ISIS Report 12/04/12
Cancer a Redox Disease
Cancer cells are universally disturbed in their electronic
energy balance, an understanding that potentially revolutionises cancer therapy
and prevention Dr. Mae-Wan
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Two opposing approaches to cancer therapy
We are losing the war on cancer, targeting specific cancer gene
mutations does not work, and for good reasons (see  Personalized
Medicine for Cancer Fact or Fiction? SiS 54). Not only are the
mutations remarkably diverse, differing between individuals and between parts
within a single tumour, cancer cells soon become resistant to new drugs.
There is growing realization that
cancer is not primarily a genetic disease, but an epigenetic response to
chronic stress  (Cancer an
Epigenetic Disease, SiS 54). Redundancy in diverse signalling
pathways means that many different ‘adaptive’ mutations can enable cells to
survive and multiply, predisposing them to malignant transformation.
One approach to cancer therapy is the much
touted ‘personalized medicine’ that tailors the cure to key genes that have
gone awry. But genetic heterogeneity poses a considerable, if not
insurmountable hurdle .
The other approach is to target
the most general characteristic of cancer cells and tumours that is distinct
from normal cells, and this is becoming popular. Cancer cells typically have
an abnormal energy metabolism, prompting some researchers to suggest that
cancer is a metabolic disease [3, 4].
I prefer to call cancer a redox
disease, as explained later, to distinguish it from the usual “inborn errors of
metabolism” that underpinned the hypothesis of “one gene one enzyme” of
biochemical genetics .
Cancer a mitochondrial disease
The abnormal energy metabolism of cancer cells was
discovered by German physiologist Otto Heinrich Warburg in the 1920s. Normal
cells obtain energy by breaking down the 6-carbon molecule glucose into two
3-carbon pyruvate molecules in a series of reactions – glycolysis - that does
not require oxygen, followed by oxidation reactions in the mitochondria in
which oxygen is needed.
Cancer cells, however, depend heavily on
glycolysis to obtain energy, even though plenty of oxygen is present. This
phenomenon – aerobic glycolysis subsequently known as the Warburg effect -
prompted Warburg to propose that mitochondrial dysfunction was the primary
cause of cancer .
As glycolysis is much less
efficient in extracting energy from glucose, cancer cells are voracious for
glucose, and that is how tumours are detected by positron emission tomography
(PET) imaging in which glucose uptake is measured by means of a radioactive
Aerobic glycolysis is a robust
hallmark of most tumours; it involves a high uptake of glucose with lactate
production in the presence of oxygen, lactate being the by-product of pyruvate,
even in those cancer cells that appear to have working mitochondria . The
reason seems to be that cancer cells need glycolysis to generate carbon skeletons
for the synthesis of proteins and nucleic acids to support rapid cell proliferation
; and blocking glycolysis does appear to inhibit cancer cells  (though it
would also affect normal cells).
Warburg’s idea fell into
disfavour as the view of cancer as a metabolic disease was gradually displaced
with one of cancer as a genetic disease caused by mutations in specific cancer
related genes, or oncogenes .
In recent years, the idea that cancer
is a metabolic disease has become fashionable again. Some commentators remark
that  “molecular biology is re-discovering biochemistry”; it is more important
Cancer is a disease of electronic
energy imbalance, and electronic energy is the life-wire that animates cells
and organisms, as the father of biochemistry Albert Szent-Györgyi had
discovered three quarters of a century ago .
Life is an electronic current
In  The
Rainbow and the Worm, The Physics of Organisms (ISIS publication) first
published in 1993, I presented theoretical and empirical evidence for the
quantum electrodynamic nature of organisms. An organism is energized by
electrons (and protons) flowing through a liquid crystalline matrix that
extends into the interior of every single cell. The movement of electrons
between chemical species is reduction (for the electron acceptor) and oxidation
(for the electron donor). Reduction and oxidation always go together, hence
‘redox’ reactions. Redox reactions are the heart of energy transduction in
living organisms. Electrons move according to the reduction
potential (also referred to as reduction-oxidation potential or redox
potential), the affinity of a substance for electrons. The redox potential for
each substance is compared to that of hydrogen, which is set arbitrarily to
zero at standard conditions of 25 °C, 1 atmosphere, and 1 M concentration.
have positive redox potentials accept electrons from hydrogen, becoming reduced, while substances that have
negative redox potentials donate electrons to hydrogen, becoming oxidized.
