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Volumn 9, Issue 11, 2010, Pages 5770-5781

Combined proteomic approaches for the identification of specific amino acid residues modified by 4-hydroxy-2-nonenal under physiological conditions

Author keywords

spectrin; 4 hydroxy 2 nonenal; bovine serum albumin; erythrocyte membrane proteins; post translational protein modification; redox proteomics

Indexed keywords

4 HYDROXYNONENAL; AMINO ACID; BOVINE SERUM ALBUMIN; MEMBRANE PROTEIN; SPECTRIN; SPECTRIN BETA SUBUNIT; UNCLASSIFIED DRUG;

EID: 78149400309     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100555v     Document Type: Article
Times cited : (24)

References (42)
  • 1
    • 0037411282 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal: A product and mediator of oxidative stress
    • Uchida, K. 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress Prog. Lipid Res. 2003, 42, 318-343
    • (2003) Prog. Lipid Res. , vol.42 , pp. 318-343
    • Uchida, K.1
  • 2
    • 0037799214 scopus 로고    scopus 로고
    • Structural basis of protein-bound endogenous aldehydes. Chemical and immunochemical characterizations of configurational isomers of a 4-hydroxy-2-nonenal-histidine adduct
    • Hashimoto, M.; Sibata, T.; Wasada, H.; Toyokuni, S.; Uchida, K. Structural basis of protein-bound endogenous aldehydes. Chemical and immunochemical characterizations of configurational isomers of a 4-hydroxy-2-nonenal-histidine adduct J. Biol. Chem. 2003, 278, 5044-5051
    • (2003) J. Biol. Chem. , vol.278 , pp. 5044-5051
    • Hashimoto, M.1    Sibata, T.2    Wasada, H.3    Toyokuni, S.4    Uchida, K.5
  • 3
    • 0037184911 scopus 로고    scopus 로고
    • Covalent modification of epithelial fatty acid-binding protein by 4-hydroxynonenal in vitro and in vivo. Evidence for a role in antioxidant biology
    • Bennaars-Eiden, A.; Higgins, L.; Hertzel, A. V.; Kapphahn, R. J.; Ferrington, D. A.; Bernlohr, D. A. Covalent modification of epithelial fatty acid-binding protein by 4-hydroxynonenal in vitro and in vivo. Evidence for a role in antioxidant biology J. Biol. Chem. 2002, 277, 50693-50702
    • (2002) J. Biol. Chem. , vol.277 , pp. 50693-50702
    • Bennaars-Eiden, A.1    Higgins, L.2    Hertzel, A.V.3    Kapphahn, R.J.4    Ferrington, D.A.5    Bernlohr, D.A.6
  • 4
    • 33751516438 scopus 로고    scopus 로고
    • Identification of 4-hydroxynonenal-modified retinal proteins induced by photooxidative stress prior to retinal degeneration
    • Tanito, M.; Haniu, H.; Elliott, M. H.; Singh, A. K.; Matsumoto, H.; Anderson, R. E. Identification of 4-hydroxynonenal-modified retinal proteins induced by photooxidative stress prior to retinal degeneration Free Radical Biol. Med. 2006, 41, 1847-1859
    • (2006) Free Radical Biol. Med. , vol.41 , pp. 1847-1859
    • Tanito, M.1    Haniu, H.2    Elliott, M.H.3    Singh, A.K.4    Matsumoto, H.5    Anderson, R.E.6
  • 6
    • 52249110951 scopus 로고    scopus 로고
    • The M18 aspartyl aminopeptidase of Plasmodium falciparum binds to human erythrocyte spectrin in vitro
    • Lauterbach, S. B.; Coetzer, T. L. The M18 aspartyl aminopeptidase of Plasmodium falciparum binds to human erythrocyte spectrin in vitro Malar. J. 2008, 7, 161
    • (2008) Malar. J. , vol.7 , pp. 161
    • Lauterbach, S.B.1    Coetzer, T.L.2
  • 7
    • 1242338830 scopus 로고    scopus 로고
