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Volumn 44, Issue 39, 2005, Pages 13071-13081

3-Nitrotyrosine modification of SERCA2a in the aging heart: A distinct signature of the cellular redox environment

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; CALCIUM; MUSCLE; RELAXATION PROCESSES;

EID: 25444450030     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051226n     Document Type: Article
Times cited : (108)

References (51)
  • 1
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos, H. (1998) Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species, Arch. Biochem. Biophys, 356, 1-11.
    • (1998) Arch. Biochem. Biophys , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 2
    • 0033564289 scopus 로고    scopus 로고
    • Protein modification during biological aging: Selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca-ATPase
    • Viner, R. I., Ferrington, D. A., Williams, T. D., Bigelow, D. J., and Schoneich, C. (1999) Protein modification during biological aging: Selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca-ATPase, Biochem. J. 340, 657-659.
    • (1999) Biochem. J. , vol.340 , pp. 657-659
    • Viner, R.I.1    Ferrington, D.A.2    Williams, T.D.3    Bigelow, D.J.4    Schoneich, C.5
  • 4
    • 0029862517 scopus 로고    scopus 로고
    • Effects of aging on sarcoplasmic reticulum function and contraction duration in skeletal muscles of the rat
    • Narayanan, N., Jones, D. L., Xu, A., and Yu, J. C. (1996) Effects of aging on sarcoplasmic reticulum function and contraction duration in skeletal muscles of the rat, Am. J. Physiol. 271, C1032-C1040.
    • (1996) Am. J. Physiol. , vol.271
    • Narayanan, N.1    Jones, D.L.2    Xu, A.3    Yu, J.C.4
  • 5
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman, J. S., and Koppenol, W. H. (1996) Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly, Am. J. Physiol. 271, C1424-C1437.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 6
    • 0033529262 scopus 로고    scopus 로고
    • Peroxynitrite-mediated modification of proteins at physiological carbon dioxide concnetrations: pH dependence of carbonyl formation, tyrosine nitration, and methionine oxidation
    • Tien, M., Berlett, B. S., Levine, R. L., Chock, P. B., and Stadtman, E. R. (1999) Peroxynitrite-mediated modification of proteins at physiological carbon dioxide concnetrations: pH dependence of carbonyl formation, tyrosine nitration, and methionine oxidation, Proc. Natl. Acad. Sci. U.S.A. 96, 7809-7814.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7809-7814
    • Tien, M.1    Berlett, B.S.2    Levine, R.L.3    Chock, P.B.4    Stadtman, E.R.5
  • 7
    • 0034693038 scopus 로고    scopus 로고
    • Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite
    • Reiter, C. D., Teng, R.-J., and Beckman, J. S. (2000) Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite, J. Biol. Chem. 275, 32460-32466.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32460-32466
    • Reiter, C.D.1    Teng, R.-J.2    Beckman, J.S.3
  • 8
    • 0036236275 scopus 로고    scopus 로고
    • Generation of reactive oxygen and nitrogen species in contracting skeletal muscle
    • Reid, M. B., and Durham, W. J. (2002) Generation of reactive oxygen and nitrogen species in contracting skeletal muscle, Ann. N.Y. Acad. Sci. 959, 108-116.
    • (2002) Ann. N.Y. Acad. Sci. , vol.959 , pp. 108-116
    • Reid, M.B.1    Durham, W.J.2
  • 9
    • 0042917516 scopus 로고    scopus 로고
    • Nitric oxide and cardiac function: Ten years after, and continuing
    • Massion, P. B., Feron, O., Dessy, C., and Balligand, J. L. (2003) Nitric oxide and cardiac function: Ten years after, and continuing, Circ. Res. 93, 388-398.
    • (2003) Circ. Res. , vol.93 , pp. 388-398
    • Massion, P.B.1    Feron, O.2    Dessy, C.3    Balligand, J.L.4
  • 10
    • 0029797602 scopus 로고    scopus 로고
    • Induction of diaphragmatic nitric oxide synthase after endotoxin administration in rats: Role on diaphragmatic contractile dysfunction
    • Boczkowski, J., Lanone, S., Ungureanu-Longrois, D., Danialou, G., Fournier, T., and Aubier, M. (1996) Induction of diaphragmatic nitric oxide synthase after endotoxin administration in rats: role on diaphragmatic contractile dysfunction, J. Clin. Invest. 98, 1550-1559.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1550-1559
    • Boczkowski, J.1    Lanone, S.2    Ungureanu-Longrois, D.3    Danialou, G.4    Fournier, T.5    Aubier, M.6
  • 11
    • 0031203481 scopus 로고    scopus 로고
    • Expression of nitric oxide synthases and GTP cyclohydrolase I in the ventilatory and limb muscles during endotoxemia
    • Hussain, S. N., Giaid, A., El Dawiri, Q., Sakkal, D., Hattori, R., and Guo, Y. (1997) Expression of nitric oxide synthases and GTP cyclohydrolase I in the ventilatory and limb muscles during endotoxemia, Am. J. Respir. Cell Mol. Biol. 17, 173-180.