In order to appreciate the redox
theory of cancer, we need to understand the core metabolic reactions common to organisms.
For a more thorough description of energy metabolism see  Living
Rainbow H2O (ISIS publication), a sequel to the Rainbow Worm
 and a unique synthesis of the quantum physics and chemistry of water as
the “means, medium and message” of life.
Energy metabolism in animal cells
All air-breathing animals, human beings included, depend on
oxygen to extract energy from their food in a universal set of core metabolic
reactions (Figure 1). The 6-carbon molecule glucose is activated by ATP and
the enzyme hexokinase, and split through a series of glycolytic reactions each
catalysed by a specific enzyme into two 3-carbon pyruvate that take place in
the cytoplasm, and do not require oxygen. Further metabolism of pyruvate
normally takes place in the mitochondria, in which pyruvate is first oxidized
by the enzyme complex pyruvate dehydrogenase and converted into a two-carbon
fragment joined to co-enzyme A (acetyl-CoA) with the release of one CO2
and water. Acetyl-CoA enters the citric acid cycle, where it is eventually fully
oxidized into further molecules of CO2 and water, generating
reduced electron carriers. The reduced electron carriers shuttle electrons down
the oxidative electron transport chain (ETC), and the energy released goes to
make ATP (adenosine triphosphate), the universal energy intermediate in living
The oxidation of glucose into
carbon dioxide and water is respiration, the reverse of photosynthesis
in green plants, algae and blue green bacteria. Photosynthesis captures energy from
sunlight to ‘fix’ or reduce carbon dioxide from the atmosphere into carbohydrates
(glucose) using electrons (and protons) obtained by splitting water, releasing
oxygen back into the atmosphere in the process. The regeneration of oxygen is
just as important as sequestering carbon dioxide, if not more so as far as
air-breathing organisms are concerned (see  O2 Dropping
Faster than CO2 Rising, SiS 44).
Water splitting and reforming is
the redox dynamo, the magic roundabout that creates practically all life out of
inanimate substances .
Figure 1 Energy
metabolism in normal animal cells, by RegisFrey
are special membrane-bound organelles that serve as ‘powerhouses’ in the cell
(Figure 2). A mitochondrion has an outer membrane enclosing the entire
structure, and a much-folded inner membrane that encloses a matrix,
projecting numerous thin plate-like folds or cristae into it. Between
the two membranes is a labyrinthine intermembrane space. Each mitochondrion
also has 5 to 10 circular molecules of mitochondrial DNA that are replicated
and inherited independently of the cell’s genome.
2 Electron micrograph of a mitochondrion in a cell of the bat pancreas, by
membrane of the mitochondrion contains many complexes of integral membrane
proteins that form channels through the membrane, where a variety of molecules
can move in and out of the mitochondrion. The inner membrane contains 5
complexes of integral membrane proteins of the oxidative electron transport
chain: NADH dehydrogenase (Complex I), succinate dehydrogenase (Complex II),
cytochrome c reductase (Complex III), cytochrome oxidase (Complex IV), and ATP
synthase (Complex V) (see Figure 3).
Figure 3 Diagram of the oxidative electron transport
chain in the mitochondrion, by Fvasconcellos, Wikimedia
The matrix of
the mitochondrion contains a mixture of enzymes that catalyse the citric acid
cycle (also called the Krebs Cycle, after British biochemist Hans Krebs who
discovered it). The citric acid cycle produces the electron donors NADH (reduced
nicotinamide adenine dinucleotide) and FADH2 (reduced flavin adenine
dinucleotide) that feed into the electron transport chain (ETC). Electron
transport down the ETC is coupled with the transport of protons H+
across the inner membrane into the intermembrane space (Figure 3), resulting in
a typically negative mitochondrial potential (Dym)
in the matrix across the inner membrane (as protons are positively charged).
The protons are returned to the matrix via ATP synthase, resulting in the
synthesis of ATP from ADP (adenosine diphosphate) and Pi (inorganic
phosphate). This oxidative phosphorylation is absolutely essential for the
life of all air-breathing animals. Most of the ATP is produced by oxidative
phosphorylation in the mitochondria. The complete oxidation of glucose generates
36 molecules of ATP, of which 32 are produced within the mitochondria, and only
4 by glycolysis in the cytoplasm.
glycolytic reactions are much faster. It is estimated that in the time it take
for the mitochondria to produce 36 molecules from one glucose, another ten
glucose molecules are turned into lactate with the generation of 20 additional
ATP molecules in the cancer cell, making a total of 56 ATP molecules compared
to the 36 in a normal cell .
