Expression and turnover of acylphosphatase (muscular isoenzyme) in L6 myoblasts during myogenesis.
Acylphosphatase (muscular isoenzyme) levels have been measured in L6J1 myoblasts either proliferating or differentiating into myotubes. Results indicated that the increase in enzyme levels during differentiation is very similar to that of creatine kinase, a specific muscular enzyme. The half-lives of acylphosphatase in myoblasts and myotubes were also determined; t1/2 values of 3 h 30 min (myoblasts), and 2 h 18 min (myotubes) were found. These results indicate that acylphosphatase could be considered a short-lived muscle-specific protein and that its increase in myotubes must be accompanied by an activation of its breakdown.
Berti
A
A
Department of Biochemical Sciences, University of Florence, Italy.
Degl'Innocenti
D
D
Stefani
M
M
Ramponi
G
G
D017766:Acid Anhydride Hydrolases; D000818:Animals; D002454:Cell Differentiation; D002460:Cell Line; D004797:Enzyme-Linked Immunosorbent Assay; D006207:Half-Life; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000166:cytology / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D051381:Rats; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D007527:Isoenzymes; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase