The effects of the interaction of myosin essential light chain isoforms with actin in skeletal muscles

• Autorzy: Nieznanska H. , Nieznanski K. , Stepkowski D.
• Języki publikacji: EN

Abstrakty

EN

In order to compare the ability of different isoforms of myosin essential light chain to interact with actin, the effect of the latter protein on the proteolytic susceptibility of myosin light chains (MLC-1S and MLC-1V — slow specific and same as ventricular isoform) from slow skeletal muscle was examined. Actin protects both slow muscle es­sential light chain isoforms from papain digestion, similarly as observed for fast skel­etal muscle myosin (Nieznańska et al., 1998, Biochim. Biophys. Acta 1383: 71). The ef­fect of actin decreases as ionic strength rises above physiological values for both fast and slow skeletal myosin, confirming the ionic character of the actin-essential light chain interaction. To better understand the role of this interaction, we examined the effect of synthetic peptides spanning the 10-amino-acid N-terminal sequences of myo­sin light chain 1 from fast skeletal muscle (MLC-1F) (MLCFpep: KKDVKKPAAA), MLC-1S (MLCSpep: KKDVPVKKPA) and MLC-1V (MLCVpep: KPEPKKDDAK) on the myofibrillar ATPase of fast and slow skeletal muscle. In the presence of MLCFpep, we observed an about 19% increase, and in the presence of MLCSpep about 36% increase, in the myofibrillar ATPase activity of fast muscle. On the other hand, in myofibrillar preparations from slow skeletal muscle, MLCSpep as well as MLCVpep caused a lowering of the ATPase activity by about 36%. The above results suggest that MLCSpep induces opposite effects on ATPase activity, depending on the type of myofibrils, but not through its specific N-terminal sequence — which differs from other MLC N-terminal peptides. Our observations lead to the conclusion that the action of different isoforms of long essential light chain is similar in slow and fast skeletal muscle. However the interaction of essential light chains with actin leads to different physiological effects probably depending on the isoforms of other myofibrillar proteins.

Słowa kluczowe

EN

proteolytic susceptibility; myofibrillar ATPase; myosin light chain; interaction; actin; protein; skeletal muscle

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2002
• Tom: 49
• Numer: 3
• Opis fizyczny: p.709-719,fig.

Twórcy

autor

Nieznanska H.

• Polish Academy of Sciences, L.Pasteura 3, 02-093 Warsaw, Poland

autor

Nieznanski K.

autor

Stepkowski D.

