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Volumn 52, Issue 12, 2006, Pages 2258-2264

Bound homocysteine, cysteine, and cysteinylglycine distribution between albumin and globulins

Author keywords

[No Author keywords available]

Indexed keywords

ALBUMIN; BINDING PROTEIN; CYSTEINE; CYSTEINYLGLYCINE; DISULFIDE; GLOBULIN; GLUTATHIONE; HOMOCYSTEINE; OROSOMUCOID; TRANSFERRIN;

EID: 33845533655     PISSN: 00099147     EISSN: None     Source Type: Journal    
DOI: 10.1373/clinchem.2006.074302     Document Type: Article
Times cited : (46)

References (37)
  • 1
    • 3142680190 scopus 로고    scopus 로고
    • Homocysteine and cardiovascular disease: Biological mechanisms, observational epidemiology, and the need for randomized trials
    • Splaver A, Lamas GA, Hennekens CH. Homocysteine and cardiovascular disease: biological mechanisms, observational epidemiology, and the need for randomized trials. Am Heart J 2004;148:34-40.
    • (2004) Am Heart J , vol.148 , pp. 34-40
    • Splaver, A.1    Lamas, G.A.2    Hennekens, C.H.3
  • 2
    • 0037164104 scopus 로고    scopus 로고
    • Homocysteine and risk of ischemic heart disease and stroke: A meta-analysis
    • Homocysteine Studies Collaboration
    • Homocysteine Studies Collaboration. Homocysteine and risk of ischemic heart disease and stroke: a meta-analysis. JAMA 2002;288:2015-22.
    • (2002) JAMA , vol.288 , pp. 2015-2022
  • 4
    • 0035967497 scopus 로고    scopus 로고
    • Plasma total cysteine as a risk factor for vascular disease: The European Concerted Action Project
    • European Concerted Action Project
    • El-Khairy L, Ueland PM, Refsum H, Graham IM, Vollset SE, European Concerted Action Project. Plasma total cysteine as a risk factor for vascular disease: The European Concerted Action Project. Circulation 2001;103:2544-9.
    • (2001) Circulation , vol.103 , pp. 2544-2549
    • El-Khairy, L.1    Ueland, P.M.2    Refsum, H.3    Graham, I.M.4    Vollset, S.E.5
  • 5
    • 9144225352 scopus 로고    scopus 로고
    • Facts and recommendations about total homocysteine determinations: An expert opinion
    • Refsum H, Smith AD, Ueland PM, Nexo E, Clarke R, McPartlin J, et al. Facts and recommendations about total homocysteine determinations: an expert opinion. Clin Chem 2004;50:3-32.
    • (2004) Clin Chem , vol.50 , pp. 3-32
    • Refsum, H.1    Smith, A.D.2    Ueland, P.M.3    Nexo, E.4    Clarke, R.5    McPartlin, J.6
  • 6
    • 0029257541 scopus 로고
    • Homocysteine species as components of plasma redox thiol status
    • Ueland PM. Homocysteine species as components of plasma redox thiol status. Clin Chem 1995;41:340-2.
    • (1995) Clin Chem , vol.41 , pp. 340-342
    • Ueland, P.M.1
  • 7
    • 0035839468 scopus 로고    scopus 로고
    • Albumin thiolate anion is an intermediate in the formation of albumin-S-S-homocysteine
    • Sengupta S, Chen H, Togawa T, DiBello PM, Majors AK, Budy B, et al. Albumin thiolate anion is an intermediate in the formation of albumin-S-S-homocysteine. J Biol Chem 2001;276:30111-7.
    • (2001) J Biol Chem , vol.276 , pp. 30111-30117
    • Sengupta, S.1    Chen, H.2    Togawa, T.3    DiBello, P.M.4    Majors, A.K.5    Budy, B.6
  • 8
    • 27744467308 scopus 로고    scopus 로고
    • Molecular targeting by homocysteine: A mechanism for vascular pathogenesis
    • Jacobsen DW, Catanescu O, Dibello PM, Barbato JC. Molecular targeting by homocysteine: a mechanism for vascular pathogenesis. Clin Chem Lab Med 2005;43:1076-83,
