Review

You have free access to this content

Myofilament proteins: From cardiac disorders to proteomic changes

  1. Chao Yuan,
  2. R. John Solaro Dr.*

Article first published online: 12 JUN 2008

DOI: 10.1002/prca.200780076

Issue

PROTEOMICS - Clinical Applications

PROTEOMICS - Clinical Applications

Special Issue: CARDIOVASCULAR PROTEOMICS

Volume 2, Issue 6, pages 788–799, No. 6 June 2008

Additional Information

How to Cite

Yuan, C. and Solaro, R. J. (2008), Myofilament proteins: From cardiac disorders to proteomic changes. Prot. Clin. Appl., 2: 788–799. doi: 10.1002/prca.200780076

Author Information

  1. Department of Physiology and Biophysics and Center for Cardiovascular Research, University of Illinois at Chicago, Chicago, IL, USA

*Department of Physiology and Biophysics (M/C 901), University of Illinois at Chicago, College of Medicine, 835 South Wolcott Avenue, Chicago, IL 60612, USA Fax: +1-312-996-1414

Publication History

  1. Issue published online: 12 JUN 2008
  2. Article first published online: 12 JUN 2008
  3. Manuscript Received: 6 OCT 2007

Funded by

  • NIH. Grant Numbers: R37/R01 HL 22231, RO1 HL 64035, PO1 HL 62426, T32 007692
  • Chicago Biomedical Consortium

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

Get PDF (312K)

