Temperature-dependent developmental variation in lobster muscle myosin heavy chain isoforms

Gene

Volumn 316, Issue 1-2, 2003, Pages 119-126

  Magnay, J L ^a   Holmes, J M ^a   Neil, D M ^b   El Haj, A J ^a  

^a KEELE UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

Fibre types; Gene; Homarus gammarus; Thermal

Indexed keywords

ACTIN; ISOPROTEIN; MESSENGER RNA; MYOSIN HEAVY CHAIN;

ABDOMINAL WALL MUSCULATURE; AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTHROPOD; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; ENVIRONMENT; FEMALE; GENE EXPRESSION; LOBSTER; MUSCLE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; STATISTICAL SIGNIFICANCE; TEMPERATURE DEPENDENCE; THERMAL ANALYSIS; UPREGULATION;

ARTHROPODA; CYPRINUS CARPIO; GAMMARUS; HOMARUS GAMMARUS; LOBSTER;

EID: 0141956600     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(03)00745-5     Document Type: Article

References (39)

1. Aiken D.E., Waddy S.L. The Biology and Management of Lobsters. 1980;275-276 Academic Press, New York.
2. Aiken D.E., Waddy S.L. Environmental influences on recruitment of the American lobster, (Homarus americanus): a perspective. Can. J. Fish Aquat. Sci. 43:1986;2258-2270.
3. Branford J.R. Incubation period for the lobster Homarus gammarus at various temperatures. Mar. Biol. 47:1978;363-368.
4. Chaen S., Nakaya M., Guo X.-F., Watabe S. Lower activation energy for sliding velocity of F-actin on a less thermostable isoform of carp myosin. J. Biochem. 120:1996;788-791.
5. Cole J.L., Lang F. Spontaneous and evoked postsynaptic potentials in an embryonic neuromuscular system of the lobster Homarus americanus. J. Neurobiol. 11:1980;459-470.
6. Cotton J.L.S., Mykles D.L. Cloning of a crustacean myosin heavy chain isoform: exclusive expression in fast muscle. J. Exp. Zool. 267:1993;578-586.
7. Ennis G.P. Biology of the Lobster Homarus americanus. 1995;23-46 Academic Press, New York.
8. Fowler W.S., Neil D.M. Histochemical heterogeneity of fibres in the abdominal superficial flexor muscles of the Norway lobster, Nephrops norvegicus (L.). J. Exp. Zool. 264:1992;406-418.
9. Galler S., Neil D.M. The mechanical properties of fibres of different phenotypes in the abdominal flexor muscles of the Norway lobster Nephrops norvegicus (L.). J. Muscle Res. Cell Motil. 15:1994;390-399.
10. Gauvry L., Mohan-Ram V., Ettelaie C., Ennion S., Goldspink G. Molecular motors designed for different tasks and to operate at different temperatures. J. Therm. Biol. 6:1997;367-373.
11. George E.L., Ober M.B., Emerson O.P. Jr. Functional domains of the Drosophila melanogaster muscle myosin heavy chain gene are encoded by alternatively spliced exons. Mol. Cell. Biol. 9:1989;2957-2974.
12. Goldspink G. Adaptation of fish to different environmental temperature by qualitative and quantitative changes in gene expression. J. Therm. Biol. 1-2:1995;167-174.
13. Goodson J.V., Warrick H.M., Spudich J.A. Specialised conservation of surface loops of myosin: evidence that loops are involved in determining functional characteristics. J. Mol. Biol. 287:1999;173-185.
14. Govind C.K., Attwood H.L. Organization of muscular systems. Atwood H.L., Sandeman D.C. The Biology of Crustacea. Neurobiology: Structure and Function. vol. 3:1982;63-103 Academic Press, New York.
15. Govind C.K., Mellon DeF. Jr., Quigley M.M. Muscle and muscle fibre type transformation in clawed crustaceans. Am. Zool. 27:1987;1079-1098.
16. Govind C.K., Kirk M.D., Pearce J. Highly active neuromuscular system in developing lobsters with programmed obsolescence. J. Comp. Neurol. 272:1988;437-449.
17. Harrington W.F., Rodgers M.E. Myosin. Ann. Rev. Biochem. 53:1984;53-73.
