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Volumn 7, Issue 1, 2000, Pages 23-25

The relation of proteoglycans, serum amyloid P and Apo E to amyloidosis current status, 2000

Author keywords

AA; Amyloid; Apo E; A ; Heparan sulfate; IAPP; Serum amyloid P

Indexed keywords

APOLIPOPROTEIN E; HEPARAN SULFATE; PERLECAN; PROTEOGLYCAN; PROTEOHEPARAN SULFATE; SERUM AMYLOID P;

EID: 0034110874     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.3109/13506120009146820     Document Type: Article
Times cited : (45)

References (26)
  • 1
    • 85017204082 scopus 로고    scopus 로고
    • Classification of amyloid fibril proteins and their precursors: An ongoing discussion
    • Westermark P (1997). Classification of amyloid fibril proteins and their precursors: an ongoing discussion. Amyloid: Int J Exp Clin Invest 4, 216-218
    • (1997) Amyloid: Int J Exp Clin Invest , vol.4 , pp. 216-218
    • Westermark, P.1
  • 3
    • 0013919085 scopus 로고
    • Mucopolysaccharides of whole human spleens in generalized amyloidosis
    • Bitter T and Muir H (1966). Mucopolysaccharides of whole human spleens in generalized amyloidosis. J Clin Invest 45, 963-975
    • (1966) J Clin Invest , vol.45 , pp. 963-975
    • Bitter, T.1    Muir, H.2
  • 4
    • 0023635450 scopus 로고
    • A close ultrastructural relationship between sulphated proteoglycans and AA amyloid fibrils
    • Snow AD and Kisilevsky R (1988). A close ultrastructural relationship between sulphated proteoglycans and AA amyloid fibrils. Lab Invest 57, 687-698
    • (1988) Lab Invest , vol.57 , pp. 687-698
    • Snow, A.D.1    Kisilevsky, R.2
  • 5
    • 0029868555 scopus 로고    scopus 로고
    • A high resolution ultrastructural study of experimental murine AA amyloid
    • Inoue S and Kisilevsky R (1996). A high resolution ultrastructural study of experimental murine AA amyloid. Lab Invest 74, 670-683
    • (1996) Lab Invest , vol.74 , pp. 670-683
    • Inoue, S.1    Kisilevsky, R.2
  • 6
    • 0027482564 scopus 로고
    • Induction of perlecan gene expression precedes amyloid formation during experimental murine AA amyloidogenesis
    • Ailles L, Kisilevsky R and Young ID (1993). Induction of perlecan gene expression precedes amyloid formation during experimental murine AA amyloidogenesis. Lab Invest 69, 443-448
    • (1993) Lab Invest , vol.69 , pp. 443-448
    • Ailles, L.1    Kisilevsky, R.2    Young, I.D.3
  • 7
    • 0023245170 scopus 로고
    • Characterization of tissue and plasma glycosaminoglycans during experimental AA amyloidosis and acute inflammation.Quantitative and qualitative analysis
    • Snow AD, Kisilevsky R, Stephens C and Anastassiades T (1987). Characterization of tissue and plasma glycosaminoglycans during experimental AA amyloidosis and acute inflammation.Quantitative and qualitative analysis. Lab Invest 56, 665-675
    • (1987) Lab Invest , vol.56 , pp. 665-675
    • Snow, A.D.1    Kisilevsky, R.2    Stephens, C.3    Anastassiades, T.4
  • 8
    • 0024212706 scopus 로고
    • Circular dichroism and fluorescence studies on two murine serum amyloid a proteins
    • McCubbin WD, Kay CM, Narindrasorasak S and Kisilevsky R (1988). Circular dichroism and fluorescence studies on two murine serum amyloid A proteins. Biochem J 256, 775-783
    • (1988) Biochem J , vol.256 , pp. 775-783
    • McCubbin, W.D.1    Kay, C.M.2    Narindrasorasak, S.3    Kisilevsky, R.4
  • 10
    • 0028913416 scopus 로고
    • Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease
    • Kisilevsky R, Lemieux LJ, Fraser PE, Kong XQ, Hultin PG and Szarek WA (1995). Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease. Nat Med 1, 143-148
    • (1995) Nat Med , vol.1 , pp. 143-148
    • Kisilevsky, R.1    Lemieux, L.J.2    Fraser, P.E.3    Kong, X.Q.4    Hultin, P.G.5    Szarek, W.A.6
  • 11
  • 12
    • 0031895939 scopus 로고    scopus 로고
    • Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation
    • Castillo GM, Cummings JA, Yang WH, Judge ME, Sheardown MJ, Rimvall K, Hansen JB and Snow AD (1998). Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation. Diabetes 47, 612-620
