메뉴 건너뛰기




Volumn 315, Issue 1, 2004, Pages 16-21

Small HDL form via apo A-I a complex with atrial natriuretic peptide

Author keywords

Amyloidosis; Apo A I; Atrial natriuretic peptide; HDL; Two dimensional gel electrophoresis

Indexed keywords

APOLIPOPROTEIN A1; ATRIAL NATRIURETIC FACTOR; ATRIAL NATRIURETIC FACTOR ALPHA; DIMER; HIGH DENSITY LIPOPROTEIN; IODINE 125; LIPOPROTEIN;

EID: 0842329663     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.01.017     Document Type: Article
Times cited : (6)

References (38)
  • 1
    • 0035137399 scopus 로고    scopus 로고
    • The changing concepts of amyloid
    • Picken M.M. The changing concepts of amyloid. Arch. Pathol. Lab. Med. 125:2001;38-43.
    • (2001) Arch. Pathol. Lab. Med. , vol.125 , pp. 38-43
    • Picken, M.M.1
  • 2
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid beta-protein and the genetics of Alzheimer's disease
    • Selkoe D.J. Amyloid beta-protein and the genetics of Alzheimer's disease. J. Biol. Chem. 271:1996;18295-18298.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 3
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway K.A., Harper J.D., Lansbury P.T. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med. 4:1998;1318-1320.
    • (1998) Nat. Med. , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 4
    • 0033372474 scopus 로고    scopus 로고
    • Nonamyloidotic monoclonal immunoglobulin deposition disease. Light-chain, heavy-chain, and light- and heavy-chain deposition diseases
    • Buxbaum J., Gallo G. Nonamyloidotic monoclonal immunoglobulin deposition disease. Light-chain, heavy-chain, and light- and heavy-chain deposition diseases. Hematol. Oncol. Clin. North. Am. 13:1999;1235-1248.
    • (1999) Hematol. Oncol. Clin. North. Am. , vol.13 , pp. 1235-1248
    • Buxbaum, J.1    Gallo, G.2
  • 5
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz M.F. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24:1999;58-63.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 6
    • 0010551538 scopus 로고
    • Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
    • Costa P.P., Figueira A.S., Bravo F.R. Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc. Natl. Acad. Sci. USA. 75:1978;4499-4503.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4499-4503
    • Costa, P.P.1    Figueira, A.S.2    Bravo, F.R.3
  • 7
    • 18744434215 scopus 로고    scopus 로고
    • Beta2-microglobulin and amyloidosis
    • Drueke T.B. Beta2-microglobulin and amyloidosis. Nephrol. Dial. Transplant. 15:2000;17-24.
    • (2000) Nephrol. Dial. Transplant. , vol.15 , pp. 17-24
    • Drueke, T.B.1
  • 10
    • 0023489743 scopus 로고
    • The prevalence of isolated atrial amyloid
    • Steiner I. The prevalence of isolated atrial amyloid. J. Pathol. 153:1987;395-398.
    • (1987) J. Pathol. , vol.153 , pp. 395-398
    • Steiner, I.1
  • 12
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra
    • Barrow C.J., Yasuda A., Kenny P.T., Zagorski M.J. Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. Analysis of circular dichroism spectra. J. Mol. Biol. 225:1992;1075-1093.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.J.4
  • 15
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7. 4 aggregates of the Alzheimer's amyloid peptide Aβ
    • Wood S.J., Maleeff B., Hart T., Wetzel R. Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ J. Mol. Biol. 256:1996;870-877.
    • (1996) J. Mol. Biol. , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4
  • 16
    • 0025997625 scopus 로고
    • Atrial amyloid deposits in the failing human heart display both atrial and brain natriuretic peptide-like immunoreactivity
    • Pucci J., Wharton E., Arbustini M., Grasso M., Diegoli P., Needleman M., Vigano J., Polak M. Atrial amyloid deposits in the failing human heart display both atrial and brain natriuretic peptide-like immunoreactivity. J. Pathol. 165:1991;235-241.
    • (1991) J. Pathol. , vol.165 , pp. 235-241
