{"id":83565,"date":"2025-04-17T13:41:27","date_gmt":"2025-04-17T11:41:27","guid":{"rendered":"https:\/\/aktuelles.uni-frankfurt.de\/?p=83565"},"modified":"2025-04-17T16:19:08","modified_gmt":"2025-04-17T14:19:08","slug":"neurodegenerative-disease-als-cellular-repair-system-could-prevent-protein-aggregation","status":"publish","type":"post","link":"https:\/\/aktuelles.uni-frankfurt.de\/en\/english\/neurodegenerative-disease-als-cellular-repair-system-could-prevent-protein-aggregation\/","title":{"rendered":"Neurodegenerative disease ALS: Cellular repair system could prevent protein aggregation"},"content":{"rendered":"

Researchers at Goethe University, Johannes Gutenberg University Mainz and Kiel University discover possible method for preventing protein aggregates \u2013 Cluster4Future PROXIDRUGS research project<\/em><\/p>\n\n\n\n

If the protein TDP-43 is defective inside a nerve cell it can form neurotoxic aggregates, which are the cause of the neurodegenerative disease amyotrophic lateral sclerosis (ALS). Nerve cells are also damaged by TDP-43 in Alzheimer’s dementia. A research team led by Goethe University has now succeeded in preventing these aggregates by manipulating the protein so that it is transported to the cell’s own repair system. The study was carried out as part of the Cluster4Future PROXIDRUGS. The cluster is researching a new class of drugs that reprogram cellular systems to render disease-relevant proteins harmless.<\/strong><\/p>\n\n\n\n

\"Die
The fluorescence microscopy images show the nuclei of cultured human cells. On the left, the protein TDP 43 (green) is seen distributed within the cell nucleus along with nuclear bodies (red), which act as repair sites. When TDP 43 is damaged by stress or mutations and coupled with SUMO proteins (right image), it is transported to the nucleoli (arrows), where it is protected from aggregation (Credit: Dr. Jan Keiten-Schmitz).<\/figcaption><\/figure>\n\n\n\n
<\/div>\n\n\n\n

2500 new cases of amyotrophic lateral sclerosis are diagnosed every year, making it a relatively rare but very serious disease of the nervous system. A cure is not yet possible. ALS slowly destroys the motor neurons in the brain and spinal cord responsible for voluntary muscle control. The result is progressive muscle paralysis, leaving many patients wheelchair dependent. As the disease progresses, individuals find it increasingly difficult to speak, swallow, and breathe.<\/p>\n\n\n\n

In ALS, poorly soluble protein aggregates accumulate in motor neurons. Among other proteins, these aggregates consist of TDP-43, which plays various critical roles in cellular RNA metabolism. While in healthy cells TDP-43 is mainly found in soluble form in the cell nucleus, in ALS patients it forms poorly soluble aggregates that mainly accumulate outside the cell nucleus. This means that TDP-43 loses its functionality, as well as ultimately leading to the death of the motor neurons.<\/p>\n\n\n\n

As part of the Cluster4Future PROXIDRUGS funded by the Federal Ministry of Education and Research (Germany), researchers from the universities of Frankfurt, Mainz and Kiel have now discovered a way to prevent the formation of harmful TDP-43 aggregates in cultured cells. To do this, scientists led by Kristina Wagner, Dr. Jan Keiten-Schmitz and Professor Stefan M\u00fcller from the Institute of Biochemistry II at Goethe University exposed cells to stress, for example by increasing the temperature or using a chemical substance. As a result, some TDP-43 was released from the cell nucleus into the cytosol, where it accumulated in so-called stress granules.<\/p>\n\n\n\n

\u201cThe formation of such stress granules is a normal process and serves the cell as a temporary protective space for proteins so that they are immediately available to the cell once the stress has subsided,\u201d explains Keiten-Schmitz. \u201cHowever, if TDP-43 is mutated, as it is in the cells of many ALS patients, the stress granules persist, increasingly solidify and ultimately damage the neurons.\u201d<\/p>\n\n\n\n

The scientists successfully prevented TDP-43 from leaving the cell nucleus under stress by linking it with the cell’s \u201croadside assistance\u201d \u2013 a protein called SUMO \u2013 which directed TDP-43 to a cellular \u201cmechanic\u201d, the so-called nuclear bodies. \u201cAs a result, TDP-43 remains soluble, and the nuclear bodies – like a mechanic – ensure that harmful forms of TDP-43 are restored or broken down by the cellular recycling system,\u201d says Kristina Wagner, a first author of the study. Insoluble protein aggregates that damage or even kill cells would therefore be prevented from forming in the first place.<\/p>\n\n\n\n

The team of researchers is now looking for future drug candidates in the form of chemical compounds that bring SUMO and TDP-43 together. PROXIDRUGS principal Investigator M\u00fcller explains: \u201cOur cell culture experiments provide a first proof-of-principle: this pathway can help cells to limit disease-promoting TDP-43 aggregates. Even if the road to developing a possible drug for treating ALS is still very long, it is definitely worth pursuing this approach further. After all, TDP-43 aggregates are also found in other neurodegenerative diseases, such as frontotemporal dementia (FTD) and in around half of all Alzheimer’s patients.\u201d<\/p>\n\n\n\n

<\/div>\n\n\n\n

Publication:<\/strong>
Kristina Wagner, Jan Keiten-Schmitz, Bikash Adhikari, Upayan Patra, Koraljka Husnjak, Fran\u00e7ois McNicoll, Dorothee Dormann, Michaela M\u00fcller-McNicoll, Georg Tascher, Elmar Wolf and Stefan M\u00fcller: Induced proximity to PML protects TDP-43 from aggregation via SUMO\u2013ubiquitin networks. Nature Chemical Biology<\/a> (2025), 10.1038\/s41589-025-01886-4<\/em>

Background information:<\/strong>
ALS Association<\/a>
Target ALS<\/a>
Les Turner ALS Foundation<\/a>
ALS Hope Foundation<\/a><\/p>","protected":false},"excerpt":{"rendered":"

Researchers at Goethe University, Johannes Gutenberg University Mainz and Kiel University discover possible method for preventing protein aggregates \u2013 Cluster4Future PROXIDRUGS research project If the protein TDP-43 is defective inside 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