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Calmodulin‐binding profiles for nebulin and dystrophin in human skeletal muscle
Author(s) -
Patel K.,
Strong P.N.,
Dubowitz V.,
Dunn M.J.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80095-4
Subject(s) - nebulin , calmodulin , biotinylation , dystrophin , duchenne muscular dystrophy , skeletal muscle , itga7 , biology , microbiology and biotechnology , biochemistry , chemistry , myocyte , titin , genetics , endocrinology , sarcomere , enzyme
Nebulin and dystrophin are two high‐molecular‐mass skeletal muscle proteins that have both been associated with the defective gene in Duchenne muscular dystrophy, although the function of neither protein is known. Other high‐molecular‐mass, calmodulin‐binding proteins have recently been implicated in regulating calcium release from skeletal muscle. Western blots of human skeletal muscle biopsy samples were probed with biotinylated calmodulin; nebulin was identified as a prominent high‐molecular‐mass calmodulin‐binding protein but dystrophin did not bind detectable amounts of biotinylated calmodulin. Dystrophin was absent in a Duchenne muscle biopsy.