New target for cancer potential - PRL2.

Text . . . Many types of human tumors show changes in the balance of protein kinases and phosphatases.
the drug that inhibits kinase activity has been a successful anti-cancer therapy in clinical practice, but targets such as phosphatase are still largely underutilized, mainly because of the lack of understanding of the mechanism of phosphatase-causing diseases.
August 11, PNAS released the latest developments in a team of Professor Zhong-Yin Zhang at Purdue University who have discovered a new phosphatase cascading reaction that plays a key role in pancreatic, liver, kidney, lung, breast, prostate, brain and many other types of cancer.
results show that phosphatase PRL2 plays a cancer-promoting role by lowering PTEN.
photo source: PNAS kinases attach phosphate groups to proteins, while phosphatases are responsible for dephosphate of proteins, both of which can cause cell carcinoma to change proteins.
has found that phosphatase PRL over-expression is highly carcinogenic, and PTEN is the second most incarceration tumor inhibitor in human cancer, after p53.
in the study, researchers found that PRL2 dephosphates PTEN's Tyr336 (Tyrosine), which causes PTEN ubibin to be "labeled" for degradation, reducing PTEN levels and the ability to fight cancer progression.
PRL2 dephosphates PTEN's Tyr336 to promote PTEN polypronination (Photo: PNAS) and when PRL2 is removed from the cancer-prone, PTEN-defective mouse model, PTEN levels return to normal and tumors stop growing.
searching the database, the researchers also found that high expression of PRL2 in human tumors was associated with low levels of PTEN, and that high levels of PRL2 also reduced the survival rate of the entire group of patients with several human malignancies.
RL2 expression in human tumors is negatively associated with PTEN levels (Photo: PNAS)" This result suggests that PRL2 may be a drug target for cancer, and restoring PTEN levels by inhibiting PRL2 phosphatase is a possible way to inhibit tumor formation.
even more exciting is that the discovery could affect a variety of cancers.
, " said Professor Zhang.
Professor Zhang's lab has previously found an effective way to suppress PRL2, and they are continuing to develop the drug.
reference: 1 . . . . . . . . . . . . . . . . . . . . . . . . . . . . Mechanism of PRL2 phosphatase-mediated PTEN pring and tumorigenesis. Proceedings of the National Academy of Sciences (2020) 2 s scientists identify new target for wide array of cancers (Source: Medical Xpress)