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Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression

  • Bin Yang
    ,
  • Oxana Ibraghimov-Beskrovnaya
    ,
  • Carolyn R. Moomaw
    ,
  • ,
  • Kevin P. Campbell(corresponding author)
*Corresponding author for this work
  • University of Iowa
    ,
  • University of Texas Southwestern Medical Center
    ,
  • Howard Hughes Medical Institute
Scholary Output:
Contribution to journal
Article
Peer-review

Abstract

The 59-kDa dystrophin-associated protein triplet (59-DAP) is a component of the dystrophin-glycoprotein complex which may directly associate with dystrophin. The cDNA encoding one component (59-1 DAP) of the 59-DAP triplet has now been cloned from rabbit skeletal muscle. The deduced amino acid sequence of 59-1 DAP predicts a 505-amino acid polypeptide containing nine potential phosphorylation sites and no predicted transmembrane domains. This is consistent with the 59-1 DAP being a peripheral membrane protein associated with the cytoplasmic face of the dystrophin-glycoprotein complex. Affinity-purified antibodies against rabbit 59-1 DAP fusion proteins only recognize the lowest band of the 59-DAP triplet in skeletal muscle sarcolemma and isolated dystrophin-glycoprotein complex. The tissue-specific expression of 59-1 DAP mRNA, which is most prominent in skeletal and cardiac muscle and is also detected in brain, parallels that of dystrophin but not of utrophin. Levels of 59-1 DAP mRNA are unaffected in mdx mouse skeletal and cardiac muscles, although all dystrophin-associated proteins, including 59-DAP, are greatly reduced in mdx mouse skeletal muscle. However, in mdx mouse cardiac muscle, the up-regulation of utrophin preserves all dystrophin-associated proteins except 59-DAP. Our results suggest that the 59-DAP triplet may contain different protein species and that the 59-1 DAP may associate more specifically with dystrophin than with utrophin.

Publication Information

Output type

Scholary Output:
Contribution to journal
Article
Peer-review

Original language

English (US)

Pages from-to (Number of pages)

Pages 6040-6044 (5 pages)

Journal (Volume, Issue Number)

Journal of Biological Chemistry (Volume 269, Issue 8)

Publication milestones

  • Published - 02/25/1994

Publication status

Published - 02/25/1994

ISSN

0021-9258

Publication IDs

  • Scopus: 0027998866
  • PubMed: 8119949

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