Изменение состава легких цепей миозина миокарда как возможный компенсаторный механизм при дилатационной кардиомиопатии
Диссертация
Целью настоящего исследования является проверка предположения о компенсаторной роли появления предсердных легких цепей в миозине желудочка при ДКМП. Для этого в работе был изучен изоформный состав легких цепей. миозина желудочков на разных стадиях этого заболевания. Для исследования функционального значения изменений, обнаруженных в составе желудочкового миозина при ДКМП, был разработан… Читать ещё >
Список литературы
- Вихлянцев И.М., Алексеева Ю. А., Шпагина М. Д., Удальцов С. Н., Подлубная З. А. (2002) Изучение свойств С-белка скелетных и сердечных мышц сусликов Citellus undulatus на разных стадиях зимней спячки. Биофизика, т. 47, № 4: 701 705
- Ибрагимов А.Ю. (1989) Клинико-морфологические сопоставления при дилятационной кардиомиопатии. Автореферат диссертации на соискание ученой степени кандидата медицинских наук
- Левицкий Д.И. (1987) Структурные особенности и функциональная роль молекул миозина. Структура и функции белков сократительных систем, Л.: Наука
- Лукоянова Н.А., Игнатьев Д. А., Колаева С. Г., Подлубная З. А. (1997) Биофизика, 42:343−347.
- Макаренко И.В., Шпагина М. Д., Вишневская З. И., Подлубная З. А. (2002) Изменение структурно-функциональных свойств цитоскелетного эластичного белка тайтина при дилатационной кардиомиопатии Биофизика, т. 47, № 4: 706 710
- Малышев С.Л. (2000) Роль легких цепей миозина в регуляции мышечного сокращения. Цитология, 42: 19−26
- Мархасин B.C., Изаков ВЛ., Шумаков В. И. (1994) Физиологические основы нарушения сократительной функции миокарда. СПб.: Наука, 256 с.
- Мацука Г. Х. (2000) Сравнительное исследование иммунореактивности тропонинового комплекса при дилатационной и ишемической кардиомиопатиях. Биополимеры и клетка, т. 16, № 2:40−45
- Моисеев B.C. (2000) Сердечная недостаточность и достижения генетики. Достижения в изучении генома человека делают все более и более значимой оценку различных генетических аспектов при конкретных видах патологии. Consilium Mudicum. Т. 1,№ 4: 121−131
- Мравян С.Р., Канвар С., Голухова Е. З. (1997) Клинико-инструментальные показатели в оценке прогноза миокардита и дилятационной кардиомиопатии. Кардиология, № 7: с. 67−72
- Мухарлямов Н.М., Попович М. И., Затушевский И. Ф. (1986) Дилатационная кардиомиопатия. Кишенев: «Штиница», 158 с.
- Пермяков Е.А. (1993) Кальцийсвязывающие белки. М., Наука, с. 191
- Подлубная З.А. (1999) Состав, структура и структурные переходы в толстых нитях поперечно-полосатых мышц позвоночных. Биофизика, т. 44, № 4: 700−707
- Терещенко С.Н., Джаиани Н. А. (2001) Дилатационная кардиомиопатия сегодня. Consilium Medicum. Т. 3, № 2
- Хубутия М.Ш. (2001) дилатационная . кардиомиопатия. Вестник трансплантологии и искусственных органов, № 3−4: 32−40
- Шумаков В.И. и Толпекин В.Е. (1999) Искуссивенное сердце состояние проблемы и перспективы. Вестник трансплантологии и искусственных органов, № 1:29−32
- Шумаков В.И., Хубутия М. Ш., Ильинский И. М. Дилатационная кардиомиопатия. ООО «Издательство Триада», 2003,448 с.
