메뉴 건너뛰기




Volumn 42, Issue 1, 2007, Pages 214-221

Shifts in the myosin heavy chain isozymes in the mouse heart result in increased energy efficiency

Author keywords

31P NMR spectroscopy; ATP; Biophysics; Cardiac energy; Cardiac specific transgenesis; Mouse heart; Myosin heavy chain isozyme; | G ATP|

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA,ALPHA MYOSIN HEAVY CHAIN; BETA,BETA MYOSIN HEAVY CHAIN; CARDIAC MYOSIN; ISOENZYME; MYOSIN HEAVY CHAIN; MYOSIN HEAVY CHAIN ALPHA; MYOSIN HEAVY CHAIN BETA;

EID: 33845627094     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2006.08.116     Document Type: Article
Times cited : (30)

References (38)
  • 4
    • 0014103605 scopus 로고
    • ATPase activity of myosin correlated with speed of muscle shortening
    • [Suppl]
    • Barany M. ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol. 50 (1967) 197-218 [Suppl]
    • (1967) J. Gen. Physiol. , vol.50 , pp. 197-218
    • Barany, M.1
  • 5
    • 0034599128 scopus 로고    scopus 로고
    • Myosin heavy chain isoform expression in the failing and nonfailing human heart
    • Miyata S., Minobe W., Bristow M.R., and Leinwand L.A. Myosin heavy chain isoform expression in the failing and nonfailing human heart. Circ. Res. 86 (2000) 386-390
    • (2000) Circ. Res. , vol.86 , pp. 386-390
    • Miyata, S.1    Minobe, W.2    Bristow, M.R.3    Leinwand, L.A.4
  • 7
    • 0032533986 scopus 로고    scopus 로고
    • Role of myosin heavy chain composition in kinetics of force development and relaxation in rat myocardium
    • Fitzsimons D.P., Patel J.R., and Moss R.L. Role of myosin heavy chain composition in kinetics of force development and relaxation in rat myocardium. J. Physiol. 513 Pt. 1 (1998) 171-183
    • (1998) J. Physiol. , vol.513 , Issue.PART 1 , pp. 171-183
    • Fitzsimons, D.P.1    Patel, J.R.2    Moss, R.L.3
  • 8
    • 0024368773 scopus 로고
    • Shortening velocity and myosin and myofibrillar ATPase activity related to myosin isoenzyme composition during postnatal development in rat myocardium
    • Cappelli V., Bottinelli R., Poggesi C., Moggio R., and Reggiani C. Shortening velocity and myosin and myofibrillar ATPase activity related to myosin isoenzyme composition during postnatal development in rat myocardium. Circ. Res. 65 (1989) 446-457
    • (1989) Circ. Res. , vol.65 , pp. 446-457
    • Cappelli, V.1    Bottinelli, R.2    Poggesi, C.3    Moggio, R.4    Reggiani, C.5
  • 9
    • 0028363522 scopus 로고
    • Thyroid hormone-induced alterations in phospholamban protein expression
    • Kiss E., Jakab G., Kranias E.G., and Edes I. Thyroid hormone-induced alterations in phospholamban protein expression. Circ. Res. 75 (1994) 245-251
    • (1994) Circ. Res. , vol.75 , pp. 245-251
    • Kiss, E.1    Jakab, G.2    Kranias, E.G.3    Edes, I.4
  • 12
    • 10644275373 scopus 로고    scopus 로고
    • Impact of beta-myosin heavy chain expression on cardiac function during stress
    • Krenz M., and Robbins J. Impact of beta-myosin heavy chain expression on cardiac function during stress. J. Am. Coll. Cardiol. 44 (2004) 2390-2397
    • (2004) J. Am. Coll. Cardiol. , vol.44 , pp. 2390-2397
    • Krenz, M.1    Robbins, J.2
  • 13
    • 0032482127 scopus 로고    scopus 로고
    • Impaired cardiac energetics in mice lacking muscle-specific isoenzymes of creatine kinase
    • Saupe K.W., Spindler M., Tian R., and Ingwall J.S. Impaired cardiac energetics in mice lacking muscle-specific isoenzymes of creatine kinase. Circ. Res. 82 (1998) 898-907
    • (1998) Circ. Res. , vol.82 , pp. 898-907
    • Saupe, K.W.1    Spindler, M.2    Tian, R.3    Ingwall, J.S.4
  • 14
    • 0019835928 scopus 로고
    • The role of wall stress in the assessment of ventricular function
    • Mirsky I., and Krayenbuehl H.P. The role of wall stress in the assessment of ventricular function. Herz 6 (1981) 288-299