Abnormal mitochondria in cancer cells
Cancer cells not only exhibit
aerobic glycolysis, they resistance apoptosis (cell suicide), a fate that would
normally befall cells with dysfunctional mitochondria. It thus appears that
aerobic glycolysis and apoptosis are linked.
Michelakis and his team at University of Alberta in Canada were among the first
to note that aerobic glycolysis and apoptosis meet up in the mitochondria .
They demonstrated the remarkable therapeutic potential of a cheap, readily
available chemical dichloroacetate (DCA) that reactivated the gate-keeper
enzyme for oxidation in the mitochondria, pyruvate dehydrogenase (see  Does
DCA cure cancer? SiS 54), and as a result the cancer cells committed
suicide and the human tumour grown in cancer-prone rats shrank. We shall look
at his results in some detail, as they are relevant to our understanding of cancer
as a redox disease.
between glycolysis and apoptosis is apparent, as many glycolytic enzymes also regulate
apoptosis, while several oncoproteins induce the expression of glycolytic
enzymes. This web of circular causation is what one has come to expect as a
consequence of the fluid genome  Living with the Fluid Genome
(ISIS publication), which also makes therapeutic interventions based on single
molecular targets often ineffective, if not also fraught with side-effects.
The protein Akt,
for example, which stimulates glycolysis and induce resistance to apoptosis,
also activates hexokinase, an enzyme catalysing the first and irreversible step
in glycolysis (see Fig. 1) in which glucose is phosphorylated by ATP to
glucose-6-phosphate. Akt induces the translocation of hexokinase - normally
residing in the cytoplasm - to the mitochondrial membrane via its downstream
mediator, glycogen synthase kinase 3 (GSK3). In the mitochondrial membrane, hexokinase
binds to the voltage-dependent anion channel (VDAC), an important part of the
mitochondrial transit pore that controls the permeability of the mitochondria
to small hydrophilic molecules. This suppresses apoptosis, presumably by making
the mitochondrial membrane impermeable. Inhibiting GSK3 in cancer cells presumably
causes hexokinase to unbind from the VDAC, making the mitochondria permeable to
small molecules, thereby inducing apoptosis and increasing sensitivity to
to Michelakis’ team that perhaps the metabolic phenotype in cancer is due to a
remodelling of the mitochondria that suppresses (or disturbs) oxidative
phosphorylation, enhances glycolysis and stops apoptosis.
with this hypothesis is the observation that cancer cell lines have more
hyperpolarized mitochondria membrane potential (more negative compared to the
outside) (see Box 1) . Cancer cells also relatively deficient in the cell
membrane voltage-gated K+ (Kv) channels (channels for K+ that
open only if the electrical potential is beyond a threshold value). K+ channel
deficiency is known to suppress apoptosis in several cell types including
Cancer cells have
negative than normal) mitochondrial electric potential Dym has been linked to malignant transformations since the
1980s. Tumours cells are typically highly heterogeneous, and within a
population of tumour cells, there are minor subpopulations with stable
differences in their Dym that survive
cell cloning. Cells with high Dym
typically have decreased sensitivity to chemoprotective agents and increased
secretion of VEGF (vascular endothelial growth factor, promoting growth of
blood vessels), and in metastatic tumours, but not in non-metatstatic tumours,
correlated with invasive potential .
mechanisms involved in generating and maintaining difference in Dym are unclear, they may reflect alterations
in the composition of the mitochondrial membranes, modulations in expression of
mitochondrial targeted nuclear genes, or enrichment in a particular
Downstream effects of DCA
Treatment with DCA decreased the hyperpolarized
mitochondrial potential to normal levels, accompanied by a decrease in tumour cell
growth in vitro and in vivo, as reported .
The mitochondrial potentials in
three human cancer cell lines: A549 (non-small-cell lung cancer), M059K
(glioblastoma), and MCF-7 (breast cancer), were compared with healthy,
noncancerous human cell lines: small airway epithelial cells (SAEC),
fibroblasts and pulmonary artery smooth muscle cells (PASMC). All cancer cell
lines had significantly more hyperpolarized mitochondrial potential compared to
normal cells, as measured by increased fluorescent of the potential sensitive
dye tetramethyl rhodamine methyl ester TMRM. Incubation of all three types of
cancer cells with DCA reversed the hyperpolarization and returned it to the
level of normal cells after 48 h. But normal cells were unaffected. The DCA
effects on mitochondrial electric potential occurred as quickly as 5-10 min and
were dose dependent.
