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Hopkins researchers discover genetic switch that turns off an oxygen-poor cell's combustion engine

hypoxia, the mitochondrion produces reactive oxygen species that threaten the life of the cell.

"But our discovery clearly shows that hypoxia doesn't simply trigger a passive shutdown of the mitochondrion," said Dang. "Instead, HIF-1 acts as a genetic switch to actively shut down mitochondrial function and prevent the production of reactive oxygen species."

The Hopkins team demonstrated that HIF-1 shuts down the TCA cycle by preventing an enzyme called PDH from converting pyruvate made by glycolysis into acetyl CoA. Specifically, HIF-1 blocks the ability of PDH to make this conversion. HIF-1 does this by activating a protein called PDK, which binds to PDH and prevents it from performing this critical task. This starves the TCA cycle of acetyl CoA and shuts it down.

The Hopkins researchers made their discovery using mouse embryo fibroblast (MEF) cells that were genetically altered to lack HIF-1. When the investigators exposed these so-called HIF-1 null MEFs to hypoxic conditions, the cells were unable to activate PDK to block mitochondrial function. This showed that HIF-1 is required to activate PDK.

The team then genetically engineered HIF-1 null MEFs and forced PDK to work-even in the absence of the HIF-1 gene. The hypoxic cells once again accelerated glycolysis and produced increased amounts of ATP; and with the PDK forced to work, the cells were also able to shut down the TCA cycle. This showed that PDK is the protein activated by HIF-1 to prevent the mitochondrion from producing ROS.

The other authors of this paper include Jung-whan Kim, Irina Tchernyshyov and Gregg L. Semenza, who discovered HIF-1 a decade ago.


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Source:Johns Hopkins Medical Institutions


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