Influence of length on force and activation-dependent changes in troponin C structure in skinned cardiac and fast skeletal muscle

Biophysical Journal

Volumn 80, Issue 6, 2001, Pages 2798-2808

  Martyn, Donald A ^a   Gordon, A M ^b  

^a University of Washington   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

5' TETRAMETHYLRHODAMINE; CALCIUM; RHODAMINE; TROPONIN C; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; CALCIUM BINDING; CONTROLLED STUDY; FAST MUSCLE; HEART MUSCLE; HEART RIGHT VENTRICLE; LINEAR DICHROISM; MUSCLE FORCE; NONHUMAN; PROTEIN ISOLATION; PROTEIN STRUCTURE; PSOAS MUSCLE; RABBIT; RAT; SARCOMERE LENGTH; STRUCTURE ANALYSIS;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0035006418     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76247-9     Document Type: Article

References (57)

1. Brenner, B. 1983. Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers. Biophys. J. 41: 99-102.
2. Brenner, B., and L. C. Yu. 1985. Equitorial x-ray diffraction from single skinned rabbit psoas fibers at various degrees of activation. Biophys. J. 48:829-834.
3. Cantino, M. E., T. S. Allen, and A. M. Gordon. 1993. Subsarcomeric distribution of calcium in demembranated fibers of rabbit psoas muscle. Biophys. J. 64:211-222.
4. 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.
5. 2+. Biophys. J. 67:1994-2001.
6. Dong, W., S. S. Rosenfeld, C. K. Wang, A. M. Gordon, and H. C. Cheung. 1996. Kinetic studies of calcium binding to the regulatory site of troponin C from cardiac muscle. J. Biol. Chem. 271:688-694.
7. 2+ activation of rat ventricular myocytes. Circ. Res. 83:602-607.
8. Fuchs, F. 1977. The binding of calcium to glycerinated muscle fibers in rigor: the effect of filament overlap. Biochem. Biophys. Acta. 491: 523-531.
9. Fuchs, F. 1978. On the relation between filament overlap and the number of calcium-binding sites on glycerinated muscle fibers. Biophys. J. 21:273-277.
10. 2+-troponin C affinity in skeletal muscle. Am. J. Physiol. 253:C541-C546.
11. 2+ binding. J. Mol. Cell. Cardiol. 28:1375-83.
12. Fuchs, F., and Y. Wang. 1997. Length-dependence of actin-myosin interaction in skinned cardiac muscle fibers in rigor. J. Mol. Cell. Cardiol. 29:3267-3274.
13. Fukuda, N., H. Kajiwara, S. Ischiwata, and S. Kurihara. 2000. Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle. Circ. Res. 86:e1-e6.
14. Geeves, M. A., and P. B. Conibear. 1995. The role of three-state docking of myosin S1 with actin in force generation. Biophys. J. 68:1945-1995.
15. Geeves, M. A., and S. S. Lehrer. 1994. Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit. Biophys. J. 67:273-282.
16. Gordon, A. M., and E. B. Ridgway. 1987. Extra calcium on shortening in barnacle muscle. Is the decrease in calcium binding related to decreased cross-bridge attachment, force, or length? J. Gen. Physiol. 90:321-340.
17. Greaser, M. L., and J. Gergeley. 1971. Reconstitution of troponin from three protein components. J. Biol. Chem. 246:4226-4233.
18. 2+-sensitive force of mammalian skeletal and cardiac muscles. J. Physiol. (Lond.). 441:305-324.
19. Hazard, A. L., S. C. Kohout, N. L. Stricker, J. A. Putkey, and J. J. Falke. 1998. The kinetic cycle of cardiac troponin C: calcium binding and dissociation at site II trigger slow conformational rearrangements. Protein Sci. 7:2451-2459.
20. Herzberg, O., and M. N. G. James. 1985. Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature. 313: 653-659.
21. Herzberg, O., and M. N. G. James. 1988. Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution. J. Mol. Biol. 203:761-779.
22. Hibberd, M. G., and B. R. Jewell. 1982. Calcium- and length-dependent force production in rat ventricular muscle. J. Physiol. 329:527-540.
23. Higuchi, H., and S. Takemori. 1989. Butanedione monoxime suppresses contraction and ATPase activity of rabbit skeletal muscle. J. Biochem. 105:638-643.
24. 2+ binding to cardiac troponin C. Am. J. Physiol. 253:C90-C96.
25. Hofmann, P. A., and F. Fuchs. 1987b. Evidence for a force-dependent component of calcium binding to cardiac troponin C. Am. J. Physiol. 253:C541-C546.
26. Horiuti, K., H. Higuchi, Y. Umazume, M. Konishi, O. Okazaki, and S. Kurihara. 1988. Mechanism of action of 2,3-butanedione 2-monoxime on contraction of frog skeletal muscle fibres. J. Muscle Res. Cell Motil. 9:156-164.
27. Kawai, M., J. S. Wray, and Y. Zhao. 1993. The effect of lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. I. Proportionality between the lattice spacing and the fiber width. Biophys. J. 64:187-196.