DCA-induced decrease in electrical potential of the mitochondria was limited by
an inhibitor of the VDAC; indicating that transport out of the mitochondria
is important for the DCA response. As consistent with this hypothesis, DCA
caused the efflux of pro-apoptotic factors from the mitochondria, as well as
increased reactive oxygen species production (see below). In untreated A549
cells, cytochrome c and the proapoptosis inducing factor (AIF) were restricted
to the mitochondria. But in DCA treated cells, cytochrome c was diffusely
present in the cytoplasm and AIF was translocated to the nucleus, both
indicative of apoptosis.
Moreover, DCA increased glucose
oxidation by 23 % and concomitantly suppressed glycolysis and fatty acid
oxidation in A549 cells. After 48 h of DCA treatment, the extracellular
lactate level was decreased, while pH increased in A549 cells compared with untreated
Mitochondria reactive oxygen
species & DCA
Reactive oxygen species (ROS)
are small molecules containing oxygen that are more reactive than ordinary
molecular oxygen. ROS are produced in mitochondria as intermediates of electron
transport  (see Box 2).
is the main source of ROS
In the process of oxidative
phosphorylation, oxygen is reduced one electron at a time in a sequence, oxygen
to superoxide to hydrogen peroxide to hydroxyl radical, and finally water:
→ ·OH → H2O
All except the first and
last have an unpaired electron, and are very reactive, hence referred to as
reactive oxygen species (ROS). Thus, oxidative phosphorylation inevitably
generates ROS as intermediates, and the mitochondria are considered the major
source of ROS; the primary ROS being superoxide anion, O2-·.
It is the precursor of all ROS species, and in vivo it is produced both
enzymatically by NADPH oxidase, and xanthine oxidase, and non-enzymatically,
when a single electron is directly transferred to O2. The superoxide
anion acquires a proton to become a hydroperoxyl radical (H O2-·),
followed by a fast rearrangement (dismutation) either spontaneously or through
a reaction catalysed by superoxide dismutases (SODs) to produce hydrogen
peroxide H2O2. H2O2 is relatively
stable and membrane permeable; and can diffuse within the cell to be eliminated
by antioxidant systems in the cell or mitochondria, such as catalase,
glutathione peroxidase, and thioredoxin peroxidase.
There is disagreement
as to whether normally functional mitochondria actually export ROS [18, 19]. I
believe it is entirely possible that ROS is only produced as the result of
diminished coherence in electron transport, resulting in partially oxidized
intermediates, because that’s what ROS consist of. DCA increased the
production of the ROS hydrogen peroxide (H2O2) in a
dose-dependent manner from 25 % at 0.05 mM DCA to 35 % at 0.5 mM DCA . This
increase was inhibited by rotenone, suggesting the involvement of complex I of
the electron transport chain, presumably in a reversed electron transport due
to a build-up of NADH, another sign that the mitochondrial ETC is not
functioning normally in cancer cells. Consistent with this hypothesis is the
observation that isolated mitochondria exposed to DCA showed an increase in
NADH levels within the mitochondria .
complication is that ROS at lower levels, characteristic of chronic stress and
inflammation, are a ‘second messenger’ for cell proliferation - a predisposition
to malignant transformation - supporting the idea that cancer is an epigenetic
disease . However, the evidence linking mitochondrial ROS, presumably at
higher concentrations, to apoptosis is equally strong.
The main ROS
produced in mitochondria is H2O2 (see Box 2). If it is
not eliminated by the cell’s antioxidant system, it can be further transformed
to hydroxyl radical (·OH) in the presence of metal ions. ·OH is
highly reactive, and damaging . A wide range of mitochondrial ROS-induced
damages has been described, to proteins, lipids and mitochondrial DNA. These
damages can result in an energetic catastrophe.
by Michelakis’ team , the major ROS target inside the mitochondria is the
permeability transition pore, which becomes highly conductive in the presence
of ROS, allowing small molecules to pass in both directions. Small solutes
flood into the mitochondrial matrix along their electrochemical gradients (from
high concentrations outside to low concentrations), dissipating the electrochemical
potential and inducing swelling of the mitochondrial matrix, eventually
rupturing the outer membrane, releasing cytochrome c and proapoptosis inducing
factor (AIF) into the cytoplasm, resulting in apoptosis. Cells use a special
form of autophagy, mitophagy , to selectively eliminate defective
mitochondria. Increases in cellullar ROS leads to loss of mitochondrial
membrane potential, which is a trigger for mitophagy. When many mitochondrial
are eliminated by mitophagy, apoptosis follows.