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 173-180
    • Hussain, S.N.1    Giaid, A.2    El Dawiri, Q.3    Sakkal, D.4    Hattori, R.5    Guo, Y.6
  • 13
    • 0033929514 scopus 로고    scopus 로고
    • Selective NOS inhibition restores myocardial contractility in endotoxemic rates; however, myocardial NO content does not correlate with myocardial dysfunction
    • Afulukwe, I. F., Cohen, R. I., Zeballos, G. A., Iqbal, M., and Scharf, S. M. (2000) Selective NOS inhibition restores myocardial contractility in endotoxemic rates; however, myocardial NO content does not correlate with myocardial dysfunction, Am. J. Respir. Crit. Care Med. 162, 21-26.
    • (2000) Am. J. Respir. Crit. Care Med. , vol.162 , pp. 21-26
    • Afulukwe, I.F.1    Cohen, R.I.2    Zeballos, G.A.3    Iqbal, M.4    Scharf, S.M.5
  • 15
    • 0037080553 scopus 로고    scopus 로고
    • Role of myocardial inducible nitric oxide synthase in contractile dysfunction and β-adrenergic hypo-responsiveness in rats with experimental volume-overload heart failure
    • Gealekman, O., Abassi, Z., Rubinstein, I., Winaver, J., and Binah, O. (2002) Role of myocardial inducible nitric oxide synthase in contractile dysfunction and β-adrenergic hypo-responsiveness in rats with experimental volume-overload heart failure, Circulation 105, 236-243.
    • (2002) Circulation , vol.105 , pp. 236-243
    • Gealekman, O.1    Abassi, Z.2    Rubinstein, I.3    Winaver, J.4    Binah, O.5
  • 16
    • 1642422773 scopus 로고    scopus 로고
    • Mitochondrial free radical production and cell signaling
    • Cadenas, E. (2004) Mitochondrial free radical production and cell signaling, Mol. Aspects Med. 25, 17-26.
    • (2004) Mol. Aspects Med. , vol.25 , pp. 17-26
    • Cadenas, E.1
  • 18
    • 0242321030 scopus 로고    scopus 로고
    • Proteomic identification of age-dependent protein nitration in rat skeletal muscle
    • Kanski, J., Alterman, M. A., and Schoneich, C. (2003) Proteomic identification of age-dependent protein nitration in rat skeletal muscle, Free Radical Biol. Med. 35, 1229-1239.
    • (2003) Free Radical Biol. Med. , vol.35 , pp. 1229-1239
    • Kanski, J.1    Alterman, M.A.2    Schoneich, C.3
  • 19
    • 0032488809 scopus 로고    scopus 로고
    • 2+-ATPase in low-frequency stimulated rabbit muscle
    • 2+-ATPase in low-frequency stimulated rabbit muscle, FEBS Lett. 422, 381-384.
    • (1998) FEBS Lett. , vol.422 , pp. 381-384
    • Klebl, B.M.1    Ayoub, A.T.2    Pette, D.3
  • 21
    • 12844266555 scopus 로고    scopus 로고
    • Increased tyrosine nitration of SERCA2a in human heart failure inhibits SR Ca-pump function
    • Lokuta, A. J., Maertz, N. A., Kamp, J. F., Valdivia, H. H., and Haworth, R. A. (2002) Increased tyrosine nitration of SERCA2a in human heart failure inhibits SR Ca-pump function, Biophys. J. 82, 597a.