References

  • 1
    Solaro, R. J., Handbook of Physiology, Section 2: The Cardiovascular System, Vol I: The Heart. Oxford University Press, New York 2001.
  • 2
    Kobayashi, T., Solaro, R. J., Calcium, thin filaments, and the integrative biology of cardiac contractility. Annu. Rev. Physiol. 2005, 67, 39–67.
  • 3
    Solaro, R. J., Integration of myofilament response to Ca2+ with cardiac pump regulation and pump dynamics. Am. J. Physiol. 1999, 277, S155–163.
  • 4
    Solaro, R. J., Wolska, B. M., Arteaga, G., Martin, A. F. et al., in: Solaro, R. J., Moss, R. L., (Eds.), Molecular Control Mechanisms in Striated Muscle Contraction, The Netherlands 2002, pp, 291–327.
  • 5
    Hernandez, O. M., Jones, M., Guzman, G., Szczesna–Cordary, D., Myosin essential light chain in health and disease. Am. J. Physiol. Heart Circ. Physiol. 2007, 292, H1643–1654.
  • 6
    Moss, R. L., Fitzsimons, D. P., Myosin light chain 2 into the mainstream of cardiac development and contractility. Circ. Res. 2006, 99, 225–227.
  • 7
    Granzier, H. L., Campbell, K. B., New insights in the role of cardiac myosin binding protein C as a regulator of cardiac contractility. Circ. Res. 2006, 99, 795–797.
  • 8
    Granzier, H., Wu, Y., Siegfried, L., LeWinter, M., Titin: physiological function and role in cardiomyopathy and failure. Heart Fail. Rev. 2005, 10, 211–223.
  • 9
    Pi, Y., Kemnitz, K. R., Zhang, D., Kranias, E. G., Walker, J. W., Phosphorylation of troponin I controls cardiac twitch dynamics: evidence from phosphorylation site mutants expressed on a troponin I-null background in mice. Circ. Res. 2002, 90, 649–656.
  • 10
    Sumandea, M. P., Burkart, E. M., Kobayashi, T., De Tombe, P. P., Solaro, R. J., Molecular and integrated biology of thin filament protein phosphorylation in heart muscle. Ann. NY Acad. Sci. 2004, 1015, 39–52.
    Direct Link:
  • 11
    Vahebi, S., Kobayashi, T., Warren, C. M., de Tombe, P. P., Solaro, R. J., Functional effects of rho-kinase-dependent phosphorylation of specific sites on cardiac troponin. Circ. Res. 2005, 96, 740–747.
  • 12
    Vahebi, S., Ota, A., Li, M., Warren, C. M. et al., p38-MAPK induced dephosphorylation of alpha-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity. Circ. Res. 2007, 100, 408–415.
  • 13
    Deng, Y., Schmidtmann, A., Redlich, A., Westerdorf, B. et al., Effects of phosphorylation and mutation R145G on human cardiac troponin I function. Biochemistry 2001, 40, 14593–14602.
  • 14
    Lim, M. S., Sutherland, C., Walsh, M. P., Phosphorylation of bovine cardiac C-protein by protein kinase C. Biochem. Biophys. Res. Commun. 1985, 132, 1187–1195.
  • 15
    Hartzell, H. C., Effects of phosphorylated and unphosphorylated C-protein on cardiac actomyosin ATPase. J. Mol. Biol. 1985, 186, 185–195.
  • 16
    Stelzer, J. E., Patel, J. R., Walker, J. W., Moss, R. L., Differential roles of cardiac myosin-binding protein C and cardiac troponin I in the myofibrillar force responses to protein kinase a phosphorylation. Circ. Res. 2007, 101, 503–511.
  • 17
    Yuan, C., Ravi, R., Murphy, A. M., Discovery of disease-induced post-translational modifications in cardiac contractile proteins. Curr. Opin. Mol. Ther. 2005, 7, 234–239.
  • 18
    McGregor, E., Dunn, M. J., Proteomics of the heart: unraveling disease. Circ. Res. 2006, 98, 309–321.
  • 19
    Stanley, B. A., Gundry, R. L., Cotter, R. J., Van Eyk, J. E., Heart disease, clinical proteomics and mass spectrometry. Dis. Markers 2004, 20, 167–178.
  • 20
    Scruggs, S. B., Walker, L. A., Lyu, T., Geenen, D. L. et al., Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation. J. Mol. Cell. Cardiol. 2006, 40, 465–473.
  • 21
    Granzier, H. L., Wang, K., Gel electrophoresis of giant proteins: solubilization and silver-staining of titin and nebulin from single muscle fiber segments. Electrophoresis 1993, 14, 56–64.
    Direct Link:
  • 22
    Yuan, C., Guo, Y., Ravi, R., Przyklenk, K. et al., Myosin binding protein C is differentially phosphorylated upon myocardial stunning in canine and rat hearts– evidence for novel phosphorylation sites. Proteomics 2006, 6, 4176–4186.
