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Parvalbumin Expression in Normal and Mutant Xenopus Embryos

  • Brian K. Kay
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)

Abstract

Our laboratory is interested in understanding the developmental regulation of the Ca2+-binding protein, parvalbumin, in embryos. We wish to learn how the various members of the parvalbumin gene family are differentially expressed, and what the individual isoforms contribute to muscle cell structure and function. Parvalbumin is a member of the troponin C superfamily and is evolutionarily related to a number of Ca2+-binding proteins, including calmodulin, troponin C., regulatory myosin light chains, oncomodulin, intestinal vitamin D-dependent calcium-binding protein, and Spec 1 protein (Goodman et al., 1979; Kretsinger, 1980; MacManus et al., 1983; Hardin et al., 1985).

Keywords

Xenopus Laevis Regulatory Myosin Light Chain Myotomal Muscle Behavioral Mutant Embryonic Muscle Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Rerefences

  1. Celio, M.R. and Heizmann, C.W., 1982, Calcium binding protein parvalbumin is associated with fast contracting muscle fibers. Nature, 297:504.PubMedCrossRefGoogle Scholar
  2. Crow, M.T. and Stockdale, F.E., 1986, Myosin expression and specialization among the earliest muscle fibers of the developing avian limb, Dev. Biol., 113:238.PubMedCrossRefGoogle Scholar
  3. Dawid, I.B., Kay, B.K. and Sargent, T.S., 1983, Gene expression during Xenopus laevis development, in: “Gene structure and regulation in development”, pp. 171–182. S. Subtelny and F.C. Kafatos, eds., Lis, Inc., New York.Google Scholar
  4. Dudek, F.E., Ide, C.F. and Tompkins, R., 1987, Unresponsive, a behavioral mutant in Xenopus laevis. Electrophysiological studies of the neuromuscular system. J. Neurobiology. 18:237.CrossRefGoogle Scholar
  5. Gauthier, G.F., Lowrey, S. and Hobbs, A.W., 1978, Fast and slow myosin in developing muscle fibers, Nature. 275:25.CrossRefGoogle Scholar
  6. Gillis, J.M., Thomason, J., Lefevre, J. and Kretsinger, R.H. 1982, Parvalbumins and muscle relaxation: a computer simulation study. J. Muscle Res. Cell Motility. 3:377.CrossRefGoogle Scholar
  7. Goodman, M., Pechere, J.-F., Haiech, J. and Demaille, J.G. 1979, Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins. J. Mol. Evol., 13:331.PubMedCrossRefGoogle Scholar
  8. Haiech, J., Derancourt, J., Pechere, J.-F and Demaille, J.G. 1979, Magnesium and calcium binding to parvalbumins: evidence for differences between parvalbumins and an explanation of their relaxing function, Biochemistry, 18:2752.PubMedCrossRefGoogle Scholar
  9. Hardin, S.H., Carpenter, C.D., Hardin, P.E., Bruskin, A.M. and Klein, W.H., 1985, Structure of the Sped gene encoding a major calcium-binding protein in the embryonic ectoderm of the sea urchin Stron-gylocentrotus purpuratus. J. Mol. Biol., 186:243.PubMedCrossRefGoogle Scholar
  10. Heizmann, C.W. and Berchtold, M.W., 1987, Expression of parvalbumin and other Ca2+-binding proteins in normal and tumor cells: a topical review. Cell Calcium. 8:1.PubMedCrossRefGoogle Scholar
  11. Heizmann, C.W., Berchtold, M.W. and Rowlerson, A.M., 1982, Correlation of parvalbumin concentration with relaxation speed in mammalian muscles, Proc. Natl. Acad. Sci., 79:7243.PubMedCrossRefGoogle Scholar
  12. Kay, B.K., Shah, A.J. and Halstead, W.E., 1987, Expression of the Ca2+-binding protein, parvalbumin, during embryo development of the frog, Xenopus laevis. J. Cell Biol., 104:841.PubMedCrossRefGoogle Scholar
  13. Kay, B.K., Schwartz, L.M., Rutishauser, U., Qui, T.H. and Peng, H.B., 1988, Patterns of N-CAM rexpression during myogenesis in Xenopus laevis. Development. 103:463.PubMedGoogle Scholar
  14. Klug, G., Reichmann, H. and Pette, D., 1985, Decreased parvalbumin contents in skeletal muscles of C57BL/6J (dy2J/dy2J) dystrophic mice. Muscle Nerve. 8:576.PubMedCrossRefGoogle Scholar
  15. Kretsinger, R.H., 1980, Structure and evolution of calcium-mediated proteins, CRC Crit. Rev. Biochem., 8:119.CrossRefGoogle Scholar
  16. Lawrence, J.B. and Singer, R.H., 1986, Intracellular localization of messenger Rnas for cytoskeletal proteins, Cell, 45:407.PubMedCrossRefGoogle Scholar
  17. MacManus, J.P., Watson, D.C. and Yaguchi, M., 1983, The complete amino acid sequence of oncomodulin -a parvalbumin-like calcium-binding protein from Morris hepatoma 5123tc. Eur. J. Biochem., 136:9.PubMedCrossRefGoogle Scholar
  18. Melton, D.A., Krieg, P.A., Rebagliati, M.R., Maniatis, T., Zinn, K. and Green, M. R., 1984, Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing the bacteriophage Sp6 promoter, Nuc. Acids Res., 12:7057.CrossRefGoogle Scholar
  19. Nieuwkoop, P. and Faber, J., 1967, “Normal tables of Xenopus laevis (Daudin)”, 2nd ed. North-Holland Publishing Co., Amsterdam.Google Scholar
  20. Peng, H.B. and Nakajima, Y., 1978, Membrane particle aggregates in innervated and noninnervated cultures of Xenopus embryonic muscle cells, Proc. Natl. Acad. Sci. USA. 75:500.PubMedCrossRefGoogle Scholar
  21. Reinschmidt, D.C. and Tompkins, R., 1984, Unresponsive, a new behavioral mutant in Xenopus laevis, Differentiation. 26:189.CrossRefGoogle Scholar
  22. Schwartz, L.M. and Kay, B.K., 1988, Differential expression of the Ca2+-binding protein parvalbumin during myogenesis in Xenopus laevis. Dev. Biol., 128:441.PubMedCrossRefGoogle Scholar
  23. Stuhfauth, I., Reininghaus, J., Jockusch, H. and Heizmann, C.W., 1984, Calcium-binding protein, parvalbumin, is reduced in mutant mammalian muscle with abnormal contractile properties, Proc. Natl. Acad. Sci. USA. 81:4814.CrossRefGoogle Scholar
  24. Towbin, H., Staehelin, T. and Gordon, J., 1979, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications, Proc. Natl. Acad. Sci. USA. 76:4350.PubMedCrossRefGoogle Scholar
  25. Wnuk, W., Cox, J.A. and Stein, E.S., 1982, Paralbumins and other soluble high-affinity calcium-binding proteins from muscle. in: “Calcium and Cell Function”, vol. II. pp. 243–278. W.Y. Cheung, ed., Academic Press, New York.Google Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Brian K. Kay
    • 1
  1. 1.Department of BiologyUniversity of North Carolina at Chapel HillChapel HillUSA

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