- Akopova I.S., Shpagina M.D., Malyshev S.L., Podlubnaya Z.A. (1998) Light chains of myosin in dilated cardiomyopathy: markers of adaptive and pathological stages. J. Mol. Cell Cardiol., v.30, p. A29
- Arrell D.K., Neverova I., Fraser H., Marban E., Van Eyk J.E. (2001) Proteomic Analysis of Pharmacologically Preconditioned Cardiomyocytes Reveals Novel Phosphorylation of Myosin Light Chain 1. Circulation Research, 89:480
- Atar D., Gao W.D., Marban E. (1995) Alterations of excitation-contraction coupling in stunning myocardium and in failing myocardium. J. Mol. Cell. Cardiol., 27: 783−791
- Auckland L.M., Lambert S.J., Cummins P. (1986) Cardiac myosin light and heavy chain isotypes in tetralogy of Fallot. Cardiovasc. Res., 20: 828−836
- Barany M. (1967) ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol., 50:197
- Behlke J., Lutsch G., Gaestel M., Bielka H. (1991) Supramolecular structure of the recombinant small heat shock protein hsp25. FEBS Lett., 288, 119−122
- Bhayana V., and Henderson A.R. (1995) Biochemical markers of myocardial damage. Clin. Biochem. 28,1
- Bouvagnet P., Leger J., Dechesne C.A., Dureau G., Anoal M., Leger J.J. (1985) Local changes in myosin types in diseased human atrial myocardium: a quantitative immunofluorescence study. Circulation. 72(2):272−9
- Bristow M. (1998) Why does the myocardium fail? Insights from basic science. Lancet. 352: 8−14
- Cantino M.E., Squire J.M. (1986) Resting myosin cross-bridge configuration in frog muscle thick filaments. J. Cell Biol., 102: 610−618
- Chantler P.D. & Szent-Gyorgyi A.G. (1979) Regulatory light-chains and scallop myosin: full dissociation, reversibility and cooperative effects. J. Mol. Biol. 138: 473 492
- Cheney R.E. and Mooseker M.S. (1992) Unconventional myosins. Curr. Opin. Cell Biol., 4(l):27−35
- Chin Т.К., Rowe A.J. (1982) Biochemical properties of native myosin filaments. J. Muscle Res. Cell Motil., v.3, № 1, p. 118
- Chowrashi P.K., Pemrick S.M., Pepe F.A. (1989) LC2 involvement in assembly of skeletal myosin filaments. Biochim. Biophys. Acta, v. 990, p. 216−223
- Dalla Libera L., Sartore S., Schiaffino S. (1979) Comparative analysis of chicken atrial and ventricular myosins. Bioch. Biophys. Acta, 574:283−294
- Dow J. & Stracher A. (1971) Identification of the essential light chains «of myosin. Proc. Natl. Acad. Sci. U S A., 68:1107−10
- Dreizen P. & Lewis C.G. (1970) relationship of structure to function in myosin. II. Salt denaturation and recombination experiments. Biochemistry, 9:1688−1693
- Eisenberg E. and Moos C. (1968) The adenosine triphosphatase activity of acto-heavy meromyosin. A kinetic analysis of actin activation. Biochemistry. 7(4):1486−1489
- Elliott „A., Offer G. (1978) Shape and flexibility of the myosin molecule. J. Mol. Biol., v.123,№ 4, p. 505−519
- Engelhard V.A., Lubimova M.N. (1939) Myosin and adenosinetriphosphatase. Nature, vol. 144, № 3650, p. 668−669
- Fewell J.G., Hewett Т.Е., Sanbe A., Klevitsky R., Hayes E., Warshaw D., Maughan D., Robbins J. (1998) Functional significance of cardiac myosin essential light chain isoform switching in transgenic mice. J.Clin.Invest. v. l01(12):2630−2639
- Figulla H., Rahlf G., Nieger M“ Luig H., Kreuzer H. (1985) Spontaneous hemodynamic improvement or stabilization and associated biopsy findings in patient with congestive cardiomyopathy. Circulation, v. 71, № 6, p. 1095−1104
- Fisher A.J., Smith C.A., Thoden J., Smith R., Sutoh K., Holden H.M., and Rayment I. (995) Structural studies of myosin: nucleotide complexes: A revised model for themolecular basis of muscle contraction. Biophys. J., 68 Suppl.:19S-28S (b)
- Franz W.M., Cremer M., Herrmann R., Grunig E., Fogel W., Scheffold Т., Goebel
