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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1988 Jun;85(12):4491–4495. doi: 10.1073/pnas.85.12.4491

Immunological identification of a high molecular weight protein as a candidate for the product of the Duchenne muscular dystrophy gene.

L Kao 1, J Krstenansky 1, J Mendell 1, K W Rammohan 1, E Gruenstein 1
PMCID: PMC280456  PMID: 3288996

Abstract

An oligopeptide was synthesized based on translation of the nucleotide sequence of the putative exon region of clone pERT87-25 from the gene for Duchenne muscular dystrophy. Immunization of rabbits with this oligopeptide induced the formation of antibodies directed against a protein present in human, rat, and rabbit skeletal muscle. This protein, which is missing in the skeletal muscle of two patients with Duchenne muscular dystrophy, has a molecular mass of approximately equal to 320-420 kDa and is clearly different from the putative Duchenne muscular dystrophy-related protein nebulin. The data suggest that this 320- to 420-kDa protein is produced by the Duchenne muscular dystrophy gene.

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Selected References

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  1. Carlsson J., Drevin H., Axén R. Protein thiolation and reversible protein-protein conjugation. N-Succinimidyl 3-(2-pyridyldithio)propionate, a new heterobifunctional reagent. Biochem J. 1978 Sep 1;173(3):723–737. doi: 10.1042/bj1730723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dighiero G., Lymberi P., Guilbert B., Ternynck T., Avrameas S. Natural autoantibodies constitute a substantial part of normal circulating immunoglobulins. Ann N Y Acad Sci. 1986;475:135–145. doi: 10.1111/j.1749-6632.1986.tb20863.x. [DOI] [PubMed] [Google Scholar]
  3. Hoffman E. P., Brown R. H., Jr, Kunkel L. M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell. 1987 Dec 24;51(6):919–928. doi: 10.1016/0092-8674(87)90579-4. [DOI] [PubMed] [Google Scholar]
  4. Hoffman E. P., Knudson C. M., Campbell K. P., Kunkel L. M. Subcellular fractionation of dystrophin to the triads of skeletal muscle. Nature. 1987 Dec 24;330(6150):754–758. doi: 10.1038/330754a0. [DOI] [PubMed] [Google Scholar]
  5. Horowits R., Kempner E. S., Bisher M. E., Podolsky R. J. A physiological role for titin and nebulin in skeletal muscle. Nature. 1986 Sep 11;323(6084):160–164. doi: 10.1038/323160a0. [DOI] [PubMed] [Google Scholar]
  6. Karsenti E., Guilbert B., Bornens M., Avrameas S. Antibodies to tubulin in normal nonimmunized animals. Proc Natl Acad Sci U S A. 1977 Sep;74(9):3997–4001. doi: 10.1073/pnas.74.9.3997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Koenig M., Hoffman E. P., Bertelson C. J., Monaco A. P., Feener C., Kunkel L. M. Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals. Cell. 1987 Jul 31;50(3):509–517. doi: 10.1016/0092-8674(87)90504-6. [DOI] [PubMed] [Google Scholar]
  8. Locker R. H., Wild D. J. A comparative study of high molecular weight proteins in various types of muscle across the animal kingdom. J Biochem. 1986 May;99(5):1473–1484. doi: 10.1093/oxfordjournals.jbchem.a135617. [DOI] [PubMed] [Google Scholar]
  9. Lutz H. U., Wipf G. Naturally occurring autoantibodies to skeletal proteins from human red blood cells. J Immunol. 1982 Apr;128(4):1695–1699. [PubMed] [Google Scholar]
  10. Monaco A. P., Neve R. L., Colletti-Feener C., Bertelson C. J., Kurnit D. M., Kunkel L. M. Isolation of candidate cDNAs for portions of the Duchenne muscular dystrophy gene. Nature. 1986 Oct 16;323(6089):646–650. doi: 10.1038/323646a0. [DOI] [PubMed] [Google Scholar]
  11. Robertson M. Muscular dystrophy: mapping the disease phenotype. Nature. 1987 Jun 4;327(6121):372–373. doi: 10.1038/327372a0. [DOI] [PubMed] [Google Scholar]
  12. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wood D. S., Zeviani M., Prelle A., Bonilla E., Salviati G., Miranda A. F., DiMauro S., Rowland L. P. Is nebulin the defective gene product in Duchenne muscular dystrophy? N Engl J Med. 1987 Jan 8;316(2):107–108. [PubMed] [Google Scholar]

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