28. Kentish, J. C., H. E. D. J. ter Keurs, L. Ricciardi, J. J. J. Bucx, and M. I. M. Noble. 1986. Comparison between the sarcomere length-force relations of intact and skinned trabeculae from rat right ventricle: influence of calcium concentration on these relations. Circ. Res. 58:755-768.
29. 2+ or myosin heads? J. Muscle Res. Cell Motil. 15:232-236.
30. Lehrer, S. S., and M. A. Geeves. 1998. The muscle thin filament as a classical cooperative/allosteric regulatory system. J. Mol. Biol. 277: 1081-1089.
31. Levine, R. J. C., R. W. Kensler, Z. Yang, J. T. Stull, and H. L. Sweeney. 1996. Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys. J. 71:898-907.
32. Levine, R. J. C., Z. Yang, N. D. Epstein, L. Fananapazir, J. T. Stull, and H. L. Sweeney. 1998. Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains. J. Struct. Biol. 122:149-161.
33. Li, H.-C., and P. G. Fajer. 1994. Orientational changes of troponin C associated with thin filament activation. Biochem. J. 33:14324-14332.
34. Li, M. X., L. Spyracopoulos, and B. D. Sykes. 1999. Binding of cardiac troponin-1147-163 induces a structural opening in human cardiac troponin C. Biochemistry: 38:8289-8298.
35. 2+ and cross-bridge induced changes in troponin C in skinned skeletal muscle fibers: effects of force inhibition. Biophys. J. 76:1480-1493.
36. 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.
37. 2+ and cross-bridge dependent changes in N- and C-terminal structure of troponin C in rat cardiac muscle. Biophys. J. 80:360-370.
38. Matsubara, I., Y. Umazume, and N. Yagi. 1985. Lateral filamentary spacing in chemically skinned murine muscles during contraction. J. Physiol. 360:135-148.
39. 2+ sensitivity of tension in mouse cardiac myocytes expressing skeletal troponin C. J. Physiol. 483:131-139.
40. 2+ sensitivity of tension at short sarcomere length. Circ. Res. 77:199-205.
41. McDonald, K. S., M. R. Wolff, and R. L. Moss. 1997. Sarcomere length dependence of the rate of tension redevelopment and submaximal tension in rat and rabbit skinned skeletal muscle fibres. J. Physiol. (Lond.). 501:607-621.
42. McKillop, D. F. A., and M. A. Geeves. 1993. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65:693-701.
43. 2+ regulation of mechanical properties of striated muscle: mechanistic studies using extraction and replacement of regulatory proteins. Circ. Res. 70:865-84.
44. Moss, R. L., G. G. Giulian, and M. L. Greaser. 1985. The effects of partial extraction of TnC upon the tension-pCa relationship in rabbit skinned skeletal muscle fibers. J. Gen. Physiol. 86:585-600.
45. 2+ sensitivity of tension development by single skeletal muscle fibers at stretched lengths. Biophys. J. 43:115-119.
46. 2+ binding as a function of sarcomere length. J. Biol. Chem. 272:6018-6027.
47. Sia, S. K., M. X. Li, L. Spyracopoulos, S. M. Gagn'e, W. Liu, J. A. Putkey, and B. D. Sykes. 1997. Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain. J. Biol. Chem. 272: 18216-18221.
48. Spyracopoulos, L., S. M. Gagne, M. X. Li, and B. D. Sykes. 1998. Dynamics and thermodynamics of the regulatory domain of human cardiac troponin C in the Apo- and calcium-saturated states. Biochemistry. 37:18032-18044.
49. Spyracopoulos, L., M. X. Li, S. K. Sia, S. M. Gagn'e, M. Chandra, R. J. Solaro, and B. D. Sykes. 1997. Calcium-induced structural transition in the regulatory domain of human cardiac troponin C. Biochemistry. 36:12138-46.
50. Stephenson, D. G., and I. R. Wendt. 1984. Length dependence of changes in sarcoplasmic calcium concentration and myofibrillar calcium sensitivity in striated muscle fibres. J. Muscle Res. Cell Motil. 5:243-272.
51. Sweeney, H. L., Z. Yang, G. Zhi, J. T. Stull, and K. M. Trybus. 1994. Charge replacement near the phosphorylatable serine of the myosin regulatory light chain mimics aspects of phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 91:1490-1494.
52. Tanner, J. W., D. D. Thomas, and Y. E. Goldman. 1992. Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibres. J. Mol. Biol. 223:185-203.
53. 2+] in intact frog skeletal muscle fibres. J. Physiol. 511:171-180.
54. 2+-troponin C affinity in cardiac and slow skeletal muscle. Am. J. Physiol. 266: C1077-C1082.
55. 2+ binding. J. Mol. Cell. Cardiol. 27:1235-1244.
56. Yang, Z., J. T. Stull, R. J. C. Levine, and H. L. Sweeney. 1998. Changes in interfilament spacing mimic the effects of myosin regulatory light chain phosphorylation in rabbit psoas fibers. J. Struct. Biol. 122: 139-148.
57. Yates, L. D., R. L. Coby, Z. Luo, and A. M. Gordon. 1993. Filament overlap affects TnC extraction from skinned muscle fibres. J. Muscle Res. Cell. Motil. 14:392-400.