- H.H., Kircheisen R., Kubler W., Voit T. (1995) X-linked dilated cardiomyopathy. Novel mutation of the dystrophin gene. Ann. NY Acad. Sci., v. 752, p. 470−491
- Freeman K., Colon-Rivera C., Olsson M.C., Moore R.L., Weinberger H.D., Grupp
- L., Vikstrom K.L., laccarino G., Koch W.J., Leinwand L.A. (2001) Progression from hypertrophic to dilated cardiomyopathy in mice that express a mutant myosin transgene. Am. J. Physiol. Heart Circ. Physiol., 280: H151-H159
- Freydina N.A., Vishnevskaya Z.I., Udaltsov S.N. & Podlubnaya Z.A. (1986) Effect of C-protein and DTNB-light chains on actomyosin ATPase activity at various ionic strengths and Ca2±level. Acta Biophys. Biochim. Hung. 21,247−256
- Godfrey J.E.& Harrington W.F. (1970) Self-assotiation in the myosin system at high ionoc strength. II. Evidence for the presence of a monomer-dimer equilibrium. Biochemistry, 9: 894−908
- Harrington W.F. (1971) A mechanochemical mechanism for muscle contraction. Prot. Natl. Acad. Sci. USA. v. 68 № 3: 685−689
- Haselgrove J.C. (1980) A model of myosin crossbridge structure consistent with the low-angel X-ray diffraction pattern of vertebrate muscle. J. Muscle Res. Cell Motil., 1: 177−191
- Hein S., Scholz D., Fujitani N., Rennollet H., Brand Т., Friedl A., Schaper J. (1994) Altered Expression of Titin and Contractile Proteins in Failing Human Myocardium. J. Mol. Cell Cardiol., v. 26, p. 1291−1306
- Henry G.D., Winstanley M.A., Dalgarno D.C., Scott G.M., Levine B.A., and Trayer I.P. (1985) Characterization of the actin-binding site on the alkali light chain of myosin. Biochim. Biophys. Acta, 830:233−243
- Heusch G., Schulz R. (1996) Hibernating myocardium: a review. J. Mol. Cell. Cardiol., 28: 2359−2372
- Hirzel HQ, Tuchschmid CR., Schneider J, Krayenbuehl HE, Schaub MC. (1985) Relationship between myosin isoenzyme composition, hemodynamics, and myocardial structure in various forms of human cardiac hypertrophy. Circ. Res., 57(5):729−40
- Ho G.Y., Chisholm R.L. (1997) Substitution mutations in the myosin essential light chain lead to reduced actin-activated ATPase activity despite stoichiometric binding to the heavy chain. J. Biol. Chem., 272, № .7:4522−4527
- Hudson L., Harford J.J., Denny R.C., Squire J.M. (1997) Myosin head configuration in relaxed fish muscle: resting state myosin heads must swing axially by up to 150 A or turn upside down to reach the rigor. J. Mol. Biol., 273: 440−455
- Huxley H.E. (1963) Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol., v.7, № 3:281−308
- Huxley H.E., Brown W. (1967) The low angle X-ray diagram of vertebrate striated muscle and its behavior during contraction and rigor. J. Mol. Biol., v.30, № 2: 383−431
- Huxley H.E. (1969) The mechanism of muscular contraction. Science, v.164, № 3886: 1356−1366
- Kaji M., Kuno H., Turn Т., Sato Y., Oizumi K. (2001) Elevated serum myosin light chain I in influenza patients. Intern. Med., V.40(7): 594−597
- Kasper E.K., Agema W.R., Hutchins G.M., Deckers J.W., Hare J.M., Baughman K.L. (1994) The causes of dilated cardiomyopathy: a clinicopathologic review of 673 consecutive patients. J. Am. Coll. Cardiol., v. 23, № 3: 586−590
- Katoh T. & Lowey S. (1989) Mapping myosin light chains by immunoelectron microscopy. Use of anti-fluorescyl antibodies as structural probes. J. Cell. Biol. 109:1549−60
- Kendrick-Jones J., Szentkiralyi E.M., Szent-Gyorgyi A.G. (1976) Regulatory light chains in myosins. J. Mol. Biol., 104:747−75
- Kensler R.W., Stewart M. (1983) Frog skeletal muscle thick filaments are three-stranded. J. Cell Biol., 96: 1797−1802
- Khaw B.A., Gold H.K., Fallon J.T., Haber E. (1978) Detection of serum cardiac myosin light chains in acute experimental myocardial infarction: radioimmunoassay of cardiac myosin light chains. Circulation, 58(6): 1130−6