DCA and electrochemical
Increase in H2O2
production by cancer cells exposed to DCA is involved in activating voltage
gated K+ channels (Kv) in the cell membrane. Michelakis team
showed that DCA treatment increased the K+ outward current significantly
in all cancer cells but not in normal cells . This increase in outward K+
current, accompanied by an increased expression of the K+ channel
Kv1.5, leads to hyperpolarization of the plasma membrane (becoming more
negative); and is blocked by intracellular catalase, which breaks down H2O2,
and by rotenone which inhibits complex I produced H2O2.
At the same
time, DCA decreased intracellular Ca2+ by inhibiting voltage-gated
Ca2+ channels, so DCA treated cells had lower intracellular Ca2+
compared with untreated cells, the decrease occurring within 5 mins and was sustained
after 48 hours of DCA exposure. The effects on Ca2+ were inhibited
by rotenone and mimicked by H2O2, among other things.
thought to decrease intracellular Ca2+ and increase Kv1.5 expression
by inhibiting NFAT (nuclear factor of activated T lymphocytes). NFAT is known
to inhibit both apoptosis and the expression of Kv1.5 in myocardial cells, and
the team found that this was also true in cancer cells. Increase in
intracellular Ca2+ activates calcinerin, which dephosphorylates
NFAT, allowing it to be translocated to the nucleus where it regulates gene
transcription. DCA-induced activation of Kv1.5 leads to hyperpolarization of
the cell membrane, inhibiting voltage gated Ca2+ channels, hence
blocking the increase in intracellular Ca2+ and inhibiting NFAT.
DCA & apoptosis
Michelakis and colleagues found
that DCA increases annexin expression, caused a ~6-fold increase in
TUNEL-positive nuclei and activates both caspase 3 and 9 in A549 cells. Terminal
deoxynucleotidyl transferase dUTP nick end labelling (TUNEL) is a method
for detecting DNA fragmentation by labelling the terminal end of nucleic acids.
to eliminate highly proliferative cells by inducing apoptosis and by decreasing
intracellular Ca2+ levels. It also decreases cell proliferation, as
measured by BrdU (bromodeoxyuridine) incorporation, and the expression of
proliferating cell nuclear antigen (PCNA). In addition, DCA decreased the
expression of survivin, a mitotic indicator.
apoptosis of cancer cells by two pathways, one in the mitochondria, where
depolarization activates mitochondria-dependent apoptosis, and the other at the
cell membrane, where upregulation of Kv1.5 channels decreases K+,
activating caspases. The mitochondrial component is thought to be more
important, as other factors and manipulations to deliver the cytoplasmic
component of apoptosis did not result in the degree of apoptosis induced by
findings, in addition to the demonstration of the ability of DCA to shrink
xenograft human tumours in rats, and glioblastomas in humans  do support
Warburg’s hypothesis that cancer is a disease involving mitochondrial malfunction;
but perhaps not in its original form, as Warburg thought mitochondrial were
Redox imbalance in cancer
Not much attention has been paid to the electronic state of
the cell or its organelles until quite recently when voltage sensitive dyes
became available. This made it much easier to measure the electric potential
of cells and organelles. As a result, researchers discovered that the cell’s
electric potential determines its vital states, from cell division and pattern
formation to differentiation, regeneration and cancer ( Membrane Potential
Rules, SiS 52). This is fully in accord with the quantum electro-dynamic
nature of life [10, 11].
