New target for cancer-fighting potential - PRL2.

Many types of human tumors exhibit changes in the balance of protein kinase and phosphatase.
drugs that inhibit kinase activity have been a successful anti-cancer therapy clinically, but targets such as phosphatase are still largely underutilized, mainly because of the current lack of understanding of the mechanism of phosphatase-causing diseases.
August 11th, PNAS published the latest developments from Purdue University's team of Professor Zhong-Yin Zhang, who 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.
source: PNAS kinases attach phosphate groups to proteins, while phosphatases are responsible for protein dephosphatification, both of which can cause cell carcinoma to cause protein changes.
studies have found that phosphatase PRL over-expression is highly carcinogenic, and PTEN is the second most insemination tumor inhibitor in human cancer, after p53.
in the study, researchers found that PRL2 dephosphates PTEN's Tyr336 (tyrosine), which causes PTEN to become generic and be labeled as degraded, reducing PTEN levels and resistance to cancer progression.
PRL2 dephosphates Tyr336 of PTEN to promote PTEN polyproteinization (Photo source: PNAS) And when PRL2 was removed from the mouse model with cancerous tendencies and PTEN defects, PTEN levels returned to normal and the tumor stopped growing.
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 patients in the whole group of several human malignancies.
PRL2 expression is negatively associated with PTEN levels in human tumors (Photo source: PNAS) "This result suggests that PRL2 may be a drug target for cancer, and that restoring PTEN levels by inhibiting PRL2 phosphatase is a possible way to inhibit tumor formation.
more exciting is that the discovery could affect a variety of cancers.
," professor Zhang said.
Professor Zhang's lab has previously found effective ways to suppress PRL2, and they are continuing to develop the drug.
: 1 s. 1 . . . . . . . . . . . . . . . . . Mechanism of PRL2 phosphatase-mediated PTEN mediated and tumorigenesis. Proceedings of the National Academy of Sciences (2020) 2 s Scientists identify new target for wide array of cancers (Source: Medical Xpress)