Modifications of myosin-regulatory light chain correlate with function of stunned myocardium

Journal of Molecular and Cellular Cardiology

Volumn 35, Issue 7, 2003, Pages 833-840

  White, Melanie Y ^a,b   Cordwell, Stuart J ^b   McCarron, Hugh C K ^a   Tchen, Adrian S ^a   Hambly, Brett D ^a   Jeremy, Richmond W ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

^b MACQUARIE UNIVERSITY   (Australia)

Author keywords

Ischemia and reperfusion; Myocardium; Myosin regulatory light chain; Protein degradation; Proteomics

Indexed keywords

ASPARTIC ACID; IMMUNOGLOBULIN LIGHT CHAIN; PROTEIN P15; SYNAPSIN I; TIOPRONIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; CORRELATION ANALYSIS; DEAMINATION; HEART FUNCTION; HEART LEFT VENTRICLE FUNCTION; HEART MUSCLE CONTRACTILITY; HEART PERFUSION; HEART RATE; HEART VENTRICLE PRESSURE; ISOELECTRIC POINT; ISOLATED HEART; MALE; MASS SPECTROMETRY; MIXED LYMPHOCYTE CULTURE; MYOFILAMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; RABBIT; REGULATORY MECHANISM; STUNNED HEART MUSCLE; TWO DIMENSIONAL GEL ELECTROPHORESIS;

ORYCTOLAGUS CUNICULUS;

EID: 0038123023     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2828(03)00141-X     Document Type: Article

References (32)

