메뉴 건너뛰기




Volumn 474, Issue 2, 2016, Pages 309-314

Heparin interactions with apoA1 and SAA in inflammation-associated HDL

Author keywords

Amyloid; Atherosclerosis; Heparan sulfate; Lipoproteins receptors; Mass spectrometry; Proteoglycans

Indexed keywords

APOLIPOPROTEIN A1; HEPARIN; HIGH DENSITY LIPOPROTEIN; SERUM AMYLOID A; PROTEIN BINDING;

EID: 84964575149     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2016.04.092     Document Type: Article
Times cited : (17)

References (27)
  • 2
    • 0023635450 scopus 로고
    • A close ultrastructural relationship between sulfated proteoglycans and AA amyloid fibrils
    • A.D. Snow, J. Willmer, and R. Kisilevsky A close ultrastructural relationship between sulfated proteoglycans and AA amyloid fibrils Lab. Invest. 57 1987 687 698
    • (1987) Lab. Invest. , vol.57 , pp. 687-698
    • Snow, A.D.1    Willmer, J.2    Kisilevsky, R.3
  • 3
    • 0025935185 scopus 로고
    • Fibronectin and basement membrane components in renal amyloid deposits in patients with primary and secondary amyloidosis
    • G.T. Westermark, B. Norling, and P. Westermark Fibronectin and basement membrane components in renal amyloid deposits in patients with primary and secondary amyloidosis Clin. Exp. Immunol. 86 1991 150 156
    • (1991) Clin. Exp. Immunol. , vol.86 , pp. 150-156
    • Westermark, G.T.1    Norling, B.2    Westermark, P.3
  • 4
    • 77958181326 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans in amyloidosis
    • X. Zhang, and J.P. Li Heparan sulfate proteoglycans in amyloidosis Prog. Mol. Biol. Transl. Sci. 93 2010 309 334
    • (2010) Prog. Mol. Biol. Transl. Sci. , vol.93 , pp. 309-334
    • Zhang, X.1    Li, J.P.2
  • 8
    • 0018187709 scopus 로고
    • Changes in human serum amyloid A and C-reactive protein after etiocholanolone-induced inflammation
    • K.P. McAdam, R.J. Elin, J.D. Sipe, and S.M. Wolff Changes in human serum amyloid A and C-reactive protein after etiocholanolone-induced inflammation J. Clin. Invest. 61 1978 390 394
    • (1978) J. Clin. Invest. , vol.61 , pp. 390-394
    • McAdam, K.P.1    Elin, R.J.2    Sipe, J.D.3    Wolff, S.M.4
  • 9
    • 0015349917 scopus 로고
    • Chemical similarity among amyloid substances associated with long standing inflammation
    • E.P. Benditt, and N. Eriksen Chemical similarity among amyloid substances associated with long standing inflammation Lab. Invest. 26 1972 615 625
    • (1972) Lab. Invest. , vol.26 , pp. 615-625
    • Benditt, E.P.1    Eriksen, N.2
  • 12
    • 84878895654 scopus 로고    scopus 로고
    • Distribution of amyloid deposits in the kidneys of a patient with reactive amyloidosis associated with rheumatoid arthritis
    • T. Kuroda, N. Tanabe, H. Sato, T. Nakatsue, Y. Wada, S. Murakami, M. Nakano, and I. Narita Distribution of amyloid deposits in the kidneys of a patient with reactive amyloidosis associated with rheumatoid arthritis BMC Res. Notes 6 2013 231
    • (2013) BMC Res. Notes , vol.6 , pp. 231
    • Kuroda, T.1    Tanabe, N.2    Sato, H.3    Nakatsue, T.4    Wada, Y.5    Murakami, S.6    Nakano, M.7    Narita, I.8
  • 14
    • 0035822274 scopus 로고    scopus 로고
    • Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein
    • J.D. Gillmore, L.B. Lovat, M.R. Persey, M.B. Pepys, and P.N. Hawkins Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein Lancet 358 2001 24 29
    • (2001) Lancet , vol.358 , pp. 24-29
    • Gillmore, J.D.1    Lovat, L.B.2    Persey, M.R.3    Pepys, M.B.4    Hawkins, P.N.5
  • 16
    • 70349661239 scopus 로고    scopus 로고
    • Heparan sulfate promotes the aggregation of HDL-associated serum amyloid A: Evidence for a proamyloidogenic histidine molecular switch
    • E. Elimova, R. Kisilevsky, and J.B. Ancsin Heparan sulfate promotes the aggregation of HDL-associated serum amyloid A: evidence for a proamyloidogenic histidine molecular switch FASEB J. 23 2009 3436 3448
    • (2009) FASEB J. , vol.23 , pp. 3436-3448
    • Elimova, E.1    Kisilevsky, R.2    Ancsin, J.B.3
  • 17
    • 84905459592 scopus 로고    scopus 로고
    • Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A
    • J.J. Aguilera, F. Zhang, J.M. Beaudet, R.J. Linhardt, and W. Colon Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A Biochimie 104 2014 70 80
    • (2014) Biochimie , vol.104 , pp. 70-80
    • Aguilera, J.J.1    Zhang, F.2    Beaudet, J.M.3    Linhardt, R.J.4    Colon, W.5
