amyloid beta tagged posts

Roots of Alzheimer’s disease can extend as far back as the Womb

Vitamin A deficiency increased the production of plaques in the brain of mice.

Vitamin A deficiency increased the production of plaques in the brains of mice.

Vitamin A deficiency could ‘program’ brain tissue. Biochemical reactions that cause Alzheimer’s disease could begin in the womb or just after birth if the fetus or newborn does not get enough vitamin A, according to new research from the University of British Columbia. These new findings, based on studies of genetically-engineered mice, also demonstrate that Vit A supplement given to newborns with low levels of vitamin A could be effective in slowing the degenerative brain disease.

“Our study clearly shows that marginal deficiency of vitamin A, even as early as in pregnancy, has a detrimental effect on brain development and has long-lasting effect that may facilitate Alzheimer’s disease in later life,” said Dr...

Read More

Human Amyloid-Beta acts as Natural Antibiotic in the Brain

beta-amyloid fibrils propagate from yeast surfaces and capture Candida albicans in culture medium. Credit: D.K.V. Kumar et al. / Science Translational Medicine (2016)

beta-amyloid fibrils propagate from yeast surfaces and capture Candida albicans in culture medium. Credit: D.K.V. Kumar et al. / Science Translational Medicine (2016)

A new study from Massachusetts General Hospital (MGH) investigators provides additional evidence that amyloid-beta protein, deposited in the form of beta-amyloid plaques in Alzheimer’s disease – is a normal part of the innate immune system, the body’s first-line defense against infection. Expression of human amyloid-beta (A-beta) was protective against potentially lethal infections in mice, in roundworms and in cultured human brain cells. The findings may lead to potential new therapeutic strategies and suggest limitations to therapies designed to eliminate amyloid plaques from patient’s brains.

“Neurodegeneration in Alzheime...

Read More

Genetic Variations that Boost PKC enzyme contribute to Alzheimer’s disease

One Alzheimer's-associated mutation in the PKC protein leads to a cavity that enhances its activity. Credit: UC San Diego Health

One Alzheimer’s-associated mutation in the PKC protein leads to a cavity that enhances its activity. Credit: UC San Diego Health

Researchers found Protein Kinase C (PKC) alpha is necessary for amyloid beta to damage neuronal connections. They also identified genetic variations that enhance PKC alpha activity in patients with Alzheimer’s disease. The study may present a new therapeutic target for the disease. “Until recently, it was thought that PKC helped cells survive, and that too much PKC activity led to cancer. Based on that assumption, many companies tested PKC inhibitors as drugs to treat cancer, but they didn’t work,” said Prof Alexandra Newton, PhD, UC SD School of Medicine.

“Instead, we recently found that the opposite is true...

Read More

Researchers identify ‘Neurostatin’ that may Reduce the Risk of Alzheimer’s disease

Schematic illustration of the drug discovery strategy described in this work. The strategy consists of four steps: (1) A fragment-based approach that allows the identification of small molecules that interact with the aggregation-prone system, here Aβ42, including FDA-approved molecules for drug repurposing. (2) An in vitro kinetic analysis that identifies the specific molecular steps in the Aβ42 aggregation mechanism responsible for the generation of toxic species. (3) A further kinetic analysis to determine the mechanism of inhibition associated with the molecules identified in step 1. (4) An evaluation of the effects of these molecules on the formation of toxic species in vivo. In particular, the inhibition of primary nucleation is predicted to delay the aggregation without affecting the total number of oligomers generated by the aggregation process, whereas inhibiting elongation or secondary nucleation is predicted either to increase or to decrease the number of toxic oligomers, respectively (see text).

Schematic illustration of the drug discovery strategy described in this work. The strategy consists of four steps: (1) A fragment-based approach that allows the identification of small molecules that interact with the aggregation-prone system, here Aβ42, including FDA-approved molecules for drug repurposing. (2) An in vitro kinetic analysis that identifies the specific molecular steps in the Aβ42 aggregation mechanism responsible for the generation of toxic species. (3) A further kinetic analysis to determine the mechanism of inhibition associated with the molecules identified in step 1. (4) An evaluation of the effects of these molecules on the formation of toxic species in vivo...

Read More