    • (2005) Clin Chem Lab Med , vol.43 , pp. 1076-1083
    • Jacobsen, D.W.1    Catanescu, O.2    Dibello, P.M.3    Barbato, J.C.4
  • 9
    • 0037163003 scopus 로고    scopus 로고
    • Homocysteine is a protein amino acid in humans: Implications for homocysteine-linked disease
    • Jakubowski H. Homocysteine is a protein amino acid in humans: implications for homocysteine-linked disease. J Biol Chem 2002;277:30425-8.
    • (2002) J Biol Chem , vol.277 , pp. 30425-30428
    • Jakubowski, H.1
  • 11
    • 14544298742 scopus 로고    scopus 로고
    • Quantification of thiol-containing amino acids linked by disulfides to LDL
    • Zinellu A, Sotgia S, Deianna L, Carru C. Quantification of thiol-containing amino acids linked by disulfides to LDL. Clin Chem 2005;51:658-60.
    • (2005) Clin Chem , vol.51 , pp. 658-660
    • Zinellu, A.1    Sotgia, S.2    Deianna, L.3    Carru, C.4
  • 12
    • 0347379933 scopus 로고    scopus 로고
    • In vitro and in vivo interactions of homocysteine with human plasma transthyretin
    • Lim A, Sengupta S, McComb ME, Theberge R, Wilson WG, Costello CE, et al. In vitro and in vivo interactions of homocysteine with human plasma transthyretin. J Biol Chem 2003;278:49707-13.
    • (2003) J Biol Chem , vol.278 , pp. 49707-49713
    • Lim, A.1    Sengupta, S.2    McComb, M.E.3    Theberge, R.4    Wilson, W.G.5    Costello, C.E.6
  • 13
    • 4344693152 scopus 로고    scopus 로고
    • Detection of genetic variants of transthyretin by liquid chromatography-dual electrospray ionization Fourier-transform ion cyclotron resonance mass spectrometry
    • Nepomuceno AI, Mason CJ, Muddiman DC, Berger HR III, Zeldenrust SR. Detection of genetic variants of transthyretin by liquid chromatography-dual electrospray ionization Fourier-transform ion cyclotron resonance mass spectrometry. Clin Chem 2004;50:1535-43.
    • (2004) Clin Chem , vol.50 , pp. 1535-1543
    • Nepomuceno, A.I.1    Mason, C.J.2    Muddiman, D.C.3    Berger III, H.R.4    Zeldenrust, S.R.5
  • 14
    • 27744557055 scopus 로고    scopus 로고
    • Characterization of the microheterogeneity of transthyretin in plasma and urine using SELDI-TOF-MS immunoassay
    • Schweigert FJ, Wirth K, Raila J. Characterization of the microheterogeneity of transthyretin in plasma and urine using SELDI-TOF-MS immunoassay. Proteome Sci 2004;2:5.
    • (2004) Proteome Sci , vol.2 , pp. 5
    • Schweigert, F.J.1    Wirth, K.2    Raila, J.3
  • 15
    • 0141497435 scopus 로고    scopus 로고
    • S-homocysteinylation of transthyretin is detected in plasma and serum of humans with different types of hyperhomocysteinemia
    • Sass JO, Nakanishi T, Sato T, Sperl W, Shimizu A. S-homocysteinylation of transthyretin is detected in plasma and serum of humans with different types of hyperhomocysteinemia. Biochem Biophys Res Commun 2003;310:242-6.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 242-246
    • Sass, J.O.1    Nakanishi, T.2    Sato, T.3    Sperl, W.4    Shimizu, A.5
  • 16
    • 0042848710 scopus 로고    scopus 로고
    • Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions
    • Zhang Q, Kelly JW. Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions. Biochemistry 2003;42:8756-61.
    • (2003) Biochemistry , vol.42 , pp. 8756-8761
    • Zhang, Q.1    Kelly, J.W.2
  • 18
    • 33745442821 scopus 로고    scopus 로고
    • The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome
    • Hortin GL. The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome. Clin Chem 2006;52:1223-37.
