Cancer cells are cells that have the ability to proliferate indefinitely. Many mutations occur in the genome of cancer cells, resulting in many dysfunctional proteins. Like all other cells, cancer cells need to constantly remove "junk" from the cells in order to survive. Now, biologists at the California Institute of Technology's biology and Ray Deshaies, a researcher at the Howard Hughes Medical School, have developed a new method to inhibit cancer cell clearance, leading to cancer cells that are full of defects. Protein, thus self-destructive.

The study was published in the February 27 issue of the journal Nature Chemical Biology.

The proteasome is a hollow cylindrical structure whose main function is to degrade undesired or defective proteins in cells, which cause the proteins to be degraded, and then the proteins are cleaved into short peptides and excreted extracellularly. When a cell produces a defective protein, it is labeled with at least four small proteins called ubiquitin, forming a "polyubiquitin chain" with the proteasome, bringing the proteasome onto the labeled protein and starting its During the degradation process, the portion of the proteasome called Rpn11 cleaves the ubiquitin chain. This step is necessary because the ubiquitin chain is too large to fit inside the proteasome.

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A new compound developed by the Deshaies team in collaboration with researchers at the University of California, San Diego, inhibits the activity of Rpn11, making it impossible for the proteasome to completely destroy harmful proteins, and the accumulation of these harmful proteins can cause catastrophic stress in cells. Causes cell death.

Although compounds affect the proteasome in all cells, there are fewer proteins with dysfunction in normal cells, so some types of cancer cells are more sensitive to proteasome inhibitors than normal cells, so even small doses of drugs have fatal effects. .

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