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Volumn 20, Issue 3, 2005, Pages 738-743

The metabolism of glycosaminoglycans is impaired in prion diseases

Author keywords

Glycosaminoglycans; Metabolism; Prion diseases

Indexed keywords

GLYCOSAMINOGLYCAN; HEPARAN SULFATE;

EID: 27744465417     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2005.05.009     Document Type: Article
Times cited : (20)

References (46)
  • 2
    • 0036830228 scopus 로고    scopus 로고
    • The neuropathogenic contributions of lysosomal dysfunction
    • B.A. Bahr, and J. Bendiske The neuropathogenic contributions of lysosomal dysfunction J. Neurochem. 83 2002 481 489
    • (2002) J. Neurochem. , vol.83 , pp. 481-489
    • Bahr, B.A.1    Bendiske, J.2
  • 5
    • 0141849861 scopus 로고    scopus 로고
    • Neuropathology of prion diseases
    • H. Budka Neuropathology of prion diseases Br. Med. Bull. 66 2003 121 130
    • (2003) Br. Med. Bull. , vol.66 , pp. 121-130
    • Budka, H.1
  • 6
    • 0027535855 scopus 로고
    • Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells
    • B. Caughey, and G.J. Raymond Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells J. Virol. 67 2 1993 643 650
    • (1993) J. Virol. , vol.67 , Issue.2 , pp. 643-650
    • Caughey, B.1    Raymond, G.J.2
  • 9
    • 0035997236 scopus 로고    scopus 로고
    • Glycosaminoglycans and beta-amyloid, prion and tau peptides in neurodegenerative diseases
    • J. Diaz-Nido, F. Wandosell, and J. Avila Glycosaminoglycans and beta-amyloid, prion and tau peptides in neurodegenerative diseases Peptides 23 2002 1323 1332
    • (2002) Peptides , vol.23 , pp. 1323-1332
    • Diaz-Nido, J.1    Wandosell, F.2    Avila, J.3
  • 10
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation
    • K. Doh-Ura, T. Iwaki, and B. Caughey Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation J. Virol. 74 2000 4894 4897
    • (2000) J. Virol. , vol.74 , pp. 4894-4897
    • Doh-Ura, K.1    Iwaki, T.2    Caughey, B.3
  • 11
    • 2342623474 scopus 로고    scopus 로고
    • Treatment of transmissible spongiform encephalopathy by intraventricular drug infusion in animal models
    • K. Doh-ura, K. Ishikawa, I. Murakami-Kubo, K. Sasaki, S. Mohri, R. Race, and T. Iwaki Treatment of transmissible spongiform encephalopathy by intraventricular drug infusion in animal models J. Virol. 78 2004 4999 5006
    • (2004) J. Virol. , vol.78 , pp. 4999-5006
    • Doh-Ura, K.1    Ishikawa, K.2    Murakami-Kubo, I.3    Sasaki, K.4    Mohri, S.5    Race, R.6    Iwaki, T.7
  • 12
    • 0021282464 scopus 로고
    • Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen
    • B. Ehlers, and H. Diringer Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen J. Gen. Virol. 65 Pt. 8 1984 1325 1330
    • (1984) J. Gen. Virol. , vol.65 , Issue.8 PART , pp. 1325-1330
    • Ehlers, B.1    Diringer, H.2
  • 13
    • 9444263075 scopus 로고    scopus 로고
    • Amyloidogenesis recapitulated in cell culture: A peptide inhibitor provides direct evidence for the role of heparan sulfate and suggests a new treatment strategy
    • E. Elimova, R. Kisilevsky, W.A. Szarek, and J.B. Ancsin Amyloidogenesis recapitulated in cell culture: a peptide inhibitor provides direct evidence for the role of heparan sulfate and suggests a new treatment strategy FASEB J. 18 2004 1749 1751
    • (2004) FASEB J. , vol.18 , pp. 1749-1751
    • Elimova, E.1    Kisilevsky, R.2    Szarek, W.A.3    Ancsin, J.B.4
  • 14
    • 0030561552 scopus 로고    scopus 로고
    • Drug-induced lysosomal storage of sulphated glycosaminoglycans
    • J. Fischer, H. Lullmann, and R. Lullmann-Rauch Drug-induced lysosomal storage of sulphated glycosaminoglycans Gen. Pharmacol. 27 1996 1317 1324
    • (1996) Gen. Pharmacol. , vol.27 , pp. 1317-1324
    • Fischer, J.1    Lullmann, H.2    Lullmann-Rauch, R.3
  • 15
    • 0027458091 scopus 로고
    • Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate
    • R. Gabizon, Z. Meiner, M. Halimi, and S.A. Ben-Sasson Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate J. Cell. Physiol. 157 1993 319 325
    • (1993) J. Cell. Physiol. , vol.157 , pp. 319-325
    • Gabizon, R.1    Meiner, Z.2    Halimi, M.3    Ben-Sasson, S.A.4
