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August 15, 2020 // -- Many types of human cancers exhibit changes in the balance of kinases and phosphatases, and drugs that inhibit kinase activity are now clinically successfully used as cancer therapies, but phosphatase remains a largely under-developed target because researchers do not know how the absence of phosphatase induces human disease.
a recent study published in the international journal Proceedings of the National Academy of Sciences found that a new phosphatase cascade system may play a key role in a variety of human cancers, including pancreatic, liver and lung cancer.
photo source: Pixabay/CC0 Public Domain, the researchers point out that a carcinogenic phosphatase called PRL2 may be able to exert its effects by lowering the expression of PTEN, a tumor that is frequently missing in human cancer; 2 or is expected to be a target for a new type of cancer drug, and researchers were more effective at suppressing PRL2 phosphatase and restoring PTEN levels to inhibit tumor formation than kinases in the targeted PI3K-AKT pathline, which often limits the effectiveness of therapy due to targeted and off-target side effects.
When phosphatase removes phosphate groups, kinases can add phosphate groups to proteins, and they can potentially alter the protein's function in a way that promotes cell carcinoma, and now researchers have found that PRL2 removes phosphate groups from 336 Tyrosine points of PTEN, and when the process occurs, PTEN is ubiquitinized or essentially labeled to degrade, reducing its level and resistance to cancer progression.
researchers found that high levels of PRL2 expression were often directly associated with lower levels of PTEN, while also reducing overall survival rates in patients with multiple human cancers, and when PRL2 was removed from the mouse model with cancer-prone and missing PTEN, PTEN levels returned to normal and cancer progression stopped. 'This study sheds light on the molecular mechanisms of PRL2-induced cancer, and we also confirm that PRL2 is promising to act as a potential target for PTEN recovery therapy,' said Zhang, a researcher at
.
Previously, researchers have developed a new method that promises to inhibit PRL2, which functions like a trijudome; researchers have found that molecules called Cmdp-43 can interfere with PRL2 aggregation, and based on the findings of this paper, researchers are now conducting more in-depth research to develop new targeted therapies that promise to treat multiple human cancers in the future.
() Original source: Ings Li, Yunpeng Bai, L. Tiffany Lyle, et al. Mechanism of PRL2 phosphatase-mediated PTEN down and tumorigenesis, Proceedings of the National Academy of Sciences (2020). DOI:10.1073/pnas.2002964117.