    • Pucci, J.1    Wharton, E.2    Arbustini, M.3    Grasso, M.4    Diegoli, P.5    Needleman, M.6    Vigano, J.7    Polak, M.8
  • 18
    • 0033990254 scopus 로고    scopus 로고
    • Molecular assembly of endogenous and synthetic big atrial natriuretic peptide (ANP) and its amyloidogenic implications
    • Maioli E., Torricelli C., Santucci A., Pacini A. Molecular assembly of endogenous and synthetic big atrial natriuretic peptide (ANP) and its amyloidogenic implications. Biochim. Biophys. Acta. 1500:2000;31-40.
    • (2000) Biochim. Biophys. Acta , vol.1500 , pp. 31-40
    • Maioli, E.1    Torricelli, C.2    Santucci, A.3    Pacini, A.4
  • 19
    • 0035978482 scopus 로고    scopus 로고
    • Plasma factors controlling atrial natriuretic peptide (ANP) aggregation: Role of lipoproteins
    • Maioli E., Torricelli C., Santucci A., Martelli P., Pacini A. Plasma factors controlling atrial natriuretic peptide (ANP) aggregation: role of lipoproteins. Biochim. Biophys. Acta. 1536:2001;123-132.
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 123-132
    • Maioli, E.1    Torricelli, C.2    Santucci, A.3    Martelli, P.4    Pacini, A.5
  • 20
    • 0032812981 scopus 로고    scopus 로고
    • Remodelling of high density lipoproteins by plasma factors
    • Rye K.A., Clay M.A., Barter P.J. Remodelling of high density lipoproteins by plasma factors. Atherosclerosis. 145:1999;227-238.
    • (1999) Atherosclerosis , vol.145 , pp. 227-238
    • Rye, K.A.1    Clay, M.A.2    Barter, P.J.3
  • 21
    • 0038352226 scopus 로고    scopus 로고
    • Hugh Sinclair Lecture: The regulation and remodelling of HDL by plasma factors
    • Barter P.J. Hugh Sinclair Lecture: the regulation and remodelling of HDL by plasma factors. Atheroscler. Suppl. 3:2002;39-47.
    • (2002) Atheroscler. Suppl. , vol.3 , pp. 39-47
    • Barter, P.J.1
  • 22
    • 0033965266 scopus 로고    scopus 로고
    • Very small apolipoprotein A-I-containing particles from human plasma: Isolation and quantification by high-performance size-exclusion chromatography
    • Nanjee M.N., Brinton E.A. Very small apolipoprotein A-I-containing particles from human plasma: isolation and quantification by high-performance size-exclusion chromatography. Clin. Chem. 46:2000;207-223.
    • (2000) Clin. Chem. , vol.46 , pp. 207-223
    • Nanjee, M.N.1    Brinton, E.A.2
  • 23
    • 0031935662 scopus 로고    scopus 로고
    • An overview of reverse cholesterol transport
    • Tall A.R. An overview of reverse cholesterol transport. Eur. Heart J. 19(Suppl. A):1998;A31-A35.
    • (1998) Eur. Heart J. , vol.19 , Issue.SUPPL. A
    • Tall, A.R.1
  • 25
    • 0028609448 scopus 로고
    • The soluble form of Alzheimer's amyloid beta protein is complexed to high density lipoprotein 3 and very high density lipoprotein in normal human plasma
    • Koudinov A., Matsubara E., Frangione B., Ghiso J. The soluble form of Alzheimer's amyloid beta protein is complexed to high density lipoprotein 3 and very high density lipoprotein in normal human plasma. Biochem. Biophys. Res. Commun. 205:1994;1164-1171.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1164-1171
    • Koudinov, A.1    Matsubara, E.2    Frangione, B.3    Ghiso, J.4
  • 26
    • 0032559575 scopus 로고    scopus 로고
    • Alzheimer's amyloid β interaction with normal human plasma high density lipoprotein: Association with apolipoprotein and lipids
    • Koudinov A.R., Berezov T.T., Kumar A., Koudinova N.V. Alzheimer's amyloid β interaction with normal human plasma high density lipoprotein: association with apolipoprotein and lipids. Clin. Chim. Acta. 270:1998;75-84.
    • (1998) Clin. Chim. Acta , vol.270 , pp. 75-84
    • Koudinov, A.R.1    Berezov, T.T.2    Kumar, A.3    Koudinova, N.V.4
  • 27
    • 0033976870 scopus 로고    scopus 로고
    • Transthyretin in high density lipoproteins: Association with apolipoprotein A-I
    • Sousa M.M., Berglund L., Saraiva M.J. Transthyretin in high density lipoproteins: association with apolipoprotein A-I. J. Lipid. Res. 41:2000;58-65.
