Not directly related but your doctor should be able to use this to create a baseline measurement of your brain prior to your getting dementia. I am assuming your doctor has told you all about this and has assigned you a protocol to prevent it.
1. A documented 33% dementia chance post-stroke from an Australian study? May 2012.
2. Then this study came out and seems to have a range from 17-66%. December 2013.
3. A 20% chance in this research. July 2013.
http://medicalxpress.com/news/2016-11-imaging-technique-toxicity-alzheimer-parkinson.html
Researchers have developed a new imaging
technique that makes it possible to study why proteins associated with
Alzheimer's and Parkinson's diseases may go from harmless to toxic. The
technique uses a technology called multi-dimensional super-resolution
imaging that makes it possible to observe changes in the surfaces of
individual protein molecules as they clump together. The tool may allow
researchers to pinpoint how proteins misfold and eventually become toxic
to nerve cells in the brain, which could aid in the development of
treatments for these devastating diseases.
The researchers, from the University of Cambridge, have studied how a phenomenon called hydrophobicity
(lack of affinity for water) in the proteins amyloid-beta and alpha
synuclein—which are associated with Alzheimer's and Parkinson's
respectively - changes as they stick together. It had been hypothesised
that there was a link between the hydrophobicity and toxicity of these
proteins, but this is the first time it has been possible to image
hydrophobicity at such high resolution. Details are reported in the
journal Nature Communications.
"These proteins start out in a relatively harmless form, but when
they clump together, something important changes," said Dr Steven Lee
from Cambridge's Department of Chemistry, the study's senior author.
"But using conventional imaging techniques, it hasn't been possible to
see what's going on at the molecular level."
In neurodegenerative diseases
such as Alzheimer's and Parkinson's, naturally-occurring proteins fold
into the wrong shape and clump together into filament-like structures
known as amyloid fibrils and smaller, highly toxic clusters known as oligomers which are thought to damage or kill neurons, however the exact mechanism remains unknown.
For the past two decades, researchers have been attempting to develop
treatments which stop the proliferation of these clusters in the brain,
but before any such treatment can be developed, there first needs to be
a precise understanding of how oligomers form and why.
"There's something special about oligomers, and we want to know what
it is," said Lee. "We've developed new tools that will help us answer
these questions."
When using conventional microscopy techniques, physics makes it
impossible to zoom in past a certain point. Essentially, there is an
innate blurriness to light, so anything below a certain size will appear
as a blurry blob when viewed through an optical microscope, simply
because light waves spread when they are focused on such a tiny spot.
Amyloid fibrils and oligomers are smaller than this limit so it's very
difficult to directly visualise what is going on.
However, new super-resolution techniques, which are 10 to 20 times
better than optical microscopes, have allowed researchers to get around
these limitations and view biological and chemical processes at the
nanoscale.
Lee and his colleagues have taken super-resolution techniques one
step further, and are now able to not only determine the location of a
molecule, but also the environmental properties of single molecules
simultaneously.
Using their technique, known as sPAINT (spectrally-resolved points
accumulation for imaging in nanoscale topography), the researchers used a
dye molecule to map the hydrophobicity of amyloid fibrils and oligomers
implicated in neurodegenerative diseases. The sPAINT technique is easy
to implement, only requiring the addition of a single transmission
diffraction gradient onto a super-resolution microscope. According to
the researchers, the ability to map hydrophobicity at the nanoscale
could be used to understand other biological processes in future.
More information:
Nature Communications, DOI: 10.1038/ncomms13544
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