Page 22 - Summer2011

across the membrane for a repeat cycle. The oxygen that is released from in the absence of insulin. However, this will
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the sulfate radical is picked up by the myoglobin, sequestered inside the lead to dangerous exposure of the cell’s proteins
molecule for safe travel to the mitochondria. Glucose breakdown products to glycation (because there is no iron sulfate
and oxygen are then delivered to the mitochondria to complete the process, to degrade the glucose). Glycation interferes
which ends with water, carbon dioxide and ATP, all while keeping the with the proteins’ ability to perform their jobs,
cell’s cytoplasmic proteins safe from glucose and oxygen exposure. and leaves them more vulnerable to oxidation
If I’m right about this role for cholesterol sulfate both in seeding the damage. One of the important affected proteins
lipid raft and in providing the sulfate ion, then this process breaks down would be myoglobin: it would no longer be able
miserably when cholesterol sulfate is not available. First of all, the lipid to effectively carry oxygen to the mitochondria.
raft is not formed. Without the lipid raft, the glucose can not enter the cell. Furthermore, oxidized myoglobin released into
Intense physical exercise can allow glucose to enter the muscle cells even the blood stream by crippled muscle cells leads

SUlfUR DEfICIENCY aND alzhEIMER’S DISEaSE

With an aging population, alzheimer’s disease is on the rise, and it has been argued that the rate of increase is dis-
proportionately high compared to the increase in the raw number of elderly people. Because of a conviction that the
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amyloid beta plaque, which is a signature of alzheimer’s, is also the cause, the pharmaceutical industry has spent hundreds
of millions, if not billions of dollars pursuing drugs that reduce the amount of plaque accumulating in the brain. Thus far,
drug trials have been so disappointing that many are beginning to believe that amyloid beta is not the cause after all.
Recent drug trials have shown not only no improvement, but actually a further decline in cognitive function, compared
to placebo. I have argued elsewhere that amyloid beta may actually be protective against alzheimer’s, and that problems
with glucose metabolism are the true culprit in the disease.
Once I began to suspect sulfur deficiency as a major factor in americans’ declining health, I looked into the relation-
ship between sulfur deficiency and alzheimer’s. Imagine my surprise when I came upon a web page posted by Ronald
Roth, which shows a plot of the levels of various minerals in the cells of a typical alzheimer’s patient relative to the normal
level (http://www.acu-cell.com/dis-alz.html). Remarkably, sulfur is almost non-existent in the alzheimer’s patient’s profile.
To quote directly from that site: “While some drugs or antibiotics may slow, or if it should happen, halt the progression
of alzheimer’s disease, sulfur supplementation has the potential of not only preventing, but actually reversing the condi-
tion, provided it has not progressed to a stage where much damage has been done to the brain. One major reason for
the increase in alzheimer’s disease over the past years has been the bad reputation eggs have been getting in respect to
being a high source of cholesterol, despite the fact of dietary intake of cholesterol having little impact on serum cholesterol,
which is now also finally acknowledged by mainstream medicine. In the meantime, a large percentage of the population
lost out on an excellent source of sulfur and a host of other essential nutrients by following the nutritional misinformation
spread on eggs. Of course, onions and garlic are another rich source of sulfur, but volume-wise, they cannot duplicate the
amounts obtained from regularly consuming eggs.”
Why should sulfur deficiency be so important for the brain? I suspect that the answer lies in the mysterious molecule
alpha-synuclein, which shows up alongside amyloid-beta in the plaque, and is also present in the lewy bodies that are
a signature of Parkinson’s disease. The alpha-synuclein molecule contains four methionine residues, and all four of the
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sulfur molecules in the methionine residues are converted to sulfoxides in the presence of oxidizing agents such as hydro-
gen peroxide. Just as in the muscle cells, insulin would cause the mitochondria of neurons to release hydrogen peroxide,
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which would then allow the alpha-synuclein to take up oxygen in a way that is very reminiscent of what myoglobin can
do in muscle cells. The lack of sufficient sulfur would directly impact the neuron’s ability to safely carry oxygen, again
paralleling the situation in muscle cells. This would mean that other proteins and fats in the neuron would suffer from
oxidative damage, leading ultimately to the neuron’s destruction.
I have argued elsewhere that biologically pro-active restriction in glucose metabolism in the brain (a so-called type-III
diabetes and a precursor to alzheimer’s disease) is triggered by a deficiency in cholesterol in the neuron cell membrane.
again, as in muscle cells, glucose entry depends upon cholesterol-rich lipid rafts, and, when the cell is deficient in cho-
lesterol, the brain goes into a mode of metabolism that prefers other nutrients besides glucose.
I suspect that a deficiency in cholesterol would come about if there is insufficient cholesterol sulfate, because choles-
terol sulfate likely plays an important role in seeding lipid rafts, while concurrently enriching the cell wall in cholesterol. The
cell also develops an insensitivity to insulin, and, as a consequence, anaerobic metabolism becomes favored over aerobic
metabolism, reducing the chances for alpha-synuclein to become oxidized. Oxidation actually protects alpha-synuclein
from fibrillation, a necessary structural change for the accumulation of lewy bodies in Parkinson’s disease (and likely also
alzheimer’s plaque). 13
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