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Specific increase of genetic expression of parvalbumin in fast skeletal muscles of mdx mice.

Bibliographic reference Gailly, Philippe ; Hermans, Emmanuel ; Octave, Jean-Noël ; Gillis, Jean-Marie. Specific increase of genetic expression of parvalbumin in fast skeletal muscles of mdx mice.. In: FEBS letters, Vol. 326, no. 1-3, p. 272-4 (1993)
Permanent URL http://hdl.handle.net/2078.1/23009
  1. Hoffman Eric P., Fischbeck Kenneth H., Brown Robert H., Johnson Margaret, Medori Rosella, Loire John D., Harris John B., Waterston Robert, Brooke Michael, Specht Linda, Kupsky William, Chamberlain Jeffrey, Caskey C. Thomas, Shapiro Frederic, Kunkel Louis M., Characterization of Dystrophin in Muscle-Biopsy Specimens from Patients with Duchenne's or Becker's Muscular Dystrophy, 10.1056/nejm198805263182104
  2. Koenig M., Monaco A.P., Kunkel L.M., The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein, 10.1016/0092-8674(88)90383-2
  3. Zubrzycka-Gaarn Elizabeth E., Bulman Dennis E., Karpati George, Burghes Arthur H. M., Belfall Bonnie, Klamut Henry J., Talbot Jim, Hodges Robert S., Ray Peter N., Worton Ronald G., The Duchenne muscular dystrophy gene product is localized in sarcolemma of human skeletal muscle, 10.1038/333466a0
  4. Dangain Josette, Vrbova Gerta, Muscle development in mdx mutant mice, 10.1002/mus.880070903
  5. Wessel Henry B, Dystrophin: A clinical perspective, 10.1016/0887-8994(90)90071-8
  6. MacLennan P A, Edwards R H T, Protein turnover is elevated in muscle ofmdxmicein vivo, 10.1042/bj2680795
  7. Turner Paul R., Westwood Tim, Regen Chester M., Steinhardt Richard A., Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice, 10.1038/335735a0
  8. MacLennan, Am. J. Physiol., 260, E594 (1991)
  9. Dunn J.F., Radda G.K., Total ion content of skeletal and cardiac muscle in the mdx mouse dystrophy: Ca2+ is elevated at all ages, 10.1016/0022-510x(91)90168-7
  10. Bertorini T. E., Bhattacharya S. K., Palmieri G. M. A., Chesney C. M., Pifer D., Baker B., Muscle calcium and magnesium content in Duchenne muscular dystrophy, 10.1212/wnl.32.10.1088
  11. Mongini T., Ghigo D., Doriguzzi C., Bussolino F., Pescarmona G., Polio B., Schiffer D., Bosia A., Free cytoplasmic Ca++ at rest and after cholinergic stimulus is increased in cultured muscle cells from Duchenne muscular dystrophy patients, 10.1212/wnl.38.3.476
  12. Gailly, Cell Calcium (1993)
  13. McArdle A., Edwards R. H. T., Jackson M. J., Accumulation of calcium by normal and dystrophin-deficient mouse muscle during contractile activityin vitro, 10.1042/cs0820455
  14. Webster Cecelia, Silberstein Laura, Hays Arthur P., Blau Helen M., Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy, 10.1016/0092-8674(88)90463-1
  15. Gillis J.M., Relaxation of vertebrate skeletal muscle. A synthesis of the biochemical and physiological approaches, 10.1016/0304-4173(85)90016-3
  16. Heizmann C. W., Berchtold M. W., Rowlerson A. M., Correlation of parvalbumin concentration with relaxation speed in mammalian muscles., 10.1073/pnas.79.23.7243
  17. Gillis J. M., Thomason D., Lef�vre J., Kretsinger R. H., Parvalbumins and muscle relaxation: a computer simulation study, 10.1007/bf00712090
  18. Sano Motoki, Yokota Tsukasa, Endo Toyoshi, Tsukagoshi Hiroshi, A developmental change in the content of parvalbumin in normal and dystrophic mouse (mdx) muscle, 10.1016/0022-510x(90)90224-b
  19. Jockusch Harald, Friedrich Gudrun, Zippel Monika, Serum parvalbumin, an indicator of muscle disease in murine dystrophy and myotonia, 10.1002/mus.880130613
  20. Chomczynski Piotr, Sacchi Nicoletta, Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, 10.1016/0003-2697(87)90021-2
  21. McMaster G. K., Carmichael G. G., Analysis of single- and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange., 10.1073/pnas.74.11.4835
  22. Schleef, Thesis (1992)
  23. Hermans, Neurosci. Lett. (1993)
  24. MacLennan, J. Physiol., 438, 153P (1991)
  25. DiMario Joseph X., Uzman Akif, Strohman R.C., Fiber regeneration is not persistent in dystrophic (mdx) mouse skeletal muscle, 10.1016/0012-1606(91)90340-9
  26. Leberer E, Pette D, Neural regulation of parvalbumin expression in mammalian skeletal muscle, 10.1042/bj2350067
  27. Edwards Y H, Lloyd J C, McMillan S L, Benham F J, Human glyceraldehyde-3-phosphate dehydrogenase: mRNA levels and enzyme activity in developing muscle., 10.1128/mcb.5.8.2147
  28. Berchtold M. W., Means A. R., The Ca2+-binding protein parvalbumin: molecular cloning and developmental regulation of mRNA abundance., 10.1073/pnas.82.5.1414
  29. Baron G., Demaille J., Dutruge E., The distribution of parvalbumins in muscle and in other tissues, 10.1016/0014-5793(75)80131-1
  30. Celio M. R., Heizmann C. W., Calcium-binding protein parvalbumin is associated with fast contracting muscle fibres, 10.1038/297504a0
  31. Anderson J. E., Bressler B. H., Ovalle W. K., Functional regeneration in the hindlimb skeletal muscle of the mdx mouse, 10.1007/bf01738755
  32. Ng Leong L., Davies Joan E., Ameen Mohammed, Intracellular free-magnesium levels in vascular smooth muscle and striated muscle cells of the spontaneously hypertensive rat, 10.1016/0026-0495(92)90319-6