Actually, it has been known since the 1950s that the cell membrane potential, measured
with microelectrodes, varies throughout the cell cycle . Cell types
with very high resting potentials such as muscle cells and neurons show little
if any tendency to divide, while a decrease in membrane potential follows
malignant transformation. In the 1970s, Clarence D. Cone Jr. induced DNA
synthesis and mitosis in fully differentiated neurons from the central nervous
system using a variety of agents that depolarized the cell membrane (made it
less negative) . In the 1990s, electric potential measurements of skin
sites over malignant tumours of the breast gave electropositive readings that
were correlated with increased depolarization in membrane potential of
cancerous cells and tissues compared with normal cells or non-cancerous cells
The other well-known sign of
redox imbalance in cancer cells is the hyperpolarized mitochondria (see Box 1).
evidence is now coming from direct measurements of redox states. The redox
pairs of the cell are NADH/NAD+ (nicotinamide adenine dinucleotide),
NADPH/NADP+ (nicotinamide adenine
dinucleotide phosphate) and GSH/GSSG (glutathione). The ratio of reduced to
oxidized forms reflect the redox state of the cell. For example, under
unstressed conditions in cultured astrocytes (brain cells that control blood
flow to neurons), the NADH/NAD+ pair is predominantly in the
oxidized state to accept electrons produced during glycolysis in the
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) reaction (see Fig. 1). In
contrast, the redox pair NADPH/NADP+ are kept in a more reduced
state to provide electrons for reductive biosynthesis, while the concentration
of GSH strongly exceeds that of GSSG to support efficient antioxidant defence.
These ratios of the redox pairs in cultured astrocytes are similar to those
reported for brain , and are intimately linked to cellular metabolism and
a class of small redox proteins present in all organisms that act as
antioxidants with redox signalling functions - is believed to integrate the
overall redox state of the cell, and are essential for life in mammals . Researchers at University of Wisconsin School
of Medicine and Public Health, Madison, in the United States, examined protein
levels and redox changes of thioredoxin 1 (Trx1) in human prostate tissues and
culture cells . They found more than 4-fold increase in Trx1 protein in the
nucleus of high-grade cancer cells compared with normal controls, and the
increase correlated with cancer progression. The protein was also increased in
the cytoplasm by about 2-fold. Despite increased protein levels, the oxidized
forms of nuclear Trx1 were higher in prostate cancer cell lines compared to
their benign counterparts, suggesting that nuclear redox imbalance occurred
selectively in cancer cells.
Trx1 has a specific role in the modulation of
redox signaling, with distinct nuclear and cytoplasmic pools, each performing
different functions. In the nucleus, Trx1 interacts with certain transcription
factors to regulate their binding to DNA; these include p53 (apoptosis
response), nuclear factor κB (NF-κB,
involved in inflammatory response) and nuclear factor-like 2 (Nrf2, involved in
antioxidant response). In the cytoplasm, Trx1 can regulate apoptotic
signal-regulating kinases. Trx1 is also known to move from the cytoplasm to the
nucleus in response to oxidative stress. Selective oxidation of Trx1 can occur
and has been detected in both the nucleus and the cytoplasm in response to
cellular redox changes. Increased Trx1 protein expression has been detected in
multiple cancer tissues and cancer cell lines, and an increase in Trx1
expression was associated with higher tumor grade and has been implicated in the
resistance of tumor cells to certain chemotherapies and ROS generating agents.
Emerging evidence suggests that cancer cells are more
oxidized relative to normal; they do not have enough electrons. This is
consistent with other indications that cancer is a redox disease, a state of
electronic imbalance. Rational therapy and prevention should start from here.
There are 11 comments on this article so far. Add your comment
|Dr. Michael Godfrey Comment left 12th April 2012 20:08:35|
The whole approach to cancer prevention and treatment warrants re-evaluation in view of this fundamentally important evidence. It seems to me that recharging by regularly earthing barefoot on the ground for an hour a day might also be beneficial as this has been shown to reduce inflammation and improve capillary blood flow. (www.earthing.com).
|Konstantin Comment left 12th April 2012 20:08:40|
Awesome article. I´ve got one question though regarding K-Channels etc. I haven´t received Gilbert Ling´s book yet, but it was my understanding that channels don´t exist and acutally represent protein-interactions which correlates to the fluid crystal structure of the cell. Is that right?
|Mae-Wan Ho Comment left 12th April 2012 20:08:36|
Michael Godfrey, you are right. I was sceptical about that for a long time, but earthing does make sense. Konstantin, you raise a very good point. I deal with the issue in more detail in my new book, Living Rainbow H2O. Gilbert will have to speak for himself. But he may be right in that what conventional cell biologists regard as a potassium channel could well be something else. Also, Gilbert doesn't actually deny the existence of potassium channel as such in some specialized epithelial cells.
