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- _4 value "In Rat1, NIH 3T3, and HEK293 cells, increases in the intracellular levels of cAMP stimulate phosphorylation of GSK-3? and -?, as demonstrated by immunoblotting with GSK-3 phosphorylation-specific antibodies. As shown in Fig. 1, the cell-permeable cAMP analogue 8-Br-cAMP induced a marked increase in phosphorylation of GSK-3? and - ? at serine 21 and 9, respectively, whereas the structurally related cGMP analogue 8-Br-cGMP had little effect. Forskolin, which activates adenyl cyclase thus raising intracellular cAMP levels (15), triggered a similar elevation in GSK-3 phosphorylation at serine 21 and 9. In Rat1 cells, isoproterenol, which activates the b-adrenergic receptor stimulating adenylate cyclase and increasing endogenous cAMP levels (16, 17), also efficiently stimulated GSK-3 phosphorylation at these serine sites. In NIH 3T3 cells that contain few of the ?-adrenergic receptors, stimulation with other G-protein-coupled receptor agonists, such as lysophosphatidic acid. also led to GSK-3 phosphorylation (data not shown)" provenance.
- _4 wasQuotedFrom 11035810 provenance.