Pinterest Email Share on Facebook LinkedIn Share on Twitter Share For decades, intensive research has been conducted on drugs all over the world to treat Alzheimer’s patients. Although major progress has been made in diagnostics (the disease can be detected increasingly early and accurately), the therapeutic options remain limited. Together with researchers in Switzerland, Germany and India, the team headed by Professor Lawrence Rajendran from the Systems and Cell Biology of Neurodegeneration at the Institute of Regenerative Medicine of the University of Zurich has now developed a targeted substance that blocks the pathogenic function of an enzyme in the cells without affecting its other vital functions.Protein deposits in the brain are hallmarks of Alzheimer’s disease and partly responsible for the chronically progressive necrosis of the brain cells. Nowadays, these plaques can be detected at very early stages, long before the first symptoms of dementia appear. The protein clumps mainly consist of the β amyloid peptide (Aβ), a protein fragment that forms when two enzymes, β and γ secretase, cleave the amyloid precursor protein (APP) into three parts, including Aβ, which is toxic.Blocking the harmful process without affecting any useful functions If β or γ secretase is blocked, this also inhibits the production of any more harmful β amyloid peptide. Consequently, for many years biomedical research has concentrated on these two enzymes as therapeutic points of attack. To date, however, the results of clinical studies using substances that block γ secretase have been sobering. The problem is that the enzyme is also involved in other key cell processes. Inhibiting the enzymes in patients therefore triggered severe side effects, such as gastrointestinal hemorrhaging or skin cancer.Thus, for a number of years researchers have also been focusing their efforts on β secretase. A large number of substances have been developed, including some highly promising ones that reduced the amount of Aβ in mouse models effectively. Nevertheless, according to cell biologist Rajendran, this presents the same challenge: “The current β secretase inhibitors don’t just block the enzyme function that drives the course of Alzheimer’s, but also physiologically important cell processes. Therefore, the substances currently being tested in clinical studies may also trigger nasty side effects – and thus fail.”Promising substance to be studied on Alzheimer’s patientsTo address this, the first author on the publication, Saoussen Ben Halima in the lab of Professor Rajendran, and her fellow researchers studied how β secretase might be inhibited selectively – in other words, the harmful property blocked without affecting any useful functions. In a series of experiments, the scientists were able to demonstrate that the Alzheimer’s protein APP is cleft by β secretase in endosomes, special areas of the cells that are separated by membrane envelopes, while the other vital proteins are processed in other areas of the cell. The researchers exploited this spatial separation of the protein processing within the cell.“We managed to develop a substance that only inhibits β secretase in the endosomes where the β amyloid peptide forms. The specific efficacy of our inhibitor opens up a promising way to treat Alzheimer’s effectively in future, without causing the patients any serious side effects,” says Rajendran in summary. The researchers’ next goal is to hone their drug candidate so that it can initially be tested in mice and ultimately in clinical studies on Alzheimer’s patients.Alzheimer’s and dementia in figuresAround eight percent of over-65s and more than 30 percent of people who are younger than 90 suffer from Alzheimer’s or another form of dementia. According to the Swiss Alzheimer’s Association, around 120,000 people living in this country currently suffer from dementia – a figure that is set to rise to 200,000 patients by 2030 on account of demographic developments. Dementia is already the most common reason for needing care in old age in Switzerland and the third most common cause of death after cardiovascular disease and cancer.The study was published in Cell Reports.
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HATTIESBURG – Time is of the essence for Central (Ala.) cornerback John Broussard.Mississippi State is making a late push for 4-star Auburn cornerback commit John Broussard.The four-star Auburn commit will graduate high school in a few weeks and enroll in college in January. Broussard has been committed to the Tigers since May, but things grew complicated when former defensive coordinator Will Muschamp left last week to become the head coach at South Carolina.“I’d say it affects me a bit because Coach Muschamp and (former Auburn defensive backs) Coach T-Rob (Travaris Robinson) were a big reason why I committed to Auburn,” Broussard said.The 6-foot, 164-pound corner is one of the top commits for Auburn in 2016, and Tigers coach Gus Malzahn is trying to keep it that way.“I talked to Coach Malzahn the last couple of days,” Broussard said. “I’ve been talking to him every day. He’s just been telling me that they’re going to hire a great guy, a great defensive coordinator, and when they do, we’re going to do a home visit.”With the dead period going into effect Monday, Broussard says he believes Auburn will visit him Sunday after he returns home from the Mississippi-Alabama All-Star Game.Still, with Auburn’s defensive coordinator hire up in the air, Broussard is being pursued by other programs hoping to flip his commitment late in the process, most notably Oklahoma and Mississippi State.“(Mississippi State) has still been recruiting me even though I’ve been committed all year,” he said. “They just say they’re going to stay on me hard. They (Bulldogs coach Dan Mullen and cornerbacks coach Deshea Townsend) went and visited my parents yesterday. Coach Townsend said it went well.”The Bulldogs were one of the first programs to offer Broussard more than two years ago. The cornerback’s bond with Townsend has grown since his sophomore year and is a factor down the stretch.“I just think it’s because me and Coach Townsend have a great relationship,” he said. “We talk about everything, and he just stayed on me the whole time.”With the amount of players MSU loses in its secondary, Broussard knows he could see the field earlier in Starkville.“Yeah, it is a good opportunity for me because all of their starters are graduating, so it’s a good opportunity to play early,” he said.While he doesn’t have any visits planned prior to graduation, Broussard has heard from a former Bulldog.“I’ve talked to (MSU alum/current Tampa Bay Bucs cornerback) Johnthan Banks,” he said. “I’ve talked to him on Twitter before. He said if I was going to take an official, he was going to come and be there.“I’m an early graduate, so I’m probably going to say something next week.”Contact Courtney Cronin at (601) 961-7091 or [email protected] Follow @CourtneyRCronin on Twitter.
Related Emma Watson in “The Circle”; STX Financing LLC(NEW YORK) — Beauty and the Beast star Emma Watson talks about the ups and downs of fame with actress Jessica Chastain in the latest edition of Interview, and why you’re odds of getting a picture with the Harry Potter alum aren’t very good.“If someone takes a photograph of me and posts it, within two seconds they’ve created a marker of exactly where I am within 10 meters,” she says. “They can see what I’m wearing and who I’m with. I just can’t give that tracking data.”What the 27-year-old actress offers instead is her time. “I’ll say, ‘I will sit here and answer every single Harry Potter fandom question you have,” she insists, “but I just can’t do a picture.’”However, there are exceptions notes Watson, explaining, “I have to carefully pick and choose my moment to interact. When am I a celebrity sighting versus when am I going to make someone’s freakin’ week? Children I don’t say no to, for example.”Watson stars opposite Tom Hanks in the sci-fi drama The Circle, opening nationwide on Friday. Copyright © 2017, ABC Radio. All rights reserved.Powered by WPeMatico