- Kielley WW & Harrington W.F. (1960) A model for the myosin molecule. Biochim. Biophys. Acta., V. 41:401−21
- Kolaeva S.G., Kramarova L.I., Ilyasova E.N., Ilyasov F.E. The kinetics and metabolism of the cell of hibernating animals during hibernation (1980) Int. Rev. Cytol., v. 66: 147−70
- Kretsinger R.H. (1980) Structure and evolution of the calcium-modulated proteins. CRC Crit. Rev. Biochem., 8: 119−174
- Kurabayashi M., Komuro I., Tsuchimochi H., Takaki F., Yazaki Y. (1988) Molecular cloning and characterization of human atrial and ventricular myosin alkali light chain cDNA clones. J. Biol. Chem., v. 263: 13 930−13 936
- Kurabayashi M., Shibasaki Y., Komuro I., Tsuchimochi H., Yazaki Y. (1990) The myosin gene switching in human cardiac hypertrophy. Jpn. Circ. J., 54(9): 1192−205
- Laemmli H. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature V. 227: 680−685
- Lanzetta P.A., Alvarez L.J., Reinach P. S., Candia O.A. (1979) An improved assay for nanomole amounts of inorganic phosphate. Analytical Biochem., 100: 95−97
- Lehman W. (1978) Thick-filament-linked calcium regulation in vertebrate skeletal muscle. Nature, v.274, № 5666: 80- 81
- Levine RJ.C. (1993) Evidence for overlapping myosin heads on relaxed thick filaments of fish, frog and scallop striated muscles. J. Struct. Biol., 110: 99−110
- Levine, R.J.C., Kensler, R.W., Yang, Z., Stull, J.T. & Sweeney, H.L. (1996) Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys. J., 71: 898−907
- Levine RJ.C. (1997) Differences in myosin head arrangement on relaxed thick filaments from Lethocerus and rabbit muscles. J. Muscle Res. Cell Motil., 18: 529−543
- Levine R.J.C., Yang, Z» Stull, J.T. & Sweeney, H.L. (1998) Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains. J. Struct. Biol., 122: 149−161
- Levine R.J., Caulfield J.B., Norton P., Chantler P.D., Deziel M.R., Slayter H.S., Margossian S.S. (1999) Myofibrillar protein structure and assembly during idiopathic dilated cardiomyopathy. Mol. Cell Biochem., 195(1−2): 1−10
- Lowey S., Slayter H.S., Weeds A.G., Baker H. (1969) Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J. Mol. Biol., v.42, № 1: 1−29
- Lowey S., Waller G.S., Trybus K.M. (1993a) Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay. J. Biol. Chem., v. 268, № 27:20 414−20 418
- Lowey S., Waller G.S., Trybus K.M. (19 936) Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature, v. 365, № 6465, p. 454−456
- Lowey S., Trybus K.M. (1995) Role of skeletal and smooth muscle myosin light chain. Biophys. J., v. 68, № 2, p. 120s-127s
- Maeda M., Holder E., Lowes В., Valent S., Bies R.D. (1997) Dilated cardiomyopathy associated with deficiency of the cytoskeletal protein metavinculin Circulation, v. 95, № 1, p. 17−20
- Margossian S.S. (1985) Reversible dissociation of dog cardiac myosin regulatory light chain 2 and its influence on ATP hydrolysis. J. Biol. Chem., V. 260. № 25: 1 374 713 754
- Margossian S.A., White H.D., Caulfield J.B., Norton P., Taylor S., Slayter H.S. (1992) Light chain 2 profile and activity of human ventricular myosin during dilated cardiomyopathy. Circulation, v. 85, № 5: 1720−1733
- Mestroni L., Milasin J., Vatta M., Pinamonti В., Sinagra G., Rocco C., Matulic M., Falaschi A., Giacca M., Camerini F. (1996) Genetic factors in dilated cardiomyopathy. Arch. Mai. Coeur. Vaiss., v. 89, spec № 2: 15−20
- Milligan R.A., Whittaker M., Safer D. (1990) Molecular structure of F-actin and location of surface binding sites. Nature, v.348:217−221
- Moos C. (1973) Cold Spring Harbor Symposium Quantitative Biology, 37: 137
- Moore R.L., Palmer B.M. (1999) Exercise training and cellular adaptations of normal and diseased hearts. Exerc. Sport Sci. Rev., v. 27: 285−315