    • (2006) Clin Chem , vol.52 , pp. 1223-1237
    • Hortin, G.L.1
  • 19
    • 23944495100 scopus 로고    scopus 로고
    • Immunoaffinity separation of plasma proteins by IgY microbeads: Meeting the needs of proteomic sample preparation and analysis
    • Huang L, Harvie G, Feitelson JS, Gramatikoff K, Herold DA, Allen DL, et al. Immunoaffinity separation of plasma proteins by IgY microbeads: meeting the needs of proteomic sample preparation and analysis. Proteomics 2005;5:3314-28.
    • (2005) Proteomics , vol.5 , pp. 3314-3328
    • Huang, L.1    Harvie, G.2    Feitelson, J.S.3    Gramatikoff, K.4    Herold, D.A.5    Allen, D.L.6
  • 21
    • 0035011308 scopus 로고    scopus 로고
    • Relationships of plasma homocysteine to cysteine and albumin levels: Potential utility of assessing cysteine levels
    • Hortin GL, Sullivan P, Csako GA. Relationships of plasma homocysteine to cysteine and albumin levels: potential utility of assessing cysteine levels. Clin Chem 2001;47:1121-4.
    • (2001) Clin Chem , vol.47 , pp. 1121-1124
    • Hortin, G.L.1    Sullivan, P.2    Csako, G.A.3
  • 22
    • 33845527559 scopus 로고    scopus 로고
    • Mass determination of major plasma proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)
    • In press
    • Hortin GL, Remaley AT. Mass determination of major plasma proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). Clin Proteomics In press.
    • Clin Proteomics
    • Hortin, G.L.1    Remaley, A.T.2
  • 23
    • 0030691945 scopus 로고    scopus 로고
    • High density lipoprotein particle size restriction in apolipoprotein A-I(Milano) transgenic mice
    • Bielicki JK, Forte TM, McCall MR, Stoltzfus LJ, Chiesa G, Sirtori CR, et al. High density lipoprotein particle size restriction in apolipoprotein A-I(Milano) transgenic mice. J Lipid Res 1997;38:2314-21.
    • (1997) J Lipid Res , vol.38 , pp. 2314-2321
    • Bielicki, J.K.1    Forte, T.M.2    McCall, M.R.3    Stoltzfus, L.J.4    Chiesa, G.5    Sirtori, C.R.6
  • 24
    • 0033977770 scopus 로고    scopus 로고
    • Metabolism of apolipoproteins AI and AII in subjects carrying similar apoAI mutations, apoAI Milano and apoAI Paris
    • Perez-Mendez O, Bruckert E, Franceschini G, Duhal N, Lacroix B, Bonte JP, et al. Metabolism of apolipoproteins AI and AII in subjects carrying similar apoAI mutations, apoAI Milano and apoAI Paris. Atherosclerosis 2000;148:317-25.
    • (2000) Atherosclerosis , vol.148 , pp. 317-325
    • Perez-Mendez, O.1    Bruckert, E.2    Franceschini, G.3    Duhal, N.4    Lacroix, B.5    Bonte, J.P.6
  • 25
    • 3142562245 scopus 로고    scopus 로고
    • Alpha 1-microglobulin: Clinical laboratory aspects and applications
    • Penders J, Delanghe JR. Alpha 1-microglobulin: clinical laboratory aspects and applications. Clin Chim Acta 2004;346:107-18.
    • (2004) Clin Chim Acta , vol.346 , pp. 107-118
    • Penders, J.1    Delanghe, J.R.2
  • 27
    • 0031815338 scopus 로고    scopus 로고
    • 1- acid glycoprotein: Generation of a three-dimensional quantitative structure-activity relationship model for drug binding to the A variant
    • 1-acid glycoprotein: generation of a three-dimensional quantitative structure-activity relationship model for drug binding to the A variant. Mol Pharmacol 1998;54:129-38.
    • (1998) Mol Pharmacol , vol.54 , pp. 129-138
    • Herve, F.1    Caron, G.2    Duche, J.C.3    Gaillard, P.4    Abd, N.5    Tsantili-Kakoulidou, A.6
  • 29
    • 1242294484 scopus 로고    scopus 로고
    • A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein
