They call it the âkiller lipidâ because it seeps into the brain, forming amyloid plaques that lead to Alzheimerâs -- but thereâs a natural way to stop it from ever happening to youâ¦
----Important Message----
Use the Kraepelin Method to neutralize the âkiller lipidâ and prevent Alzheimerâs
I discovered a way to burn up this killer lipid safely in the body, BEFORE it gets to the brain, and convert it into usable energy insteadâ¦Â
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With the Kraepelin Method, the killer lipid is destroyed before it slips past the blood-brain barrier and forms amyloid plaques that cause Alzheimerâs.
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[Hereâs exactly how to use the Kraepelin Method to safely destroy the killer lipid and prevent Alzheimerâs.](
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This is what really causes Alzheimerâs disease in men (and THIS prevents it)
In the aging brain, a few notable changes take place.
And the most salient of those is the presence of lipofuscin.
Lipofuscin is a nonâdegradable material composed of tangles of proteins crosslinked by lipid peroxidation products.Â
Lipid aldehydes, such as hydroxynonenal, are formed as a result of lipid peroxidation...
These covalently bond to nitrogen-containing protein side chains such as lysine and histidine.Â
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This is catalyzed by iron and PUFA â prevented by vitamin E.Â
The result is a nonâdegradable material called lipofuscin that crowds out the intracellular space.Â
In dividing cells, nonâdegradable lipofuscin is diluted through cell division.
But in post-mitotic cells and in nerves, it builds up.
And it increases with agingâ¦
Even within the same species, the rate of accumulation is directly correlated with longevity.Â
âIn such cells, the amount of lipofuscin may increase dramatically; in some motor neurons of human centenarians, lipofuscin occupied 75% of the cytoplasmic volume.â
The result is a lowered metabolism in neuronsâ¦
Their inner volume is greatly reduced â displaced by lipofuscin.Â
So much lipofuscin leads to less space for metabolic activity.Â
The cell desperately tries to degrade this stuff, yet it cannot.Â
The cellâs main organelle for degrading larger proteins is the lysosome.Â
These are small vesicles filled with enzymes. And they have a method of lowering pH â catalyzing protein breakdown.Â
Lysosomes are like a cell within a cell, and can be viewed under a highâpower microscope.Â
In addition to reducing the formation of lipofuscin by taking vitamin E, limiting iron, and limiting polyunsaturated fatty acids (PUFAs), there are a few more things you can do.Â
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Over the years, itâs become clear that intracellular waste builds up faster in Alzheimerâs disease compared to control subjects.
You could almost consider this a form of accelerated aging.Â
Intracellular recycling of proteins happens constantly â in some cells more than others.Â
Cells of the brain and heart have a relatively low rate of recycling.
When a crosslinked protein cannot be broken down, it causes the accumulation of proteinsâ¦
A cellular traffic jam...Â
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Although not generally talked about these days, aluminum can actually crosslink proteins forming neurofibrillary tanglesâ¦
And that is the one true characteristic feature of Alzheimerâs disease.Â
This had been demonstrated in rabbits, cats, and monkeys.Â
To this day, nothing besides aluminum has been shown to be capable of reproducing all the defining features of Alzheimerâs.
âThese observations suggested that the normally efficient autophagic process in neurons is stalled in Alzheimerâs disease.â
Seeing Alzheimerâs under this paradigm (of reduced autophagy) suggests a hypothesis:Â
Can the induction of autophagy reverse this disease? Can it degrade the inclusion bodies?
There has actually been work done in this area:
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Up to this point, a few lines of thought converged to the dogma that âneurons in the brain cannot do autophagy.â
But these were simply the result of primitive assumptions.Â
âThe scarcity of recognizable autophagosomes and other...intermediates in healthy neurons has raised the possibility that baseline autophagy in neurons is normally lowâ¦â
Although normally done at a relatively low rate (compared to other cells), autophagy really can be induced in brain cells.
Autophagy is a process in which very large cellular components are engulfed by autophagosomes.
And then those fuse with lysosomes that donate enzymes to break down the cargo.Â
Even entire mitochondria can be digested this way.Â
This is in contrast to the smallerâscale micro-autophagy and proteasome degradation⦠the minor recycling processes.Â
These researchers used a cell transfected with DNA that codes for a fluorescent protein attached to a unique autophagosome proteinâ¦
Then they looked for changes:
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They showed beyond all doubt that brain neurons can undergo autophagyâ¦
...which is normally kept in check by dietary leucine.Â
The cell actually has a leucine sensor protein â which senses only this one amino acid.Â
In the absence of leucine, autophagy is initiated.Â
This process happens through the mTOR pathway.Â
So using the drug rapamycin â as the experimenters did â will also work.
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Restricting leucine alone has been shown to induce autophagy.Â
So, from this and other evidence, youâd expect leucine restriction (or intermittent fasting) would induce autophagy.
And autophagy could help break down and recycle intracellular proteins before they have a chance to irreversibly polymerize.
âWe conclude that macro-autophagy is constitutively active and highly efficient in healthy neurons and that the autophagic pathology observed in Alzheimerâs disease most likely arises from impaired clearanceâ¦â
Since lipofuscin is crosslinked by reactive lipids and builds up over time, youâd almost have to think that the longer it persists the harder it would be to break down.Â
Lipofuscin also traps iron.Â
And iron gives it a catalytic surface for enhanced lipid peroxidation. Â
This would lead to a self-amplifying, feed-forward, and exponential accumulation curve.
So perhaps if we fast two days a month, we can reduce lipofuscin, stave off dementia, and lose weight:
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Up until this point, autophagy in the brain had only been shown to occur in vitro, leaving doubt as to whether it could occur in vivo.
For example, there could always be enough leucine in the blood coming from autophagy elsewhere to keep it in check.Â
The brain always gets the first choice of nutrients during a fast.Â
â...but current dogma holds that the brain escapes this effect, perhaps because it is a metabolically privileged site.â
By using the same technique as in the previous study (the fluorescent protein), these researchers showed brain autophagy in rats â after a fast of only fortyâeight hours:
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But it must be said that rats have a quicker metabolismâ¦
So this would correspond to a longer time period for a human.
Nonetheless, there is now little doubt that autophagy can be induced in the brain during a fast.Â
Could this perhaps slow lipofuscin formation?Â
And perhaps even enhance its breakdown?
âOur data demonstrate that, contrary to current dogma, food restriction causes a rapid and profound upregulation of autophagy in the brain.â
Maybe this is why philosophers such as Pythagoras fastedâ¦
Maybe itâs why the classic fasting physicians of the previous century (such as Herbert Shelton and John Tilden) remarked on increased clarity of thought after a fast.Â
Despite the unpleasant sounding nature of fasting for a few days every other week, it doesnât sound like a bad idea from a scientific standpoint.Â
Autophagy is tissue-specific and occurs relatively late in muscle cells.
We lose negligible amounts of muscle during a threeâday fast⦠Bodybuilders routinely do this to shed fat before competition.
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