Professor Hilmar Bading and his team’s research focused on NMDA receptors. This receptor is an ion channel protein, activated by the neurotransmitter glutamate, allowing calcium to flow into the cell. The calcium signal plays a role in the plasticity of synapses, but it also spreads to the nucleus, where it activates a protective genetic program. The NMDA receptors activated by glutamate are located at the junctions of nerve cells and play a key role in the brain, contributing to the learning and memory process and neuroprotection. But the same receptors also exist outside the synapse. These additional synaptic NMDA receptors pose a threat because their activation can cause cell death. However, under normal circumstances, an effective cellular uptake system of glutamate ensures that these receptors are not activated, and nerve cells therefore remain intact.
But when diseases occur, for example, if certain parts of the brain cannot get enough oxygen after a stroke, the interruption of blood circulation can destroy the glutamate intake system. The level of extra-synaptic glutamate increases, thereby activating the extra-synaptic NMDA receptors. The result is nerve cell damage and death, accompanied by brain function limitations. “The increase in extra-synaptic glutamate levels does not only occur during circulatory disorders in the brain,” Professor Bading explained. “Evidence shows that the toxic properties of extra synaptic NMDA receptors play an important role in many neurodegenerative diseases.” According to the scientist, this situation is in Alzheimer’s disease and amyotrophic lateral sclerosis. It is very common even after infection with viruses or parasites.
When glutamate activates NMDA receptors in neuronal junctions, they help to build a protective barrier, and outside the synapse, NMDA receptors form a “death complex” with another ion channel protein. This protein called TRPM4 has multiple functions in the body and plays a role in the cardiovascular system and immune response. According to Heidelberg’s latest findings, TRPM4 has a toxic effect on extra-synaptic NMDA receptors.
Through molecular and protein biochemical methods, scientists have determined the interface between these two interacting proteins. Armed with this knowledge, they used structure-based searches to identify substances that could disrupt this bond, thereby destroying and inactivating the “death complex.”
This class of new inhibitors-what Heidelberg researchers call “interface inhibitors” because they disrupt the bonds formed on the interface between the extra synaptic NMDA receptor and TRPM4-have proven to be extremely effective nerves Cell protection agent. “We are studying a new therapeutic drug principle. Interface inhibitors provide us with a tool that can selectively remove the toxicity of extra-synaptic NMDA receptors,” explained Professor Bading.
Professor Bading and his team have demonstrated the effectiveness of the new inhibitor in mouse models of stroke or retinal degeneration. Therefore, there are good reasons to expect this interface inhibitor-as a broad-spectrum neuroprotective agent-to provide a treatment option for neurodegenerative diseases that are currently untreatable. “However, since new substances must first successfully pass the preclinical and clinical trials, it will take several years before they may be approved as drugs for human use.”
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