Scientists resolve new-found way of cell apoptosis

Researchers from St. Jude Children's Research Hospital revealed a new way of mitochondrial cell death, which is associated with the BOK protein. The study found that it is possible to induce the development of new ways to trigger cell death in certain types of cancer cells. Related papers were published online in the journal Cell.

Corresponding author of the paper, the director of St. Jude Children's Research Hospital Immunology Department Doug Green said, "newly-discovered mechanism of cell death of mitochondria is mediated by the effector BOK protein. BOK protein usually suffers from destruction pointedly in the endoplasmic reticulum. This molecular event signaling pathway seems to be intrinsically linked with pressure level the cells feel, ensuring the programmatically rapid destruction of cells and its contents."

Cell death is a kind of mechanism used by multicellular organisms to remove the cells with infection, damage or cells which are unnecessary to help them survive. Mitochondria are known as cellular capacity organelles. But they also activate cell death under certain conditions, helping the body remove damaged cells.

Mitochondrial cell death pathway (apoptosis) is obtained from the mitochondrial outer membrane permeabilization and is full of holes. Then cytochrome c protein and other molecules leak into the cytoplasm from a class gap between the inner and outer membranes of mitochondria, activating caspase proteases to initiate a series of reactions which leads to rapid cell death.

The first author of the paper, Fabien Llambi at St. Jude Children's Research Hospital said, "BOK is a effector protein of mitochondrial apoptotic, but it seems to pay its role in a different way with some known proteins which start the mitochondrial cell death. The stability of BOK protein is directly related to the amount of cell pressure felt in endoplasmic reticulum."

The researchers revealed that element in Endoplasmic reticulum associated protein degradation (ERAD) signaling pathway controls the stability of BOK protein. ERAD is a quality control mechanism which helps to detect proteins which are damaged and unfolded.

The scientists also confirmed that BOK is independent of the other two members of the BCL-2 protein family: BAK and BAX play. BCL-2 family of proteins and contribute to the regulation of mitochondrial cell death.

Green said, "The pressure signaling pathway in the process of cell fate seems to trigger some of the mitochondrial cell death, such as the BOK signal pathway we found intricately linked our research also showed that cancer cells expressing high levels of BOK possible. For targeting the proteasome or ERAD signaling pathway inhibitors are especially sensitive."

ERAD developed targeting signaling pathway specific inhibitor may become known to be useful alternatives to terminate cancer cell growth inhibitor of the proteasome. Some proteasome inhibitors can affect multiple targets, cannot achieve the desired level of specificity. ERAD inhibitors may be able to overcome this shortcoming. But further work identified easily controlled by such interference, the appropriate target protein.

The main research interest of Dr. Doug Green is a central mechanism of apoptosis of cancer and immune system, in recent years, in Science, Nature, and Cell published a number of important research results. April 2009, he was the first to reveal the P53 protein in the cytoplasm of the mode of action in the journal Nature. In March 2012, he resolved release of cytochrome C which is related to cell apoptosis in the journal Cell, providing important information for revealing the secret of cell apoptosis. In July 2015, he revealed the tumor suppressor P53 can trigger apoptosis in the cytoplasm through a new mechanism. Research papers were published in the journal Molecular Cell.

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