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PP2A Calpha in osteoblasts was also potentially involved in controlling adipocyte differentiation through a paracrine mechanism.
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these data demonstrate that phosphatase PP2A is essential for TH17 differentiation and that inhibition of PP2A could be a possible therapeutic approach to controlling TH17-driven autoimmune diseases.
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miR-203-3p target Ppp2ca aggravates status epilepticus model in mice.
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Data (including data from studies in knockout/transgenic mice) suggest Ppp2ca supports cortical neuronal growth and cognitive function via regulating p73/Gls2 signal transduction in neurons of hippocampus. Ppp2ca gene knock-out results in embryonic cortical atrophy with learning/memory deficits. (Ppp2ca = protein phosphatase 2a catalytic subunit alpha isoform; p73 = transformation related protein 73; Gls2 = glutaminase-2)
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Results indicate that Dlx5 and Runx2 are critical factors for the upregulated Osterix expression in shPP2A cells, which is considered to be important for the accelerated osteoblast differentiation in these cells.
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Data (including data from studies in transgenic mice) suggest that Esr1 signaling promotes activation of Pp2a; here, central activation of Pp2a during estrogen replacement therapy is involved in prevention of menopause-induced obesity and glucose intolerance (that is, induced by lack of membrane-initiated Esr1 signaling). (Esr1 = estrogen receptor 1; Pp2a = protein phosphatase 2A)
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The data also suggest that H2A.Z restricts transcription, which is moderated by ANP32e at the promoter and gene bodies of expressed genes. Thus, ANP32e, through inhibition of PP2A, is required for nucleosomal inclusion of H2A.Z and the regulation of gene expression
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PP2A is a target of piperine, which induces autophagy in a rotenone-induced Parkinson's disease model
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In vitro, SCF induced the phosphorylation of p38 MAPK and cofilin, leading to the migration of cardiac stem cells.
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We describe a novel mechanism of signal transduction enriched in medium spiny neurons of striatum that likely mediates effects of the neurotransmitter dopamine acting on these cells. We find that the protein ARPP-16, which is highly expressed in striatal medium spiny neurons, acts as a selective inhibitor of certain forms of the serine/threonine protein phosphatase, PP2A, when phosphorylated by the kinase, MAST3.
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data show that Fyn kinase is activated after TLR4 triggering and exerts an important negative control on LPS-dependent TNF production in mast cells controlling the inactivation of PP2Ac and activation of PKCalpha/beta necessary for the secretion of TNF by VAMP3(+) carriers
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endogenous siRNA (PTEN-sh-3p21) cleaved from PTEN-sh within PTEN mRNA 3'UTR modulates PPP2CA and PTEN at the post-transcriptional level in liver cells
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PP2A activation both limited and prevented inflammation and tissue injury in two direct injury models of Acute respiratory distress syndrome.
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critical role in the proliferation and metastasis of osteosarcoma cells
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PP2A regulates kinetochore-microtubule attachment during meiosis I in oocyte.
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Study demonstrates that PPP2Ac-alpha plays important roles in both hair follicle and skin development.
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these results suggest that inhibiting PP2Ac nitration using a mimic peptide is a potential preventive strategy for Endothelial-to-mesenchymal transition in renal fibrosis
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Data suggest a critical role for the I2PP2A protein (SET)-protein phosphatase-2A (PP2A) signaling axis in Pten phosphohydrolase
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that loss of glucocerebrosidase function may contribute to SNCA accumulation through inhibition of autophagy via PPP2A inactivation
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Data indicate that protein phosphatase PP2A is required for the function of T(reg) cells and the prevention of autoimmunity.
