Stimulation of FA and phosphatase‐1 activities by insulin in 3T3‐L1 cells
- 4 December 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 258 (2), 208-210
- https://doi.org/10.1016/0014-5793(89)81654-0
Abstract
The phosphatase-1 activator FA and phosphatase-1 were assayed in 3T3-L1 cells exposed to insulin. The cytosolic FA activity was transiently stimulated (7-8-fold) 1 and 2 min after exposure to 10−8 M insulin and returned to control values within 5–10 min. Cytosolic phosphatase-1 (assayed after trypsin treatment) was activated (120–140% of controls) between 2 and 5 min and returned to control values within 10 min. Insulin effects were dose-dependent, with maximum stimulation of both activities at 10−8 M insulin. The possibility that FA and other kinases mediate phosphatase activation by insulin is discussed.Keywords
This publication has 13 references indexed in Scilit:
- THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASESAnnual Review of Biochemistry, 1989
- Insulin-like growth factor I and insulin rapidly increase casein kinase II activity in BALB/c 3T3 fibroblasts.Journal of Biological Chemistry, 1988
- Stimulation of protein phosphatase activity by insulin and growth factors in 3T3 cells.Proceedings of the National Academy of Sciences, 1988
- Differential regulation of S6 phosphorylation by insulin and epidermal growth factor in Swiss mouse 3T3 cells: insulin activation of type 1 phosphatase.Proceedings of the National Academy of Sciences, 1988
- Insulin induces activation and translocation of protein kinase FA (a multifunctional protein phosphatase activator) in human plateletBiochemical and Biophysical Research Communications, 1988
- Activation of casein kinase II in response to insulin and to epidermal growth factor.Proceedings of the National Academy of Sciences, 1987
- Induction of casein kinase II during differentiation of 3T3-L1 cells.Journal of Biological Chemistry, 1987
- Subunit Structure and Regulation of Phosphorylase PhosphataseCurrent Topics in Cellular Regulation, 1985
- Synergistic phosphorylation and activation of ATP-Mg-dependent phosphoprotein phosphatase by F A/GSK-3 and casein kinase II (PC0.7).Journal of Biological Chemistry, 1984
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976