메뉴 건너뛰기




Volumn 6, Issue 6, 2000, Pages 643-651

Receptor-dependent cell stress and amyloid accumulation in systemic amyloidosis

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT; SERUM AMYLOID A;

EID: 0001358519     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/76216     Document Type: Article
Times cited : (295)

References (43)
  • 3
    • 0030682237 scopus 로고    scopus 로고
    • Amyloidosis: A review of recent diagnostic and therapeutic developments
    • Gillmore, J., Hawkins, P. & Pepys, M. Amyloidosis: a review of recent diagnostic and therapeutic developments. Br. J. Haematol. 99, 245-256 (1997).
    • (1997) Br. J. Haematol. , vol.99 , pp. 245-256
    • Gillmore, J.1    Hawkins, P.2    Pepys, M.3
  • 4
    • 0030756579 scopus 로고    scopus 로고
    • Amyloid a protein amyloidosis induced in ApoE-deficient mice
    • Hoshii, Y. et al. Amyloid A protein amyloidosis induced in ApoE-deficient mice. Am. J. Pathol. 151, 911-917 (1997).
    • (1997) Am. J. Pathol. , vol.151 , pp. 911-917
    • Hoshii, Y.1
  • 5
    • 0026542786 scopus 로고
    • ApoE: A pathological chaperone protein in patients with cerebral and systemic amyloid
    • Wisniewski, T. & Frangione, B. ApoE: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci. Lett. 135:235-238 (1992).
    • (1992) Neurosci. Lett. , vol.135 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2
  • 6
    • 0031899218 scopus 로고    scopus 로고
    • Reduction in amyloid A amyloid formation in apolipoprotein E-deficient mice
    • Kindy, M. & Rader, D. Reduction in amyloid A amyloid formation in apolipoprotein E-deficient mice. Am. J. Pathol. 152, 1387-1395 (1998).
    • (1998) Am. J. Pathol. , vol.152 , pp. 1387-1395
    • Kindy, M.1    Rader, D.2
  • 7
    • 0028844427 scopus 로고
    • Association of apolipoprotein E with murine amyloid A protein amyloid
    • Kindy, M., King, A., Perry, G., deBeer, M. & deBeer, F. Association of apolipoprotein E with murine amyloid A protein amyloid. Lab. Invest. 73, 469-475 (1995).
    • (1995) Lab. Invest. , vol.73 , pp. 469-475
    • Kindy, M.1    King, A.2    Perry, G.3    DeBeer, M.4    DeBeer, F.5
  • 8
    • 0025752708 scopus 로고
    • Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis
    • Hawkins, P., Tennent, G., Woo, P. & Pepys, M. Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis. Clin. Exp. Immunol. 84, 308-316 (1991).
    • (1991) Clin. Exp. Immunol. , vol.84 , pp. 308-316
    • Hawkins, P.1    Tennent, G.2    Woo, P.3    Pepys, M.4
  • 9
    • 0030757182 scopus 로고    scopus 로고
    • Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene
    • Botto, M. et al. Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Nature Med. 3, 855-859 (1997).
    • (1997) Nature Med. , vol.3 , pp. 855-859
    • Botto, M.1
  • 10
    • 0028913416 scopus 로고
    • Arresting amyloidosis in vivo using small molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease
    • Kisilevsky, R. et al. Arresting amyloidosis in vivo using small molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nature Med. 1, 143-148 (1995).
    • (1995) Nature Med. , vol.1 , pp. 143-148
    • Kisilevsky, R.1
  • 11
    • 0344417095 scopus 로고    scopus 로고
    • Can serum amyloid A or macrophage colony stimulating factor serve as a marker of amyloid formation?
    • Rysava, R., Merta, M., Tesar, V., Jirsa, M. & Zima, T. Can serum amyloid A or macrophage colony stimulating factor serve as a marker of amyloid formation? Biochem. Mol. Biol. Int. 47, 845-850 (1999).