    Direct Link:
  • 23
    Arrell, D. K., Neverova, I., Fraser, H., Marban, E., Van Eyk, J. E., Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1. Circ. Res. 2001, 89, 480–487.
  • 24
    McDonough, J. L., Neverova, I., Van Eyk, J. E., Proteomic analysis of human biopsy samples by single two-dimensional electrophoresis: Coomassie, silver, mass spectrometry, and Western blotting. Proteomics 2002, 2, 978–987.
    Direct Link:
  • 25
    Kane, L. A., Neverova, I., Van Eyk, J. E., Subfractionation of heart tissue: the “in sequence” myofilament protein extraction of myocardial tissue. Methods Mol. Biol. 2007, 357, 87–90.
  • 26
    Holroyde, M. J., Small, D. A., Howe, E., Solaro, R. J., Isolation of cardiac myofibrils and myosin light chains with in vivo levels of light chain phosphorylation. Biochim. Biophys. Acta 1979, 587, 628–637.
  • 27
    Pan, B. S., Solaro, R. J., Calcium-binding properties of troponin C in detergent-skinned heart muscle fibers. J. Biol. Chem. 1987, 262, 7839–7849.
  • 28
    Layland, J., Cave, A. C., Warren, C., Grieve, D. J. et al., Protection against endotoxemia-induced contractile dysfunction in mice with cardiac-specific expression of slow skeletal troponin I. FASEB J. 2005, 19, 1137–1139.
  • 29
    Miegel, A., Kobayashi, T., Maeda, Y., Isolation, purification and partial characterization of tropomyosin and troponin subunits from the lobster tail muscle. J. Muscle Res. Cell. Motil. 1992, 13, 608–618.
  • 30
    Tobacman, L. S., Lee, R., Isolation and functional comparison of bovine cardiac troponin T isoforms. J. Biol. Chem. 1987, 262, 4059–4064.
  • 31
    Gao, W. D., Atar, D., Liu, Y., Perez, N. G. et al., Role of troponin I proteolysis in the pathogenesis of stunned myocardium. Circ. Res. 1997, 80, 393–399.
  • 32
    Van Eyk, J. E., Powers, F., Law, W., Larue, C. et al., Breakdown and release of myofilament proteins during ischemia and ischemia/reperfusion in rat hearts: identification of degradation products and effects on the pCa-force relation. Circ. Res. 1998, 82, 261–271.
  • 33
    McDonough, J. L., Arrell, D. K., Van Eyk, J. E., Troponin I degradation and covalent complex formation accompanies myocardial ischemia/reperfusion injury. Circ. Res. 1999, 84, 9–20.
  • 34
    Yu, Z. B., Zhang, L. F., Jin, J. P., A proteolytic NH2-terminal truncation of cardiac troponin I that is up-regulated in simulated microgravity. J. Biol. Chem. 2001, 276, 15753–15760.
  • 35
    Labugger, R., Organ, L., Collier, C., Atar, D., Van Eyk, J. E., Extensive troponin I and T modification detected in serum from patients with acute myocardial infarction. Circulation 2000, 102, 1221–1226.
  • 36
    Morjana, N. A., Degradation of human cardiac troponin I after myocardial infarction. Biotechnol. Appl. Biochem. 1998, 28, 105–111.
  • 37
    Madsen, L. H., Christensen, G., Lund, T., Serebruany, V. L. et al., Time course of degradation of cardiac troponin I in patients with acute ST-elevation myocardial infarction: the ASSENT-2 troponin substudy. Circ. Res. 2006, 99, 1141–1147.
  • 38
    Zeitz, O., Maass, A. E., Van Nguyen, P. et al., Hydroxyl radical-induced acute diastolic dysfunction is due to calcium overload via reverse-mode Na(+)-Ca(2+) exchange. Circ. Res. 2002, 90, 988–995.
  • 39
    Fishbein, M. C., Wang, T., Matijasevic, M., Hong, L., Apple, F. S., Myocardial tissue troponins T and I. An immunohistochemical study in experimental models of myocardial ischemia. Cardiovasc. Pathol. 2003, 12, 65–71.
  • 40
    Wu, A. H., Feng, Y. J., Moore, R., Apple, F. S. et al., Characterization of cardiac troponin subunit release into serum after acute myocardial infarction and comparison of assays for troponin T and I. American Association for Clinical Chemistry Subcommittee on cTnI Standardization. Clin. Chem. 1998, 44, 1198–1208.
  • 41
    Michielsen, E. C., Diris, J. H., Kleijnen, V. W., Wodzig, W. K., Van Dieijen-Visser, M. P., Investigation of release and degradation of cardiac troponin T in patients with acute myocardial infarction. Clin. Biochem. 2007, 40, 851–855.
  • 42