18. Harrison P., El Haj A.J. Actin mRNA levels and myofibrillar growth in leg muscles of the European lobster (Homarus gammarus) in response to passive stretch. Mol. Mar. Biol. Biotechnol. 3(1):1994;35-41.
19. Hazel J.R., Prosser C.L. Molecular mechanisms of temperature compensation in poikilotherms. Physiol. Rev. 54:1974;620-668.
20. Hirayama Y., Watabe S. Structural differences in the crossbridge head of temperature-associated myosin subfragment-1 isoforms from carp fast skeletal muscle. Eur. J. Biochem. 246:1997;380-387.
21. Hirayama Y., Sutoh K., Watabe S. Structure-function relationships of the two surface loops of myosin heavy chain isoforms from thermally acclimated carp. Biochem. Biophys. Res. Commun. 269:2000;237-241.
22. Holmes J.M., Whiteley N.M., Magnay J.L., El Haj A.J. Comparison of the variable loops of myosin heavy chain genes from Antarctic and temperate isopods. Comp. Biochem. Physiol., B. 131:2002;349-359.
23. Hwang G.C., Ochiai Y., Watabe S., Hashimoto K. Changes in carp myosin subfragment-1 induced by temperature acclimation. J. Comp. Physiol., B. 161:1991;141-146.
24. Imai J., Hirayama Y., Kikuchi K., Kakinuma M., Watabe S. cDNA cloning of myosin heavy chain isoforms from carp fast skeletal muscle and their gene expression associated with temperature acclimation. J. Exp. Biol. 200:1997;27-34.
25. Johnston I.A., Goldspink G. Thermodynamic activation parameters of fish myofibrillar ATPase enzyme and evolutionary adaptations to temperature. Nature. 257:1975;620-622.
26. Johnston I.A., Temple G.K. Thermal plasticity of skeletal muscle phenotype in ectothermic vertebrates and its significance for locomotory behaviour. J. Exp. Biol. 205:2002;2305-2322.
27. LaFramboise W.A., Griffis B., Bonner P., Warren W., Scalise D., Guthrie R.D., Cooper R.L. Muscle-type specific isoforms in crustacean muscles. J. Exp. Zool. 1:2000;36-48.
28. Li Y., Mykles D.L. Analysis of myosins from lobster muscles: fast and slow isozymes differ in heavy-chain composition. J. Exp. Zool. 255:1990;163-170.
29. Lowey S., Slayter H.S., Weeds A.G., Baker H. Substructure of the myosin molecule. 1. Subfragments of the myosin by enzymatic degradation. J. Mol. Biol. 42:1969;1-29.
30. Mykles D.L. Heterogeneity of myofibrillar proteins in lobster fast and slow muscles: variants of troponin, paramyosin and myosin light chains comprise four distinct protein assemblages. J. Exp. Zool. 234:1985;23-32.
31. Mykles D.L. Multiple variants of myofibrillar proteins in single fibres of lobster claw muscles. Evidence for two types of fibres in the cutter claw. Biol. Bull. 169:1985;476-483.
32. Mykles D.L., Cotton J.L.S. Isolation of cDNAs encoding fast and slow isoforms of lobster myosin heavy chain. J. Cell. Biochem. Suppl. 18D:1994;520.
33. Mykles D.L., Cotton J.L.S., Taniguchi H., Sano K.I., Maeda Y. Cloning of tropomyosin from lobster (Homarus americanus) striated muscles: fast and slow isoforms may be generated from the same transcript. J. Muscle Res. Cell Motil. 19:1998;105-115.
34. Neil D.M., Fowler W.S., Tobasnick G. Myofibrillar protein composition correlates with histochemistry in fibres of the abdominal flexor muscles of the Norway lobster Nephrops norvegicus. J. Exp. Biol. 183:1993;185-201.
35. Perkins H.C. Development rates at various temperatures of embryos of the northern lobster Homarus americanus. Fish Bull. 70:1972;95-99.
36. Spudich J.A. How molecular motors work. Nature. 372:1994;515-518.
37. Uyeda T.Q.P., Ruppel K.M., Spudich J.A. Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature. 368:1994;567-569.
38. Weiss A., Schiaffino S., Leinwand L.A. Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity. J. Mol. Biol. 290:1999;61-75.
39. Wine J.J., Krasne F.B. The Biology of Crustacea. vol. 4:1982;241-292 Academic Press, New York.