    • (1999) Biochem. Mol. Biol. Int. , vol.47 , pp. 845-850
    • Rysava, R.1    Merta, M.2    Tesar, V.3    Jirsa, M.4    Zima, T.5
  • 12
    • 0344286498 scopus 로고    scopus 로고
    • Activation of RAGE: A mechanism for chronic dysfunction in diabetic vasculopathy and atherosclerosis
    • Schmidt, A-M., Yan, S-D., Wautier, J-L. & Stern, D. Activation of RAGE: a mechanism for chronic dysfunction in diabetic vasculopathy and atherosclerosis. Circ. Res. 84, 489-497 (1999).
    • (1999) Circ. Res. , vol.84 , pp. 489-497
    • Schmidt, A.-M.1    Yan, S.-D.2    Wautier, J.-L.3    Stern, D.4
  • 13
    • 0033603241 scopus 로고    scopus 로고
    • RAGE mediates a novel proinflammatory axis: The cell surface receptor for 5100/calgranulin polypeptides
    • Hofmann, M. et al. RAGE mediates a novel proinflammatory axis: the cell surface receptor for 5100/calgranulin polypeptides. Cell 97, 889-901 (1999).
    • (1999) Cell , vol.97 , pp. 889-901
    • Hofmann, M.1
  • 14
    • 0032706735 scopus 로고    scopus 로고
    • Cellular cofactors for amyloid beta-peptide induced by cell stress: Moving from cell culture to in vivo
    • Yan, S-D., Roher, A., Schmidt, A-M. & Stern D. Cellular cofactors for amyloid beta-peptide induced by cell stress: moving from cell culture to in vivo. Am. J. Pathol. 155, 1403-1411 (1999).
    • (1999) Am. J. Pathol. , vol.155 , pp. 1403-1411
    • Yan, S.-D.1    Roher, A.2    Schmidt, A.-M.3    Stern, D.4
  • 15
    • 0342563452 scopus 로고    scopus 로고
    • Specific deposition of serum amyloid A protein 2 in the mouse
    • Shiroo, M., Kawahara, E., Nakanishi, I. & Migita, S. Specific deposition of serum amyloid A protein 2 in the mouse. Scand. J. Immunol. 332, 721-728 (1998).
    • (1998) Scand. J. Immunol. , vol.332 , pp. 721-728
    • Shiroo, M.1    Kawahara, E.2    Nakanishi, I.3    Migita, S.4
  • 16
    • 0023915726 scopus 로고
    • Identification of three isoform patterns of human serum amyloid A protein
    • Strachen, A., deBeer, F., van der Westhuyzen, D. & Coetzee, G. Identification of three isoform patterns of human serum amyloid A protein. Biochem. J. 250, 203-207 (1988).
    • (1988) Biochem. J. , vol.250 , pp. 203-207
    • Strachen, A.1    DeBeer, F.2    Van Der Westhuyzen, D.3    Coetzee, G.4
  • 17
    • 0027165834 scopus 로고
    • Structural prerequisites for serum amyloid A fibril formation
    • DeBeer, M., deBeer, F., McCubin, W., Kay, C. & Kindy, M. Structural prerequisites for serum amyloid A fibril formation. J. Biol. Chem. 268, 20606-20612 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 20606-20612
    • DeBeer, M.1    DeBeer, F.2    McCubin, W.3    Kay, C.4    Kindy, M.5
  • 18
    • 0027769913 scopus 로고
    • Characterization of the inbred CE/J mouse strain as amyloid resistant
    • Sipe, J. et al. Characterization of the inbred CE/J mouse strain as amyloid resistant. Am. J. Pathol. 143, 1480-1485 (1993).
    • (1993) Am. J. Pathol. , vol.143 , pp. 1480-1485
    • Sipe, J.1
  • 19
    • 0031717894 scopus 로고    scopus 로고
    • Suppression of accelerated diabetic atherosclerosis by sRAGE
    • Park, L. et al. Suppression of accelerated diabetic atherosclerosis by sRAGE. Nature Med. 4, 1025-1031 (1998).
    • (1998) Nature Med. , vol.4 , pp. 1025-1031
    • Park, L.1
  • 20
    • 0026681218 scopus 로고
    • An immortalized cell line expresses properties of activated microglial cells
    • Bocchini, V. et al. An immortalized cell line expresses properties of activated microglial cells. J. Neurosci. Res. 31, 616-621 (1992).
