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Originally published by Nik Papageorgiou, Ecole Polytechnique Federale de Lausanne , on May 29, 2024  Credit: Cell Reports (2024). DOI: 10.1016/j.celrep.2024.114256 A new study by EPFL scientists shows that age-related decline in motor ability can be countered in fruit flies by enhancing the expression of the protein Trio , suggesting potential treatments for age-related movement decline. As we age , we suffer a noticeable decline in motor ability , which affects our quality of life and independence. This can be traced t o changes occurring at neuromuscular junctions , the critical points where nerve cells communicate with muscles .   The deterioration of motor ability is closely linked to the degeneration of motor synaptic terminals , where signals pass from nerves in the spine to muscles. As we age, the terminals u ndergo structural fragmentation , reducing the release of neurotransmitters , which is crucial for initiating muscle movements. In the end, this translates into decr

Originally published by Osaka University, on January 1, 2024 Overview: Both mitochondrial and lysosomal stress stimulate TFEB nuclear translocation, followed by increased HKDC1 expression. HKDC1 stabilizes PINK1 through interaction with TOM70, thereby facilitating PINK1/Parkin-dependent mitophagy. Additionally, HKDC1 and the VDAC proteins with which it interacts are important for repair of damaged lysosomes and maintaining mitochondria–lysosome contact. HKDC1 prevents DNA damage–induced cellular senescence by maintaining mitochondrial and lysosomal homeostasis. Credit: 2024 Cui et al., HKDC1, a target of TFEB, is essential to maintain both mitochondrial and lysosomal homeostasis, preventing cellular senescence, PNAS . Just as healthy organs are vital to our well-being, healthy organelles are vital to the proper functioning of the cell . These subcellular structures carry out specific jobs within the cell; for example, mitochondria power the cell, and lysosomes keep the cell tidy.

Originally published by Delthia Ricks , Medical Xpress, on August 30, 2023 Credit: Pixabay/CC0 Public Domain Losing the activity of a key ion channel in the brain may contribute to the buildup of a devastating and toxic protein responsible for the clumps of plaque that accumulate in Alzheimer's disease , a team of neurobiologists in China has found. Stunningly, this team has also shown—at least in animal-model studies—that this protein, a key hallmark of Alzheimer's, can be diminished in the living brain by manipulating the ion channel . The suspect protein is amyloid-beta , which becomes pervasive in the brain tissue of patients with Alzheimer's disease. Toxic, gooey amyloid-β accumulates in wads between neurons and disrupts the function of these vital brain cells . The ion channel is known simply as TRPM7 , and it may contribute to the buildup of toxic amyloid-β when the channel itself ceases to function properly, according to scientists at State Key Laborator