    • (1981) Herz , vol.6 , pp. 288-299
    • Mirsky, I.1    Krayenbuehl, H.P.2
  • 15
    • 0034733648 scopus 로고    scopus 로고
    • Kinetic, thermodynamic, and developmental consequences of deleting creatine kinase isoenzymes from the heart. Reaction kinetics of the creatine kinase isoenzymes in the heart
    • Saupe K.W., Spindler M., Hopkins J.C., Shen W., and Ingwall J.S. Kinetic, thermodynamic, and developmental consequences of deleting creatine kinase isoenzymes from the heart. Reaction kinetics of the creatine kinase isoenzymes in the heart. J. Biol. Chem. 275 (2000) 19742-19746
    • (2000) J. Biol. Chem. , vol.275 , pp. 19742-19746
    • Saupe, K.W.1    Spindler, M.2    Hopkins, J.C.3    Shen, W.4    Ingwall, J.S.5
  • 17
    • 0015755808 scopus 로고
    • Microassay of free and total creatine from tissue extracts by combination of chromatographic and fluorometric methods
    • Kammermeier H. Microassay of free and total creatine from tissue extracts by combination of chromatographic and fluorometric methods. Anal. Biochem. 56 (1973) 341-345
    • (1973) Anal. Biochem. , vol.56 , pp. 341-345
    • Kammermeier, H.1
  • 18
    • 0014077032 scopus 로고
    • An improved procedure for serum creatine phosphokinase determination
    • Rosalki S.B. An improved procedure for serum creatine phosphokinase determination. J. Lab. Clin. Med. 69 (1967) 696-705
    • (1967) J. Lab. Clin. Med. , vol.69 , pp. 696-705
    • Rosalki, S.B.1
  • 19
    • 0024255830 scopus 로고
    • Phosphofructokinase in the rat nervous system: regional differences in activity and characteristics of axonal transport
    • Oblinger M.M., Foe L.G., Kwiatkowska D., and Kemp R.G. Phosphofructokinase in the rat nervous system: regional differences in activity and characteristics of axonal transport. J. Neurosci. Res.. 21 (1988) 25-34
    • (1988) J. Neurosci. Res.. , vol.21 , pp. 25-34
    • Oblinger, M.M.1    Foe, L.G.2    Kwiatkowska, D.3    Kemp, R.G.4
  • 20
    • 0016420225 scopus 로고
    • Determination of the isoenzyme levels of lactate dehydrogenase
    • Bernstein L.H., and Everse J. Determination of the isoenzyme levels of lactate dehydrogenase. Methods Enzymol. 41 (1975) 47-52
    • (1975) Methods Enzymol. , vol.41 , pp. 47-52
    • Bernstein, L.H.1    Everse, J.2
  • 21
    • 0001647511 scopus 로고
    • The citrate condensing enzyme of pigeon breast muscle and moth flight muscle
    • Srere P., BH, and Gowen L. The citrate condensing enzyme of pigeon breast muscle and moth flight muscle. Acta Chem. Scand. 17 Suppl. 1 (1963) S129-S134
    • (1963) Acta Chem. Scand. , vol.17 , Issue.SUPPL. 1
    • Srere, P.1    BH2    Gowen, L.3
  • 22
    • 0025239273 scopus 로고
    • Isolation of subcellular organelles
    • Storrie B., and Madden E.A. Isolation of subcellular organelles. Methods Enzymol. 182 (1990) 203-225
    • (1990) Methods Enzymol. , vol.182 , pp. 203-225
    • Storrie, B.1    Madden, E.A.2
  • 24
    • 0021244062 scopus 로고
    • Rabbit papillary muscle myosin isozymes and the velocity of muscle shortening
    • Pagani E.D., and Julian F.J. Rabbit papillary muscle myosin isozymes and the velocity of muscle shortening. Circ. Res. 54 (1984) 586-594
    • (1984) Circ. Res. , vol.54 , pp. 586-594
    • Pagani, E.D.1    Julian, F.J.2
  • 26
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley A.F. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7 (1957) 255-318
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 28
    • 33845662653 scopus 로고    scopus 로고
    • Human β-myosin heavy chain gene expression directly attenuates cardiac contractility in α-myosin heavy chain dominant single myocytes
    • Herron T.J., Fomicheva E., Vandenboom R., and Metzger J.M. Human β-myosin heavy chain gene expression directly attenuates cardiac contractility in α-myosin heavy chain dominant single myocytes. Circulation 112 Suppl. II (2005) 185