    • Identification of 4-hydroxy-2-nonenal-modified peptides within unfractionated digests using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Fenaille, F.; Tabet, J. C.; Guy, P. A. Identification of 4-hydroxy-2-nonenal-modified peptides within unfractionated digests using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Anal. Chem. 2004, 76, 867-873
    • (2004) Anal. Chem. , vol.76 , pp. 867-873
    • Fenaille, F.1    Tabet, J.C.2    Guy, P.A.3
  • 8
    • 33748567134 scopus 로고    scopus 로고
    • Gel-free mass spectrometry-based high throughput proteomics: Tools for studying biological response of proteins and proteomes
    • Roe, M. R.; Griffin, T. J. Gel-free mass spectrometry-based high throughput proteomics: tools for studying biological response of proteins and proteomes Proteomics 2006, 6, 4678-4687
    • (2006) Proteomics , vol.6 , pp. 4678-4687
    • Roe, M.R.1    Griffin, T.J.2
  • 9
    • 0030016626 scopus 로고    scopus 로고
    • Determination of site-specific modifications of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal using matrix assisted laser desorption time-of-flight mass spectrometry
    • Grace, J. M.; MacDonald, T. L.; Roberts, R. J.; Kinter, M. Determination of site-specific modifications of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal using matrix assisted laser desorption time-of-flight mass spectrometry Free Radical Res. 1996, 25, 23-29
    • (1996) Free Radical Res. , vol.25 , pp. 23-29
    • Grace, J.M.1    MacDonald, T.L.2    Roberts, R.J.3    Kinter, M.4
  • 10
    • 0029952814 scopus 로고    scopus 로고
    • First direct evidence for lipid/protein conjugation in oxidized human low density lipoprotein
    • Bolgar, M. S.; Yang, C. Y.; Gaskell, S. J. First direct evidence for lipid/protein conjugation in oxidized human low density lipoprotein J. Biol. Chem. 1996, 271, 27999-28001
    • (1996) J. Biol. Chem. , vol.271 , pp. 27999-28001
    • Bolgar, M.S.1    Yang, C.Y.2    Gaskell, S.J.3
  • 11
    • 0036127167 scopus 로고    scopus 로고
    • Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues
    • Crabb, J. W.; O'Neil, J.; Miyagi, M.; West, K.; Hoff, H. F. Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues Protein Sci. 2002, 11, 831-840
    • (2002) Protein Sci. , vol.11 , pp. 831-840
    • Crabb, J.W.1    O'Neil, J.2    Miyagi, M.3    West, K.4    Hoff, H.F.5
  • 12
    • 0027326559 scopus 로고
    • Immunochemical detection of 4-hydroxynonenal protein adducts in oxidized hepatocytes
    • Uchida, K.; Szweda, L. I.; Chae, H. Z.; Stadtman, E. R. Immunochemical detection of 4-hydroxynonenal protein adducts in oxidized hepatocytes Proc. Natl. Acad. Sci. U. S. A. 1993, 90, 8742-8746
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 8742-8746
    • Uchida, K.1    Szweda, L.I.2    Chae, H.Z.3    Stadtman, E.R.4
  • 13
    • 3042596594 scopus 로고    scopus 로고
    • Mass spectrometry for detection of 4-hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins
    • Carini, M.; Aldini, G.; Facino, R. M. Mass spectrometry for detection of 4-hydroxy-trans-2-nonenal (HNE) adducts with peptides and proteins Mass Spectrom. Rev. 2004, 23, 281-305
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 281-305
    • Carini, M.1    Aldini, G.2    Facino, R.M.3
  • 14
    • 0346634902 scopus 로고    scopus 로고
    • Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal- and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry
    • Fenaille, F.; Tabet, J. C.; Guy, P. A. Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal- and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry Anal. Chem. 2002, 74, 6298-6304
    • (2002) Anal. Chem. , vol.74 , pp. 6298-6304
    • Fenaille, F.1    Tabet, J.C.2    Guy, P.A.3
  • 15
    • 52049088770 scopus 로고    scopus 로고
    • Oxidative stress and covalent modification of protein with bioactive aldehydes
    • Grimsrud, P. A.; Xie, H.; Griffin, T. J.; Bernlohr, D. A. Oxidative stress and covalent modification of protein with bioactive aldehydes J. Biol. Chem. 2008, 283, 21837-21841
    • (2008) J. Biol. Chem. , vol.283 , pp. 21837-21841
    • Grimsrud, P.A.1    Xie, H.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 16
    • 33746616420 scopus 로고    scopus 로고
    • In-depth analysis of the membrane and cytosolic proteome of red blood cells
    • Pasini, E. M.; Kirkegaard, M.; Mortensen, P.; Lutz, H. U.; Thomas, A. W.; Mann, M. In-depth analysis of the membrane and cytosolic proteome of red blood cells Blood 2006, 108, 791-801
    • (2006) Blood , vol.108 , pp. 791-801
    • Pasini, E.M.1    Kirkegaard, M.2    Mortensen, P.3    Lutz, H.U.4    Thomas, A.W.5    Mann, M.6
  • 17
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A. T.; H. Havlis, J.; Olsen, J.; Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes Nat. Protoc. 2006, 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.T.1    Havlis J, H.2    Olsen, J.3    Mann, M.4
  • 19
    • 73949083731 scopus 로고    scopus 로고
    • The covalent modification of spectrin in red cell membranes by the lipid peroxidation product 4-hydroxy-2-nonenal
    • Arashiki, N.; Otsuka, Y.; Ito, D.; Yang, M.; Komatsu, T.; Sato, K.; Inaba, M. The covalent modification of spectrin in red cell membranes by the lipid peroxidation product 4-hydroxy-2-nonenal Biochem. Biophys. Res. Commun. 2010, 391, 1543-1547
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 1543-1547
    • Arashiki, N.1    Otsuka, Y.2    Ito, D.3    Yang, M.4    Komatsu, T.5    Sato, K.6    Inaba, M.7
  • 20
    • 0037805209 scopus 로고    scopus 로고
    • Study of protein modification by 4-hydroxy-2-nonenal and other short chain aldehydes analyzed by electrospray ionization tandem mass spectrometry
    • Fenaille, F.; Guy, P. A.; Tabet, J. C. Study of protein modification by 4-hydroxy-2-nonenal and other short chain aldehydes analyzed by electrospray ionization tandem mass spectrometry J. Am. Soc. Mass Spectrom. 2003, 14, 215-226
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 215-226
    • Fenaille, F.1    Guy, P.A.2    Tabet, J.C.3
  • 22
    • 1242284991 scopus 로고    scopus 로고
    • Theoretical and experimental prospects for protein identification based solely on accurate mass measurement
    • He, F.; Emmett, M. R.; Hakansson, K.; Hendrickson, C. L.; Marshall, A. G. Theoretical and experimental prospects for protein identification based solely on accurate mass measurement J. Proteome Res. 2004, 3, 61-67
    • (2004) J. Proteome Res. , vol.3 , pp. 61-67
    • He, F.1    Emmett, M.R.2    Hakansson, K.3    Hendrickson, C.L.4    Marshall, A.G.5
  • 24
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry
    • Roe, M. R.; Xie, H.; Bandhakavi, S.; Griffin, T. J. Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry Anal. Chem. 2007, 79, 3747-3756
    • (2007) Anal. Chem. , vol.79 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4
  • 25
    • 60549083972 scopus 로고    scopus 로고
    • Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: Neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation
    • Rauniyar, N.; Stevens, S. M.; Prokai-Tatrai, K.; Prokai, L. Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation Anal. Chem. 2009, 81, 782-789
    • (2009) Anal. Chem. , vol.81 , pp. 782-789
    • Rauniyar, N.1    Stevens, S.M.2    Prokai-Tatrai, K.3    Prokai, L.4
  • 26
    • 75149140183 scopus 로고    scopus 로고
    • Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: Protein carbonylation is diminished by ascorbic acid
    • Chavez, J.; Chung, W. G.; Miranda, C. L.; Singhal, M.; Stevens, J. F.; Maier, C. S. Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid Chem. Res. Toxicol. 2010, 23, 37-47
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 37-47
    • Chavez, J.1    Chung, W.G.2    Miranda, C.L.3    Singhal, M.4    Stevens, J.F.5    Maier, C.S.6
  • 27
    • 0037172778 scopus 로고    scopus 로고
    • Identification of bovine heart cytochrome c oxidase subunits modified by the lipid peroxidation product 4-hydroxy-2-nonenal
    • Musatov, A.; Carroll, C. A.; Liu, Y. C.; Henderson, G. I.; Weintraub, S. T.; Robinson, N. C. Identification of bovine heart cytochrome c oxidase subunits modified by the lipid peroxidation product 4-hydroxy-2-nonenal Biochemistry 2002, 41, 8212-8220
    • (2002) Biochemistry , vol.41 , pp. 8212-8220
    • Musatov, A.1    Carroll, C.A.2    Liu, Y.C.3    Henderson, G.I.4    Weintraub, S.T.5    Robinson, N.C.6
  • 28
    • 0026606054 scopus 로고
    • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal
    • Uchida, K.; Stadtman, E. R. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal Proc. Natl. Acad. Sci. U. S. A. 1992, 89, 4544-4548
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 4544-4548
    • Uchida, K.1    Stadtman, E.R.2
  • 29
    • 0031459806 scopus 로고    scopus 로고
    • Covalent attachment of 4-hydroxy-2-nonenal to erythrocyte proteins
    • Uchida, K.; Hasui, Y.; Osawa, T. Covalent attachment of 4-hydroxy-2-nonenal to erythrocyte proteins J. Biochem. 1997, 122, 1246-1251
    • (1997) J. Biochem. , vol.122 , pp. 1246-1251
    • Uchida, K.1    Hasui, Y.2    Osawa, T.3
  • 30
    • 27844579180 scopus 로고    scopus 로고
    • Band 3/complement-mediated recognition and removal of normally senescent and pathological human erythrocytes
    • Arese, P.; Turrini, F.; Schwarzer, E. Band 3/complement-mediated recognition and removal of normally senescent and pathological human erythrocytes Cell Physiol. Biochem. 2005, 16, 133-146
    • (2005) Cell Physiol. Biochem. , vol.16 , pp. 133-146
    • Arese, P.1    Turrini, F.2    Schwarzer, E.3
  • 31
    • 72149087442 scopus 로고    scopus 로고
    • Red blood cell (RBC) membrane proteomics - Part II: Comparative proteomics and RBC patho-physiology
    • Pasini, E. M.; Lutz, H. U.; Mann, M.; Thomas, A. W. Red blood cell (RBC) membrane proteomics - Part II: Comparative proteomics and RBC patho-physiology J. Proteomics 2010, 73, 421-435
    • (2010) J. Proteomics , vol.73 , pp. 421-435
    • Pasini, E.M.1    Lutz, H.U.2    Mann, M.3    Thomas, A.W.4
  • 32
    • 72149106170 scopus 로고    scopus 로고
    • Red blood cell (RBC) membrane proteomics - Part I: Proteomics and RBC physiology
    • Pasini, E. M.; Lutz, H. U.; Mann, M.; Thomas, A. W. Red blood cell (RBC) membrane proteomics - Part I: Proteomics and RBC physiology J. Proteomics 2010, 73, 403-420
