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Volumn 369, Issue 2, 2008, Pages 686-691

Abacavir and warfarin modulate allosterically kinetics of NO dissociation from ferrous nitrosylated human serum heme-albumin

Author keywords

Abacavir; Allostery; Drug dependent denitrosylation kinetics; Ferrous nitrosylated human serum heme albumin; Warfarin

Indexed keywords

ABACAVIR; FERROUS ION; HEME; HUMAN SERUM ALBUMIN; NITRIC OXIDE; WARFARIN;

EID: 40849114506     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.02.077     Document Type: Article
Times cited : (22)

References (54)
  • 1
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow G., Birkett D.J., and Wade D.N. The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11 (1975) 824-832
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 2
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter D.C., and Ho J.X. Structure of serum albumin. Adv. Protein Chem. 45 (1994) 153-203
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 4
    • 0035992779 scopus 로고    scopus 로고
    • Reversible and covalent binding of drugs to human serum albumin: methodological approaches and physiological relevance
    • Bertucci C., and Domenici E. Reversible and covalent binding of drugs to human serum albumin: methodological approaches and physiological relevance. Curr. Med. Chem. 9 (2002) 1463-1481
    • (2002) Curr. Med. Chem. , vol.9 , pp. 1463-1481
    • Bertucci, C.1    Domenici, E.2
  • 5
    • 0037591928 scopus 로고    scopus 로고
    • Beyond expansion: structural studies on the transport roles of human serum albumin
    • Curry S. Beyond expansion: structural studies on the transport roles of human serum albumin. Vox Sang. 83 1 (2002) 315-319
    • (2002) Vox Sang. , vol.83 , Issue.1 , pp. 315-319
    • Curry, S.1
  • 6
    • 0036599564 scopus 로고    scopus 로고
    • Practical aspects of the ligand-binding and enzymatic properties of human serum albumin
    • Kragh-Hansen U., Chuang V.T., and Otagiri M. Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol. Pharm. Bull. 25 (2002) 695-704
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 695-704
    • Kragh-Hansen, U.1    Chuang, V.T.2    Otagiri, M.3
  • 7
    • 1242337279 scopus 로고    scopus 로고
    • Esterase-like activity of serum albumin: characterization of its structural chemistry using p-nitrophenyl esters as substrates
    • Sakurai Y., Ma S.F., Watanabe H., Yamaotsu N., Hirono S., Kurono Y., Kragh-Hansen U., and Otagiri M. Esterase-like activity of serum albumin: characterization of its structural chemistry using p-nitrophenyl esters as substrates. Pharm. Res. 21 (2004) 285-292
    • (2004) Pharm. Res. , vol.21 , pp. 285-292
    • Sakurai, Y.1    Ma, S.F.2    Watanabe, H.3    Yamaotsu, N.4    Hirono, S.5    Kurono, Y.6    Kragh-Hansen, U.7    Otagiri, M.8
  • 8
    • 2642586736 scopus 로고    scopus 로고
    • Competition of drugs to serum albumin in combination therapy
    • Sułkowska A., Bojko B., Równicka J., and Sułkowski W. Competition of drugs to serum albumin in combination therapy. Biopolymers 74 (2004) 256-262
    • (2004) Biopolymers , vol.74 , pp. 256-262
    • Sułkowska, A.1    Bojko, B.2    Równicka, J.3    Sułkowski, W.4
  • 10
    • 29144461887 scopus 로고    scopus 로고
    • Allosteric modulation of anti-HIV drug and ferric heme binding to human serum albumin
    • Bocedi A., Notari S., Menegatti E., Fanali G., Fasano M., and Ascenzi P. Allosteric modulation of anti-HIV drug and ferric heme binding to human serum albumin. FEBS J. 272 (2005) 6287-6296
    • (2005) FEBS J. , vol.272 , pp. 6287-6296
    • Bocedi, A.1    Notari, S.2    Menegatti, E.3    Fanali, G.4    Fasano, M.5    Ascenzi, P.6
  • 14
    • 33748766072 scopus 로고    scopus 로고
    • Drug binding to human serum albumin: abridged review of results obtained with high-performance liquid chromatography and circular dichroism
    • Ascoli G.A., Domenici E., and Bertucci C. Drug binding to human serum albumin: abridged review of results obtained with high-performance liquid chromatography and circular dichroism. Chirality 18 (2006) 667-679