    • (2005) Circulation , vol.112 , Issue.SUPPL. II , pp. 185
    • Herron, T.J.1    Fomicheva, E.2    Vandenboom, R.3    Metzger, J.M.4
  • 30
    • 21844463045 scopus 로고    scopus 로고
    • α-Myosin heavy chain: a sarcomeric gene associated with dilated and hypertrophic phenotypes of cardiomyopathy
    • Carniel E., Taylor M.R., Sinagra G., Di Lenarda A., Ku L., Fain P.R., et al. α-Myosin heavy chain: a sarcomeric gene associated with dilated and hypertrophic phenotypes of cardiomyopathy. Circulation 112 (2005) 54-59
    • (2005) Circulation , vol.112 , pp. 54-59
    • Carniel, E.1    Taylor, M.R.2    Sinagra, G.3    Di Lenarda, A.4    Ku, L.5    Fain, P.R.6
  • 31
    • 3342967512 scopus 로고    scopus 로고
    • Is the failing heart energy starved? On using chemical energy to support cardiac function
    • Ingwall J.S., and Weiss R.G. Is the failing heart energy starved? On using chemical energy to support cardiac function. Circ. Res. 95 (2004) 135-145
    • (2004) Circ. Res. , vol.95 , pp. 135-145
    • Ingwall, J.S.1    Weiss, R.G.2
  • 32
    • 0036872230 scopus 로고    scopus 로고
    • Functional consequences of mutations in the myosin heavy chain at sites implicated in familial hypertrophic cardiomyopathy
    • Lowey S. Functional consequences of mutations in the myosin heavy chain at sites implicated in familial hypertrophic cardiomyopathy. Trends Cardiovasc. Med. 12 (2002) 348-354
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 348-354
    • Lowey, S.1
  • 33
    • 0029024879 scopus 로고
    • Structural interpretation of the mutations in the β-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy
    • Rayment I., Holden H.M., Sellers J.R., Fananapazir L., and Epstein N.D. Structural interpretation of the mutations in the β-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 3864-3868
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3864-3868
    • Rayment, I.1    Holden, H.M.2    Sellers, J.R.3    Fananapazir, L.4    Epstein, N.D.5
  • 35
    • 12144286221 scopus 로고    scopus 로고
    • Human homozygous R403W mutant cardiac myosin presents disproportionate enhancement of mechanical and enzymatic properties
    • Keller D.I., Coirault C., Rau T., Cheav T., Weyand M., Amann K., et al. Human homozygous R403W mutant cardiac myosin presents disproportionate enhancement of mechanical and enzymatic properties. J. Mol. Cell. Cardiol. 36 (2004) 355-362
    • (2004) J. Mol. Cell. Cardiol. , vol.36 , pp. 355-362
    • Keller, D.I.1    Coirault, C.2    Rau, T.3    Cheav, T.4    Weyand, M.5    Amann, K.6
  • 36
    • 29144445177 scopus 로고    scopus 로고
    • Changes in the chemical and dynamic properties of cardiac troponin T cause discrete cardiomyopathies in transgenic mice
    • Ertz-Berger B.R., He H., Dowell C., Factor S.M., Haim T.E., Nunez S., et al. Changes in the chemical and dynamic properties of cardiac troponin T cause discrete cardiomyopathies in transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 18219-18224
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18219-18224
    • Ertz-Berger, B.R.1    He, H.2    Dowell, C.3    Factor, S.M.4    Haim, T.E.5    Nunez, S.6
  • 37
    • 0036787237 scopus 로고    scopus 로고
    • Molecular Mechanisms of inherited cardiomyopathies
    • Fatkin D., and Graham R.M. Molecular Mechanisms of inherited cardiomyopathies. Physiol. Rev. 82 (2002) 945-980
    • (2002) Physiol. Rev. , vol.82 , pp. 945-980
    • Fatkin, D.1    Graham, R.M.2
  • 38
    • 4444286823 scopus 로고    scopus 로고
    • Transgenesis and cardiac energetics: new insights into cardiac metabolism
    • Ingwall J.S. Transgenesis and cardiac energetics: new insights into cardiac metabolism. J. Mol. Cell. Cardiol. 37 (2004) 613-623
    • (2004) J. Mol. Cell. Cardiol. , vol.37 , pp. 613-623
    • Ingwall, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.