Effects of temperature, ionic strength and pH on the function of skeletal muscle myosin from a eurythermal fish, Fundulus heteroclitus

Journal of Muscle Research and Cell Motility

Volumn 26, Issue 4-5, 2005, Pages 191-197

  Grove, Theresa J ^a   Mcfadden, Lori A ^a   Chase, P Bryant ^a   Moerland, Timothy S ^a  

^a FLORIDA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

ACTIN FILAMENT; ANIMAL CELL; ARTICLE; ENERGY; ENTHALPY; ENVIRONMENTAL FACTOR; ENVIRONMENTAL TEMPERATURE; ENZYME ACTIVITY; ENZYME ASSAY; FISH; IONIC STRENGTH; MALE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FUNCTION; SKELETAL MUSCLE; UPREGULATION; VELOCITY;

ACTINS; ANIMALS; FUNDULIDAE; HYDROGEN-ION CONCENTRATION; MICROFILAMENTS; MUSCLE CONTRACTION; MUSCLE, SKELETAL; MYOSINS; OSMOLAR CONCENTRATION; RABBITS; TEMPERATURE;

ANIMALIA; FUNDULUS; FUNDULUS HETEROCLITUS;

EID: 28444478089     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-005-9010-0     Document Type: Article

References (33)

1. Anson M (1992) Temperature dependence and Arrhenius activation energy of F-actin velocity generated in vitro by skeletal myosin. J Mol Biol 224: 1029-1038.
2. Armitage P (1971) Statistical Methods in Medical Research. (pp. 279-301) Blackwell Scientific, Oxford.
3. Chaen S, Nakaya M, Guo X-F and Watabe S (1996) Lower activation energy for sliding of F-actin on a less thermostable isoform of carp myosin. J Biochem 120: 788-791.
4. Chase PB and Kushmerick MJ (1988) Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers. Biophys J 53: 935-946.
5. Chase PB, Chen Y, Kulin K and Daniel TL (2000) Viscosity and solute dependence of F-actin translocation by rabbit skeletal heavy meromyosin. Am J Physiol 278: C1088-C10981.
6. Chidester FE (1920) The behavior of Fundulus heteroclitus on Salt Marshes of New Jersey. Am Naturalist 54: 551-557.
7. Gordon AM, LaMadrid MA, Chen Y, Luo Z and Chase PB (1997) Calcium regulation of skeletal muscle thin filament motility in vitro. Biophys J 12: 1295-1307.
8. Hartshorne DJ, Barns EM, Parker L and Fuchs F (1972) The effect of temperature on actomyosin. Biochim Biophys Acta 267: 190-202.
9. Homsher E, Wang F and Sellers JR (1992) Factors affecting movement of F-actin filaments propelled by skeletal muscle heavy meromyosin. Am J Physiol 262: C714-C723.
10. Homsher E, Wang F and Sellers JR (1993) Factors affecting filament velocity in in vitro motility assays and their relation to unloaded shortening velocity in muscle fibers. In: Sugi H and Pollach GH (eds.) Mechanism of Myofilament Sliding in Muscle Contraction. (pp. 279-290). Plenum Press, New York.
11. Homsher E, Kim B, Bobkova A and Tobacman LS (1996) Calcium regulation of thin filament movement in an in vitro motility assay. Biophys J 70: 1881-1892.
12. Hwang GC, Watabe S and Hashimoto K (1990) Changes in carp myosin ATPase induced by temperature acclimation. J Comp Physiol B 160: 233-239.
13. Johnson T and Bennett A (1995) The thermal acclimation of burst escape performance in fish: an integrated study of molecular and cellular physiology and organismal performance. J Exp Biol 198: 2165-2175.
14. Johnston IA and Goldspink G (1975) Thermodynamic activation parameters of fish myofibrillar ATPase enzyme and evolutionary adaptations to temperature. Nature 257: 620-622.
15. Johnston IA and Walesby NJ (1977) Molecular mechanisms of temperature adaptation in fish myofibrillar adenosine triphosphatases. J Comp Physiol 119: 195-206.
16. Jones RH and Molitoris BA (1984) A statistical method for determining the breakpoint of two lines. Anal Biochem 141: 287-290.
17. Julian FJ and Moss RL (1981) Effects of calcium and ionic strength on shortening velocity and tension development in frog skinned muscle fibers. J Physiol 311: 179-199.
18. Kron SJ, Toyoshima YY, Uyeda TQ and Spudich JA (1991) Assays for actin sliding movement over myosin-coated surfaces. Meth Enzymol 196: 399-416.
19. Margossian SS and Lowey S (1982) Preparation of myosin and its subfragments from rabbit skeletal muscle. Meth Enzymol 85B: 55-71.
20. 31P NMR measurements in a stenothermal Antarctic teleost (Harpagifer antarcticus). J Therm Biol 23: 275-282.
21. Pardee JD and Spudich JA (1982) Purification of muscle actin. Meth Enzymol 85B: 164-181.
22. Peyser YM, Ajtai K, Burghardt TP and Muhlrad A (2001) Effect of ionic strength on the conformation of myosin subfragment 1-nucleotide complexes. Biophys J 81: 1101-1114.
23. Prosser CL (1973) Inorganic ions. In: Prosser CL (ed.) Comparative Animal Physiology, 3rd edn. (pp. 79-110). W.B. Saunders Company, Philadelphia.
24. Reeves RB (1972) An imidazole alphastat hypothesis for vertebrate acid-base regulation: tissue carbon dioxide content and body temperature in bullfrogs. Resp Physiol 14: 219-236.
25. 31P-NMR. J Thermal Biol 28: 3632-3671.
26. Schägger H and von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
27. Seow CY and Ford LE (1993) High ionic strength and low pH detain activated skinned rabbit skeletal muscle crossbridges in a low force state. J Gen Physiol 101: 487-511.
28. Sidell BD, Johnston IA, Moerland TS and Goldspink G (1983) The eurythermal myofibrillar protein complex of the mummichog: adaptation to a functional thermal environment. J Comp Physiol 153: 167-173.
29. Siemankowski RF, Wiseman MO and White HD (1985) ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci USA 82: 658-662.
30. Stein LA, Chock PB and Eisenberg E (1984) The rate-limiting step in the actomyosin adenosine triphosphatase cycle. Biochemistry 23: 1555-1563.
31. von Hippel PH and Wong KY (1964) Neutral Salts: The generality of their effects on the stability of macromolecular conformations. Science 145: 577-580.
32. White HD (1982) Special instrumentation and techniques for kinetic studies of contractile systems. Meth Enzymol 85B: 698-708.
33. Willmer P, Stone G and Johnston I (2000) Environmental Physiology of Animals. (pp. 57-84) Blackwell Science, London.