Dopamine and cyclic-AMP activated Mr32kDa phosphoprotein (DARPP-32) is a central signaling proteins in neurotransmission. Here DARPP-32 phosphorylation by protein kinase A (PKA), DARPP-32 into a powerful protein phosphatase 1 (PP1) inhibitor. DARPP-32 can itself inhibit the following PKA DARPP-32 phosphorylation by cyclin-dependent kinase 5 (Cdk5). Increasing evidence suggests a role for DARPP-32 and signal pathways related to cancer;
However, its role in ovarian cancer remains unclear. Using immunohistochemistry, expression of DARPP-32, PP1 and Cdk5 is determined in a large cohort of primary tumors from ovarian cancer patients (n = 428, 445 and 434 respectively) to evaluate the relationship between clinical outcome and clinicopathological criteria.
Low cytoplasmic and nuclear DARPP-32 expression was associated with a shorter overall patient survival and progression-free survival (P = 0.001, 0.001, 0.004 and 0.037 respectively). Low nuclear and cytoplasmic DARPP-32 expression remained significantly associated with overall survival in multivariate Cox regression (P = 0.045, hazard ratio (HR) = 0.734, 95% confidence interval (CI) = 0.542 to 0.993 and P = 0.001, HR = 0.494, 95% CI = 0.325 to 0.749, respectively).
cytoplasmic and nuclear high PP1 expression was associated with a shorter overall patient survival and expression of cytoplasmic PP1 high with progression-free survival shorter (P = 0.005, 0.033, and 0.037, respectively). Cdk5 high expression was associated with progression-free survival shorter (P = 0.006). These data demonstrate the role of DARPP-32 and related kinase signaling as a prognostic marker in ovarian cancer clinical utility.
Dopamine and cAMP-regulated phosphoprotein 32kDa (DARPP-32), proteinphosphatase–1 and cyclin-dependent kinase 5 expression in ovarian cancer
Protein phosphatase one alpha Increase glucocorticoid receptor activity by a mechanism that involves phosphorylation of serine-2 one one < / em>
By acting as a ligand-dependent transcription factor of the glucocorticoid receptor (GR) mediates the action of glucocorticoids and regulates many physiological processes. A disturbed regulation of glucocorticoid action has been associated with various disorders. Thus, an explanation of the underlying signaling pathway is important for understanding the mechanisms of glucocorticoid impaired function and contribute to disease.
This study found an increase in excess GR transcriptional activity of protein phosphatase 1 alpha (PP1α) in HEK-293 cells and a decrease in the expression levels of GR-responsive gene knockdown following PP1α model A549 cells endogenously. Mechanistic investigations revealed reduce GR-Ser211 phosphorylation following PP1α silencing and provide the first indication of the involvement of glycogen synthase kinase 3 (GSK-3).
Thus, this study identified PP1α as a novel post-translational activator of GR signaling, indicating that PP1α function disorders can lead to disorders glucocorticoid action and thereby contribute to diseases.Ewing sarcoma (ES) is a pediatric malignant bone and soft tissue tumors. Patients with metastatic ES have dismal outcomes were not improved in decades. The major challenge in the treatment of metastatic ES is the lack of specific targets and rational combination therapy.
Description: A polyclonal antibody against PPP1CA. Recognizes PPP1CA from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;WB:1:500-1:2000, IHC:1:50-1:200
Description: A polyclonal antibody against PPP1CA. Recognizes PPP1CA from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;WB:1:500-1:2000, IHC:1:50-1:200
Description: A polyclonal antibody against PPP1CA. Recognizes PPP1CA from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC, IF; Recommended dilution: IHC:1:20-1:200, IF:1:50-1:200
Description: A polyclonal antibody against PPP1CA. Recognizes PPP1CA from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: WB, IHC, ELISA;WB:1/500-1/2000.IHC:1/100-1/300.ELISA:1/5000
We recently discovered a protein phosphatase 1 regulatory subunit 1A (PPP1R1A) specifically highly expressed in ES and promote tumor growth and metastasis in ES. In the current investigation, we showed that PPP1R1A regulate ES cell growth cycle at the G1 / S phase to down-regulate the cell cycle inhibitor p21Cip1 and p27KIP1, which leads to retinoblastoma (Rb) protein hyperphosphorylation. In addition, we show that the normal transcription PPP1R1A promotes histone genes during cell cycle progression.
