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Volumn 48, Issue 3, 2004, Pages 315-323

Effects of β-AP peptides on activation of the transcription factor NF-κB and in cell proliferation in glial cell cultures

Author keywords

Glial activation; Glial proliferation; NF B Transcription factor activation; Peptide aggregation; Amyloid

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID BETA PROTEIN[25-35]; GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TRANSCRIPTION FACTOR;

EID: 1242271257     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neures.2003.11.006     Document Type: Article
Times cited : (25)

References (17)
  • 1
    • 0032084331 scopus 로고    scopus 로고
    • The NF-κB/Rel family of proteins mediates Aβ-induced neurotoxicity and glial activation
    • Bales K.R., Du Y., Dodel R.C., Yan M.G., Hamilton-Byrd E., Paul S.M. The NF-κB/Rel family of proteins mediates Aβ-induced neurotoxicity and glial activation. Mol. Brain Res. 57:1998;63-72.
    • (1998) Mol. Brain Res. , vol.57 , pp. 63-72
    • Bales, K.R.1    Du, Y.2    Dodel, R.C.3    Yan, M.G.4    Hamilton-Byrd, E.5    Paul, S.M.6
  • 2
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB ten years after
    • Baeuerle P.A., Baltimore D. NF-κB ten years after. Cell. 87:1996;13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 3
    • 0035947056 scopus 로고    scopus 로고
    • Role of calmodulin in the differentiation/activation of microglial cells
    • Casal C., Tusell J.M., Serratosa J. Role of calmodulin in the differentiation/activation of microglial cells. Brain Res. 902:2001;101-107.
    • (2001) Brain Res. , vol.902 , pp. 101-107
    • Casal, C.1    Tusell, J.M.2    Serratosa, J.3
  • 4
    • 0037154851 scopus 로고    scopus 로고
    • Relationship between β-AP peptide aggregation and microglial activation
    • Casal C., Serratosa J., Tusell J.M. Relationship between β-AP peptide aggregation and microglial activation. Brain Res. 928:2002;76-84.
    • (2002) Brain Res. , vol.928 , pp. 76-84
    • Casal, C.1    Serratosa, J.2    Tusell, J.M.3
  • 5
    • 0032589298 scopus 로고    scopus 로고
    • Sodium salicilate and 17β-estradiol attenuate nuclear transcription factor NF-κB translocation in cultured rat astroglial cultures following exposure to amyloid Aβ 1-40 and lipopolysaccharides
    • Dodel R.C., Du Y., Bales K.R., Gao F., Paul S.M. Sodium salicilate and 17β-estradiol attenuate nuclear transcription factor NF-κB translocation in cultured rat astroglial cultures following exposure to amyloid Aβ 1-40 and lipopolysaccharides. J. Neurochem. 73:1999;1453-1460.
    • (1999) J. Neurochem. , vol.73 , pp. 1453-1460
    • Dodel, R.C.1    Du, Y.2    Bales, K.R.3    Gao, F.4    Paul, S.M.5
  • 6
    • 0022922108 scopus 로고
    • Characterization of ameboid microglia isolated from developing mammalian brain
    • Giulian G., Baker T.J. Characterization of ameboid microglia isolated from developing mammalian brain. J. Neurosci. 6:1986;2163-2178.
    • (1986) J. Neurosci. , vol.6 , pp. 2163-2178
    • Giulian, G.1    Baker, T.J.2
  • 7
    • 0032473596 scopus 로고    scopus 로고
    • Amyloid-β peptide activates cultured astrocytes alterations, cytokine induction and nitric oxide release
    • Hu J., Akama K.T., Grant G.A., Chromy B.A., Van Eldik L.J. Amyloid-β peptide activates cultured astrocytes alterations, cytokine induction and nitric oxide release. Brain Res. 785:1998;195-206.
    • (1998) Brain Res. , vol.785 , pp. 195-206
    • Hu, J.1    Akama, K.T.2    Grant, G.A.3    Chromy, B.A.4    Van Eldik, L.J.5
  • 8
    • 0030983079 scopus 로고    scopus 로고
    • Transcription factor NF-kappaB is activated in primary neurons by amyloid β peptides and in neurons surrounding early plaques from patients with Alzheimer disease
