National Institutes For Quantum Science &Technology

STOCKHOLM, April 11, 2024 /PRNewswire/ -- RaySearch Laboratories AB (publ) announces that QST, National Institutes for Quantum Science and Technology in Chiba, Japan, has selected the treatment planning system RayStation®* for clinical use at the QST hospital. The order was received and delivered in the first quarter of 2024. Already in 2018 RaySearch and NIRS (today known as QST) entered a partnership, including a long-term licensing agreement that enabled RaySearch to integrate the microdosimetric kinetic model (MKM) developed at NIRS, into the RayStation treatment planning system. This was followed by a research collaboration agreement in 2022, with focus on advancing ion beam therapy via the pencil beam scanning technique. The aim of the researchers from RaySearch and NIRS was to explore areas such as radiobiological modeling of ion-beam irradiation and dose fractionation, robust beam delivery and plan optimization algorithms. QST's purchase of RayStation is a logical step and manifests the long and fruitful research collaboration. Some of the advanced technologies included are multicriteria optimization, deformable image registration, dose tracking over multiple treatments and adaptive radiotherapy. Ion beam therapy is a highly advanced form of radiation therapy in which tumors are treated with protons or heavier ions such as helium or carbon. NIRS pioneered the clinical application of ion beam therapy during the 1990s and today, QST is a leading center for carbon ion therapy with more than 15,000 patients who have been treated at the HIMAC facility in Chiba. In 2016 an expansion from two to three treatment rooms for delivery of pencil beam scanning plans was completed, where the third room has the additional capability of a rotating gantry. Dr Shigeru Yamada, former Director General of QST Hospital, says: "We are very pleased to have RayStation which will expand our research capabilities and also improve our ability to treat patients with high precision." Johan Löf, founder and CEO, RaySearch, says: "We look forward to continuing our long and close collaboration with QST, to bring new solutions with speed, efficiency and optimization to healthcare providers around the world who are at the forefront of fighting cancer." The order value is JPY 265 million (approximately SEK 18.6 million), excluding service contract, most of which will be recognized as revenue in the first quarter of 2024. For more information, please contact: Johan Löf, founder and CEO, RaySearch Laboratories AB (publ) Telephone: +46 (0) 8 510 530 00 [email protected] *Subject to regulatory clearance in some markets This information was brought to you by Cision The following files are available for download: SOURCE RaySearch Laboratories

Scientists have taken a promising step towards a new generation of accurate, affordable and portable devices to detect concussion, epilepsy and dementia. Scientists have taken a promising step towards a new generation of accurate, affordable and portable devices to detect concussion, epilepsy and dementia. The international research team developed a laser-based diamond sensor that can measure magnetic fields up to 10 times more precisely than standard techniques. Their results are published in Science Advances. Their innovation could help improve on existing magnetic-field sensing techniques for mapping brain activity to identify disorders. With sufficient funding and collaboration with industry, the team say they could develop a proof-of-concept device using their new sensor within five years. Concussion in sport has been in the spotlight recently with prominent athletes sharing their stories about the significant ramifications of head injuries sustained during their careers. Meanwhile, about 250,000 Australians live with epilepsy, while nearly 500,000 Australians have some form of dementia. The research is also relevant to a range of sectors beyond healthcare including mining, where it could lead to improved mineral exploration applications. The study was led by Fraunhofer Institute for Applied Solid State Physics (IAF) in Germany -- one of the leading organisations for applied research in Europe -- working with RMIT University experts in diamond sensing technology Professor Andrew Greentree, Professor Brant Gibson and Dr Marco Capelli. What's the scientific breakthrough? Diamond is already used for sensing magnetic fields, where the amount of light that comes from quantum defects in the diamond changes with the strength of the magnetic field. The problem with today's approach is that most of that light is lost. "Our breakthrough was to make a laser from the defects," Greentree said. "By collecting all the light -- instead of just a small amount of it -- we can detect the magnetic field 10 times more precisely with our sensor compared with current best practice." How would the portable brain imaging device work? Today's magnetoencephalography, or MEG, technology is very sensitive, but also bulky, expensive to install and needs to operate at ultra-cold temperatures with liquid helium and patients must remain still. "Current MEG machines are huge devices, with dedicated facilities, and they require magnetic shielding around them as well," Greentree said. MEG technology based on the new diamond-laser sensor would be much smaller than today's devices, would operate at room temperature and could be fitted to patients who can move around. "We really want to have something that we can place on a patient's head and we want them to be able to move around -- and there'd be no need for expensive liquid helium to operate such a device," Greentree said. "With Alzheimer's, you want to be able to monitor the progression of the disease and know the effect of any treatments. It's similar with concussion, you want to be able to measure what's happening in the brain after each knock. "With this MEG technology we envisage, you might be able to pick up early-onset dementia. "With epilepsy, you could find out where it's occurring, and that would help you to better target interventions." Fraunhofer's Dr Jan Jeske and Dr Felix Hahl were corresponding authors for this study, which also involved researchers at the National Institutes for Quantum and Radiological Science and Technology in Japan and The College of Staten Island in the United States.