1. Bolli R., Marban E. Molecular and cellular mechanisms of myocardial stunning. Physiol Rev. 79:1999;609-634.
2. 2+ responsiveness and altered diastolic function in intact ventricular muscle. Circ Res. 76:1995;1036-1048.
3. Gao W.D., Atar D., Liu Y., Perez N.G., Murphy A.M., Marban E. Role of troponin I proteolysis in the pathogenesis of stunned myocardium. Circ Res. 80:1997;393-399.
4. McDonough J.L., Arrell D.K., Van Eyk J.E. Troponin I degradation and covalent complex formation accompanies myocardial ischemia/reperfusion injury. Circ Res. 84:1999;9-20.
5. Thomas S.A., Fallavollita J.A., Lee T.C., Feng J., Canty J.M. Jr. Absence of troponin I degradation or altered sarcoplasmic reticulum uptake protein expression after reversible ischemia in swine. Circ Res. 85:1999;446-456.
6. Prasan A.M., McCarron H.C.K., Hambly B.D., Fermanis G.G., Sullivan D.R., Jeremy R.J. Effect of treatment on ventricular function and troponin I proteolysis in reperfused myocardium. J Mol Cell Cardiol. 34:2002;401-411.
7. Matsumura Y., Saeki E., Inoue M., Hori M., Kamada T., Kusuoka H. Inhomogeneous disappearance of myofilament-related cytoskeletal proteins in stunned myocardium of guinea pig. Circ Res. 79:1996;447-454.
8. Foster D.B., Van Eyk J.E. In search of the proteins that cause myocardial stunning. Circ Res. 85:1999;470-472.
9. 2+ handling. Circ Res. 89:2001;831-837.
10. Akiyama K., Akopian G., Jinadasa P., Gluckman T.L., Terhakopian A., Massey B., et al. Myocardial infarction and regulatory myosin light chain. J Mol Cell Cardiol. 29:1997;2641-2652.
11. Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.C., et al. Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis. Electrophoresis. 19:1998;837-844.
12. Nouwens A.S., Cordwell S.J., Larsen M.R., Molloy M.P., Gillings M., Willcox M.D., et al. Complementing genomics with proteomics: the membrane subproteome of Pseudomonas aeruginosa PAO1. Electrophoresis. 21:2000;3797-3809.
13. Cordwell S.J. Acquisition and archiving of information for bacterial proteomics - from sample preparation to databasing. Meth Enzymol. 358:2002;207-227.
14. Morano I. Tuning the human heart molecular motors by myosin light chains. J Mol M. 77:1999;544-555.
15. Morano I. Effects of different expression and posttranslational modifications of myosin light chains on contractility of skinned human cardiac fibers. Basic Res Cardiol. 87:(Suppl 1):1992;129-141.
16. van Der Velden J., Klein L.J., Zaremba R., Boontje N.M., Huybregts M.A., Stooker W., et al. Effects of calcium, inorganic phosphate, and pH on isometric force in single skinned cardiomyocytes from donor and failing human hearts. Circulation. 104:2001;1140-1146.
17. Westwood S.A., Perry S.V. The effect of adrenaline on the phosphorylation of the P light chain of myosin and troponin I in the perfused rabbit heart. Biochem J. 197:1981;185-193.
18. Matsuda G., Maita T., Kato Y., Chen J.I., Umegane T. Amino acid sequences of the cardiac L-2A, L-2B and gizzard 17 000-Mr light chains of chicken muscle myosin. FEBS Lett. 135:1981;232-236.
19. Wright H.T. Sequence and structure determinants of the nonenzymatic deamidation of asparagine and glutamine residues in proteins. Protein Eng. 4:1991;283-294.
20. Sarioglu H., Lottspeich F., Walk T., Jung G., Eckerskorn C. Deamidation as a widespread phenomenon in two-dimensional polyacrylamide gel electrophoresis of human blood plasma proteins. Electrophoresis. 21:2000;2209-2218.
21. Robinson N.E. Protein deamidation. Proc Natl Acad Sci USA. 99:2002;5283-5288.
22. Robinson N.E., Robinson A.B. Deamidation of human proteins. Proc Natl Acad Sci USA. 98:2001;12409-12413.
23. Westwood S.A., Perry S.V. Two forms of the p light chain of myosin in rabbit and bovine hearts. FEBS Lett. 142:1982;31-34.
24. Levine R.J., Yang Z., Epstein N.D., Fananapazir L., Stull J.T., Sweeney H.L. Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains. J Struct Biol. 122:1998;149-161.
25. Margossian S.S., White H.D., Caulfield J.B., Norton P., Taylor S., Slayter H.S. Light chain 2 profile and activity of human ventricular myosin during dilated cardiomyopathy. Identification of a causal agent for impaired myocardial function. Circulation. 85:1992;1720-1733.
26. 2+-sensitivity. Mol Cell Biochem. 194:1999;301-313.
27. Corbett J.M., Why H.J., Wheeler C.H., Richardson P.J., Archard L.C., Yacoub M.H., et al. Cardiac protein abnormalities in dilated cardiomyopathy detected by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis. 19:1998;2031-2042.
28. Holt J.C., Caulfield J.B., Norton P., Chantler P.D., Slayter H.S., Margossian S.S. Human cardiac myosin light chains: sequence comparisons between myosin LC1 and LC2 from normal and idiopathic dilated cardiomyopathic hearts. Mol Cell Biochem. 145:1995;89-96.
29. Levine R.J., Caulfield J.B., Norton P., Chantler P.D., Deziel M.R., Slayter H.S., et al. Myofibrillar protein structure and assembly during idiopathic dilated cardiomyopathy. Mol Cell Biochem. 195:1999;1-10.
30. Podlubnaya Z.A., Kakol I., Moczarska A., Stepkowski D., Udaltsov S. Truncation of vertebrate striated muscle myosin light chains disturbs calcium-induced structural transitions in synthetic myosin filaments. J Struct Biol. 131:2000;225-233.
31. Sweeney H.L., Straceski A.J., Leinwand L.A., Tikunov B.A., Faust L. Heterologous expression of a cardiomyopathic myosin that is defective in its actin interaction. J Biol Chem. 269:1994;1603-1605.
32. Laster S.B., Becker L.C., Ambrosio G., Jacobus W.E. Reduced aerobic metabolic efficiency in globally 'stunned' myocardium. J Mol Cell Cardiol. 21:1989;419-426.