Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy (original) (raw)

References

1. Hoffman, E.P., Brown, R.H. Jr. & Kunkel, L.M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 51, 919–928 (1987).
   Article CAS PubMed Google Scholar
2. Monaco, A.P. et al. Isolation of candidate cDNA clones for portions of the Duchenne muscular dystrophy gene. Nature 323, 646–650 (1986).
   Article CAS PubMed Google Scholar
3. Ahn, A.H. & Kunkel, L.M. The structural and functional diversity of dystrophin. Nature Genet. 3, 283–291 (1993).
   Article CAS PubMed Google Scholar
4. Byers, T.J., Lidov, H.G.W. & Kunkel, L.M. An alternative dystrophin transcript specific to peripheral nerve. Nature Genet. 4, 77–81 (1993).
   Article CAS PubMed Google Scholar
5. Lederfein, D. et al. A 71-kilodalton protein is a major product of the Duchenne muscular dystrophy gene in brain and other nonmuscie tissues. Proc. natn. Acad. Sci. U.S.A. 89, 5346–5350 (1992).
   Article CAS Google Scholar
6. Koenig, M., Monaco, A.P. & Kunkel, L.M. The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 53, 219–226 (1988).
   Article CAS PubMed Google Scholar
7. Way, M., Pope, B., Cross, R.A., Kendrick-Jones, J. & Weeds, A.G. Expression of the N-terminal domain of dystrophin in E. coil and demonstration of binding to F-actin. FEBS Lett. 301, 243–245 (1992).
   Article CAS PubMed Google Scholar
8. Senter, L. et al. Interaction ofdystrophin with cytoskeletal proteins: Binding to talin and actin. Biochem. Biophys. Res. Commun. 192, 899–904 (1993).
   Article CAS PubMed Google Scholar
9. Corrado, K., Mills, P.L. & Chamberlain, J.S. Deletion analysis of the dystrophin actin binding domain. FEBS Lett. 344, 255–260 (1994).
   Article CAS PubMed Google Scholar
10. Ervasti, J.M. & Campbell, K.P. Membrane organization of the dystrophin glycoprotein complex. Cell 66, 1121–1131 (1991).
    Article CAS PubMed Google Scholar
11. Ervasti, J.M. & Campbell, K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. cell Biol. 122, 809–823 (1993).
    Article CAS PubMed Google Scholar
12. Suzuki, A., Yoshida, M., Yamamoto, H. & Ozawa, E. Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxy-terminal domain. FEBS Lett. 308, 154–160 (1992).
    Article CAS PubMed Google Scholar
13. Suzuki, A. et al. Molecular organization at the glycoprotein-complex-binding site of dystrophin — Three dystrophin-associated proteins bind directly to the carboxy-terminal portion of dystrophin. Eur. J. Biochem. 220, 283–292 (1994).
    Article CAS PubMed Google Scholar
14. England, S.B. et al. Very mild muscular dystrophy associated with the deletion of 46% of dystrophin. Nature 343, 180–182 (1990).
    Article CAS PubMed Google Scholar
15. Passos-Bueno, M.R., Vainzof, M., Marie, S.K. & Zatz, M. Half the dystrophin gene is apparently enough for a mild clinical course: confirmation of its potential use for gene therapy. Hum. molec. Genet. 3, 919–922 (1994).
    Article CAS PubMed Google Scholar
16. Koenig, M. et al. The molecular basis for Duchenne versus Becker muscular dystrophy: correlation of severity with type of deletion. Am. J. hum. Genet. 45, 498–506 (1989).
    CAS PubMed PubMed Central Google Scholar
17. Prior, T.W. et al. A missense mutation in the dystrophin gene in a Duchenne muscular dystrophy patient. Nature Genet. 4, 357–360 (1993).
    Article CAS PubMed Google Scholar
18. Malhotra, S.B. et al. Frame-shift deletions in patients with Duchenne and Becker muscular dystrophy. Science 242, 755–759 (1988).
    Article CAS PubMed Google Scholar
19. Hoffman, E.P. et al. Is the carboxyl-terminus of dystrophin required for membrane association? A novel, severe case of Duchenne muscular dystrophy. Ann. Neurol. 30, 605–610 (1991).
    Article CAS PubMed Google Scholar
20. Matsumura, K. et al. Deficiency of dystrophin-associated proteinsin Duchenne muscular dystrophy patients lacking COOH-terminal domains of dystrophin. J. clin. Invest. 92, 866–871 (1993).