    • Kaltschmidt B., Uherek M., Volk B., Baeuerle P.A., Kaltschmidt C. Transcription factor NF-kappaB is activated in primary neurons by amyloid β peptides and in neurons surrounding early plaques from patients with Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 94:1997;2642-2647.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2642-2647
    • Kaltschmidt, B.1    Uherek, M.2    Volk, B.3    Baeuerle, P.A.4    Kaltschmidt, C.5
  • 10
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:2001;741-766.
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 11
    • 0036429923 scopus 로고    scopus 로고
    • Astrocytes enhance lipopolysaccharide-induced nitric oxide production by microglial cells
    • Solà C., Casal C., Tusell J.M., Serratosa J. Astrocytes enhance lipopolysaccharide-induced nitric oxide production by microglial cells. Eur. J. Neurosci. 16:2002;1275-1283.
    • (2002) Eur. J. Neurosci. , vol.16 , pp. 1275-1283
    • Solà, C.1    Casal, C.2    Tusell, J.M.3    Serratosa, J.4
  • 12
    • 0029935764 scopus 로고    scopus 로고
    • Microglial ramification requires nondiffusible factors derived from astrocytes
    • Tanaka J., Maeda N. Microglial ramification requires nondiffusible factors derived from astrocytes. Exp. Neurol. 137:1996;367-375.
    • (1996) Exp. Neurol. , vol.137 , pp. 367-375
    • Tanaka, J.1    Maeda, N.2
  • 13
    • 0032880901 scopus 로고    scopus 로고
    • Methionine residue 35 is important in amyloid β-peptide-associated free radical oxidative stress
    • Varadarajan S., Yatin S., Kanski J., Jahanshahi F., Butterfield D.A. Methionine residue 35 is important in amyloid β-peptide-associated free radical oxidative stress. Brain Res. Bull. 50:1999;133-141.
    • (1999) Brain Res. Bull. , vol.50 , pp. 133-141
    • Varadarajan, S.1    Yatin, S.2    Kanski, J.3    Jahanshahi, F.4    Butterfield, D.A.5
  • 14
    • 0034801348 scopus 로고    scopus 로고
    • Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ(25-35)
    • Varadarajan S., Kanski J., Aksenova M., Lauderback C., Butterfield D.A. Different mechanisms of oxidative stress and neurotoxicity for Alzheimer's Aβ(1-42) and Aβ(25-35). J. Am. Chem. Soc. 123:2001;5625-5631.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5625-5631
    • Varadarajan, S.1    Kanski, J.2    Aksenova, M.3    Lauderback, C.4    Butterfield, D.A.5
  • 15
    • 0030174758 scopus 로고    scopus 로고
    • Gradual inhibition of inducible nitric oxide synthase but not interleukin-1β production in rat microglial cells of endotoxin-treated mixed glial cell cultures
    • Vincent V.A.M., Van Dam A.M., Persoons J.H.A., Schotanus K., Steinbusch H.W.M., Schoffelmeer A.N.M., Berkenbosch F. Gradual inhibition of inducible nitric oxide synthase but not interleukin-1β production in rat microglial cells of endotoxin-treated mixed glial cell cultures. Glia. 17:1996;94-102.
    • (1996) Glia , vol.17 , pp. 94-102
    • Vincent, V.A.M.1    Van Dam, A.M.2    Persoons, J.H.A.3    Schotanus, K.4    Steinbusch, H.W.M.5    Schoffelmeer, A.N.M.6    Berkenbosch, F.7
  • 16
    • 0037180823 scopus 로고    scopus 로고
    • Inflammation and therapeutic vaccination in CNS diseases
    • Weiner H.L., Selkoe D.J. Inflammation and therapeutic vaccination in CNS diseases. Nature. 420:2002;879-884.
    • (2002) Nature , vol.420 , pp. 879-884
    • Weiner, H.L.1    Selkoe, D.J.2
  • 17
    • 0029076397 scopus 로고
    • Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide
    • Yan S.D., Yan S.F., Chen X., Fu J., Chen M., Kuppusamy P., Smith M.A., Perry G., Godman G.C., Nawroth P., Zweier J.L., Stern D. Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide. Nat. Med. 1:1995;693-699.
    • (1995) Nat. Med. , vol.1 , pp. 693-699
    • Yan, S.D.1    Yan, S.F.2    Chen, X.3    Fu, J.4    Chen, M.5    Kuppusamy, P.6    Smith, M.A.7    Perry, G.8    Godman, G.C.9    Nawroth, P.10    Zweier, J.L.11    Stern, D.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.