    Alpert, J. S., Thygesen, K., Antman, E., Bassand, J. P., Myocardial infarction redefined–a consensus document of The Joint European Society of Cardiology/American College of Cardiology Committee for the redefinition of myocardial infarction. J. Am. Coll. Cardiol. 2000, 36, 959–969.
  • 43
    Altinier, S., Mion, M., Cappelletti, A., Zaninotto, M., Plebani, M., Rapid measurement of cardiac markers on Stratus CS. Clin. Chem. 2000, 46, 991–993.
  • 44
    Hickman, P. E., Koerbin, G., Southcott, E., Tate, J. R. et al., Newer cardiac troponin I assays have similar performance to troponin T in patients with end-stage renal disease. Ann. Clin. Biochem. 2007, 44, 285–289.
  • 45
    Saadeddin, S. M., Habbab, M. A., Siddieg, H. H., Al Seeni, M. N. et al., Evaluation of 6 cardiac troponin assays in patients with acute coronary syndrome. Saudi Med. J. 2003, 24, 1092–1097.
  • 46
    White, M. Y., Cordwell, S. J., McCarron, H. C., Prasan, A. M. et al., Proteomics of ischemia/reperfusion injury in rabbit myocardium reveals alterations to proteins of essential functional systems. Proteomics 2005, 5, 1395–1410.
    Direct Link:
  • 47
    Decker, R. S., Decker, M. L., Kulikovskaya, I., Nakamura, S. et al., Myosin-binding protein C phosphorylation, myofibril structure, and contractile function during low-flow ischemia. Circulation 2005, 111, 906–912.
  • 48
    Zolk, O., Schenke, C., Sarikas, A., The ubiquitin-proteasome system: focus on the heart. Cardiovasc. Res. 2006, 70, 410–421.
  • 49
    Willis, M. S., Patterson, C., Into the heart: the emerging role of the ubiquitin-proteasome system. J. Mol. Cell. Cardiol. 2006, 41, 567–579.
  • 50
    Weekes, J., Wheeler, C. H., Yan, J. X., Weil, J. et al., Bovine dilated cardiomyopathy: proteomic analysis of an animal model of human dilated cardiomyopathy. Electrophoresis 1999, 20, 898–906.
    Direct Link:
  • 51
    Weekes, J., Morrison, K., Mullen, A., Wait, R. et al., Hyperubiquitination of proteins in dilated cardiomyopathy. Proteomics 2003, 3, 208–216.
    Direct Link:
  • 52
    Solomon, V., Goldberg, A. L., Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J. Biol. Chem. 1996, 271, 26690–26697.
  • 53
    Williams, A. B., Decourten-Myers, G. M., Fischer, J. E., Luo, G. et al., Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism. FASEB J. 1999, 13, 1435–1343.
  • 54
    Goll, D. E., Thompson, V. F., Li H, Wei, W., Cong, J., The calpain system. Physiol. Rev. 2003, 83, 731–801.
  • 55
    Marban, E., Kitakaze, M., Koretsune, Y., Yue, D. T. et al., Quantification of [Ca2+]i in perfused hearts. Critical evaluation of the 5F-BAPTA and nuclear magnetic resonance method as applied to the study of ischemia and reperfusion. Circ. Res. 1990, 66, 1255–1267.
  • 56
    Blunt, B. C., Creek, A. T., Henderson, D. C., Hofmann, P. A., H2O2 activation of HSP25/27 protects desmin from calpain proteolysis in rat ventricular myocytes. Am. J. Physiol. Heart Circ. Physiol. 2007, 293, H1518–H1525.
  • 57
    Barta, J., Toth, A., Edes, I., Vaszily, M. et al., Calpain-1-sensitive myofibrillar proteins of the human myocardium. Mol. Cell. Biochem. 2005, 278, 1–8.
  • 58
    Maekawa, A., Lee, J. K., Nagaya, T., Kamiya, K. et al., Overexpression of calpastatin by gene transfer prevents troponin I degradation and ameliorates contractile dysfunction in rat hearts subjected to ischemia/reperfusion. J. Mol. Cell. Cardiol. 2003, 35, 1277–1284.
  • 59
    Kane, L. A., Yung, C. K., Agnetti, G., Neverova, I., Van Eyk, J. E., Optimization of paper bridge loading for 2-DE analysis in the basic pH region: application to the mitochondrial subproteome. Proteomics 2006, 6, 5683–5687.
    Direct Link:
  • 60
    Unlu, M., Morgan, M. E., Minden, J. S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071–2077.
    Direct Link:
  • 61
    Tonge, R., Shaw, J., Middleton, B., Rowlinson, R. et al., Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 2001, 1, 377–396.
    Direct Link:
  • 62
    Filatov, V. L., Katrukha, A. G., Bereznikova, A. V., Esakova, T. V. et al., Epitope mapping of anti-troponin I monoclonal antibodies. Biochem. Mol. Biol. Int. 1998, 45, 1179–1187.