    • Bass R, Ruddock LW, Klappa P, Freedman RB. A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 2004;279:5257-62.
    • (2004) J Biol Chem , vol.279 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4
  • 30
    • 22044437820 scopus 로고    scopus 로고
    • The S-thiolating activity of membrane gamma-glutamyltransferase: Formation of cysteinyl-glycine mixed disulfides with cellular proteins and in the cell microenvironment
    • Corti A, Paolicchi A, Franzini M, Dominici S, Casini AF, Pompella A. The S-thiolating activity of membrane gamma-glutamyltransferase: formation of cysteinyl-glycine mixed disulfides with cellular proteins and in the cell microenvironment. Antioxid Redox Signal 2005;7:911-8.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 911-918
    • Corti, A.1    Paolicchi, A.2    Franzini, M.3    Dominici, S.4    Casini, A.F.5    Pompella, A.6
  • 31
    • 0141450396 scopus 로고    scopus 로고
    • Elevated plasma homocysteine leads to alterations in fibrin clot structure and stability: Implications for the mechanism of thrombosis in hyperhomocysteinemia
    • Sauls DL, Wolberg AS, Huffman M. Elevated plasma homocysteine leads to alterations in fibrin clot structure and stability: implications for the mechanism of thrombosis in hyperhomocysteinemia. J Thromb Haemost 2003;1:300-6.
    • (2003) J Thromb Haemost , vol.1 , pp. 300-306
    • Sauls, D.L.1    Wolberg, A.S.2    Huffman, M.3
  • 33
    • 0027932744 scopus 로고
    • A new substitution, gamma 358 Ser→Cys, in fibrinogen Milano VII causes defective fibrin polymerization
    • Steinmann C, Bogli C, Jungo M, Lammle B, Heinemann G, Wermuth B, et al. A new substitution, gamma 358 Ser→Cys, in fibrinogen Milano VII causes defective fibrin polymerization. Blood 1994;84:1874-80.
    • (1994) Blood , vol.84 , pp. 1874-1880
    • Steinmann, C.1    Bogli, C.2    Jungo, M.3    Lammle, B.4    Heinemann, G.5    Wermuth, B.6
  • 34
    • 0034575124 scopus 로고    scopus 로고
    • Apolipoprotein E far more than a lipid transport protein
    • Mahley RW, Rail SC Jr. Apolipoprotein E. far more than a lipid transport protein. Annu Rev Genomics Hum Genet 2000;1:507-37.
    • (2000) Annu Rev Genomics Hum Genet , vol.1 , pp. 507-537
    • Mahley, R.W.1    Rail Jr., S.C.2
  • 35
    • 0030035470 scopus 로고    scopus 로고
    • Consensus of a group of professional societies and diagnostic companies on guidelines for interim reference ranges for 14 protein in serum based on the standardization against the IFCC/BCR/CAP reference material (CRM 470)
    • Dati F, Schumann G, Thomas L, Aguzzi F, Baudner S, Bienvenu J, et al. Consensus of a group of professional societies and diagnostic companies on guidelines for interim reference ranges for 14 protein in serum based on the standardization against the IFCC/BCR/CAP reference material (CRM 470). Eur J Clin Chem Clin Biochem 1996;34:517-20.
    • (1996) Eur J Clin Chem Clin Biochem , vol.34 , pp. 517-520
    • Dati, F.1    Schumann, G.2    Thomas, L.3    Aguzzi, F.4    Baudner, S.5    Bienvenu, J.6
  • 36
    • 0002219603 scopus 로고
    • α, β, γ, ω - The roster of the plasma proteins
    • Putnam FW, ed. New York: Academic Press
    • Putnam FW. α, β, γ, ω-the roster of the plasma proteins. In: Putnam FW, ed. The Plasma Proteins, 2nd ed., Vol. 1. New York: Academic Press, 1975:57-130.
    • (1975) The Plasma Proteins, 2nd Ed. , vol.1 , pp. 57-130
    • Putnam, F.W.1


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