PP2A-γ Inhibitors

Okadaic Acid is a potent inhibitor of protein phosphatases PP1 and PP2A. Inhibition of PP2A by Okadaic Acid can lead to increased phosphorylation levels of various substrates, which can functionally inhibit PP2A-γ by preventing it from dephosphorylating its specific substrates within its signaling pathways.

Cantharidin inhibits protein phosphatases PP1 and PP2A. By inhibiting PP2A-γ, Cantharidin increases the phosphorylation status of proteins, which disrupts the normal function of PP2A-γ as a serine/threonine phosphatase in cellular signaling.

Endothall acts as an inhibitor of protein phosphatases PP1 and PP2A. It inhibits the activity of PP2A-γ by preventing the dephosphorylation of proteins within signaling pathways where PP2A-γ is an active component, thereby causing functional inhibition of PP2A-γ.

Calyculin A, like Okadaic Acid, is a potent inhibitor of PP1 and PP2A. It inhibits PP2A-γ by stabilizing the phosphorylated state of proteins, which impedes the phosphatase activity of PP2A-γ, leading to functional inhibition within its action spectrum in the cell.

Fostriecin selectively inhibits PP2A over PP1. This selective inhibition leads to reduced activity of PP2A-γ, which results in an increased phosphorylation state of proteins that are normally regulated by PP2A-γ, functionally inhibiting its role in dephosphorylation processes.

LB-100 is a small molecule inhibitor of protein phosphatases PP2A. It inhibits PP2A-γ by reducing its ability to dephosphorylate its substrates, which leads to a functional inhibition of PP2A-γ in its relevant signaling pathways.

Cerulenin is an inhibitor of fatty acid synthase which indirectly affects the function of enzymes like PP2A-γ by altering lipid metabolism and membrane composition, potentially disrupting PP2A-γ interactions and its associated signaling pathways, leading to functional inhibition.

Bisindolylmaleimide I acts as a protein kinase C inhibitor. By inhibiting PKC, it can indirectly lead to the functional inhibition of PP2A-γ by disrupting downstream signaling pathways where the balance between phosphorylation by kinases and dephosphorylation by phosphatases like PP2A-γ are critical.

Ionomycin is a calcium ionophore that raises intracellular calcium levels. Elevated calcium can activate calmodulin-dependent protein kinases, which can then enhance the phosphorylation of proteins that are substrates for PP2A-γ, leading to the functional inhibition of PP2A-γ due to the increased phosphorylation state of these proteins.