  • 18
    • 19444376065 scopus 로고    scopus 로고
    • PrPSc incorporation to cells requires endogenous glycosaminoglycan expression
    • N. Hijazi, Z. Kariv-Inbal, M. Gasset, and R. Gabizon PrPSc incorporation to cells requires endogenous glycosaminoglycan expression J. Biol. Chem. 280 17 2005 17057 17061
    • (2005) J. Biol. Chem. , vol.280 , Issue.17 , pp. 17057-17061
    • Hijazi, N.1    Kariv-Inbal, Z.2    Gasset, M.3    Gabizon, R.4
  • 21
    • 0021872436 scopus 로고
    • Glycosaminoglycan excretion in random samples of urine
    • K.C. Huang, K. Sukegawa, and T. Orii Glycosaminoglycan excretion in random samples of urine Clin. Chim. Acta 151 1985 141 146
    • (1985) Clin. Chim. Acta , vol.151 , pp. 141-146
    • Huang, K.C.1    Sukegawa, K.2    Orii, T.3
  • 22
    • 0021857120 scopus 로고
    • Screening test for urinary glycosaminoglycans and differentiation of various mucopolysaccharidoses
    • K.C. Huang, K. Sukegawa, and T. Orii Screening test for urinary glycosaminoglycans and differentiation of various mucopolysaccharidoses Clin. Chim. Acta 151 1985 147 156
    • (1985) Clin. Chim. Acta , vol.151 , pp. 147-156
    • Huang, K.C.1    Sukegawa, K.2    Orii, T.3
  • 23
    • 0023813491 scopus 로고
    • Methods for analysis of urinary glycosaminoglycans
    • C. Kodama, T. Kodama, and Z. Yosizawa Methods for analysis of urinary glycosaminoglycans J. Chromatogr. 429 1988 293 313
    • (1988) J. Chromatogr. , vol.429 , pp. 293-313
    • Kodama, C.1    Kodama, T.2    Yosizawa, Z.3
  • 24
    • 0033987067 scopus 로고    scopus 로고
    • Upregulation of the genes encoding lysosomal hydrolases, a perforin-like protein, and peroxidases in the brains of mice affected with an experimental prion disease
    • J. Kopacek, S. Sakaguchi, K. Shigematsu, N. Nishida, R. Atarashi, R. Nakaoke, R. Moriuchi, M. Niwa, and S. Katamine Upregulation of the genes encoding lysosomal hydrolases, a perforin-like protein, and peroxidases in the brains of mice affected with an experimental prion disease J. Virol. 74 2000 411 417
    • (2000) J. Virol. , vol.74 , pp. 411-417
    • Kopacek, J.1    Sakaguchi, S.2    Shigematsu, K.3    Nishida, N.4    Atarashi, R.5    Nakaoke, R.6    Moriuchi, R.7    Niwa, M.8    Katamine, S.9
  • 25
    • 0035859806 scopus 로고    scopus 로고
    • Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
    • C. Korth, B.C. May, F.E. Cohen, and S.B. Prusiner Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease Proc. Natl. Acad. Sci. U. S. A. 98 2001 9836 9841
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9836-9841
    • Korth, C.1    May, B.C.2    Cohen, F.E.3    Prusiner, S.B.4
  • 29
    • 0842284040 scopus 로고    scopus 로고
    • Neurons and astrocytes respond to prion infection by inducing microglia recruitment
    • M. Marella, and J. Chabry Neurons and astrocytes respond to prion infection by inducing microglia recruitment J. Neurosci. 24 2004 620 627
    • (2004) J. Neurosci. , vol.24 , pp. 620-627
    • Marella, M.1    Chabry, J.2
  • 30
    • 27744575015 scopus 로고    scopus 로고
    • Pathological prion protein exposure switches on neuronal MAP-kinase pathway resulting in microglia recruitment
    • M. Marella, C. Gaggioli, M. Batoz, M. Deckert, S. Tartare-Deckert, and J. Chabry Pathological prion protein exposure switches on neuronal MAP-kinase pathway resulting in microglia recruitment J. Biol. Chem. 2004
    • (2004) J. Biol. Chem.
    • Marella, M.1    Gaggioli, C.2    Batoz, M.3    Deckert, M.4    Tartare-Deckert, S.5    Chabry, J.6
  • 32
    • 0027474271 scopus 로고
    • Combined alcian blue and silver staining of subnanogram quantities of proteoglycans and glycosaminoglycans in sodium dodecyl sulfate-polyacrylamide gels
    • H.J. Moller, D. Heinegard, and J.H. Poulsen Combined alcian blue and silver staining of subnanogram quantities of proteoglycans and glycosaminoglycans in sodium dodecyl sulfate-polyacrylamide gels Anal. Biochem. 209 1993 169 175
    • (1993) Anal. Biochem. , vol.209 , pp. 169-175
    • Moller, H.J.1    Heinegard, D.2    Poulsen, J.H.3
  • 33
    • 0016183648 scopus 로고
    • The biochemical basis for mucopolysaccharidoses and mucolipidoses