  • 18
    • 79958856214 scopus 로고    scopus 로고
    • Identification of regions responsible for heparin-induced amyloidogenesis of human serum amyloid A using its fragment peptides
    • M. Egashira, H. Takase, I. Yamamoto, M. Tanaka, and H. Saito Identification of regions responsible for heparin-induced amyloidogenesis of human serum amyloid A using its fragment peptides Arch. Biochem. Biophys. 511 2011 101 106
    • (2011) Arch. Biochem. Biophys. , vol.511 , pp. 101-106
    • Egashira, M.1    Takase, H.2    Yamamoto, I.3    Tanaka, M.4    Saito, H.5
  • 19
    • 84864105671 scopus 로고    scopus 로고
    • Heparan sulfate dissociates serum amyloid A (SAA) from acute-phase high-density lipoprotein, promoting SAA aggregation
    • F. Noborn, J.B. Ancsin, W. Ubhayasekera, R. Kisilevsky, and J.P. Li Heparan sulfate dissociates serum amyloid A (SAA) from acute-phase high-density lipoprotein, promoting SAA aggregation J. Biol. Chem. 287 2012 25669 25677
    • (2012) J. Biol. Chem. , vol.287 , pp. 25669-25677
    • Noborn, F.1    Ancsin, J.B.2    Ubhayasekera, W.3    Kisilevsky, R.4    Li, J.P.5
  • 20
    • 33745026603 scopus 로고
    • The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum
    • R.J. Havel, H.A. Eder, and J.H. Bragdon The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum J. Clin. Invest. 34 1955 1345 1353
    • (1955) J. Clin. Invest. , vol.34 , pp. 1345-1353
    • Havel, R.J.1    Eder, H.A.2    Bragdon, J.H.3
  • 22
    • 84929000422 scopus 로고    scopus 로고
    • Overexpression of heparanase lowers the amyloid burden in amyloid-beta precursor protein transgenic mice
    • C.B. Jendresen, H. Cui, X. Zhang, I. Vlodavsky, L.N. Nilsson, and J.P. Li Overexpression of heparanase lowers the amyloid burden in amyloid-beta precursor protein transgenic mice J. Biol. Chem. 290 2015 5053 5064
    • (2015) J. Biol. Chem. , vol.290 , pp. 5053-5064
    • Jendresen, C.B.1    Cui, H.2    Zhang, X.3    Vlodavsky, I.4    Nilsson, L.N.5    Li, J.P.6
  • 23
    • 84931260240 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are important for islet amyloid formation and islet amyloid polypeptide-induced apoptosis
    • M.E. Oskarsson, K. Singh, J. Wang, I. Vlodavsky, J.P. Li, and G.T. Westermark Heparan sulfate proteoglycans are important for islet amyloid formation and islet amyloid polypeptide-induced apoptosis J. Biol. Chem. 290 2015 15121 15132
    • (2015) J. Biol. Chem. , vol.290 , pp. 15121-15132
    • Oskarsson, M.E.1    Singh, K.2    Wang, J.3    Vlodavsky, I.4    Li, J.P.5    Westermark, G.T.6
  • 24
    • 33947644267 scopus 로고    scopus 로고
    • Heparan sulfate as a therapeutic target in amyloidogenesis: Prospects and possible complications
    • R. Kisilevsky, J.B. Ancsin, W.A. Szarek, and S. Petanceska Heparan sulfate as a therapeutic target in amyloidogenesis: prospects and possible complications Amyloid 14 2007 21 32
    • (2007) Amyloid , vol.14 , pp. 21-32
    • Kisilevsky, R.1    Ancsin, J.B.2    Szarek, W.A.3    Petanceska, S.4
  • 25
    • 84938091306 scopus 로고    scopus 로고
    • Lipid-free apolipoprotein A-I structure: Insights into HDL formation and atherosclerosis development
    • X. Mei, and D. Atkinson Lipid-free apolipoprotein A-I structure: insights into HDL formation and atherosclerosis development Arch. Med. Res. 46 2015 351 360
    • (2015) Arch. Med. Res. , vol.46 , pp. 351-360
    • Mei, X.1    Atkinson, D.2
  • 26
    • 84941282386 scopus 로고    scopus 로고
    • Thermal transitions in serum amyloid A in solution and on the lipid: Implications for structure and stability of acute-phase HDL
    • S. Jayaraman, C. Haupt, and O. Gursky Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL J. Lipid Res. 56 2015 1531 1542
    • (2015) J. Lipid Res. , vol.56 , pp. 1531-1542
    • Jayaraman, S.1    Haupt, C.2    Gursky, O.3
  • 27
    • 57549113290 scopus 로고    scopus 로고
    • Acute-phase-HDL remodeling by heparan sulfate generates a novel lipoprotein with exceptional cholesterol efflux activity from macrophages
    • S.P. Tam, R. Kisilevsky, and J.B. Ancsin Acute-phase-HDL remodeling by heparan sulfate generates a novel lipoprotein with exceptional cholesterol efflux activity from macrophages PLoS One 3 2008 e3867
    • (2008) PLoS One , vol.3 , pp. e3867
    • Tam, S.P.1    Kisilevsky, R.2    Ancsin, J.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.