    • (2002) Biophys. J. , vol.82
    • Lokuta, A.J.1    Maertz, N.A.2    Kamp, J.F.3    Valdivia, H.H.4    Haworth, R.A.5
  • 22
    • 0032489434 scopus 로고    scopus 로고
    • Altered turnover of calcium regulatory proteins of the SR in aged skeletal muscle
    • Ferrington, D. A., Krainev, A. G., and Bigelow, D. J. (1998) Altered turnover of calcium regulatory proteins of the SR in aged skeletal muscle, J. Biol. Chem. 273, 5885-5891.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5885-5891
    • Ferrington, D.A.1    Krainev, A.G.2    Bigelow, D.J.3
  • 23
    • 0023880226 scopus 로고
    • Site-specific derivatives of wheat germ calmodulin: Interactions with troponin and sarcoplasmic reticulum
    • Strasburg, G., Hogan, M., Birmachu, W., Thomas, D. D., and Louis, C. F. (1988) Site-specific derivatives of wheat germ calmodulin: Interactions with troponin and sarcoplasmic reticulum, J. Biol. Chem. 263, 542-548.
    • (1988) J. Biol. Chem. , vol.263 , pp. 542-548
    • Strasburg, G.1    Hogan, M.2    Birmachu, W.3    Thomas, D.D.4    Louis, C.F.5
  • 24
    • 0027080374 scopus 로고
    • The MgATPase activity of rat cardiac sarcoplasmic reticulum is a function of the calcium ATPase protein
    • Taffet, G. E., and Tate, C. A. (1992) The MgATPase activity of rat cardiac sarcoplasmic reticulum is a function of the calcium ATPase protein, Arch. Biochem. Biophys. 299, 287-294.
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 287-294
    • Taffet, G.E.1    Tate, C.A.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0030719457 scopus 로고    scopus 로고
    • In vivo aging of rat skeletal muscle sarcoplasmic reticulum Ca-ATPase: Chemical analysis and quantitative simulation by exposure to low levels of peroxyl radicals
    • Viner, R. I., Ferrington, D. A., Aced, G. I., Miller-Schlyer, M., Bigelow, D. J., and Schoneich, C. (1997) In vivo aging of rat skeletal muscle sarcoplasmic reticulum Ca-ATPase: Chemical analysis and quantitative simulation by exposure to low levels of peroxyl radicals, Biochim. Biophys. Acta 1329, 321-335.
    • (1997) Biochim. Biophys. Acta , vol.1329 , pp. 321-335
    • Viner, R.I.1    Ferrington, D.A.2    Aced, G.I.3    Miller-Schlyer, M.4    Bigelow, D.J.5    Schoneich, C.6
  • 28
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., and Candia, D. A. (1979) An improved assay for nanomole amounts of inorganic phosphate, Anal. Biochem. 100, 95-97.
    • (1979) Anal. Biochem. , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, D.A.4
  • 29
    • 0036774546 scopus 로고    scopus 로고
    • Quantification of oxidative/nitrosative modification of Cys34 in human serum albumin using a fluorescence-based SDS-PAGE assay
    • Fabisiak, J. P., Sedlov, A., and Kagan, V. (2002) Quantification of oxidative/nitrosative modification of Cys34 in human serum albumin using a fluorescence-based SDS-PAGE assay, Antioxid. Redox Signaling 4, 855-865.
    • (2002) Antioxid. Redox Signaling , vol.4 , pp. 855-865
    • Fabisiak, J.P.1    Sedlov, A.2    Kagan, V.3
  • 30
    • 0037108986 scopus 로고    scopus 로고
    • Two-dimensional separation of the membrane protein sarcoplasmic reticulum Ca-ATPase for high-performance liquid chromatography-tandem mass spectrometry analysis of posttranslational protein modifications
    • Sharov, V. S., Galeva, N. A., Knyushko, T. V., Bigelow, D. J., Williams, T. D., and Schoneich C. (2002) Two-dimensional separation of the membrane protein sarcoplasmic reticulum Ca-ATPase for high-performance liquid chromatography-tandem mass spectrometry analysis of posttranslational protein modifications, Anal. Biochem. 308, 328-335.
    • (2002) Anal. Biochem. , vol.308 , pp. 328-335
    • Sharov, V.S.1    Galeva, N.A.2    Knyushko, T.V.3    Bigelow, D.J.4    Williams, T.D.5    Schoneich, C.6
  • 32
    • 0036990053 scopus 로고    scopus 로고
    • A quantitative and validated SAGE transcriptome reference for adult mouse heart
    • Anisimov, S. V., Tarasov, K. V., Stern, M. D., Lakatta, E. G., and Boheler, K. R. (2002) A quantitative and validated SAGE transcriptome reference for adult mouse heart, Genomics 80, 213-222.