Neurodegenerative diseases like Alzheimer's and Parkinson's are defined by pathogenic accumulation of toxic proteins in the brain. Now, however, scientists have established that the p62 protein, which is involved in cellular protein degradation, can prevent the accumulation of toxic oligomeric tau species in mouse brains, proving the 'neuroprotective' function of p62 in a living model. Neurodegenerative diseases like Alzheimer's and Parkinson's are defined by pathogenic accumulation of toxic proteins in the brain. Now, however, scientists from the National Institutes for Quantum Science and Technology have established that the p62 protein, which is involved in cellular protein degradation, can prevent the accumulation of toxic oligomeric tau species in mouse brains, proving -- for the first time -- the "neuroprotective" function of p62 in a living model. In order to maintain cellular homeostasis (i.e., a state of equilibrium), cells undergo selective autophagy or self-degradation of unwanted proteins. Autophagy receptors control this process, by mediating the selection of a target protein that is then "cleared." Tau proteins -- which otherwise play an important role in stabilizing and maintaining the internal organization of neurons in the brain -- abnormally accumulate inside neurons in conditions like dementia and Alzheimer's disease. This build-up of hyper-phosphorylated tau proteins (or tau oligomers) causes the formation of neurofibrillary tangles (NFTs) and eventual cell death of neurons in the brains of people with dementia, contributing to the disease's progressive neurodegenerative symptoms. Now, while tau proteins can be degraded by selective autophagy, the exact mechanism of how this occurs remains a mystery. In a recent breakthrough, however, a study done by scientists at the National Institutes for Quantum Science and Technology in Japan proved the critical role played by a certain gene -- the p62 gene -- in the selective autophagy of tau oligomers. The team included researcher Maiko Ono, and group leader Naruhiko Sahara -- both from the Department of Functional Brain Imaging at the National Institutes for Quantum Science and Technology in Japan. Their paper, published in Aging Cell, was made available online on 5 June 2022. Previous studies have reported that the abnormal accumulation of the tau proteins may be selectively suppressed by autophagy pathways, through the p62 receptor protein (which is a selective autophagy receptor protein). Says Maiko Ono, "This protein's ubiquitin-binding ability helps in the identification of toxic protein aggregates (like tau oligomers), which can then be degraded by cellular processes and organelles." This study's novelty, however, lay in the demonstration of p62's "neuroprotective" role in a living model, which had never been done before. So, how did the researchers achieve this? They used mouse models of dementia. The p62 gene had been deleted (or knocked out) in one group of these mice, so they did not express p62 receptor proteins. On studying the brains of these mice using immunostaining and comparative biochemical analyses, an interesting picture was revealed. Neurotoxic tau protein aggregates were found in the hippocampus -- the area of the brain associated with memory -- and brainstem -- the center that coordinates the body's breathing, heartbeat, blood pressure, and other voluntary processes -- of p62 knockout (KO) mice. When we consider this along with the symptoms of dementia, which include memory loss, confusion, and mood changes, these findings make a lot of sense. MRI scans revealed that the hippocampus of p62 KO mice was degenerated (atrophied) and inflamed. A postmortem assessment of their brains revealed a greater loss of neurons in their hippocampus. Further immunofluorescent studies showed that the abnormal tau species aggregates can cause cytotoxicity leading to inflammation and cell death of neurons in p62 KO mice. Oligomeric tau, specifically, accumulated more in the brains of p62 KO mice. Overall, the findings of this study prove that by eliminating and, hence, preventing the aggregation of oligomeric tau species in the brain, p62 played a neuroprotective role in models of dementia. At a time when researchers across the word are trying to develop drugs for dementia and other related neurodegenerative disorders, the findings of this study will be of great importance in providing evidence for the accurate targeting of tau oligomers. The global population of ageing humans is increasing each year; hence, the need to develop methods to slow down the onset and progression of various neurodegenerative diseases is also expanding. This study provides a positive step towards addressing that need.