    • (1992) J. Neurosci. Res. , vol.31 , pp. 616-621
    • Bocchini, V.1
  • 21
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
    • Yan, S-D. et al. RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease. Nature 382, 685-691 (1996).
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.-D.1
  • 23
    • 0027193894 scopus 로고
    • Endothelial nuclear factor kB and the initiation of the atherosclerotic lesion
    • Collins, T. Endothelial nuclear factor kB and the initiation of the atherosclerotic lesion. Lab. Invest. 68, 499-508 (1993).
    • (1993) Lab. Invest. , vol.68 , pp. 499-508
    • Collins, T.1
  • 24
    • 0021909988 scopus 로고
    • Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo
    • Husebekk, A., Skogen, B., Husby, G. & Marbaug, G. Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo. Scan. J. Immunol. 21, 283-287 (1985).
    • (1985) Scan. J. Immunol. , vol.21 , pp. 283-287
    • Husebekk, A.1    Skogen, B.2    Husby, G.3    Marbaug, G.4
  • 25
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibrils in Alzheimer's disease indicates cross-beta conformation
    • Kirschner, D., Abraham, C. & Selkoe, D. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibrils in Alzheimer's disease indicates cross-beta conformation. Proc. Natl. Acad. Sci. USA 83, 503-507 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 503-507
    • Kirschner, D.1    Abraham, C.2    Selkoe, D.3
  • 27
    • 0033023004 scopus 로고    scopus 로고
    • Microglia in Alzheimer's disease and transgenic models
    • Dickson, D. Microglia in Alzheimer's disease and transgenic models. Am. J. Pathol. 154, 1627-1631 (1999).
    • (1999) Am. J. Pathol. , vol.154 , pp. 1627-1631
    • Dickson, D.1
  • 28
    • 0030691019 scopus 로고    scopus 로고
    • Activated microglial cells are colocalized with perivascular deposits of amyloid beta-peptide in Alzheimer's disease brain
    • Uchihara, T., Akiyama, H., Kondo, H. & Ikeda, K. Activated microglial cells are colocalized with perivascular deposits of amyloid beta-peptide in Alzheimer's disease brain. Stroke 28, 1948-1950 (1997).
    • (1997) Stroke , vol.28 , pp. 1948-1950
    • Uchihara, T.1    Akiyama, H.2    Kondo, H.3    Ikeda, K.4
  • 29
    • 0000920292 scopus 로고    scopus 로고
    • Amyloid beta peptide-RAGE interaction elicits neuronal expression of M-CSF: A proinflammatory pathway in Alzheimer disease
    • Yan, S-D. et al. Amyloid beta peptide-RAGE interaction elicits neuronal expression of M-CSF: a proinflammatory pathway in Alzheimer disease. Proc. Natl. Acad. Sci. USA 94, 5296-5301 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5296-5301
    • Yan, S.-D.1
  • 30
    • 0031952262 scopus 로고    scopus 로고
    • M-CSF: Haematopoietic growth factor or inflammatory cytokine?
    • Fixe, P. & Praloran, V. M-CSF: haematopoietic growth factor or inflammatory cytokine? Cytokine 10, 32-37 (1998).
    • (1998) Cytokine , vol.10 , pp. 32-37
    • Fixe, P.1    Praloran, V.2
  • 31
    • 0030768744 scopus 로고    scopus 로고
    • CSF-1 signal transduction
    • Hamilton, J. CSF-1 signal transduction. J. Leukoc. Biol. 62:145-155 (1997).
    • (1997) J. Leukoc. Biol. , vol.62 , pp. 145-155
    • Hamilton, J.1
  • 32
    • 0031033054 scopus 로고    scopus 로고
    • Regulation of CSF-1 receptor expression
    • Hume, D. et al. Regulation of CSF-1 receptor expression. Mol. Reprod. Dev. 46, 46-52 (1997).