- Morano I., Hadicke K., Grom S., Koch A., Schwinger R.H., Bohm M., Bartel S., Erdmann E., Krause E.G. (1994) Titin, myosin light chains and C-protein in the developing and failing human heart. J. Mol. Cell Cardiol., 26(3):361−8
- Morano I., Ritter O., Bonz A., Timek Т., Vahl C.F., Michel G. (1995) Myosin Light Chain Actin Interaction Regulates Cardiac Contractility. Circ. Res., v. 76, № 5: 720 725
- Morano I. and Haase H. (1997) Different actin affinities of human cardiac essential myosin light chain isoforms. FEBS Lett. 408: 71−74
- Morano I. (1999) Tuning the human heart molecular motors by myosin light chains. J. Mol. Med., 77: 544−555
- Pardee J.D. & Spudich J.A. (1982) Purification of muscle actin. Methods Enzymol. V.85 Pt. B:164−181
- Pemrick S.M. (1977) Comparison of the calcium sensitivity of actomyosin from native and LC-deficient myosin. Biochemistry, v. 16:4047−4054
- Pepe F.A. (1971) Structure of the myosin filament of striated muscle. Progr. Biophys. Mol. Biol., v.22: 75−95
- Perrie W.T. & Репу S.V. (1970) An electrophoretic study of the Iow-molecular-weight components of myosin. Biochem. J., 119:31−8
- Pissarek M., Bigard X., Mateo P., Guezennec C.Y., Hoerter J.A. (1997) Adaptation of cardiac myosin and creatine kinase to chronic hypoxia: role of anorexia and hypertension. Am. J. Physiol., v. 272, № 4, pt.2: H1690-H1695
- Podlubnaya Z.A., Kakol I., Moczarska A., Stepkowski D., Udaltsov S. (1999) Calcium-induced structural changes in synthetic myosin filaments of vertebrate striated muscles. J. Struct. Biol., v. 127, № 1: 1−15
- Prince H.P., Trayer H.R., Hemy G.D., Trayer I.P., Dalgamo D.C., Levine B.A., Cary P.D., Turner C. (1981) Proton nuclear-magnetic-resonance spectroscopy of myosin subfragment 1 isoenzymes. Eur. J. Biochem., v. 121:213−219
- Pulliam D.L., Sawina V., Levine R.J.C. (1983) Calcium sensitivity of vertebrate skeletal muscle myosin. Biochemistry, v.22, № 10: 2324−2331
- Rarick H.M., Opgenorth T.J., von Geldem T.W., Wu-Wong J.R., Solaro R.J. (1996) An essential myosin light chain peptide induces supramaximal stimulation of cardiac myofibrillar ATPase activity. J. Biol. Chem., 271(43):27 039−43
- Rayment I., Rypniewski W.R., Schmidt-Base K., Smith R., Tomchicl D.R., Benning M.W., Winkelmann D.A., Wesenberg G., Holden H.M. (1993) Three-dimensional structure of myosin sub fragment-1: a molecular motor. Science, v. 261: 50−58
- Rayment I. (1996) The structural basis of the myosin ATPase activity. J. Biol. Chem., 271:15 850−15 853
- Rees M. & Young M. (1967) Studies on the isolation and molecular properties of homogeneous globular actin. Evidence for a single polypeptide chain structure. J. Biol. Chem., 242:4449−4458
- Ritter O., Haase H., Schulte H.D., Lange P.E., Morano I. (1999) Remodeling of the hypertrophied human myocardium by cardiac bHLH transcription factors. J. Cell. Biochem. 74:551−61
- Schaper J., Froede R., Hein St., Buck A., Hashezume H., Speiser В., Friedl A., Bleese N. (1991) Impairment of the myocardial ultrastructure and changes of the cytoskeleton in dilated cardiomyopathy. Circulation, v. 83: 504−514
- Schaub M.C., Tuhcshmid C.R., Srihari Т., Hirzel H.O. (1984) Myosin isoenzimes in human hypertophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains. Eur. Heart I, 5 (Suppl): 85−93
- Schaub M.C., Hirzel H.O. (1987) Atrial and ventricular isomyosin composition in patients with different forms of cardiac hypertrophy. Basic Res. Cardiol., 82 Suppl. 2:357−67
- Shaub M.C., Hefti M.A., Zuellig R.A., Morano I. (1998) Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms. Cardiovasc. Res., 37: 381−404
- Schiaffino S & Reggiany C. (1996) Molecular diversity of myofibrillar priteins: gene regulation and functional significance. Physiol. Rew., 76 371 423
- Schlant R. & Sonnenblink A. (1998) Pathophysiology of heart failure. In: Hurst’s The heart. Ed. Alexander R. Et al. McGraw-Hill, 687
