Abstract
We have examined the localization of phospholipid/calcium-dependent protein kinase (protein kinase C) in thymoma cells, which were resected from a patient with myasthenia gravis. Upon stimulation with 4 μg/ml of Concanavalin A (Con A) for 30 min, protein kinase C activity in the cytosolic fraction was increased from 7.44 pmol/min per 10 7 cells to 11.42 pmol/min per 10 7 cells. On the other hand, membrane-associated protein kinase C activity was decreased from 1.69 to 0.71 pmol/min per 10 7 cells. On the contrary, 10 −7 mol/l tetradecanoyl phorbol acetate (TPA) decreased cytosolic protein kinase C activity from 9.31 to 8.04 pmol/min per 10 7 cells, while membrane-associated protein kinase C activity was increased from 1.69 to 2.94 pmol/min per 10 7 cells. Several endogenous phosphorylated proteins (mol wt 20000, 23000) were observed as inferred by SDS-polyacrylamide gel electrophoresis. These findings indicated that Con A and TPA produce differential translocation of protein kinase C.
Published Version
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