    • (1997) Mol. Reprod. Dev. , vol.46 , pp. 46-52
    • Hume, D.1
  • 33
    • 0031575827 scopus 로고    scopus 로고
    • Oxidative stress is found in amyloid deposits in systemic amyloidosis
    • Ando, Y. et al. Oxidative stress is found in amyloid deposits in systemic amyloidosis. Biochem. Biophys. Res. Commun. 232, 497-502 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 497-502
    • Ando, Y.1
  • 34
    • 0028919426 scopus 로고
    • Expression of RAGE in peripheral occlusive vascular disease
    • Ritthaler, U. et al. Expression of RAGE in peripheral occlusive vascular disease. Am. J. Pathol. 146, 688-694 (1995).
    • (1995) Am. J. Pathol. , vol.146 , pp. 688-694
    • Ritthaler, U.1
  • 35
    • 0030061699 scopus 로고    scopus 로고
    • Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy: Soluble RAGE blocks hyperpermeability
    • Wautier, J-L. et al. Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy: soluble RAGE blocks hyperpermeability. J. Clin. Invest. 97, 238-243 (1996).
    • (1996) J. Clin. Invest. , vol.97 , pp. 238-243
    • Wautier, J.-L.1
  • 36
    • 0026784628 scopus 로고
    • Glucose and diabetic vascular disease
    • Rudderman, N., Williamson, J. & Brownlee, M. Glucose and diabetic vascular disease. FASEB J. 6, 2905-2914 (1992).
    • (1992) FASEB J. , vol.6 , pp. 2905-2914
    • Rudderman, N.1    Williamson, J.2    Brownlee, M.3
  • 37
    • 0027718105 scopus 로고
    • Tissue distribution of RAGE: Expression in smooth muscle, cardiac myocytes, and neural tissue in addition to the vasculature
    • Brett, J. et al. Tissue distribution of RAGE: expression in smooth muscle, cardiac myocytes, and neural tissue in addition to the vasculature. Am. J. Pathol. 143, 1699-1712 (1993).
    • (1993) Am. J. Pathol. , vol.143 , pp. 1699-1712
    • Brett, J.1
  • 38
    • 0028851635 scopus 로고
    • RAGE is a cellular binding site for amphoterin: Mediation of neurite outgrowth and co-expression of RAGE and amphoterin in the developing nervous system
    • Hori, O. et al. RAGE is a cellular binding site for amphoterin: mediation of neurite outgrowth and co-expression of RAGE and amphoterin in the developing nervous system. J. Biol. Chem. 270, 25752-25761 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25752-25761
    • Hori, O.1
  • 39
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schafer, B. & Heizmann, C. The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biochem. Sci. 21, 134-140 (1996).
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 134-140
    • Schafer, B.1    Heizmann, C.2
  • 40
    • 0033538467 scopus 로고    scopus 로고
    • HMG1 as a late mediator of endotoxin lethality in mice
    • Wang, H. et al. HMG1 as a late mediator of endotoxin lethality in mice. Science 285, 248-251, 1999.
    • (1999) Science , vol.285 , pp. 248-251
    • Wang, H.1
  • 41
    • 0342997730 scopus 로고    scopus 로고
    • Blockade of RAGE/amphoterin axis suppresses tumor growth and metastases
    • in the press
    • Taguchi, A. et al. Blockade of RAGE/amphoterin axis suppresses tumor growth and metastases. Nature (in the press).
    • Nature
    • Taguchi, A.1
  • 42
    • 0023544346 scopus 로고
    • Degradation and deposition of amyloid A fibrils are tissue specific
    • Prelli, F., Pras, M. & Frangione, B. Degradation and deposition of amyloid A fibrils are tissue specific. Biochemistry 26, 8251-8256 (1987).
    • (1987) Biochemistry , vol.26 , pp. 8251-8256
    • Prelli, F.1    Pras, M.2    Frangione, B.3
  • 43
    • 0007208690 scopus 로고
    • Mathematical models for ligand-receptor binding
    • Klotz, I. & Hunston, D. Mathematical models for ligand-receptor binding. J. Biol. Chem. 258, 11442-11445 (1984).
    • (1984) J. Biol. Chem. , vol.258 , pp. 11442-11445
    • Klotz, I.1    Hunston, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.