    • (2010) J. Proteomics , vol.73 , pp. 403-420
    • Pasini, E.M.1    Lutz, H.U.2    Mann, M.3    Thomas, A.W.4
  • 33
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis, M. A.; Morrow, J. S. Spectrin tethers and mesh in the biosynthetic pathway J. Cell Sci. 2000, 113 (Pt 13) 2331-2343
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 13 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 34
    • 34247123673 scopus 로고    scopus 로고
    • Spectrin-bases skeleton in red blood cells and malaria
    • Dhermy, D. S.; Lecomte, M. J. Spectrin-bases skeleton in red blood cells and malaria Curr. Opin. Hematol. 2007, 19, 198-202
    • (2007) Curr. Opin. Hematol. , vol.19 , pp. 198-202
    • Dhermy, D.S.1    Lecomte, M.J.2
  • 35
    • 0025730273 scopus 로고
    • The spectrin skeleton: From red cells to brain
    • Bennett, V.; Lambert, S. The spectrin skeleton: from red cells to brain J. Clin. Invest. 1991, 87, 1483-1489
    • (1991) J. Clin. Invest. , vol.87 , pp. 1483-1489
    • Bennett, V.1    Lambert, S.2
  • 36
    • 0027301038 scopus 로고
    • Erythroid and nonerythroid spectrins
    • Winkelmann, J. C.; Forget, B. G. Erythroid and nonerythroid spectrins Blood 1993, 81, 3173-3185
    • (1993) Blood , vol.81 , pp. 3173-3185
    • Winkelmann, J.C.1    Forget, B.G.2
  • 37
    • 26944444345 scopus 로고    scopus 로고
    • Membrane phospholipid redistribution in cytokinesis: A theoretical model
    • An, M. W.; Wu, W. Z.; Chen, W. Y. Membrane phospholipid redistribution in cytokinesis: a theoretical model Acta Biochim. Biophys. Sin. 2005, 37, 643-648
    • (2005) Acta Biochim. Biophys. Sin. , vol.37 , pp. 643-648
    • An, M.W.1    Wu, W.Z.2    Chen, W.Y.3
  • 38
    • 14844314119 scopus 로고    scopus 로고
    • Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation
    • Manno, S.; Takakuwa, Y.; Mohandas, N. Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation J. Biol. Chem. 2005, 280, 7581-7587
    • (2005) J. Biol. Chem. , vol.280 , pp. 7581-7587
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 39
    • 0028953284 scopus 로고
    • Modulation of erythrocyte membrane mechanical function by beta-spectrin phosphorylation and dephosphorylation
    • Manno, S.; Takakuwa, Y.; Nagao, K.; Mohandas, N. Modulation of erythrocyte membrane mechanical function by beta-spectrin phosphorylation and dephosphorylation J. Biol. Chem. 1995, 270, 5659-5665
    • (1995) J. Biol. Chem. , vol.270 , pp. 5659-5665
    • Manno, S.1    Takakuwa, Y.2    Nagao, K.3    Mohandas, N.4
  • 41
    • 0037133206 scopus 로고    scopus 로고
    • Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability
    • Manno, S.; Takakuwa, Y.; Mohandas, N. Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 1943-1948
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1943-1948
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 42
    • 67650751550 scopus 로고    scopus 로고
    • Identification of phosphorylated proteins in erythrocytes infected by the human malaria parasite Plasmodium falciparum
    • Wu, Y.; Nelson, M. M.; Quaile, A.; Xia, D.; Wastling, J. M.; Craig, A. Identification of phosphorylated proteins in erythrocytes infected by the human malaria parasite Plasmodium falciparum Malar. J. 2009, 8, 105
    • (2009) Malar. J. , vol.8 , pp. 105
    • Wu, Y.1    Nelson, M.M.2    Quaile, A.3    Xia, D.4    Wastling, J.M.5    Craig, A.6


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