    • (2006) Chirality , vol.18 , pp. 667-679
    • Ascoli, G.A.1    Domenici, E.2    Bertucci, C.3
  • 15
    • 33644681693 scopus 로고    scopus 로고
    • Stereoselective binding of human serum albumin
    • Chuang V.T., and Otagiri M. Stereoselective binding of human serum albumin. Chirality 18 (2006) 159-166
    • (2006) Chirality , vol.18 , pp. 159-166
    • Chuang, V.T.1    Otagiri, M.2
  • 16
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He X., and Carter D.C. Atomic structure and chemistry of human serum albumin. Nature 358 (1992) 209-215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.1    Carter, D.C.2
  • 17
  • 19
    • 3042673067 scopus 로고    scopus 로고
    • Crystal structural analysis of human serum albumin complexed with hemin and fatty acid
    • Zunszain P.A., Ghuman J., Komatsu T., Tsuchida E., and Curry S. Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. BMC Struct. Biol. 3 (2003) 6
    • (2003) BMC Struct. Biol. , vol.3 , pp. 6
    • Zunszain, P.A.1    Ghuman, J.2    Komatsu, T.3    Tsuchida, E.4    Curry, S.5
  • 20
    • 0035210356 scopus 로고    scopus 로고
    • Effect of ibuprofen and warfarin on the allosteric properties of haem-human serum albumin: a spectroscopic study
    • Baroni S., Mattu M., Vannini A., Cipollone R., Aime S., Ascenzi P., and Fasano M. Effect of ibuprofen and warfarin on the allosteric properties of haem-human serum albumin: a spectroscopic study. Eur. J. Biochem. 268 (2001) 6214-6220
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6214-6220
    • Baroni, S.1    Mattu, M.2    Vannini, A.3    Cipollone, R.4    Aime, S.5    Ascenzi, P.6    Fasano, M.7
  • 21
    • 0019359357 scopus 로고
    • Human serum albumin as an allosteric two-state protein: evidence from effects of calcium and warfarin on proton binding behaviour
    • Janssen L.H., Van Wilgenburg M.T., and Wilting J. Human serum albumin as an allosteric two-state protein: evidence from effects of calcium and warfarin on proton binding behaviour. Biochim. Biophys. Acta 669 (1981) 244-250
    • (1981) Biochim. Biophys. Acta , vol.669 , pp. 244-250
    • Janssen, L.H.1    Van Wilgenburg, M.T.2    Wilting, J.3
  • 22
    • 25444527458 scopus 로고    scopus 로고
    • Allosteric modulation of myristate and Mn(III)heme binding to human serum albumin: optical and NMR spectroscopy characterization
    • Fanali G., Fesce R., Agrati C., Ascenzi P., and Fasano M. Allosteric modulation of myristate and Mn(III)heme binding to human serum albumin: optical and NMR spectroscopy characterization. FEBS J. 272 (2005) 4672-4683
    • (2005) FEBS J. , vol.272 , pp. 4672-4683
    • Fanali, G.1    Fesce, R.2    Agrati, C.3    Ascenzi, P.4    Fasano, M.5
  • 23
    • 34548138940 scopus 로고    scopus 로고
    • Modulation of heme and myristate binding to human serum albumin by anti-HIV drugs. An optical and NMR spectroscopic study
    • Fanali G., Bocedi A., Ascenzi P., and Fasano M. Modulation of heme and myristate binding to human serum albumin by anti-HIV drugs. An optical and NMR spectroscopic study. FEBS J. 274 (2007) 4491-4502
    • (2007) FEBS J. , vol.274 , pp. 4491-4502
    • Fanali, G.1    Bocedi, A.2    Ascenzi, P.3    Fasano, M.4
  • 24
    • 0024346192 scopus 로고
    • Flash photolysis of the serum albumin-heme-CO complex
    • Marden M.C., Hazard E.S., Leclerc L., and Gibson Q.H. Flash photolysis of the serum albumin-heme-CO complex. Biochemistry 28 (1989) 4422-4426
    • (1989) Biochemistry , vol.28 , pp. 4422-4426
    • Marden, M.C.1    Hazard, E.S.2    Leclerc, L.3    Gibson, Q.H.4
  • 25
    • 0031006612 scopus 로고    scopus 로고
    • Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase
    • Kharitonov V.G., Sharma V.S., Magde D., and Koesling D. Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase. Biochemistry 36 (1997) 6814-6818
    • (1997) Biochemistry , vol.36 , pp. 6814-6818
    • Kharitonov, V.G.1    Sharma, V.S.2    Magde, D.3    Koesling, D.4
  • 27
    • 0035321821 scopus 로고    scopus 로고
    • Effect of bezafibrate and clofibrate on the heme-iron geometry of ferrous nitrosylated heme-human serum albumin: an EPR study