- Sellers J.R., Chantler P.D., Szent-Gyorgyi A.G. (1980) Hybrid formation between scallop myofibrils and foreign regulatory light-chains. J. Mol. Biol., 144:223−45
- Sellers J.R. and Goodson H.V. (1995) in: Protein Profile, v.2, Motor protein 2: myosin. Sheterline, P., Ed., Academic Press, London, 1323−1423
- Sivaramakrishnan M. & Burke M. (1982) The free heavy chain of vertabrate skeletal myosin subfragment 1 shows full enzymatic activity. J. Biol. Chem., 257: 1102−1105
- Siu S.C., Sole M. J. (1994) Dilated cardiomyopathy. Curr. Opin. Cardiol., v. 9, № 3: 337−343
- Skubiszak L. (1993) Force generation in muscle. I. Molecular organization in the thick filament. Biocyb. Biomed. Eng., v. 13, № 1: 75−96
- Skubiszak L. (1996) Structure and functional significance of the thick filament. Biophysics, 41:40−57
- Solaro R.J., Pang D.C., Briggs F.N. (1971) The purification of cardiac myofibrils with triton X-protein-100. Biochim. Biophys. Acta., V. 245:259−262
- Spry C.J. and Tai P.C. (1991) Dilated cardiomyopathy and myocarditis: monoclonal antibodies to diseased heart tissues. Eur. Heart. J., v. 12, Suppl. D: 130−133
- Squire J. (1981) The structural basis of muscle contraction. N.- Y.-Lond., Plenum Press
- Squire J.M., Luther P.K., Knupp C. (2003) Structural evidence for the interaction of C-protein (mybp-C) with actin and sequence identification of a possible actin-binding domain. J. Mol. Biol., 331(3):713−24
- Stepkowski D., Babiychuk E.B., Danilova V.M. and Kakol I. (1994) Skeletal muscle myosin regulatory light chains conformation affects the papain cleavage of Al light chains. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1209:253−259
- Stepkowski D., Efimova N., Paczynska A., Moczarska A., Nieznanska H., Kakol I. (1997) The possible role of myosin Al light chain in the weakening of actin-myosin interaction. Biochim. Biophys. Acta., v. 1340, № 1: 105−114
- Strynadka N.C.J., James M.N.G. (1989) Crystal structures of the helix-loop-helix calcium binding proteins. Annu. Rev. Biochem., 58: 951−998
- Sutoh K. (1982) Identification of myosin-binding sites on the actin sequence. Biochemistry, v. 21, № 15: 3654−3661
- Sweeney H.L., Boeman B.F., Stull J.T. (1993) Myosin light chain phosphorylation in vertebrate striated muscle: regulation and function. Am. J. Physiol., v. 264: С1085-C1095
- Sweeney H.L., Straceski A.J., Leinwand L.A., Tikunov B.A. Faust L. (1994) Heterologous expression of a cardiomyopathic myosin that is defective in its actin interaction. J. Biol. Chem., 269:1603−1605
- Sweeney H.L. (1995) Function of the N terminus of the myosin essential light chain of vertebrate striated muscle. Biophys. J., 68 Suppl.:l 12S-119S
- Swynghedauw B. (1986) Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiological reviews, v. 66, № 3: 710−771
- Swynghedauw B. (1998) Molecular biology of heart failure. In: Advances in Cardiomyopathies. Eds. Camerini F., Gavazzi A., De Mira R. 147−159
- Syrovy I. (1987) Isoforms of contractile proteins. Prog. Biophys. Molec. Biol., v. 49, No 1:1−27
- Takahashi S. (1978) Topography of the myosin molecule as visualized by an improved negative staining method. J. Biochem., v.83, № 3: 905−908
- Tate C.A., Hyerk M.F., Taffet G.E. (1994) Mechanisms for the responses of cardiac muscle to physical activity in old age. Medicine and science in sports and exercise, p. 561−567
- Timson D.J., Trayer I.P. (1997) The myosin essential light chain: how it fine tunes a protein machine. J. Muscle Res. Cell. Motil., 18:260
- Timson D.J., Trayer I.P. (1997a) The role of the proline-rich region in A 1-type myosin essential light chains: implications for information transmission in the actomyosin complex. FEBS Lett., 400: 31−36
