Modulation of the activity of calpain II by phosphorylation--changes in the proteolysis of cyclic AMP-dependent protein kinase (peak II, DEAE).
The proteolysis of the 32P-labeled holoenzyme of cyclic AMP-dependent protein kinase (A-PKII:DEAE, peak II fraction) was analysed by SDS-polyacrylamide gel electrophoresis and autoradiography. The contaminants of the A-PKII and calpain II apparently did not interfere with the accuracy of this highly sensitive analysis. Phosphorylation of calpain II by the catalytic subunit of cyclic AMP-dependent protein kinase (A-PK) greatly enhanced the proteolysis of A-PKII, whereas phosphorylation by protein kinase C (PK-C) or cyclic GMP-dependent protein kinase (G-PK) slightly altered the proteolysis.
Kuo
W N
WN
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, FL 32115.
Ganesan
U
U
Walbey
D L
DL
Davis
D L
DL
Allen
K
K
McCall
L K
LK
D002154:Calpain / Q000378:metabolism*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D010447:Peptide Hydrolases; D010766:Phosphorylation
D017868:Cyclic AMP-Dependent Protein Kinases; D010447:Peptide Hydrolases; D002154:Calpain