Changes of the expression of protein substrates of Ca2+/calmodulin-dependent protein kinase II in neonate and adult rats.
We studied the expression of whole protein substrates of Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) in the forebrain of neonate and adult rats. Protein substrates were determined by phosphorylation of the soluble and particulate fractions by CaM kinase II with [gamma-33P]ATP. Phosphorylated proteins were analyzed by SDS-PAGE and two-dimensional gel electrophoresis. More than 50 endogenous proteins were found to be phosphorylated by CaM kinase II in both soluble and particulate fractions. The expression of about 15 protein substrates increased in the particulate fraction from neonate to adult rats, and that of several proteins also changed in the soluble fraction. These findings suggest that the expression of protein substrates was regulated during development as well as that of CaM kinase II itself.
Sugiura
H
H
Department of Cell Biology, Tokyo Metropolitan Institute for Neuroscience, Japan.
Yamauchi
T
T
D000375:Aging / Q000378:metabolism*; D000818:Animals; D000831:Animals, Newborn; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D010766:Phosphorylation; D014176:Protein Biosynthesis; D011506:Proteins / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D013379:Substrate Specificity
D011506:Proteins; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases