Premium
Isolation and identification of a μ‐calpain‐protein kinase Cα complex in skeletal muscle
Author(s) -
Savart Michel,
Verret Catherine,
Dutaud Dominique,
Touyarot Katia,
Elamrani Najat,
Ducastaing André
Publication year - 1995
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(95)00014-z
Subject(s) - calpain , skeletal muscle , isolation (microbiology) , microbiology and biotechnology , identification (biology) , chemistry , protein kinase a , itga7 , biochemistry , kinase , biology , anatomy , bioinformatics , enzyme , botany
A μ‐calpain‐PKC complex was isolated from rabbit skeletal muscle by ultracentrifugation and by anion‐exchange chromatography. The PKC associated to μ‐calpain was stimulated by calcium, phosphatidylserine and diacylglycerol, and corresponds to a conventional PKC (cPKC). This complex presents an apparent molecular mass close to 190 kDa and is composed of one μ‐calpain molecule and of one cPKC molecule. Using monoclonal antibodies specific for the different cPKC isoforms, the isoenzyme associated to μ‐calpain was identified as cPKCα. Immunofluorescence staining reveals a co‐localization of μ‐calpain and cPKCα on the muscle fibre plasma membranes.