Isolation and identification of a mu-calpain-protein kinase C alpha complex in skeletal muscle.
A mu-calpain-PKC complex was isolated from rabbit skeletal muscle by ultracentrifugation and by anion-exchange chromatography. The PKC associated to mu-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 mu-calpain molecule and of one cPKC molecule. Using monoclonal antibodies specific for the different cPKC isoforms, the isoenzyme associated to mu-calpain was identified as cPKC alpha. Immunofluorescence staining reveals a co-localization of mu-calpain and cPKC alpha on the muscle fibre plasma membranes.
ISTAB, Université Bordeaux 1, Talence, France.
M
M
Savart
C
C
Verret
D
D
Dutaud
K
K
Touyarot
N
N
Elamrani
A
A
Ducastaing
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002154:Calpain / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004075:Diglycerides / Q000494:pharmacology; D005455:Fluorescent Antibody Technique; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D018482:Muscle, Skeletal / Q000201:enzymology*; D010718:Phosphatidylserines / Q000494:pharmacology; D011493:Protein Kinase C / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D011817:Rabbits; D014461:Ultracentrifugation
D004075:Diglycerides; D046911:Macromolecular Substances; D010718:Phosphatidylserines; D011493:Protein Kinase C; D002154:Calpain; D002118:Calcium