|Anita Allen Comment left 13th April 2012 08:08:03|
Your attention is drawn to Eleni Papadopulos-Eleopulos’ Oxidative Stress Theory, first proposed in 1982 as the cause of cancer (Papadopulos-Eleopulos, E. (1982) ‘A Mitotic Theory’. Journal of Theoretical Biology 96, pg 741-758) and then applied to AIDS in the a 1988 paper (Papadopulos-Eleopulos, E. (1988) ‘Reappraisal of AIDS: Is the oxidation caused by the risk factors the primary cause?’ Medical Hypotheses 25;151-162) and elaborated in another paper in 1992 (Papadopulos-Eleopulos E., Turner V.F., Papadimitriou J.M. (1992) ‘Oxidative Stress, HIV and AIDS’ Research in Immunology 143: 145-148). According to this proposal, normal cellular functioning is determined by the level and oscillations of cellular redox - oxidation and its chemical opposite reduction. When oxidation is prolonged or excessive, cells become abnormal, injured and susceptible to diseases. As far as I know, Papadopulos-Eleopolus is the first to advance the theory that cellular processes have a cyclic nature controlled by a periodic charge exchange between actin and myosin, regulated by the oxidation and reduction of sulphydryl moieties. Also, she is the first to apply oxidative stress as the mechanism leading to AIDS.
Regarding treatment, she proposes that oxidative stress requires that the patient be treated with antioxidants in general and –SH (sulphydryl) containing compounds in particular. The oxidative theory demands that the underlying cause, cellular oxidation, must be addressed – that is treatment with –SH containing compounds under the supervision of a doctor who has access to laboratory facilities to measure redox and at least until the redox is normalised. The treatment may include adjunct measures such as diet and stress reduction management. At the same time, exposure to oxidising substances should be minimised, or if possible, eliminated.
|Konstantin Comment left 15th April 2012 06:06:04|
Most of the stuff discussed here is still way beyond me. Science is complicated and you have to learn a lot of names :)
But one thing i start to understand is, that life is a flow of electrons and its this flow that connects all living matter. If people would start to understand this, the way we live would change tremendously. I think its really important to spread this idea, if one wants to make a positive change in this world. Basically this is how indigenous people used to understand their presence.
What do you think about violet rays, rife-machines etc.? They were eventually banned by the FDA, but there is a lot of evidence that these high-frequency gadets helped with many ailments. If electronical flow is the basic of life, "charging" the cell with these machines sounds like a good idea to me.
|Ren Comment left 3rd May 2012 15:03:11|
On DCA and cancer cells metabolism:
|Danilo Comment left 31st August 2012 21:09:21|
From “Cancer as a Metabolic Disease: On the Origin, Management, and Prevention of Cancer” ( http://www.amazon.com/Cancer-Metabolic-Disease-Management-Prevention/dp/0470584920 ) by
Thomas Seyfried (Professor of biology, Boston College): “The gene theory has deceived us into thinking that cancer is more than a single disease (…) Cancer is a singular disease”.
|Irucka Embry Comment left 29th September 2012 08:08:05|
Is cancer caused by a fungus? See http://www.cancerfungus.com/ . Thank-you.
|David Lowenfels Comment left 7th December 2012 20:08:10|
May I refer you to the work of Dr.med. Heinrich Kremer who has written much about the topic of redox, mitochondria, cancer, and HIV. http://www.amazon.com/Silent-Revolution-Cancer-AIDS-Medicine/dp/1436350832
|Zoco Comment left 11th January 2013 11:11:51|
Hi, Great article ! !
I have come across a so called redox therapy peoduct Asea,
Its Terribly pricy, first product of marketing company. Says biggest breakthrough ever. I think its a scam. Have you heard of it?
Budwig diet is supposed to renew redox state if cell , its lipid membranes.
Dca is great but some cancers have dual metabolism (also fatty acid) like colorectal, most leukemias and Dca makes there thing worse, forcing fatty acid oxidation instead of glycolysis.
|C.DELARGE Comment left 10th May 2013 12:12:06|
You should try a perfectly balanced REDOX signaling molecules stabized solution called ASEA, it is not a scam and really works,is highly patented and stabilized after many years of research.
You can have more informations or even order it for research on http://cedel.myasealive.com
I would behappy to send you all the tests conducted so far or even put you in contact with Dr Gary L. Samuelson who helped stabilize those redox molecules.