  • 63
    Murphy, A. M., Kogler, H., Georgakopoulos, D., McDonogh, J. L. et al., Transgenic mouse model of stunned myocardium. Science 2000, 287, 488–491.
  • 64
    Marston, S. B., Redwood, C. S., Modulation of thin filament activation by breakdown or isoform switching of thin filament proteins: physiological and pathological implications. Circ. Res. 2003, 93, 1170–1178.
  • 65
    Anderson, P. A., in: Solaro, R. J., Moss, R. L. (Eds.), Molecular Control Mechanisms in Striated Muscle Contraction. Kluwer Academic Publishers, The Netherlands, 2002, pp 329–377.
  • 66
    VanBuren, P., Okada, Y., Thin filament remodeling in failing myocardium. Heart Fail. Rev. 2005, 10, 199–209.
  • 67
    Ritter, O., Luther, H. P., Haase, H., Baltas, L. G. et al., Expression of atrial myosin light chains but not alpha-myosin heavy chains is correlated in vivo with increased ventricular function in patients with hypertrophic obstructive cardiomyopathy. J. Mol. Med. 1999, 77, 677–685.
  • 68
    Reiser, P. J., Portman, M. A., Ning, X. H., Schomisch Moravec, C., Human cardiac myosin heavy chain isoforms in fetal and failing adult atria and ventricles. Am. J. Physiol. Heart Circ. Physiol. 2001, 280, H1814–1820.
  • 69
    Thijssen, V. L., Ausma, J., Gorza, L., van der Velden, H. M. et al., Troponin I isoform expression in human and experimental atrial fibrillation. Circulation 2004, 110, 770–775.
  • 70
    Warren, C. M., Jordan, M. C, Roos, K. P., Krzesinski, P. R., Greaser, M. L., Titin isoform expression in normal and hypertensive myocardium. Cardiovasc. Res. 2003, 59, 86–94.
  • 71
    Goldspink, G., Gene expression in muscle in response to exercise. J. Muscle Res. Cell. Motil. 2003, 24, 121–126.
  • 72
    Schiaffino, S., Reggiani, C., Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 1996, 76, 371–423.
  • 73
    Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680–685.
  • 74
    Bodor, G. S., Oakeley, A. E., Allen, P. D., Crimmins, D. L. et al., Troponin I phosphorylation in the normal and failing adult human heart. Circulation 1997, 96, 1495–1500.
  • 75
    Reiser, P. J., Kline, W. O., Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species. Am. J. Physiol. 1998, 274, H1048–1053.
  • 76
    Biesiadecki, B. J., Elder, B. D., Yu, Z. B., Jin, J. P., Cardiac troponin T variants produced by aberrant splicing of multiple exons in animals with high instances of dilated cardiomyopathy. J. Biol. Chem. 2002, 277, 50275–50285.
  • 77
    Warren, C. M., Krzesinski, P. R., Greaser, M. L., Vertical agarose gel electrophoresis and electroblotting of high-molecular-weight proteins. Electrophoresis 2003, 24, 1695–1702.
    Direct Link:
  • 78
    van der Velden, J., Papp, Z., Zaremba, R., Boontje, N. M. et al., Increased Ca2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins. Cardiovasc. Res. 2003, 57, 37–47.
  • 79
    Gautel, M., Leonard, K., Labeit, S., Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts. EMBO J. 1993, 12, 3827–3834.
  • 80
    Mohamed, A. S., Dignam, J. D., Schlender, K. K., Cardiac myosin-binding protein C (MyBP-C): identification of protein kinase A and protein kinase C phosphorylation sites. Arch. Biochem. Biophys. 1998, 358, 313–319.
  • 81
    Geisler, N., Weber, K., Phosphorylation of desmin in vitro inhibits formation of intermediate filaments; identification of three kinase A sites in the aminoterminal head domain. EMBO J. 1988, 7, 15–20.
  • 82
    Jideama, N. M., Noland, T. A., Jr., Raynor, R. L. Blobe, G. C. et al., Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties. J. Biol. Chem. 1996, 271, 23277–23283.
  • 83
    Noland, T. A., Jr., Raynor, R. L., Kuo, J. F., Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites. J. Biol. Chem. 1989, 264, 20778–20785.
  • 84
    Ikebe, M., Hartshorne, D. J., Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase. J. Biol. Chem. 1985, 260, 10027–10031.
  • 85
    Layland, J., Solaro, R. J., Shah, A. M., Regulation of cardiac contractile function by troponin I phosphorylation. Cardiovasc. Res. 2005, 66, 12–21.