    Article CAS PubMed PubMed Central Google Scholar
21. Sicinski, P. et al. The molecular basis of muscular dystrophy in the mdx mouse: a point mutation. Science 244, 1578–1580 (1989).
    Article CAS PubMed Google Scholar
22. Ohlendieck, K. & Campbell, K.P. Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J. Cell Biol. 115, 1685–1694 (1991).
    Article CAS PubMed Google Scholar
23. Ohlendieck, K., et al. Duchenne muscular dystrophy: Deficiency of dystrophin associated proteins in the sarcolemma. Neurology 43, 795–800 (1993).
    Article CAS PubMed Google Scholar
24. Rapaport, D. et al. Characerization and cell type distribution of a novel, major transcript of the Duchenne muscular dystrophy gene. Differentiation 49, 187–193 (1992).
    Article CAS PubMed Google Scholar
25. Ibraghimov-Beskrovnaya, O. et al. Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 355, 696–702 (1992).
    Article CAS PubMed Google Scholar
26. Jaynes, J.B., Chamberlain, J.S., Buskin, J.N., Johnson, J.E. & Hauschka, S.D. Transcriptional regulation of the muscle creatine kinase gene and regulated expression in transfected mouse myoblasts. Molec. cell. Biol. 6, 2855–2864 (1986).
    Article CAS PubMed PubMed Central Google Scholar
27. Johnson, J.E., Wold, B.J. & Hauschka, S.D. Muscle creatine kinase sequence elements regulating skeletal and cardiac muscle expression in transgenic mice. Molec. cell. Biol. 9, 3393–3399 (1989).
    Article CAS PubMed PubMed Central Google Scholar
28. Cox, G.A., Phelps, S.F., Chapman, V.M. & Chamberlain, J.S. New mdx mutation disrupts expression of muscle and non muscle isoforms of dystrophin. Nature Genet. 4, 87–93 (1993).
    Article CAS PubMed Google Scholar
29. Feener, C.A., Koenig, M. & Kunkel, L.M. Alternative splicing of human dystrophin mRNA generates isoforms at the carboxy terminus. Nature 338, 509–511 (1989).
    Article CAS PubMed Google Scholar
30. Bies, R.D. et al. Human and murine dystrophin mRNA transcripts are differentially expressed during skeletal muscle, heart, and brain development. Nucl. Acids Res. 20, 1725–1731 (1992).
    Article CAS PubMed PubMed Central Google Scholar
31. Bennett, V. Spectrin-based membrane skeleton: a multipotential adaptor between plasma membrane and cytoplasm. Physiol. Rev. 70, 1029–1065 (1990).
    Article CAS PubMed Google Scholar
32. Luise, M. et al. Dystrophin is phosphorylated by endogenous protein kinases. Biochem. J. 293, 243–247 (1993).
    Article CAS PubMed PubMed Central Google Scholar
33. Milner, R.E., Busaan, J.L., Holmes, C.F.B., Wang, J.H. & Michalak, M. Phosphorylation ofdystrophin. The carboxyl-terminal region of dystrophin is a substrate for in vitro phosphorylation by p34cdc2 protein kinase. J. biol. Chem. 268, 21901–21905 (1993).
    CAS PubMed Google Scholar
34. Madhavan, R. & Jarrett, H.W. Calmodulin-activated phosphorylation of dystrophin. Biochemistry 33, 5797–5804 (1994).
    Article CAS PubMed Google Scholar
35. Tinsley, J.M. et al. Primary structure of dystrophin-related protein. Nature 360, 591–593 (1992).
    Article CAS PubMed Google Scholar
36. Tanaka, H., Ishiguro, T., Eguchi, C., Saito, K. & Ozawa, E. Expression of a dystrophin-related protein associated with the skeletal muscle cell membrane. Histochemistry 96, 1–5 (1991).
    Article CAS PubMed Google Scholar
37. Ohlendieck, K. et al. Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle. Neuron. 7, 499–508 (1991).
    Article CAS PubMed Google Scholar
38. Milke, T., Miyatake, M., Zhao, J., Yoshioka, K. & Uchino, M. Immunohistochemical dystrophin reaction in synaptic regions. Brain Dev. 11, 344–346 (1989).
    Article Google Scholar
39. Shimizu, T., Matsumura, K., Sunada, Y. & Mannen, T. Dense immunostaining of both neuromuscular and myotendon junctions with an anti-dystrophin antibody. Biomed. Res. 10, 405–409 (1989).
    Article CAS Google Scholar
40. Lyons, P.R. & Slater, C.R. Structure and function of the neuromuscular junction in young adult mdx mice. J. Neurocyt. 20, 969–981 (1991).
    Article CAS Google Scholar
41. Partridge, T. Animal models of muscular dystrophy — What can they teach us? Neuropathol. Appl. Neurobiol. 17, 353–363 (1991).
    Article CAS PubMed Google Scholar
42. Wagner, K.R., Cohen, J.B. & Huganir, R.L. The 87K postsynaptic membrane protein from torpedo is a protein-tyrosine kinase substrate homologous to dystrophin. Neuron 10, 511–522 (1993).
    Article CAS PubMed Google Scholar
43. Cox, G.A. et al. Overexpression of dystrophin in transgenic mdx mice eliminates dystrophic symptoms without toxicity. Nature 384, 725–729 (1993).
    Article Google Scholar
44. Rafael, J.A. et al. Prevention of dystrophic pathology in mdx mice by a truncated dystrophin isoform. Hum. molec. Genet. 3, 1725–1733 (1994).
    Article CAS PubMed Google Scholar
45. Roberds, S.L et al. Missense mutations in the adhalin gene linked to autosomal recessive muscular dystrophy. Cell 78, 625–633> (1994).
    Article CAS PubMed Google Scholar
46. Tome, F.M.S. et al. Congenital muscular dystrophy with merosin deficiency. C. R. Acad. Sci. Paris 317, 351–357 (1994).
    CAS PubMed Google Scholar
47. Passos-Bueno, M.R. et al. Genetic heterogeneity for Duchenne-like muscular dystrophy (DLMD) based on linkage and 50 DAG analysis. Hum. molec. Genet. 2, 1945–1947 (1993).
    Article CAS PubMed Google Scholar
48. Greenberg, D.S., Sunada, Y., Campbell, K.P., Yaffe, D. & Nudel, U. Nature Genet. 8, 340–344 (1994).
49. Ohlendieck, K. & Campbell, K.P. Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle. FEBS Lett. 283, 230–234 (1991).
    Article CAS PubMed Google Scholar
50. Hogan, B., Constantini, F. & Lacey, E. Manipulating the mouse embryo: a laboratory manual. (Cold Spring Harbor Laboratory Press, New York, (1986).
    Google Scholar
51. Chamberlain, J.S., Phelps, S.F., Cox, G.A., Maichele, A.J. & Greenwood, A.D., PCR Analysis of muscular dystrophy in mdx mice. in Molecular and cell biology of muscular dystrophy, (ed. Partridge T.), 167–189 (Chapman & Hall, London, (1993).
    Chapter Google Scholar
52. Lee, C.C., Pearlman, J.A., Chamberlain, J.S. & Caskey, C.T. Expression of recombinant dystrophin and its localization to the cell membrane. Nature 349, 334–336 (1991).
    Article CAS PubMed Google Scholar
53. Ausubel, F.M. Current protocols in molecular biology (John Wiley & Sons, Inc., New York, (1987).
    Google Scholar
54. Harlow, E. & Lane, D.P. Antibodies: A laboratory manual Cold Spring Harbor Laboratory Press, New York, (1988).
    Google Scholar
55. Bulman, D.E., Murphy, E.G., Zubrzycka-Gaarn, E.E., Worton, R.G. & Ray, P.N. Differentiation of Duchenne and Becker muscular dystrophy phenotypes with amino- and carboxy-terminal antisera specific for dystrophin. Am. J. hum. Genet. 48, 295–304 (1991).
    CAS PubMed PubMed Central Google Scholar
56. Ohlendieck, K., Ervasti, J.M., Snook, J.B. & Campbell, K.P. Dystrophin glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma. J. Cell Biol. 112, 135–148 (1991).
    Article CAS PubMed Google Scholar
57. Roberds, S.L., Anderson, R.D., Ibraghimov-Beskrovnaya, O. & Campbell, K.P. Primary structure and muscle-specific expression of the 50-kDa dystrophin-associated glycoprotein (Adhalin). J. Biol. Chem. 268, 23739–23742 (1993).
    CAS PubMed Google Scholar
58. Sambrook, J., Fritsch, E.F., Maniatis, T. Molecular cloning: a laboratory manual, 2nd ed. (Cold Spring Harbor Laboratory Press, New York, (1989).
    Google Scholar
59. Meisenhelder, J. & Hunter, T. Phosphorylation of phospholipase C in vivo and in vitro . Methods Enzymol. 197, 288–305 (1991).
    Article CAS PubMed Google Scholar
60. Chamberlain, J.S. et al. Mouse dystrophin cDNA Sequence: Genbank accession ♯M68859.

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