Alzheimer's, Dementia & Mental Health
Latest Potential for Early Detection of Alzheimer’s
Disease Analyzes Spinal Fluid
Other recent claims of success with early detection
of Alzheimer’s have used blood test or eye abnormalities in lab rats
March 21, 2014 - Researchers announced this week
they are close to being able to diagnose the early stages of Alzheimer’s
disease by the detection of tiny, misfolded protein fragments in
cerebrospinal fluid taken from patients. Just in a matter of days
similar claims for early discovery of the disease has been made by
scientists using a
blood test and others studying
eye abnormalities in
Scientists, with hefty financing from drug-makers,
government and non-profits, have been burning the midnight oil in
efforts to find a means of detecting Alzheimer’s disease at its very
early stages, while treatments might have a better chance of working
before extensive brain damage and dementia develop. Nothing, however,
seems close to clearing all the hurdles necessary to become available
for clinical use with humans.
These misfolded protein fragments have been
suggested to be the main culprit in Alzheimer's disease, according to
the report on this research in the Cell Press journal Cell Reports.
The authors point out, too, that scientists used to think amyloid
plaques were the problem in Alzheimer's disease.
"Now it seems clear that the aggregates are not the
main culprits, it's their precursors," so-called Aβ oligomers, said
Claudio Soto of the University of Texas Medical School at Houston.
"This is the key molecule and could be the best,
most reliable way to make an early diagnosis. That's been the biggest
problem in the field: you can't identify patients until they are already
"Those Aβ oligomers may be circulating in the body
years if not decades before cognitive symptoms arise," Soto added. This
speculation set him on the quest to detect them.
Soto and his colleagues applied a technology they
developed earlier for detection of the misfolded proteins responsible
for prion diseases including mad cow disease. Their protein misfolding
cyclic amplification (PMCA) technology works by amplifying existing
misfolded proteins and then breaking them up into smaller pieces. When
mixed with the equivalent, normal protein, the misfolded fragments act
as seeds for the formation, in the case of Aβ, of amyloid clumps like
those found in the Alzheimer's brain.
The researchers showed that their PMCA technology
can detect Aβ oligomers at incredibly low concentrations. In principle,
their earlier prion work suggests it might be possible to detect even a
single particle of misfolded Aβ.
Most importantly, Soto and his
colleagues were able to distinguish between patients with Alzheimer's
disease and those with other neurodegenerative or neurological disorders
with 90% sensitivity and 92% specificity by applying their test to
cerebrospinal fluid samples.
The next step, Soto says, is to adapt the
technology for use with blood or urine samples, which would be much
easier to obtain for screening perfectly healthy people for biochemical
signs of Alzheimer's disease. They will also continue to explore its
utility for detecting the disease before symptoms appear.
If additional research can confirm the utility of
the test in Alzheimer's and perhaps other conditions (e.g. Parkinson's
disease), Soto says an FDA-approved test could be on the market in as
little as three years. His team is already involved in commercializing
the PCMA technology for application in prion diseases.
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