- Timson D.J., Trayer H.R., Trayer I.P. (1998) The N-terminus of Al-type myosin essential light chains binds actin and modulates myosin motor function. Eur. J. Biochem., 255: 654−662
- Towbin J.A. (1993) Molecular genetic aspects of cardiomyopathy. Biochemical Medicine and Metabolic Biology, v. 49: 285−319
- Trahern C.A., Gere J.B., Krauth G.H., Bigham D.A. (1978) Clinical assessment of serum myosin light chains in the diagnosis of acute myocardial infarction. Am. J. Cardiol., v. 41: 641−645
- Trahair Т., Yeoh Т., Keogh A., Spratt P., Chang V., dosRemedios C., Ganniog P.1993) Myosin Light Chain Gene Expression Associated with Disease States of the Human Heart. J. Mol. Cell Cardiol., v. 26: 577−585
- Trayer I.P., Trayer H.R., and Levine B.A. (1987) Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. A proton magnetic resonance study. Eur. J. Biochem., 164:259−266
- Trybus K.M. (1994) Role of myosin light chain. J. Muscle Res. Cell Motil., v. 15: 587−594
- Van Buren P., Waller G.S., Harris D.E., Trybus K.M., Warshaw D.M., Lowey S.1994) The essential light chain is required for full force production by skeletal muscle myosin. Proc. Natl. Acad. Sci. USA, v. 91: 12 403−12 407
- Wagner P. & Giniger E. (1981) Hydrolysis of ATP and reversible binding to F-actin by myosin heavy chains free of all light chains. Nature, v.292, № 5823, p. 560−562
- Wagner P. (1985) Preparation and fractionation of myosin light chains and exchange of the essential light chains. In: Methods in enzymology, 85: 72−81
- Wagner P.D. & Weeds A.G. (1997) Studies on the role of myosin alkali light chains. Recombination and hybridization of light chains and heavy chains in subfragment-1 preparations. J. Mol. Biol., 109:455−473
- Walker M., Knight P., Trinick J. (1985) Negative staining of myosin molecules. J. Mol. Biol. 184:535−542
- Walzthony D., Bahler M., Wallimann Т., Eppenberger H.M., Moor H. (1983) Vizualization of freeze-dried and shadowed myosin molecules immobilized on electron microscopic films. Eur. J. Cell Biol., v.30, № 2: 177−181
- Watterson J.G., Kohler L., Schaub M.C. (1979) Evidence for two distinct binding affinities in the binding of divalent metal ions to myosin. J. Biol. Chem., 254: 64 706 477
- Weeds A.G., Pope B. (1977) Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol., v. l 11, № 1, p. 129−157
- Weeds A.G., Lowey S. (1971) Substructure of’the myosin molecule. II. The light chains of myosin. J. Mol. Biol. v. 61 № 3:701−25
- Wells J.A. and Yount R.G. (1979) Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin subfragment 1. Proc. Natl. Acad. Sci. USA, 76: 4966−4970
- Williamson M.P. (1994) The structure and function of proline-rich regions in proteins. Biochem. J., 279: 249−260
- Wikman-Coffelt J. (1980) Properties of the non-specific calcium-binding sites of rabbit skeletal-muscle myosin. Biochem. J. 185(l):265−268
- Xie X., Harrison D.H., Schlichting I., Sweet R.M., Kalabokis V.N., Szent-Gyrgyi A.G., and Cohen C. (1994) Structure of the regulatory domain of scallop myosin at 2.8° resolution. Nature, 368:306−312
- Yamashita H., Tyska M.J., Warshaw D.M., Lowey S., Tiybus K.M. (2000) Functional consequences of mutation in the smooth muscle myosin heavy chain at sites implicated in Familial Hypertrophic Cardiomyopathy. J. Biol. Chem., v.275:36, 28 045−28 052
- Zimmermann К., Kautz S., Hajdu G., Winter C., Whalen R.G., Starzinski-Powitz A. (1990) Heterogenic mRNAs with an identical protein-coding region of the human embryonic myosin alkali light chain in skeletal muscle cells. J. Mol. Biol., 211: 505 513
- Protein expression profiles, HEART-2D PAGE The human myocardial two-dimensional electrophoresis protein database, German Heart Institute, Berlin, http://userpage.chemie.fu-berlin.de/~pleiss/DCM-profiles.html