  • 86
    Sadayappan, S., Gulick, J., Osinska, H., Martin, L. A. et al., Cardiac myosin-binding protein-C phosphorylation and cardiac function. Circ. Res. 2005, 97, 1156–1163.
  • 87
    Kobayashi, T., Yang, X., Walker, L. A., Van Breemen, R. B., Solaro, R. J., A non-equilibrium isoelectric focusing method to determine states of phosphorylation of cardiac troponin I: identification of Ser-23 and Ser-24 as significant sites of phosphorylation by protein kinase C. J. Mol. Cell. Cardiol. 2005, 38, 213–218.
  • 88
    Zhan, X., Desiderio, D. M., The human pituitary nitroproteome: detection of nitrotyrosyl-proteins with two-dimensional Western blotting, and amino acid sequence determination with mass spectrometry. Biochem. Biophys. Res. Commun. 2004, 325, 1180–1186.
  • 89
    White, M. Y., Cordwell, S. J., McCarron, H. C., Tchen, A. S. et al., Modifications of myosin-regulatory light chain correlate with function of stunned myocardium. J. Mol. Cell. Cardiol. 2003, 35, 833–840.
  • 90
    Wang, H., Grant, J. E., Doede, C. M., Sadayappan, S. et al., PKC-betaII sensitizes cardiac myofilaments to Ca2+ by phosphorylating troponin I on threonine-144. J. Mol. Cell. Cardiol. 2006, 41, 823–833.
  • 91
    Karczewski, P., Bartel, S., Krause, E. G., Differential sensitivity to isoprenaline of troponin I and phospholamban phosphorylation in isolated rat hearts. Biochem. J. 1990, 266, 115–122.
  • 92
    Goldspink, P. H., Montgomery, D. E., Walker, L. A., Urboniene, D. et al., Protein kinase Cepsilon overexpression alters myofilament properties and composition during the progression of heart failure. Circ. Res. 2004, 95, 424–432.
  • 93
    Messer, A. E., Jacques, A. M., Marston, S. B., Troponin phosphorylation and regulatory function in human heart muscle: dephosphorylation of Ser23/24 on troponin I could account for the contractile defect in end-stage heart failure. J. Mol. Cell. Cardiol. 2007, 42, 247–259.
  • 94
    Wu, S. C., Solaro, R. J., Protein kinase c zeta : A novel regulator of both phosphorylation and de-phosphorylation of cardiac sarcomeric proteins. J. Biol. Chem. 2007.
  • 95
    Xiao, L., Zhao, Q., Du, Y., Yuan, C. et al., PKCepsilon increases phosphorylation of the cardiac myosin binding protein C at serine 302 both in vitro and in vivo. Biochemistry 2007, 46, 7054–7061.
  • 96
    MacCoss, M. J., McDonald, W. H., Saraf, A., Sadygov, R. et al., Shotgun identification of protein modifications from protein complexes and lens tissue. Proc. Natl. Acad. Sci. USA 2002, 99, 7900–7905.
  • 97
    Kange, R., Selditz, U., Granberg, M., Lindberg, V. et al., Comparison of different IMAC techniques used for enrichment of phosphorylated peptides. J. Biomol. Tech. 2005, 16, 91–103.
  • 98
    Yang, X., Wu, H., Kobayashi, T., Solaro, R. J., van Breemen, R. B., Enhanced ionization of phosphorylated peptides during MALDI TOF mass spectrometry. Anal. Chem. 2004, 76, 1532–1536.
  • 99
    Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J. et al., Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat. Biotechnol. 2002, 20, 301–305.
  • 100
    Larsen, M. R., Thingholm, T. E., Jensen, O. N., Roepstorff, P., Jorgensen, T. J., Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 2005, 4, 873–86.
  • 101
    Kweon, H. K., Hakansson, K., Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis. Anal. Chem. 2006, 78, 1743–1749.
  • 102
    Cooper, H. J., Hakansson, K., Marshall, A. G., The role of electron capture dissociation in biomolecular analysis. Mass Spectrom. Rev. 2005, 24, 201–222.
    Direct Link:
  • 103
    Mikesh, L. M., Ueberheide, B., Chi, A., Coon, J. J. et al., The utility of ETD mass spectrometry in proteomic analysis. Biochim. Biophys. Acta 2006, 1764, 1811–1822.
  • 104
    Yuan, C., Solaro, R. J., Quantitative comparison of myofilament phospho-proteomes of neonatal and adult rat hearts. In: ASMS, Indianoplis, IN 2007.
  • 105
    Seddon, M., Looi, Y. H., Shah, A. M., Oxidative stress and redox signalling in cardiac hypertrophy and heart failure. Heart 2007, 93, 903–907.
  • 106
