title: Modulation of the activity of calpain II by phosphorylation--changes in the proteolysis of cyclic AMP-dependent protein kinase (peak II, DEAE).
abstract: 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.
authors.affiliation: Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, FL 32115.
authors.forename: W N
authors.initials: WN
authors.lastname: Kuo
authors.forename: U
authors.initials: U
authors.lastname: Ganesan
authors.forename: D L
authors.initials: DL
authors.lastname: Walbey
authors.forename: D L
authors.initials: DL
authors.lastname: Davis
authors.forename: K
authors.initials: K
authors.lastname: Allen
authors.forename: L K
authors.initials: LK
authors.lastname: McCall
mesh_terms: D002154:Calpain / Q000378:metabolism*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D010447:Peptide Hydrolases; D010766:Phosphorylation
chemical_list: D017868:Cyclic AMP-Dependent Protein Kinases; D010447:Peptide Hydrolases; D002154:Calpain