Positive inotropic effects of low dATP/ATP ratios on mechanics and kinetics of porcine cardiac muscle

Biophysical Journal

Volumn 91, Issue 6, 2006, Pages 2216-2226

  Schoffstall, Brenda ^a   Clark, Amanda ^a   Chase, P Bryant ^a,b  

^a FLORIDA STATE UNIVERSITY   (United States)

^b FAMU FSU COLLEGE OF ENGINEERING   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; CALCIUM; DEOXYADENOSINE TRIPHOSPHATE; MAGNESIUM; MYOSIN ADENOSINE TRIPHOSPHATASE;

ANIMAL CELL; ARTICLE; CALCIUM TRANSPORT; CELL MOTILITY; CONTROLLED STUDY; HEART CONTRACTION; HEART MUSCLE; HEART MUSCLE CONTRACTILITY; IN VITRO STUDY; INOTROPISM; KINETICS; MUSCLE ISOMETRIC CONTRACTION; NONHUMAN; NONLINEAR SYSTEM; STEADY STATE; THIN FILAMENT; UPREGULATION;

SUIDAE;

EID: 33748452105     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.079061     Document Type: Article

References (36)

1. Regnier, M., A. J. Rivera, Y. Chen, and P. B. Chase. 2000. 2-deoxy-ATP enhances contractility of rat cardiac muscle. Circ. Res. 86:1211-1217.
2. Regnier, M., and E. Homsher. 1998. The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers. Biophys. J. 74:3059-3071.
3. Regnier, M., D. M. Lee, and E. Homsher. 1998. ATP analogs and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis. Biophys. J. 74:3044-3058.
4. Regnier, M., D. A. Martyn, and P. B. Chase. 1998. Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle. Biophys. J. 74:2005-2015.
5. Regnier, M., H. Martin, R. J. Barsotti, A. J. Rivera, D. A. Martyn, and E. Clemmens. 2004. Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle. Biophys. J. 87:1815-1824.
6. Gordon, A. M., E. Homsher, and M. Regnier. 2000. Regulation of contraction in striated muscle. Physiol. Rev. 80:853-924.
7. Fitzsimons, D. P., J. R. Patel, and R. L. Moss. 2001. Cross-bridge interaction kinetics in rat myocardium are accelerated by strong binding of myosin to the thin filament. J. Physiol. 530:263-272.
8. Clemmens, E. W., and M. Regnier. 2004. Skeletal regulatory proteins enhance thin filament sliding speed and force by skeletal HMM. J. Muscle Res. Cell Motil. 25:515-525.
9. Houser, S. R., and K. B. Margulies. 2003. Is depressed myocyte contractility centrally involved in heart failure? Circ. Res. 92:350-358.
10. Malmqvist, U. P., A. Aronshtam, and S. Lowey. 2004. Cardiac myosin isoforms from different species have unique enzymatic and mechanical properties. Biochemistry. 43:15058-15065.
11. Schoffstall, B., A. Clark, and P. B. Chase. 2005. Increasing ratios of 2-dATP/ATP linearly enhances isometric force of porcine cardiac papillary muscle. J. Mol. Cell. Cardiol. 38:817.
12. Schoffstall, B., Clark, A., and Chase, P. B. 2005. Porcine cardiac muscle contractility is enhanced by increasing ratios of 2-dATP/ATP. Circ. Res. 97:199 (online suppl. page e-42).
13. Pardee, J. D., and J. A. Spudich. 1982. Purification of muscle actin. Methods Enzymol. 85:164-181.
14. Schoffstall, B., A. Kataoka, A. Clark, and P. B. Chase. 2005. Effects of rapamycin on cardiac and skeletal muscle contraction and crossbridge cycling. J. Pharmacol. Exp. Ther. 312:12-18.
15. (2+) sensitivity of force development in the presence of slow skeletal troponin I: insights into the role of troponin T isoforms in the fetal heart. J. Biol. Chem. 279:49579-49587.
16. Palmiter, K. A., M. J. Tyska, J. R. Haeberle, N. R. Alpert, L. Fananapazir, and D. M. Warshaw. 2000. R403Q and L908V mutant beta-cardiac myosin from patients with familial hypertrophic cardiomyopathy exhibit enhanced mechanical performance at the single molecule level. J. Muscle Res. Cell Motil. 21:609-620.
17. Chase, P. B., and M. J. Kushmerick. 1988. Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers. Biophys. J. 53:935-946.
18. 2+. Biophys. J. 67:1994-2001.
19. (2+) relations. J. Physiol. 540:485-497.
20. Chase, P. B., D. A. Martyn, and J. D. Hannon. 1994. Activation dependence and kinetics of force and stiffness inhibition by aluminiofluoride, a slowly dissociating analogue of inorganic phosphate, in chemically skinned fibres from rabbit psoas muscle. J. Muscle Res. Cell Motil. 15:119-129.
21. Martyn, D. A., and A. M. Gordon. 1988. Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibres: effects of pH and ionic strength. J. Muscle Res. Cell Motil. 9:428-445.
22. Chase, P. B., and M. J. Kushmerick. 1995. Effect of physiological ADP concentrations on contraction of single skinned fibers from rabbit fast and slow muscles. Am. J. Physiol. 268:C480-C489.
23. Chase, P. B., Y. Chen, K. L. Kulin, and T. L. Daniel. 2000. Viscosity and solute dependence of F-actin translocation by rabbit skeletal heavy meromyosin. Am. J. Physiol. Cell Physiol. 278:C1088-C1098.
24. Uyeda, T. Q., S. J. Kron, and J. A. Spudich. 1990. Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin. J. Mol. Biol. 214:699-710.
25. Kron, S. J., Y. Y. Toyoshima, T. Q. Uyeda, and J. A. Spudich. 1991. Assays for actin sliding movement over myosin-coated surfaces. Methods Enzymol. 196:399-416.
26. Gordon, A. M., M. A. LaMadrid, Y. Chen, Z. Luo, and P. B. Chase. 1997. Calcium regulation of skeletal muscle thin filament motility in vitro. Biophys. J. 72:1295-1307.
27. Sellers, J. R., G. Cuda, F. Wang, and E. Homsher. 1993. Myosin-specific adaptations of the motility assay. Methods Cell Biol. 39:23-49.
28. White, H. D. 1982. Special instrumentation and techniques for kinetic studies of contractile systems. Methods Enzymol. 85:698-708.
29. Segel, I. H. 1993. Enzyme Kinetics: Behaviour and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. John Wiley & Sons, New York.
30. Cooke, R., and W. Bialek. 1979. Contraction of glycerinated muscle fibers as a function of the ATP concentration. Biophys. J. 28:241-258.
31. Brenner, B., and E. Eisenberg. 1986. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc. Natl. Acad. Sci. USA. 83:3542-3546.
32. 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc. Natl. Acad. Sci. USA. 85:3265-3269.
33. 2+ affinities. Biophys. J. 76:2664-2672.
34. Sweeney, H. L., and J. T. Stull. 1990. Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction. Proc. Natl. Acad. Sci. USA. 87:414-418.
35. Huxley, A. F. 1957. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7:255-318.
36. Traut, T. W. 1994. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140:1-22.