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    Home > Biochemistry News > Natural Products News > EMBO J: Researchers find how protein inhibits cancer development

    EMBO J: Researchers find how protein inhibits cancer development

    • Last Update: 2020-06-17
    • Source: Internet
    • Author: User
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    , June 6, 2020 /PRNewswire/ --BiovalleyBIOON/-- Proteins are present in our cells and regulate biological processes that are critical to survivalBut some of them also regulate the process that can make us sickNow, an international team of researchers from researchers from the University of Copenhagen has gained a deeper understanding of one of the proteinsin a new study, researchers have found how the protein PP2A works at the molecular level and how it inhibits the development oftumorin miceThe new findings have been published in the scientific journal EMBO Journal"," we call PP2A the butler protein, because it is almost ubiquitous and exists in all living things, from simpleyeastcells to complex cells in humansPP2A removes phosphate groups from other proteins, and now we've discovered these proteins and how PP2A inhibits cancer development through one of these proteins," said Jakob Nilsson, a professor at the Novo Nordisk Foundation's Protein Research Centerphoto source: The University of Copenhagen
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    According to researchers, both academia and the pharmaceutical industry are very interested in pp2A proteins, as pp2A is known to inhibit tumors in a so-calledtumor inhibitor But it is still unclear which proteins PP2A regulates to suppress cancer Now, researchers have a deeper understanding of this " The new finding in our study is that we show how PP2A chooses the phosphate base that should be removed from other proteins." At the same time, we found that PP2A shuts down an enzyme called ADAM17 Marie Kveiborg, an associate professor at the Center for Biotechnology Research and Innovation, explains researchers used advanced methods to demonstrate that PP2A can shut down the activity of ADAM17 outside the cell by removing the phosphoric acid group located in the ADAM17 part inside the cell function is inhibited
    under normal circumstances, ADAM17 is located in the outer membrane of the cell and, like a molecular scissors, splits other proteins from the cell surface -- for example, growth factors that stimulate cell growth But when PP2A removes the phosphate from ADAM17, this function stops researchers have learned from previous studies that ADAM17 stimulates a variety of cancers, including breast and bowel cancer But this is the first time that PP2A has been shown to actively shut down ADAM17 activities next, the researchers hope their new cancer discovery will also apply to human tumors Now, the researchers' next step is to figure out whether the activity of ADAM17 can be regulated with substances that activate PP2A In addition, the researchers wanted to study how PP2A regulates other proteins, which may be important for understanding their tumor inhibition ( References: Researchers Discover How Protein Camp Apr cancer development in mice Thomas Kruse et al, Mechanisms of the site-specific dephosphorylation and kinase opposition by PP2A a regulatory sios , the EMBO Journal (2020) DOI: 10.15252/embj.2019103695
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