neprilysin chimeric proteins targeted to subcellular compartments on amyloid β peptide clearance in primary neurons. J. Biol. Chem. 279, 30259-30269 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 30259-30269
    • Hama, E.1    Shirotani, K.2    Iwata, N.3    Saido, T.C.4
  • 15
    • 0035877747 scopus 로고    scopus 로고
    • Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases
    • Shirotani, K. et al. Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases. J. Biol. Chem. 276, 21895-21901 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21895-21901
    • Shirotani, K.1
  • 17
    • 0031028364 scopus 로고    scopus 로고
    • Somatostatin receptor subtype specificity in human fetal pituitary cultures
    • Shimon, I. et al. Somatostatin receptor subtype specificity in human fetal pituitary cultures. J. Clin. Invest. 99, 789-798 (1997).
    • (1997) J. Clin. Invest. , vol.99 , pp. 789-798
    • Shimon, I.1
  • 18
    • 17644364495 scopus 로고    scopus 로고
    • G-protein regulation of signal transduction in Alzheimer's disease
    • Garcia-Jimenez, A., Fastbom, J., Winbland, B. & Cowburn, R.F. G-protein regulation of signal transduction in Alzheimer's disease. Brain Aging 2, 7-15 (2002).
    • (2002) Brain Aging , vol.2 , pp. 7-15
    • Garcia-Jimenez, A.1    Fastbom, J.2    Winbland, B.3    Cowburn, R.F.4
  • 20
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock, G., De Angelis, D. A. & Rothman, J.E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 334, 192-195 (1998).
    • (1998) Nature , vol.334 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 21
    • 0026453393 scopus 로고
    • Molecular cloning and functional expression of a brain-specific somatostatin receptor
    • Bruno, J.F., Xu, Y., Song, J. & Berelowitz, M. Molecular cloning and functional expression of a brain-specific somatostatin receptor. Proc. Natl. Acad. Sci. USA 89, 11151-11155 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11151-11155
    • Bruno, J.F.1    Xu, Y.2    Song, J.3    Berelowitz, M.4
  • 22
    • 1642514618 scopus 로고    scopus 로고
    • The potential of activation of somatostatinergic neurotransmission with FK960 in Alzheimer's disease
    • Doggrell, S.A. The potential of activation of somatostatinergic neurotransmission with FK960 in Alzheimer's disease. Expert Opin. Investig. Drugs 13, 69-72 (2004).
    • (2004) Expert Opin. Investig. Drugs , vol.13 , pp. 69-72
    • Doggrell, S.A.1
  • 23
    • 17644398302 scopus 로고    scopus 로고
    • β-secretase: Progress and open questions
    • (ed. Saido, T.C.) (Landes Bioscience, Georgetown)
    • Citron, M. β-Secretase: progress and open questions. in Aβ Metabolism and Alzheimer's Disease, (ed. Saido, T.C.) 17-25 (Landes Bioscience, Georgetown, 2003).
    • (2003) Aβ Metabolism and Alzheimer's Disease , pp. 17-25
    • Citron, M.1
  • 24
    • 17644414577 scopus 로고    scopus 로고
    • γ-secretase and presenilin
    • (ed. Saido, T.C.) (Landes Bioscience, Georgetown)
    • Wolfe, M.S. γ-Secretase and presenilin. in Aβ Metabolism and Alzheimer's Disease. (ed. Saido, T.C.) 33-47 (Landes Bioscience, Georgetown, 2003).
    • (2003) Aβ Metabolism and Alzheimer's Disease , pp. 33-47
    • Wolfe, M.S.1
  • 25
    • 0035659917 scopus 로고    scopus 로고
    • Clearance of extracellular and cell-associated amyloid β peptide by viral expression of neprilysin in primary culture
    • Hama, E. et al. Clearance of extracellular and cell-associated amyloid β peptide by viral expression of neprilysin in primary culture. J. Biochem. 130, 721-726 (2001).
    • (2001) J. Biochem. , vol.130 , pp. 721-726
    • Hama, E.1
  • 26
    • 0024790716 scopus 로고
    • Histochemical visualization of neutral endopeptidase-24.11 (enkephalinase) activity in rat brain: Cellular localization and codistribution with enkephalins in the globus pallidus
    • Back, S.A. & Gorestein, C. Histochemical visualization of neutral endopeptidase-24.11 (enkephalinase) activity in rat brain: cellular localization and codistribution with enkephalins in the globus pallidus. J. Neurosci. 9, 4439-4455 (1989).
    • (1989) J. Neurosci. , vol.9 , pp. 4439-4455
    • Back, S.A.1    Gorestein, C.2
  • 27
    • 0033931805 scopus 로고    scopus 로고
    • Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues
    • Takano, J., Watanabe, M., Hitomi, K. & Maki, M. Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues. J. Biochem. 128, 83-92 (2000).
    • (2000) J. Biochem. , vol.128 , pp. 83-92
    • Takano, J.1    Watanabe, M.2    Hitomi, K.3    Maki, M.4
  • 28
    • 0037764868 scopus 로고    scopus 로고
    • Patterns of expression of neuropeptides in GABAergic nonprincipal neurons in the mouse hippocampus: Quantitative analysis with optical disector
    • Jinno, S. & Kosaka, T. Patterns of expression of neuropeptides in GABAergic nonprincipal neurons in the mouse hippocampus: Quantitative analysis with optical disector. J. Comp. Neurol. 461, 333-349 (2003).
    • (2003) J. Comp. Neurol. , vol.461 , pp. 333-349
    • Jinno, S.1    Kosaka, T.2
  • 29
    • 0032727561 scopus 로고    scopus 로고
    • Tyramide signal amplification method in multiple-label immunofluorescence confocal microscopy
    • Wang, G. et al. Tyramide signal amplification method in multiple-label immunofluorescence confocal microscopy. Methods 18, 459-464 (1999).
    • (1999) Methods , vol.18 , pp. 459-464
    • Wang, G.1


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