    • Mattu M., Vannini A., Coletta M., Fasano M., and Ascenzi P. Effect of bezafibrate and clofibrate on the heme-iron geometry of ferrous nitrosylated heme-human serum albumin: an EPR study. J. Inorg. Biochem. 84 (2001) 293-296
    • (2001) J. Inorg. Biochem. , vol.84 , pp. 293-296
    • Mattu, M.1    Vannini, A.2    Coletta, M.3    Fasano, M.4    Ascenzi, P.5
  • 29
    • 0037199866 scopus 로고    scopus 로고
    • The heme-iron geometry of ferrous nitrosylated heme-serum lipoproteins, hemopexin, and albumin: a comparative EPR study
    • Fasano M., Mattu M., Coletta M., and Ascenzi P. The heme-iron geometry of ferrous nitrosylated heme-serum lipoproteins, hemopexin, and albumin: a comparative EPR study. J. Inorg. Biochem. 91 (2002) 487-490
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 487-490
    • Fasano, M.1    Mattu, M.2    Coletta, M.3    Ascenzi, P.4
  • 30
    • 0036933340 scopus 로고    scopus 로고
    • Spectroscopic studies on human serum albumin and methemalbumin: optical, steady-state, and picosecond time-resolved fluorescence studies, and kinetics of substrate oxidation by methemalbumin
    • Kamal J.K., and Behere D.V. Spectroscopic studies on human serum albumin and methemalbumin: optical, steady-state, and picosecond time-resolved fluorescence studies, and kinetics of substrate oxidation by methemalbumin. J. Biol. Inorg. Chem. 7 (2002) 273-283
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 273-283
    • Kamal, J.K.1    Behere, D.V.2
  • 31
    • 27844506038 scopus 로고    scopus 로고
    • 2 and CO binding properties of artificial hemoproteins formed by complexing iron protoporphyrin IX with human serum albumin mutants
    • 2 and CO binding properties of artificial hemoproteins formed by complexing iron protoporphyrin IX with human serum albumin mutants. J. Am. Chem. Soc. 127 (2005) 15933-15942
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15933-15942
    • Komatsu, T.1    Ohmichi, N.2    Nakagawa, A.3    Zunszain, P.A.4    Curry, S.5    Tsuchida, E.6
  • 33
    • 33845750255 scopus 로고    scopus 로고
    • Abacavir modulates peroxynitrite-mediated oxidation of ferrous nitrosylated human serum heme-albumin
    • Ascenzi P., and Fasano M. Abacavir modulates peroxynitrite-mediated oxidation of ferrous nitrosylated human serum heme-albumin. Biochem. Biophys. Res. Commun. 353 (2007) 469-474
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 469-474
    • Ascenzi, P.1    Fasano, M.2
  • 34
    • 34347219413 scopus 로고    scopus 로고
    • Effect of prototypic drugs ibuprofen and warfarin on global chaotropic unfolding of human serum heme-albumin: a fast-field-cycling 1H-NMR relaxometric study
    • Fanali G., Ascenzi P., and Fasano M. Effect of prototypic drugs ibuprofen and warfarin on global chaotropic unfolding of human serum heme-albumin: a fast-field-cycling 1H-NMR relaxometric study. Biophys. Chem. 129 (2007) 29-35
    • (2007) Biophys. Chem. , vol.129 , pp. 29-35
    • Fanali, G.1    Ascenzi, P.2    Fasano, M.3
  • 36
    • 0017112413 scopus 로고
    • Cooperativity in the dissociation of nitric oxide from hemoglobin
    • Moore E.G., and Gibson Q.H. Cooperativity in the dissociation of nitric oxide from hemoglobin. J. Biol. Chem. 251 (1976) 2788-2794
    • (1976) J. Biol. Chem. , vol.251 , pp. 2788-2794
    • Moore, E.G.1    Gibson, Q.H.2
  • 41
    • 17644393552 scopus 로고    scopus 로고
    • Mechanistic studies of the oxygen-mediated oxidation of nitrosylhemoglobin
    • Herold S., and Röck G. Mechanistic studies of the oxygen-mediated oxidation of nitrosylhemoglobin. Biochemistry 44 (2005) 6223-6231
    • (2005) Biochemistry , vol.44 , pp. 6223-6231
    • Herold, S.1    Röck, G.2
  • 43
    • 34247495006 scopus 로고    scopus 로고
    • 2 -mediated oxidation of ferrous nitrosylated Mycobacterium leprae truncated hemoglobin O
    • 2 -mediated oxidation of ferrous nitrosylated Mycobacterium leprae truncated hemoglobin O. Biochem. Biophys. Res. Commun. 357 (2007) 809-814
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 809-814
    • Ascenzi, P.1    Bolognesi, M.2    Visca, P.3
  • 45
    • 0037177162 scopus 로고    scopus 로고
    • Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis
    • Mukai M., Savard P.Y., Ouellet H., Guertin M., and Yeh S.R. Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis. Biochemistry 41 (2002) 3897-3905
    • (2002) Biochemistry , vol.41 , pp. 3897-3905
    • Mukai, M.1    Savard, P.Y.2    Ouellet, H.3    Guertin, M.4    Yeh, S.R.5
  • 46
    • 0038624089 scopus 로고    scopus 로고
    • A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O
    • Milani M., Savard P.Y., Ouellet H., Ascenzi P., Guertin M., and Bolognesi M. A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O. Proc. Natl. Acad. Sci. USA 100 (2003) 5766-5771
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5766-5771
    • Milani, M.1    Savard, P.Y.2    Ouellet, H.3    Ascenzi, P.4    Guertin, M.5    Bolognesi, M.6
  • 47
    • 33748804669 scopus 로고    scopus 로고
    • Ligand selectivity of soluble guanylyl cyclase: effect of the hydrogen-bonding tyrosine in the distal heme pocket on binding of oxygen, nitric oxide, and carbon monoxide
    • Martin E., Berka V., Bogatenkova E., Murad F., and Tsai A.L. Ligand selectivity of soluble guanylyl cyclase: effect of the hydrogen-bonding tyrosine in the distal heme pocket on binding of oxygen, nitric oxide, and carbon monoxide. J. Biol. Chem. 281 (2006) 27836-27845
    • (2006) J. Biol. Chem. , vol.281 , pp. 27836-27845
    • Martin, E.1    Berka, V.2    Bogatenkova, E.3    Murad, F.4    Tsai, A.L.5
  • 48
    • 0346096863 scopus 로고    scopus 로고
    • Crystallographic analysis of the interaction of nitric oxide with quaternary-T human haemoglobin
    • Chan N.L., Kavanaugh J.S., Rogers P.H., and Arnone A. Crystallographic analysis of the interaction of nitric oxide with quaternary-T human haemoglobin. Biochemistry 43 (2004) 118-132
    • (2004) Biochemistry , vol.43 , pp. 118-132
    • Chan, N.L.1    Kavanaugh, J.S.2    Rogers, P.H.3    Arnone, A.4
  • 49
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains
    • Paoli M., Anderson B.F., Baker H.M., Morgan W.T., Smith A., and Baker E.N. Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains. Nat. Struct. Biol. 6 (1999) 926-931
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 50
    • 0141480853 scopus 로고    scopus 로고
    • Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane
    • Copeland D.M., West A.H., and Richter-Addo G.B. Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane. Proteins 53 (2003) 182-192
    • (2003) Proteins , vol.53 , pp. 182-192
    • Copeland, D.M.1    West, A.H.2    Richter-Addo, G.B.3
  • 52
    • 17144408393 scopus 로고    scopus 로고
    • Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family
    • Erratum in: IUBMB Life 57 (2005) 459-460
    • de Sanctis D., Pesce A., Nardini M., Bolognesi M., Bocedi A., and Ascenzi P. Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family. IUBMB Life 56 (2004) 643-651 Erratum in: IUBMB Life 57 (2005) 459-460
    • (2004) IUBMB Life , vol.56 , pp. 643-651
    • de Sanctis, D.1    Pesce, A.2    Nardini, M.3    Bolognesi, M.4    Bocedi, A.5    Ascenzi, P.6
  • 53
    • 10644251786 scopus 로고    scopus 로고
    • The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for-control of ligand affinity
    • Vallone B., Nienhaus K., Matthes A., Brunori M., and Nienhaus G.U. The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for-control of ligand affinity. Proc. Natl. Acad. Sci. USA 101 (2004) 17351-17356
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17351-17356
    • Vallone, B.1    Nienhaus, K.2    Matthes, A.3    Brunori, M.4    Nienhaus, G.U.5
  • 54
    • 0033842504 scopus 로고    scopus 로고
    • Five recombinant fragments of human serum albumin-tools for the characterization of the warfarin binding site
    • Dockal M., Chang M., Carter D.C., and Rüker F. Five recombinant fragments of human serum albumin-tools for the characterization of the warfarin binding site. Protein Sci. 9 (2000) 1455-1465
    • (2000) Protein Sci. , vol.9 , pp. 1455-1465
    • Dockal, M.1    Chang, M.2    Carter, D.C.3    Rüker, F.4


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