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Monday, September 19, 2016

Study Offers ‘Critical Insights’ for Treating and Preventing Alzheimer’s

NEUROSCIENCE NEWS
Summary: A new study provides novel insights into the molecular basis of Alzheimer’s.


Source: Northeastern University.

Northeastern professor Lee Makowski and his colleagues suggest that Alzheimer’s disease may progress not like falling dominoes, with one molecular event sparking the formation of plaques throughout the brain, but rather like a fireworks display, with a unique flare launching each plaque, one by one. The finding provides “critical insights for developing therapies to slow, halt, or reverse” the disease. NeuroscienceNews.com image is adapted from the Northeastern press release.

New research led by North­eastern Uni­ver­sity sug­gests that Alzheimer’s dis­ease may not progress like falling domi­noes, as con­ven­tional wisdom holds, with one mol­e­c­ular event sparking the for­ma­tion of plaques throughout the brain. Instead, it may progress like a fire­works dis­play, with a unique flare launching each plaque, one by one.

The study, headed by Lee Makowski, pro­fessor and chair of the Depart­ment of Bio­engi­neering, was pub­lished Thursday in the journal Sci­en­tific Reports.
“I believe the find­ings will pro­vide us with a new way of thinking about the mol­e­c­ular basis for Alzheimer’s dis­ease pro­gres­sion,” says Makowski. “Once you do that, you can start asking the right ques­tions about how to pre­vent it.”

More than 5 mil­lion Amer­i­cans are living with Alzheimer’s dis­ease, according to the Alzheimer’s Asso­ci­a­tion. It is the sixth leading cause of death in the U.S., the asso­ci­a­tion reports, killing more people than breast and prostate can­cers combined.
Yet much about its cause and the mech­a­nisms dri­ving its pro­gres­sion remain unknown. Alzheimer’s dis­ease typ­i­cally starts with the death of brain cells, or “neu­rons,” in one part of the brain and then, over time, slowly spreads to other regions. Amy­loid fibrils—thin rigid strands of pro­tein aggregates—accumulate in these areas of neu­ronal death, packing together to form dense plaques.

“Just as there are dif­ferent strains of a virus, there appear to be dif­ferent strains of fib­rils,” explains Makowski. “Remark­ably, the dif­ferent strains have the same chem­ical makeup but dif­ferent three-​​dimensional structures.”

Insight into therapies
It was the struc­tures that Makowski’s team zeroed in on.
In col­lab­o­ra­tion with researchers from Mass­a­chu­setts Gen­eral Hos­pital and Argonne National Laboratory’s Advanced Photon Source, Makowski and former research asso­ciate Jil­iang Liu, PhD’15, scanned slices of brain tissue retrieved at autopsy from four people with Alzheimer’s and one with no his­tory of dementia using an X-​​ray beam just five microns across. They then built images of the fibrous struc­tures within the plaques from the thou­sands of dif­frac­tion pat­terns they collected.

Because fib­rils self-​​propagate, researchers have spec­u­lated that all fib­rils in a given brain are of the same strain and hence have the same struc­ture. That led to the assump­tion that a single mol­e­c­ular event ini­ti­ated their accu­mu­la­tion into plaques and the sub­se­quent cas­cading pro­gres­sion of the disease.

“Our data wasn’t con­sis­tent with that,” says Makowski. “We found that fib­rils with dis­tinctly dif­ferent struc­tures can accu­mu­late in the same brain, even in plaques quite close to one another. This strongly sug­gests that there is not one event that ini­ti­ates fibril for­ma­tion throughout the brain but many. Our research indi­cates that it is the con­di­tion under which fib­rils form that slowly prop­a­gates through the brain and trig­gers a dis­tinct ini­ti­a­tion event for each plaque.”

Think of a cold front trav­eling south from Mass­a­chu­setts to Vir­ginia. It’s raining up and down the East Coast. When con­di­tions are right in Massachusetts—that is, when the tem­per­a­ture drops to 32 degrees—the rain turns to snow (the ini­ti­a­tion event). Vir­ginia, how­ever, doesn’t get any snow until a week later when its tem­per­a­ture drops to the freezing point. As in the brain, the con­di­tions drive the event.

“The find­ings are impor­tant because they change the way we think about dis­ease pro­gres­sion,” says Makowski. “It gives us a new point of view from which to develop hypotheses about the con­di­tions that lead to the for­ma­tion of fib­rils and plaques.”
The researchers also showed that the struc­ture of the fib­rils may vary based on a person’s clin­ical his­tory. For example, the fib­rils of one woman who had exhib­ited no signs of dementia prior to death were dis­tinctly dif­ferent from those found in the others, who had Alzheimer’s disease.

“This may mean that some strains of fib­rils are asso­ci­ated with dis­ease whereas others are not,” says Makowski. “Dis­tin­guishing between them may pro­vide crit­ical insights for devel­oping ther­a­pies to slow, halt, or reverse the neu­rode­gen­er­a­tion asso­ci­ated with Alzheimer’s disease.”
ABOUT THIS ALZHEIMER’S DISEASE RESEARCH ARTICLE
Source: Mehdi Moussaïd – Northeastern University
Image Source: NeuroscienceNews.com image is adapted from the Northeastern press release.
Original Research: Full open access research for “Amyloid structure exhibits polymorphism on multiple length scales in human brain tissue” by Jiliang Liu, Isabel Costantino, Nagarajan Venugopalan, Robert F. Fischetti, Bradley T. Hyman, Matthew P. Frosch, Teresa Gomez-Isla and Lee Makowski in Sci­en­tific Reports. Published online September 15 2016 doi:10.1038/srep33079


Abstract
Amyloid structure exhibits polymorphism on multiple length scales in human brain tissue
Aggregation of Aβ amyloid fibrils into plaques in the brain is a universal hallmark of Alzheimer’s Disease (AD), but whether plaques in different individuals are equivalent is unknown. One possibility is that amyloid fibrils exhibit different structures and different structures may contribute differentially to disease, either within an individual brain or between individuals. However, the occurrence and distribution of structural polymorphisms of amyloid in human brain is poorly documented. Here we use X-ray microdiffraction of histological sections of human tissue to map the abundance, orientation and structural heterogeneities of amyloid. Our observations indicate that (i) tissue derived from subjects with different clinical histories may contain different ensembles of fibrillar structures; (ii) plaques harboring distinct amyloid structures can coexist within a single tissue section and (iii) within individual plaques there is a gradient of fibrillar structure from core to margins. These observations have immediate implications for existing theories on the inception and progression of AD.

“Amyloid structure exhibits polymorphism on multiple length scales in human brain tissue” by Jiliang Liu, Isabel Costantino, Nagarajan Venugopalan, Robert F. Fischetti, Bradley T. Hyman, Matthew P. Frosch, Teresa Gomez-Isla and Lee Makowski in Sci­en­tific Reports. Published online September 15 2016 doi:10.1038/srep33079

http://neurosciencenews.com/alzheimers-treatment-prevention-5059/

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