    • (1998) Diabetes , vol.47 , pp. 612-620
    • Castillo, G.M.1    Cummings, J.A.2    Yang, W.H.3    Judge, M.E.4    Sheardown, M.J.5    Rimvall, K.6    Hansen, J.B.7    Snow, A.D.8
  • 13
    • 0033548474 scopus 로고    scopus 로고
    • The heparin/heparan sulfate-binding site on apo-serum amyloid A: Implications for the therapeutic intervention of amyloidosis
    • Ancsin JB and Kisilevsky R (1999). The heparin/heparan sulfate-binding site on apo-serum amyloid A: implications for the therapeutic intervention of amyloidosis. J Biol Chem 274, 7172-7181
    • (1999) J Biol Chem , vol.274 , pp. 7172-7181
    • Ancsin, J.B.1    Kisilevsky, R.2
  • 16
    • 0023013825 scopus 로고
    • Ciculating amyloid P component is the precursor of amyloid P component in tissue amyloid deposits
    • Baltz ML, Caspi D, Evans DJ, Rowe IF, Hind CRK and Pepys MB (1986). Ciculating amyloid P component is the precursor of amyloid P component in tissue amyloid deposits. Clin Exp Immunol 66, 691-700
    • (1986) Clin Exp Immunol , vol.66 , pp. 691-700
    • Baltz, M.L.1    Caspi, D.2    Evans, D.J.3    Rowe, I.F.4    Hind, C.R.K.5    Pepys, M.B.6
  • 18
    • 0030901604 scopus 로고    scopus 로고
    • Calcium-dependent and -independent binding of the pentraxin serum amyloid P component to glycosaminoglycans and amyloid proteins: Enhanced binding at slightly acid pH
    • Danielsen B, Sorensen IJ, Nybo M, Nielsen EH, Kaplan B and Svehag SE (1997). Calcium-dependent and -independent binding of the pentraxin serum amyloid P component to glycosaminoglycans and amyloid proteins: Enhanced binding at slightly acid pH. Biochim Biophys Acta 1339, 73-78
    • (1997) Biochim Biophys Acta , vol.1339 , pp. 73-78
    • Danielsen, B.1    Sorensen, I.J.2    Nybo, M.3    Nielsen, E.H.4    Kaplan, B.5    Svehag, S.E.6
  • 19
    • 0027255997 scopus 로고
    • Scintigraphic quantification and serial monitoring of human visceral amyloid deposits provide evidence for turnover and regression
    • Hawkins PN, Richardson S, Macsweeney JE, King AD, Vigushin DM, Lavender JP and Pepys MB (1993). Scintigraphic quantification and serial monitoring of human visceral amyloid deposits provide evidence for turnover and regression. Quart J Med 86, 365-374
    • (1993) Quart J Med , vol.86 , pp. 365-374
    • Hawkins, P.N.1    Richardson, S.2    Macsweeney, J.E.3    King, A.D.4    Vigushin, D.M.5    Lavender, J.P.6    Pepys, M.B.7
  • 21
    • 0032839621 scopus 로고    scopus 로고
    • Apolipoprotein E: From atherosclerosis to Alzheimer's disease and beyond
    • Mahley RW and Huang YD (1999). Apolipoprotein E: from atherosclerosis to Alzheimer's disease and beyond. Curr Opin Lipidol 10, 207-217
    • (1999) Curr Opin Lipidol , vol.10 , pp. 207-217
    • Mahley, R.W.1    Huang, Y.D.2
  • 23
    • 0031899218 scopus 로고    scopus 로고
    • Reduction in amyloid a amyloid formation in apolipoprotein-E- Deficient mice
    • Kindy MS and Rader DJ (1998). Reduction in amyloid A amyloid formation in apolipoprotein-E- deficient mice. Am J Pathol 152, 1387-1395
    • (1998) Am J Pathol , vol.152 , pp. 1387-1395
    • Kindy, M.S.1    Rader, D.J.2
  • 24
    • 0029905421 scopus 로고    scopus 로고
    • Native complex formation between apolipoprotein e isoforms and the Alzheimer's disease peptide Aβ
    • Chan W, Fornwald J, Brawner M and Wetzel R (1996). Native complex formation between apolipoprotein E isoforms and the Alzheimer's disease peptide Aβ. Biochemistry 35, 7123-7130
    • (1996) Biochemistry , vol.35 , pp. 7123-7130
    • Chan, W.1    Fornwald, J.2    Brawner, M.3    Wetzel, R.4
  • 25
    • 0029866177 scopus 로고    scopus 로고
    • The interaction between apolipoprotein e and Alzheimer's amyloid b-peptide is dependent on β-peptide conformation
    • Golabek AA, Soto C, Vogel T and Wisniewski T (1996). The interaction between apolipoprotein E and Alzheimer's amyloid b-peptide is dependent on β-peptide conformation. J Biol Chem 271, 10602-10606
    • (1996) J Biol Chem , vol.271 , pp. 10602-10606
    • Golabek, A.A.1    Soto, C.2    Vogel, T.3    Wisniewski, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.