    • E.F. Neufeld The biochemical basis for mucopolysaccharidoses and mucolipidoses Prog. Med. Genet. 10 1974 81 101
    • (1974) Prog. Med. Genet. , vol.10 , pp. 81-101
    • Neufeld, E.F.1
  • 37
    • 4444229470 scopus 로고    scopus 로고
    • Widespread correction of lysosomal storage following intrahepatic injection of a recombinant adeno-associated virus in the adult MPS VII mouse
    • T.J. Sferra, K. Backstrom, C. Wang, R. Rennard, M. Miller, and Y. Hu Widespread correction of lysosomal storage following intrahepatic injection of a recombinant adeno-associated virus in the adult MPS VII mouse Mol. Ther. 10 2004 478 491
    • (2004) Mol. Ther. , vol.10 , pp. 478-491
    • Sferra, T.J.1    Backstrom, K.2    Wang, C.3    Rennard, R.4    Miller, M.5    Hu, Y.6
  • 38
    • 0025243737 scopus 로고
    • Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie
    • A.D. Snow, T.N. Wight, D. Nochlin, Y. Koike, K. Kimata, S.J. DeArmond, and S.B. Prusiner Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie Lab. Invest. 63 5 1990 601 611
    • (1990) Lab. Invest. , vol.63 , Issue.5 , pp. 601-611
    • Snow, A.D.1    Wight, T.N.2    Nochlin, D.3    Koike, Y.4    Kimata, K.5    Dearmond, S.J.6    Prusiner, S.B.7
  • 39
    • 0033149962 scopus 로고    scopus 로고
    • Urinary glycosaminoglycans in recurrent urinary tract infections in kidney transplant patients
    • G. Stabellini, C. Calastrini, P. Gilli, and P.L. Bedani Urinary glycosaminoglycans in recurrent urinary tract infections in kidney transplant patients Biomed. Pharmacother. 53 1999 274 277
    • (1999) Biomed. Pharmacother. , vol.53 , pp. 274-277
    • Stabellini, G.1    Calastrini, C.2    Gilli, P.3    Bedani, P.L.4
  • 40
    • 0034718598 scopus 로고    scopus 로고
    • Microglial activation precedes acute neurodegeneration in Sandhoff disease and is suppressed by bone marrow transplantation
    • R. Wada, C.J. Tifft, and R.L. Proia Microglial activation precedes acute neurodegeneration in Sandhoff disease and is suppressed by bone marrow transplantation Proc. Natl. Acad. Sci. U. S. A. 97 2000 10954 10959
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10954-10959
    • Wada, R.1    Tifft, C.J.2    Proia, R.L.3
  • 41
    • 0034088131 scopus 로고    scopus 로고
    • The association of elevated urinary total to sulfated glycosaminoglycan ratio and high molecular mass hyaluronic acid with interstitial cystitis
    • D.C. Wei, V.A. Politano, M.G. Selzer, and V.B. Lokeshwar The association of elevated urinary total to sulfated glycosaminoglycan ratio and high molecular mass hyaluronic acid with interstitial cystitis J. Urol. 163 2000 1577 1583
    • (2000) J. Urol. , vol.163 , pp. 1577-1583
    • Wei, D.C.1    Politano, V.A.2    Selzer, M.G.3    Lokeshwar, V.B.4
  • 42
    • 0141738255 scopus 로고    scopus 로고
    • PrP knock-out and PrP transgenic mice in prion research
    • C. Weissmann, and E. Flechsig PrP knock-out and PrP transgenic mice in prion research Br. Med. Bull. 66 2003 43 60
    • (2003) Br. Med. Bull. , vol.66 , pp. 43-60
    • Weissmann, C.1    Flechsig, E.2
  • 44
    • 0043169474 scopus 로고    scopus 로고
    • Up-regulation of cathepsin B and cathepsin L activities in scrapie-infected mouse Neuro2a cells
    • Y. Zhang, E. Spiess, M.H. Groschup, and A. Burkle Up-regulation of cathepsin B and cathepsin L activities in scrapie-infected mouse Neuro2a cells J. Gen. Virol. 84 2003 2279 2283
    • (2003) J. Gen. Virol. , vol.84 , pp. 2279-2283
    • Zhang, Y.1    Spiess, E.2    Groschup, M.H.3    Burkle, A.4
  • 46
    • 4043174204 scopus 로고    scopus 로고
    • Retrovirally transduced bone marrow has a therapeutic effect on brain in the mouse model of mucopolysaccharidosis IIIB
    • Y. Zheng, S. Ryazantsev, K. Ohmi, H.Z. Zhao, N. Rozengurt, D.B. Kohn, and E.F. Neufeld Retrovirally transduced bone marrow has a therapeutic effect on brain in the mouse model of mucopolysaccharidosis IIIB Mol. Genet. Metab. 82 2004 286 295
    • (2004) Mol. Genet. Metab. , vol.82 , pp. 286-295
    • Zheng, Y.1    Ryazantsev, S.2    Ohmi, K.3    Zhao, H.Z.4    Rozengurt, N.5    Kohn, D.B.6    Neufeld, E.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.