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INS — PPP2CA

Text-mined interactions from Literome

Müller et al., Biochemistry 2000 : PP2A was activated about 2-fold by insulin in spheroplasts and in intact cells, whereas the fraction of active PKA was significantly reduced in a cAMP independent manner as well as through a subsequent up to 3-fold increase in particulate cAMP-PDE activity accompanied by a 50 % decrease in cytosolic cAMP levels
Ugi et al., Mol Cell Biol 2002 : Insulin , IGF-1, and EGF stimulation also inhibited PP2A activity
Højlund et al., Eur J Clin Invest 2002 (Diabetes Mellitus, Type 2...) : This study was carried out to investigate the effect of insulin on PP2A expression in skeletal muscles of type 2 diabetic and control subjects ... Insulin down-regulated PP2A-C alpha expression in skeletal muscle of the control subjects ( P < 0.05 ) but not in the type 2 diabetic subjects
Palanivel et al., Am J Physiol Endocrinol Metab 2004 : More recent studies have suggested direct inhibitory effects of glucose metabolites on PP2A activity in isolated beta-cells, implying that inhibition of PP2A leads to stimulation of insulin secretion
Yang et al., Atherosclerosis 2008 : We wished to see whether insulin stimulated cGMP stimulates protein phosphatase-2A (PP-2A) thereby inhibiting autonomous CaM kinase II and migration, and whether insulin , in the presence of Ang II, inhibits PP-2A and stimulates autonomous CaM kinase II in a NAD ( P ) H oxidase dependent manner ... Insulin plus Ang II inhibited PP-2A activity by 57+/-7 % ( P < 0.05 ) and stimulated autonomous CaM kinase II activity by 120+/-14 % ( P < 0.05 ), both by an apocynin-sensitive pathway ... It is concluded that insulin in the presence of NO stimulates cGMP which stimulates PP-2A activity causing inhibition of autonomous CaM kinase II activity and thus VSMC migration, and that insulin in the presence of Ang II inhibits PP-2A and stimulates autonomous CaM kinase II activities by a NAD ( P ) H oxidase dependent mechanism which are associated with insulin stimulated NAD ( P ) H oxidase dependent migration
Reusch et al., Endocrinology 1995 : Insulin inhibited nuclear PP-2A activity and enhanced cAMP response element binding protein phosphorylation in HIRc cells, but not in delta CT cells ... The delta CT cells exhibited normal ras activation and blunted mitogen activating protein kinase phosphorylation and activation in response to insulin ( 16-fold in HIRc cells vs. 3-fold in delta CT cells ), indicating that the mitogen activating protein kinase pathway is important for the regulation of nuclear PP-2A activity by insulin ... We conclude that insulin inhibits nuclear PP-2A activity, and that the carboxy-terminal domain of the insulin receptor is important for this effect
Reusch et al., Endocrinology 1994 : Using in vitro protein kinase-A phosphorylated activating transcription factor-1 as a substrate, we found that insulin inhibited nuclear PP-2A activity by 80 % ( P < 0.001 ), which represents approximately 50 % of the total nuclear phosphatase activity
Begum et al., Endocrinology 1996 : As reported by us earlier ( Srinivasan, M., and N. Begum, J Biol Chem 269 : 16662-16667, 1994 ), insulin rapidly stimulated PP-1 and concomitantly inhibited PP-2A activities in L6 cells
Begum et al., Eur J Biochem 1996 : As reported by us earlier, insulin rapidly stimulated PP-1 and concomitantly inhibited PP-2A activities in control cells