TY - JOUR
T1 - Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression
AU - Yang, Bin
AU - Ibraghimov-Beskrovnaya, Oxana
AU - Moomaw, Carolyn R.
AU - Slaughter, Clive A.
AU - Campbell, Kevin P.
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1994/2/25
Y1 - 1994/2/25
N2 - 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.
AB - 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.
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M3 - Article
C2 - 8119949
AN - SCOPUS:0027998866
SN - 0021-9258
VL - 269
SP - 6040
EP - 6044
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 8
ER -