![]() Now that we know Hsp70 is a target of Rember™, we can develop similarly-acting drugs that will more specifically target this chaperone protein in affected areas of the brain, resulting in fewer side effects,” continues Dickey.ĭickey claimed that the USF team initially thought that activating Hsp70 would direct the chaperone protein to decrease the tau which had gone bad. “The drug does help prevent the protein (tau) from clumping together, but that in itself doesn’t mean it’s actively getting rid of the toxic tau. These clinical trials were noted to have been held at the International Conference on Alzheimer’s disease.ĭickey further stated that, “But Rember™ and its derivatives do have some inherent problems they’re not very potent so effective therapy would require fairly high doses,” Last year, the results in early clinical trials seem to have announced Rember as a chief development in the fight against Alzheimer’s. Experts discovered that one of the more effective Hsp70-inhibitor drugs seems to be a derivative of methylthioninium chloride, or Rember.Īdditionally, it appears to be the foremost experimental medication which was reported to directly attack the tau tangles in patients suffering from Alzheimer’s disease. The findings revealed that some compounds seem to have activated Hsp70, and others were Hsp70-inhibitors. They also analyzed brain tissue from genetically modified mice in order to develop the memory-choking tau tangles. The therapeutic strategy may also be applicable to other neurodegenerative diseases involving Hsp70, such as Huntington disease, Amyotrophic lateral sclerosis (ALS), and some cancers.”ĭuring the study, the USF team along with researchers at the University of Michigan examined the effects of numerous compounds on Hsp70 in cell models. Senior author of the study, Chad Dickey, PhD, assistant professor of molecular medicine who works out of the Byrd Alzheimer’s Institute at USF Health, stated that, “Now that we’ve discovered that targeting the chaperone protein Hsp70 can clear tau, it could be helpful in finding more effective drugs for Alzheimer’s disease. Tau is known to be present inside nerve cells, while one more hallmark protein associated with Alzheimer’s, beta amyloid, appears outside the neurons. The usual function of tau is to support the structure of nerve cells, similar to the skeleton which provides a scaffold in order to support the body. Hsp70 is believed to be one of several ‘chaperone’ proteins which supervise the activity of tau inside nerve cells. It appears to be associated with Alzheimer’s disease. Tau is known to be a protein which builds up abnormally inside nerve cells thereby affecting memory. Neuroscientists from the University of South Florida have discovered that inhibiting the protein Hsp70 quickly seems to reduce brain levels of tau. ![]()
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