    • (2002) Genomics , vol.80 , pp. 213-222
    • Anisimov, S.V.1    Tarasov, K.V.2    Stern, M.D.3    Lakatta, E.G.4    Boheler, K.R.5
  • 33
    • 0027456408 scopus 로고
    • 2+-ATPase isoforms in rat muscle
    • Cell Physiol. 33
    • 2+-ATPase isoforms in rat muscle, Am. J. Physiol. 264 (Cell Physiol. 33), C333-C341.
    • (1993) Am. J. Physiol. , vol.264
    • Wu, K.-D.1    Lytton, J.2
  • 36
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C., and Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium, Nature 418, 605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 37
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sorenson, T. L.-M., Moeller, J. V., and Nissen, P. (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump, Science 304, 1672-1675.
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sorenson, T.L.-M.1    Moeller, J.V.2    Nissen, P.3
  • 38
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution, Nature 405, 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 40
    • 0037646515 scopus 로고    scopus 로고
    • Transmembrane nitration of hydrophobic tyrosyl peptides: Localization, characterization, mechanism of nitration, and biological implications
    • Zhang, H., Bhargava, K., Keszler, A., Feix, J., Hogg, N., Joseph, J., and Kalyanaraman, B. (2003) Transmembrane nitration of hydrophobic tyrosyl peptides: Localization, characterization, mechanism of nitration, and biological implications, J. Biol. Chem. 278, 8969-6978.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8969-16978
    • Zhang, H.1    Bhargava, K.2    Keszler, A.3    Feix, J.4    Hogg, N.5    Joseph, J.6    Kalyanaraman, B.7
  • 42
    • 0031460696 scopus 로고    scopus 로고
    • Peroxynitrite rapidly permeates phospholipid membranes
    • Maria, S. S., Lee, J., and Groves, J. T. (1997) Peroxynitrite rapidly permeates phospholipid membranes, Proc. Natl. Acad. Sci. U.S.A. 94, 14243-14248.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14243-14248
    • Maria, S.S.1    Lee, J.2    Groves, J.T.3
  • 43
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune, T., Merker, K., Sandig, G., and Davies, K. J. (2003) Selective degradation of oxidatively modified protein substrates by the proteasome, Biochem. Biophys. Res. Commun. 305, 709-718.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 44
    • 8544273285 scopus 로고    scopus 로고
    • Hsp90 enhances degradation of oxidized calmodulin by the 20S proteasome
    • Whittier, J. E., Xiong, Y., Rechsteiner, M. C., and Squier, T. C. (2004) Hsp90 enhances degradation of oxidized calmodulin by the 20S proteasome, J. Biol. Chem. 279, 46135-46142.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46135-46142
    • Whittier, J.E.1    Xiong, Y.2    Rechsteiner, M.C.3    Squier, T.C.4
  • 46
    • 0037948843 scopus 로고    scopus 로고
    • Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins
    • Irie, Y., Saeki, M., Kamisaki, Y., Martin, E., and Murad, F. (2003) Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins, Proc. Natl. Acad. Sci. U.S.A. 100, 5634-5639.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5634-5639
    • Irie, Y.1    Saeki, M.2    Kamisaki, Y.3    Martin, E.4    Murad, F.5
  • 48
    • 2542494826 scopus 로고    scopus 로고
    • Modulation of iNOS activity in age-related cardiac dysfunction
    • Yang, B., Larson, D. F., and Watson, R. R. (2005) Modulation of iNOS activity in age-related cardiac dysfunction, Life Sci. 75, 655-667.
    • (2005) Life Sci. , vol.75 , pp. 655-667
    • Yang, B.1    Larson, D.F.2    Watson, R.R.3
  • 49
    • 0242606147 scopus 로고    scopus 로고
    • Role: For calcineurin in striated muscle: Development, adaptation, and disease
    • Bassel-Duby, R., and Olson, E. N. (2003) Role: for calcineurin in striated muscle: Development, adaptation, and disease, Biochem. Biophys. Res. Commun. 11, 1133-1141.
    • (2003) Biochem. Biophys. Res. Commun. , vol.11 , pp. 1133-1141
    • Bassel-Duby, R.1    Olson, E.N.2
  • 51
    • 0033592423 scopus 로고    scopus 로고
    • Peroxynitrite modification of protein thiols: Oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase
    • Viner, R. I., Williams, T. D., and Schoneich, C. (1999) Peroxynitrite modification of protein thiols: Oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase Biochemistry 38, 12408-12415.
    • (1999) Biochemistry , vol.38 , pp. 12408-12415
    • Viner, R.I.1    Williams, T.D.2    Schoneich, C.3


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