Protein kinase C and its endogenous substrate proteins in isolated cow liver parenchymal cells.
Protein kinase C activity was evaluated and its endogenous substrate proteins were explored in isolated cow liver parenchymal cells. Protein kinase C activity was detected in both cytosolic and total particulate fractions of the cells. At least four proteins in cytosolic and seven proteins in total particulate fractions were found to be substrates for protein kinase C. These results suggested that protein kinase C-catalyzed protein phosphorylation was involved in the regulation of functions of cow liver parenchymal cells.
Katoh
N
N
National Institute of Animal Health, Hokkaido Branch Laboratory, Sapporo, Japan.
Miyamoto
T
T
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001345:Autoradiography; D002417:Cattle; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007774:Lactation; D008099:Liver / Q000166:cytology / Q000201:enzymology*; D008970:Molecular Weight; D010750:Phosphoproteins / Q000302:isolation & purification / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D011493:Protein Kinase C / Q000378:metabolism*; D013379:Substrate Specificity
D010750:Phosphoproteins; D010761:Phosphorus Radioisotopes; D000255:Adenosine Triphosphate; D011493:Protein Kinase C