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Printable Handouts
Navigable Slide Index
- Introduction
- Amyloid-β can seed from an exogenous source
- Inoculation of Amyloid-β seeds in cerebral blood vessels
- Amyloid-β and iCJD in humans
- Transmission of amyloid-β in humans
- Routes of exogenous amyloid-β in humans
- Amyloid-β dissemination after dural grafting
- CAA after dural grafting
- It is not all about head trauma
- It is not all about head surgery
- From pathological reports to clinical cases - case 1
- From pathological reports to clinical cases - case 2
- From pathological reports to clinical cases - case 3
- From pathological reports to clinical cases - case 4
- Lyodura as an exogenous amyloid-β source
- Iatrogenic Cerebral Amyloid Angiopathy (CAA)
- Iatrogenic CAA: UCL diagnostic criteria
- Iatrogenic CAA: The largest case collection
- Iatrogenic CAA: An international perspective
- Iatrogenic CAA: An illustrative case
- Iatrogenic CAA: Some final considerations
- Acknowledgments
Topics Covered
- Iatrogenic Cerebral Amyloid Angiopathy (CAA)
- Amyloid-β transmission
- Inoculation of amyloid-β seeds in cerebral blood vessels
- Amyloid-β and iCJD in humans
- Creutzfedt-Jakob Disease (CJD)
- Prion proteins
- Dural grafting
- Lyodura
Talk Citation
Storti, B. (2024, July 31). Iatrogenic cerebral amyloid angiopathy [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved August 25, 2024, from https://doi.org/10.69645/SXAT8035.Export Citation (RIS)
Publication History
Financial Disclosures
- There are no commercial/financial matters to disclose.
A selection of talks on Clinical Practice
Transcript
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0:00
My name is Benedetta Storti.
I am a neurologist at
Carlo Besta Neurological
Institute in Milan, Italy.
I work in the Department of
Cerebrovascular Disease and
I have a special interest
in small vessel pathology.
In this presentation,
I will discuss
Iatrogenic Cerebral
Amyloid Angiopathy
which is an entity that
has been known for
only a few years.
Iatrogenic cerebral
amyloid angiopathy
is considered to be
clinically and
pathologically identical
to sporadic amyloid angiopathy.
But on the contrary,
it is not spontaneous and
has a well-defined etiology.
The underlying
hypothesis is that
there is a point of origin,
a focus of the
dissemination of amyloid.
This seed consists of
a dura patch applied
during surgery several
decades earlier.
But let's start this
interesting story
from the beginning.
0:60
Misfolded proteins can
form aggregates and
induce a self-perpetuating
process leading to
the amplification
and spreading of
pathological protein assemblies.
The intracerebral injection of
prion protein-containing
human brain homogenates
into animals led to
the discovery of
transmissible prion
disease approach in 1966.
Proteins with this
prion-like ability
include alpha-synuclein,
tau, TDP-43,
but also amyloid-β.
The observation that amyloid-β
can seed from an
exogenous source
was tested in animals
as early as 1993 in
wild-type marmosets,
a New World monkey that
express a human-type
sequence of amyloid-β.
Intracerebral infusion
of brain tissue material
from an Alzheimer's
disease patient
resulted in amyloid-β
deposits that
could not be observed
in control animals.
Interestingly, the
distribution pattern of
exogenously induced
plaques was similar to
those in elderly
uninjected controls
that developed
cerebral amyloidosis.
Another strong evidence
for prion-like seeding of
misfolded amyloid-β
aggregates in vivo
was documented in
experiments carrying
out the inoculation of
diluted brain
extracts derived from
confirmed Alzheimer's
disease patients into
young amyloid-β precursor
protein transgenic mice.
Most of those amyloid-β
seeding studies
were carried out in
transgenic mice over-expressing
mutant human amyloid
precursor protein gene.
Also, amyloid-β
deposits can also
be induced de novo
in rodents that
would never exhibits
amyloid-β plaque pathology
spontaneously within
their normal lifespan.
This is a strong indication that
exogenously applied seeds
act as a template
for misfolding of
endogenous amyloid-β and
that seeding is not
solely promoting
the premature
deposition of amyloid.
In the work of Eisele,