GSK3beta (Phospho-Ser9) and total GSK3beta ELISA Kit (DEIA3523V2)

Regulatory status: For research use only, not for use in diagnostic procedures.

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cell lysates
Species Reactivity
Human, Mouse and Rat
Intended Use
GSK3beta (Phospho-Ser9) and total GSK3beta ELISA Kit is a very rapid, convenient and sensitive assay kit that can monitor the activation or function of important biological pathways in Human, Mouse and Rat cell lysates. By determining phosphorylated GSK-3 beta protein in your experimental model system, you can verify pathway activation in your cell lysates.
The entire kit may be stored at -20°C for up to 6 months from the date of shipment. Avoid repeated freeze-thaw cycles. For extended storage, it is recommended to store at -80°C.
General Description
Glycogen synthase kinase 3β (GSK-3β) is a unique serine/threonine kinase that is inactivated by phosphorylation. In response to insulin binding, PKB/Akt phosphorylates GSK-3β on serine, which prevents GSK-3β from phosphorylating glycogen synthase. Unphosphorylated glycogen synthase is active and able to synthesize glycogen. GSK-3β is also unique in that it requires a substrate that has been phosphorylated by a distinct kinase before it can phosphorylate the substrate. This phosphate priming mechanism explains why phosphorylation of serine 9 inactivates GSK-3β. The phosphorylated serine binds to the GSK-3β priming phosphate position and prevents binding of alternative substrates 3. In addition to insulin signaling, GSK-3β participates in the Wnt signaling pathway, where it forms a complex with axin, β-catenin and adenomatous polyposis coli (APC) protein. In the presence of Wnts, GSK-3β is unable to phosphorylate β-catenin, which leads to stabilization of β-catenin. The Wnt pathway inactivates GSK-3β via the proteins, Dishevelled and FRAT, which disrupt the interaction of GSK-3β with axin, β-catenin, and APC. Clinically, there is considerable interest in GSK-3β inhibitors because they may mimic the effect of insulin or reduce the hyperphosphorylation of Tau that is observed in Alzheimer's Disease.


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The Phosphatidyl Inositol 3 Kinase-Glycogen Synthase Kinase 3 beta Pathway Mediates Bilobalide-Induced Reduction in Amyloid beta-Peptide


Authors: Shi, Chun; Zheng, Dong-dan; Wu, Feng-ming; Liu, Jun; Xu, Jie

Bilobalide (BB), a sesquiterpenoid extract of Ginkgo biloba leaves, has been demonstrated to have neuroprotective effects. The neuroprotective mechanisms were suggested to be associated with modulation of intracellular signaling cascades such as the phosphatidyl inositol 3-kinase (PI3K) pathway. Since some members of intracellular signalling pathways such as PI3K have been demonstrated to be involved in amyloid precursor protein (APP) processing, the present study investigated whether BB has an influence on the beta-secretase-mediated APP cleavage via PI3K-dependent pathway. Using HT22 cells and SAMP8 mice (a senescence-accelerated strain of mice), this study showed that BB treatment reduced generation of two beta-secretase cleavage products of APP, the amyloid beta-peptide (A beta) and soluble APP beta (sAPP beta), via PI3K-dependent pathway. Additionally, glycogen synthase kinase 3 beta (GSK3 beta) signaling might be involved in BB-induced A beta reduction as a downstream target of the activated PI3K pathway. BB showed no significant effects on beta-site APP cleaving enzyme 1 (BACE-1) or gamma-secretase but inhibited the beta-secretase activity of another protease cathepsin B, suggesting that BB-induced A beta reduction was probably mediated through modulation of cathepsin B rather than BACE-1. Similarly, inhibition of GSK3b did not affect BACE-1 activity but decreased cathepsin B activity, suggesting that the PI3K-GSK3 beta pathway was probably involved in BB-induced A beta reduction. Increasing evidence suggests that decreasing A beta production in the brain via modulation of APP metabolism should be beneficial for the prevention and treatment of Alzheimer's disease (AD). BB may offer such an approach to combat AD.

Mcl-1 Degradation Is Required for Targeted Therapeutics to Eradicate Colon Cancer Cells


Authors: Tong, Jingshan; Wang, Peng; Tan, Shuai; Chen, Dongshi; Nikolovska-Coleska, Zaneta; Zou, Fangdong; Yu, Jian; Zhang, Lin

The Bcl-2 family protein Mcl-1 is often degraded in cancer cells subjected to effective therapeutic treatment, and defective Mcl-1 degradation has been associated with intrinsic and acquired drug resistance. However, a causal relationship between Mcl-1 degradation and anticancer drug responses has not been directly established, especially in solid tumor cells where Mcl-1 inhibition alone is insufficient to trigger cell death. In this study, we present evidence that Mcl-1 participates directly in determining effective therapeutic responses in colon cancer cells. In this setting, Mcl-1 degradation was induced by a variety of multikinase inhibitor drugs, where it relied upon GSK3b phosphorylation and FBW7-dependent ubiquitination. Specific blockade by genetic knock-in (KI) abolished apoptotic responses and conferred resistance to kinase inhibitors. Mcl-1-KI also suppressed the antiangiogenic and anti-hypoxic effects of kinase inhibitors in the tumor microenvironment. Interestingly, these same inhibitors also induced the BH3-only Bcl-2 family protein PUMA, which is required for apoptosis. Degradation-resistant Mcl-1 bound and sequestered PUMA from other prosurvival proteins to maintain cell survival, which was abolished by small-molecule Mcl1 inhibitors. Our findings establish a pivotal role for Mcl-1 degradation in the response of colon cancer cells to targeted therapeutics, and they provide a useful rational platform to develop Mcl-1-targeting agents that can overcome drug resistance. (C) 2017 AACR.

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