Background[1-3]
Phosphatase-2AC antibody is a type of polyclonal antibody that can specifically bind to phosphatase-2AC protein. It is mainly used for in vitro immunological detection of phosphatase-2AC protein.
Polyclonal antibodies are a group of immunoglobulins secreted by plasma cells of the organism that are stimulated by heterologous antigens (macromolecule antigens, hapten conjugates) to produce an immune response. Polyclonal antibodies are widely used in research and diagnosis because they can recognize multiple epitopes, can cause precipitation reactions, have short preparation time, and are low cost.
Phosphatase-2AC
Phosphatase usually refers to the general name of enzymes that catalyze the hydrolysis of orthophosphate compounds, or the general name of enzymes that hydrolyze phosphate and polyphosphate compounds.
Phosphatase is an enzyme that dephosphorylates the corresponding substrate, that is, it removes the phosphate group on the substrate molecule by hydrolyzing phosphate monoesters and generates phosphate ions and free hydroxyl groups. The role of phosphatase is the opposite of that of kinase. Kinase is a phosphorylase that can use energy molecules, such as ATP, to add phosphate groups to corresponding substrate molecules. One phosphatase that is ubiquitous in many organisms is alkaline phosphatase.
The phosphorylation effect of phosphatase is opposite to that of kinase or phosphorylase. Phosphorylation can activate or inactivate an enzyme (e.g., kinase signaling pathway), or it can cause a protein-protein interaction to occur (e.g., SH3 domain); therefore, phosphatases are a component of many signal transduction pathways that control phosphorylation required. It is worth mentioning that phosphorylation or dephosphorylation does not necessarily correspond to enzyme activation or inhibition, and some enzymes have multiple phosphorylation sites involved in the regulation of activation or inhibition.
Apply[4][5]
For research on the regulation of protein phosphatase 2A by zinc ions and its role in Alzheimer’s disease
Elucidate whether zinc ions promote abnormal hyperphosphorylation of tau protein and regulate PP2A activity by regulating PP2A activity.
Methods: Experiments were performed at whole-body and cellular levels. At the overall level, male SD rats were used, and zinc sulfate was injected into the lateral ventricle. The groups were as follows: saline control group, 30mM zinc sulfate administration group, 30mM zinc sulfate administration + intraperitoneal injection of zinc ion specific chelator CQ group.
Six days after injection into the lateral ventricle, the brain was anesthetized and the hippocampal tissue homogenate was isolated. Nanya epoxy resin was used to detect changes in tau phosphorylation levels and changes in PP2Ac Y307 phosphorylation levels by immunoblotting to detect the activity of PP2A; at the cellular level The mouse neuroblastoma N2a cell line was used, treated with 100 μM zinc sulfate for 3 hours, and then the protein was extracted. The PP2Ac Y307 phosphorylation and tau phosphorylation levels were detected in the same way.
At the same time, PP2 or DES was preincubated at the cellular level for 30 minutes or transfected with wild-type PP2A and mutant PP2A. After treatment with 100 μM zinc sulfate for 3 hours, the protein was extracted. The PP2Ac phosphorylation and tau phosphorylation levels were detected in the same way.
At the level of transgenic animals, transgenic mice transformed with human tau were used and the zinc ion chelator CQ was administered intragastrically for 35 days to detect the changes in PP2Ac phosphorylation and tau phosphorylation levels as well as soluble tau and insoluble tau.
Results: Zinc ions were directly injected into the lateral ventricle of whole animals. After 6 days, the phosphorylation level of PP2Ac Y307 in the hippocampus was significantly increased. Along with the decrease in PP2A activity, tau protein phosphorylated at multiple serine/threonine sites such as Ser214, Thr205, and Ser396. , Ser404 is hyperphosphorylated; intraperitoneal injection of zinc ion chelator CQ into animals at the same time can partially reverse the inhibition of PP2Ac Y307 phosphorylation level and PP2A activity.
Treatment of mouse neuroblastoma N2a cells with zinc sulfate also led to tyrosine phosphorylation modification and decreased activity of PP2Ac. The tau protein was hyperphosphorylated at multiple sites, accompanied by the inactivation of Src phosphorylation site tyrosine. The phosphorylation level of amino acid 529 (Tyr529) is reduced and Src is activated.
Administration of zinc together with PP2A agonists or overexpression of wild-type PP2A can reverse the zinc-induced decrease in PP2Ac activity and hyperphosphorylation of tau protein. Administration of PP2, a specific inhibitor of the Src family, can also partially reverse the inhibition of PP2Ac Y307 phosphorylation and PP2A activity as well as the phosphorylation of tau protein.