Bibliografia

• Andreev OA, Borejdo J. (1995) Binding of heavy-chain and essential light-chain 1 of S1 to actin depends on the degree of saturation of F-actin filaments with S1. Biochemistry..; 34: 14829-33.
• Bacou F, Rouanet P, Barjot C, Janmot C, Vigneron P, d'Albis A. (1996) Expression of myosin isoforms in denervated cross-reinnervated and electrically stimulated rabbit muscles. Eur JBiochem.; 236: 539-47.
• Barton PJ, Cohen A, Robert B, Fiszman MY, Bonhomme F, Guenet JL, Leader DP, Buckingham ME. (1985) The myosin alkali light chains of mouse ventricular and slow skeletal muscle are indistinguishable and are encoded by the same gene. J Biol Chem.; 260: 8578-84.
• Deleage G, Clerc FF, Roux B, Gautheron DC. (1989) ANTHEPROT: IBM PC and Apple Macintosh versions. Comput Appl Biosci.; 5: 159-60.
• deNardi C, Ausoni S, Moretti P, Gorza L, Velleca M, Buckingham M, Schiaffino S. (1993) Type 2X-myosin heavy chain is coded by a muscle fiber type-specific and developmentally regulated gene. J Cell Biol.; 123: 823-35.
• Ebashi S, Kodama A, Ebashi F. (1968) Troponin I preparation and physiological function. J Biochem (Tokyo).; 64: 465-77.
• Fabiato A, Fabiato F. (1979) Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J Physiol (Paris).; 75: 463-505.
• Fiske CH, SubbaRow Y. (1925) The colorimetric determination of phosphorus. J Biol Chem.; 66: 375-400.
• Frank G, Weeds AG. (1974) The amino-acid sequence of the alkali light chains of rabbit skeletal-muscle myosin. Eur J Biochem.; 44: 317-34.
• Gornall AG, Bardawill CJ, David MM. (1949) Determination of serum proteins by means of the biuret reaction. J Biol Chem.; 177: 751-66.
• Greaser ML, Moss RL, Reiser PJ. (1988) Variations in contractile properties of rabbit single muscle fibres in relation to troponin T isoforms and myosin light chains. J Physiol.; 406: 85-98.
• Hailstones DL, Gunning PW. (1990) Characterization of human myosin light chains 1sa and 3nm: implications for isoform evolution and function. Mol Cell Biol.; 10: 1095-104.
• Hayashibara T, Miyanishi T. (1994) Binding of the amino-terminal region of myosin alkali 1 light chain to actin and its effect on actin-myosin interaction. Biochemistry.; 33: 12821-7.
• Herrmann C, Sleep J, Chaussepied P, Travers F, Barman T. (1993) A structural and kinetic study on myofibrils prevented from shortening by chemical cross-linking. Biochemistry.; 32: 7255-63.
• Janmot C, d'Albis A. (1994) Electrophoretic separation of developmental and adult rabbit skeletal muscle myosin heavy chain isoforms: example of application to muscle denervation study. FEBSLett.; 353: 13-5.
• Kurabayashi M, Komuro I, Tsuchimochi H, Takaku F, Yazaki Y. (1988) Molecular cloning and characterization of human atrial and ventricular myosin alkali light chain cDNA clones. J Biol Chem.; 263: 13930-6.
• Laemmli UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature.; 227: 680-5.
• Lees-Miller JP, Helfman DM. (1991) The molecular basis for tropomyosin isoform diversity. BioEssays.; 13: 429-37.
• Lompre AM, Nadal-Ginard B, Mahdavi V. (1984) Expression of the cardiac ventricular alpha- and beta-myosin heavy chain genes is developmentally and hormonally regulated. J Biol Chem.; 259: 6437-46.
• Lowey S, Waller GS, Trybus KM. (1993) Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature.; 365: 454-6.
• Morano I. (1999) Tuning the human heart molecular motors by myosin light chains. JMolMed.; 77: 544-5.
• Morano I, Haase H. (1997) Different actin affinities of human cardiac essential myosin light chain isoforms. FEBS Lett.; 408: 71-4.
• Morano I, Bletz C, Wojciechowski R, Ruegg JC. (1991) Modulation of crossbridge kinetics by myosin isoenzymes in skinned human heart fibers. CirculRes.; 68: 614-8.
• Morano I, Ritter O, Bonz A, Timek T, Vahl C, Michel G. (1995) Myosin light chain-actin interaction regulates cardiac contractility. Cirulc Res.; 76: 720-5.
• Nieznanska H, Nieznanski K, Efimova N, Kakol I, Stepkowski D. (1998) Dual effect of actin on the accessibility of myosin essential light chain A1 to papain cleavage. Biochim Biophys Acta.; 1383: 71-81.
• Periasamy M, Strehler EE, Garfinkel LI, Gubits RM, Ruiz-Opazo N, Nadal-Ginard B. (1984) Fast skeletal muscle myosin light chains 1 and 3 are produced from a single gene by a combined process of differential RNA transcription and splicing. J Biol Chem.; 259: 13595-604.
• Podlubnaya Z, Malyshev SL, Nieznanski K, Stepkowski D. (2000) Order-disorder structural transitions in synthetic filaments of fast and slow skeletal muscle myosins under relaxing and activating conditions. Acta Biochim Polon.; 47: 1007-17.
• Price KM, Littler WA, Cummins P. (1980) Human atrial and ventricular myosin light-chains subunits in the adult and during development. Biochem J.; 191: 571-80.
• Prince HP, Trayer HR, Henry GD, Trayer IP, Dalgarno DC, Levine BA, Cary PD, Turner C. (1981) Proton nuclear- magnetic-resonance spectroscopy of myosin subfragment 1 isoenzymes. Eur J Biochem. ; 121: 213-19.
• Rarick HM, Opgenorth TJ, von Geldern TW, Wu-Wong JR, Solaro RJ. (1996) An essential myosin light chain peptide induces supramaximal stimulation of cardiac myofibrillar ATPase activity. J Biol Chem.; 271: 27039-43.
• Schaub MC, Hefti MA, Zuellig RA, Morano I. (1998) Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms. Cardiovasc Res.; 37: 381-404.
• Smillie LB. (1982) Preparation and identification of a- and b-tropomyosin. Methods Enzymol.; 85: 234-41.
• Stepkowski D, Szczesna D, Wrotek M, Kakol I. (1985) Factors influencing interaction of phosphorylated and dephosphorylated myosin with actin. Biochim Biophys Acta.; 831: 321-9.
• Strzelecka-Golaszewska H, Jakubiak M, Drabikowski W. (1975) Changes in the state of actin during superprecipitation of actomyosin. Eur J Biochem.; 55: 221-30.
• Sutoh K. (1982) Identification of myosin-binding sites on the actin sequence. Biochemistry.; 21: 3654-61.
• Sweeney HL. (1995) Function of the N terminus of the myosin essential light chain of vertebrate striated muscle. Biophys J; 68: 112s-9s.
• Sweeney HL, Kushmerick M, Mabuchi K, Sreter FA, Gergely J. (1988) Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers. J Biol Chem.; 263: 9034-99.
• Swynghedauw B. (1986) Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiol Rev.; 66: 710-74.
• Tartakowski AD. (1978) Methods of isolation and characterisation of skeletal striated muscle myosin and its subunits. In Biophysical and biochemical methods of investigation of muscle proteins. Pinaev GP. ed, pp 55-76. Nauka, Leningrad.
• Timson DJ, Trayer HR, Smith KJ, Trayer IP. (1999) Size and charge requirements for kinetic modulation and actin binding by alkali 1-type myosin essential light chains. J Biol Chem.; 274: 18271-7.