    Takimoto, E., Kass, D. A., Role of oxidative stress in cardiac hypertrophy and remodeling. Hypertension 2007, 49, 241–248.
  • 107
    Ungvari, Z., Gupte, S. A., Recchia, F. A., Batkai, S., Pacher, P., Role of oxidative-nitrosative stress and downstream pathways in various forms of cardiomyopathy and heart failure. Curr. Vasc. Pharmacol. 2005, 3, 221–229.
  • 108
    Prasan, A M., McCarron, H. C., Zhang, Y., Jeremy, R. W., Myocardial release of nitric oxide during ischaemia and reperfusion: Effects of l-arginine and hypercholesterolaemia. Heart Lung Circ. 2007, 16, 274–281.
  • 109
    Duncan, J. G., Ravi, R., Stull, L. B., Murphy, A. M., Chronic xanthine oxidase inhibition prevents myofibrillar protein oxidation and preserves cardiac function in a transgenic mouse model of cardiomyopathy. Am. J. Physiol. Heart Circ. Physiol. 2005, 289, H1512–1518.
  • 110
    Mihm, M. J., Yu, F., Weinstein, D. M., Reiser, P. J., Bauer, J. A., Intracellular distribution of peroxynitrite during doxorubicin cardiomyopathy: evidence for selective impairment of myofibrillar creatine kinase. Br. J. Pharmacol. 2002, 135, 581–588.
    Direct Link:
  • 111
    Dai, T., Tian, Y., Tocchetti, C. G., Katori, T. et al., Nitroxyl increases force development in rat cardiac muscle. J. Physiol. 2007, 580, 951–960.
    Direct Link:
  • 112
    Shacter, E., Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev. 2000, 32, 307–326.
  • 113
    Canton, M., Neverova, I., Menabo, R., Van Eyk, J., Di Lisa, F., Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts. Am. J. Physiol. Heart Circ. Physiol. 2004, 286, H870–877.
  • 114
    Kanski, J., Behring, A., Pelling, J., Schoneich, C., Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging. Am. J. Physiol. Heart Circ. Physiol. 2005, 288, H371–381.
  • 115
    Kanski, J., Alterman, M. A., Schoneich, C., Proteomic identification of age-dependent protein nitration in rat skeletal muscle. Free Radic. Biol. Med. 2003, 35, 1229–1239.
  • 116
    Kanski, J., Hong, S. J., Schoneich, C., Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine-containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry. J. Biol. Chem. 2005, 280, 24261–24266.
  • 117
    Hong, S. J., Gokulrangan, G., Schoneich, C., Proteomic analysis of age dependent nitration of rat cardiac proteins by solution isoelectric focusing coupled to nanoHPLC tandem mass spectrometry. Exp. Gerontol. 2007, 42, 639–651.
  • 118
    Sethuraman, M., McComb, M. E., Huang, H., Huang, S. et al., Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 2004, 3, 1228–1233.
  • 119
    Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F. et al., Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 1999, 17, 994–999.
  • 120
    Dalle-Donne, S., Scaloni, A., Butterfield, D. A., Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases. John Wiley & Sons, Hoboken, NJ 2006.
  • 121
    Kislinger, T., Gramolini, A. O., MacLennan, D. H., Emili, A., Multidimensional protein identification technology (MudPIT): technical overview of a profiling method optimized for the comprehensive proteomic investigation of normal and diseased heart tissue. J. Am. Soc. Mass Spectrom. 2005, 16, 1207–1220.
  • 122
    Ge, Y., Walker, J. W., Gumerov, D. R., Easterling, M. L., Speir, J. P., Localization of phosphorylation sites in human cardiac troponin I by top down electron capture dissociation mass spectrometry In: HUPO 5th World Congress. Long Beach, CA 2006.
  • 123
    Verduyn, S. C., Zaremba, R., van der Velden, J., Stienen, G. J., Effects of contractile protein phosphorylation on force development in permeabilized rat cardiac myocytes. Basic Res. Cardiol. 2007, 102, 476–487.
  • 124
    Di Lisa, F., De Tullio, R., Salamino, F., Barbato, R. et al., Specific degradation of troponin T and I by mu-calpain and its modulation by substrate phosphorylation. Biochem. J. 1995, 308, 57–61.
  • 125
    Zhang, Z., Biesiadecki, B. J., Jin, J. P., Selective deletion of the NH2-terminal variable region of cardiac troponin T in ischemia reperfusion by myofibril-associated mu-calpain cleavage. Biochemistry 2006, 45, 11681–11694.
Get PDF (312K)