    • (2000) J. Lipid. Res. , vol.41 , pp. 58-65
    • Sousa, M.M.1    Berglund, L.2    Saraiva, M.J.3
  • 29
    • 0037387168 scopus 로고    scopus 로고
    • Proteins from bovine tissues and biological fluids: Defining a reference electrophoresis map for liver, kidney, muscle, plasma and red blood cells
    • Talamo F., D'Ambrosio C., Arena S., Del Vecchio P., Ledda L., Zehender G., Ferrara L., Scaloni A. Proteins from bovine tissues and biological fluids: defining a reference electrophoresis map for liver, kidney, muscle, plasma and red blood cells. Proteomics. 3:2003;440-460.
    • (2003) Proteomics , vol.3 , pp. 440-460
    • Talamo, F.1    D'Ambrosio, C.2    Arena, S.3    Del Vecchio, P.4    Ledda, L.5    Zehender, G.6    Ferrara, L.7    Scaloni, A.8
  • 31
    • 0025826915 scopus 로고
    • Kinetic analysis of amyloid fibril polymerization in vitro
    • Naiki H., Higuchi K., Nakakuki K., Takeda T. Kinetic analysis of amyloid fibril polymerization in vitro. Lab. Invest. 65:1991;104-110.
    • (1991) Lab. Invest. , vol.65 , pp. 104-110
    • Naiki, H.1    Higuchi, K.2    Nakakuki, K.3    Takeda, T.4
  • 32
    • 0035900217 scopus 로고    scopus 로고
    • The levels of soluble amyloid beta in different high density lipoprotein subfractions distinguish Alzheimer's and normal aging cerebrospinal fluid: Implication for brain cholesterol pathology?
    • Koudinov A.R., Berezov T.T., Koudinova N.V. The levels of soluble amyloid beta in different high density lipoprotein subfractions distinguish Alzheimer's and normal aging cerebrospinal fluid: implication for brain cholesterol pathology? Neurosci. Lett. 314:2001;115-118.
    • (2001) Neurosci. Lett. , vol.314 , pp. 115-118
    • Koudinov, A.R.1    Berezov, T.T.2    Koudinova, N.V.3
  • 33
    • 0027161044 scopus 로고
    • Two-dimensional electrophoresis of plasma lipoproteins: Recognition of new apo A-I-containing subpopulations
    • Asztalos B.F., Sloop C.H., Wong L., Roheim P.S. Two-dimensional electrophoresis of plasma lipoproteins: recognition of new apo A-I-containing subpopulations. Biochim. Biophys. Acta. 1169:1993;291-300.
    • (1993) Biochim. Biophys. Acta , vol.1169 , pp. 291-300
    • Asztalos, B.F.1    Sloop, C.H.2    Wong, L.3    Roheim, P.S.4
  • 34
    • 0034673999 scopus 로고    scopus 로고
    • The conformation of apolipoprotein A-I in high-density lipoproteins is influenced by core lipid composition and particle size: A surface plasmon resonance study
    • Curtiss L.K., Bonnet D.J., Rye K.A. The conformation of apolipoprotein A-I in high-density lipoproteins is influenced by core lipid composition and particle size: a surface plasmon resonance study. Biochemistry. 39:2000;5712-5721.
    • (2000) Biochemistry , vol.39 , pp. 5712-5721
    • Curtiss, L.K.1    Bonnet, D.J.2    Rye, K.A.3
  • 35
    • 0029938009 scopus 로고    scopus 로고
    • Interaction between human amphipathic apolipoproteins, amyloid beta-peptide: Surface plasmon resonance studies
    • Shuvaev V.V., Siest G. Interaction between human amphipathic apolipoproteins, amyloid beta-peptide: surface plasmon resonance studies. FEBS Lett. 383:1996;9-12.
    • (1996) FEBS Lett. , vol.383 , pp. 9-12
    • Shuvaev, V.V.1    Siest, G.2
  • 36
    • 0025190483 scopus 로고
    • Structure activity in the atrial natriuretic peptide (ANP) family
    • Bovy P.R. Structure activity in the atrial natriuretic peptide (ANP) family. Med. Res. Rev. 10:1990;115-142.
    • (1990) Med. Res. Rev. , vol.10 , pp. 115-142
    • Bovy, P.R.1
  • 37
    • 0034112069 scopus 로고    scopus 로고
    • Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B
    • Wilkins D.K., Dobson C.M., Gross M. Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B. Eur. J. Biochem. 267:2000;2609-2616.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2609-2616
    • Wilkins, D.K.1    Dobson, C.M.2    Gross, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.