We need oxygen, but it is also toxic to all life forms and we know Bb doesn't want a lot of it, but it needs SOME. It is not a STRICT anaerobe. Oxygen breathing life forms protect themselves against oxygen toxicity (too much) by catalase and superoxide dismutase (SOD) which destroy toxic peroxides and superoxides.
These are 2 of our 3 antioxidant ENZYMES:
SOD works first:
SOD happens to be the ``fastest enzyme known and protects the cells by breaking down superoxide to give
hydrogen peroxide.''
Now...it's not unusual for bacteria to have SODs. ``Most bacterial and mitochondrial SODs are iron (Fe) or * manganese* containing enzymes and all are homologous in amino acid sequence. The SOD of eukaryotic cytoplasm is a Cu2+/Zn2+ enzyme and has a totally different sequence.''
Okay...stopping here to look up a definition...
A eukaryote is an organism with a complex cell or cells, in which the genetic material is organized into a membrane-bound nucleus or nuclei. Eukaryotes comprise animals, plants, and fungi--which are mostly multicellular--as well as various other groups that are collectively classified as protists (many of which are unicellular). In contrast, prokaryotes are organisms, such as bacteria, that lack nuclei and other complex cell structures.
And Bb is no exception:
Year 1997...
Infective and noninfective strains of Borrelia burgdorferi, along with Borrelia afzelii and Borrelia garinii, possessed a
single iron-containing superoxide dismutase (SOD).
None of the Lyme disease spirochetes tested possessed catalase or peroxidase activities. The borrelial SOD was not inducible by growth with increased oxygen concentrations and thus appeared to be produced constitutively.
PMID: 9353077
Science. 2000 Jun 2;288(5471):1651-3. Lack of a role for iron in the Lyme disease pathogen.
Posey JE, Gherardini FC.
Department of Microbiology, University of Georgia, Athens, GA 30602, USA.
A fundamental tenet of microbial pathogenesis is that bacterial pathogens must overcome host iron limitation to establish a successful infection. Surprisingly, the Lyme disease pathogen Borrelia burgdorferi has bypassed this host defense by eliminating the need for iron. B. burgdorferi grew normally and did not alter gene expression in the presence of iron chelators.
Furthermore, typical bacterial iron-containing proteins were not detected in cell lysates, nor were the genes encoding such proteins identified in the genome sequence.
The intracellular concentration of iron in B. burgdorferi was estimated to be less than 10 atoms per cell,
well below a physiologically relevant concentration.
PMID: 10834845
Below a ``physiologically relevant concentration''?
Genetic research indicates Bb is ``PFK dependent''. This is the enzyme phosphofructokinase. It is ``rate limiting'' for glycolysis. A drop in this enzyme can lead to anemia:
This happens to our astronauts who happen to also undergo ``oxidative stress'' when they are up in space. To counter this...right now researchers are trying to figure out how to monitor and deliver Mg to our astronauts!
``Postflight there was a significant decrease of phosphofructokinase''
``Early hematology studies done on Gemini and Apollo missions indicated decreased red blood cell mass in returning astronauts, which initiated investigation on Skylab into space flight induced anemia.
Red blood cell mass, red blood cell life span, and plasma volume were measured to determine the mechanisms that caused the decrease in red blood cell mass on previous flights. Data on red blood cell metabolism as well as changes in cellular shape (morphology) supplemented the previous investigation into the altered red blood cell mass.''
The case for a subcutaneous magnesium product and delivery device for space missions.
Rowe WJ.
Cardiovascular (CV) complications, associated with space flight (SF), are caused by microgravity, hypokinesia and radiation, particularly beyond earth orbit, with all three conducive to oxidative stress.
PMID: 15466957
Also re: iron:
Susceptibility of iron-loaded Borrelia burgdorferi to killing by hydrogen peroxide and human polymorphonuclear leucocytes.
Sambri V, Cevenini R, La Placa M.
Institute of Microbiology, University of Bologna, S. Orsola Hospital, Italy.
Borrelia burgdorferi grew more slowly in iron-depleted than in iron-sufficient media. The addition of increasing concentrations of iron stimulated borrelial growth and resulted in the intracellular accumulation of this element.
Compared with iron-starved borrelia, iron-enriched organisms showed enhanced sensitivity to hydrogen peroxide.
Intracellular iron-content did not, however, influence susceptibility to killing by human polymorphonuclear leucocytes [corrected].
PMID: 1874405
Also in the year 2000...(Even with antibiotics, there is ``further activation of free radicals''):
``RESULTS: The results of our examinations prove that beta-lactamase
antibiotic therapy
brings non-enzymatic antioxidant parameters to control values, though the treatment causes
no change in enzymatic antioxidant parameters, resulting in
the further activation of free radicals. (!!!)
CONCLUSIONS: In patients with Erythema migrans, the decreased capability to reduce lipid superoxidants leads to maintaining a high concentration of membrane lipid peroxidation products.''
PMID: 11687735
And in 2001:
A single superoxide dismutase (Sod) gene was identified in Borrelia burgdorferi strains, Borrelia afzelii Ple and Borrelia garinii Pbi.
PMID: 10650199
So...thus far... Bb can breakdown superoxides yielding H2O2.
We make H2O2 inside our cells all the time for a really brief moment in time. This acid, hydrogen peroxide, normally kills many pathogens ( bacteria, viruses, fungi and even some spores) that try to invade our cells.
``Hydrogen peroxide is also toxic but not so rapid or dangerous in its reactions as superoxide. The main danger from H2O2 is its conversion to hydroxyl radicals by reaction with transition metal ions such as Fe2+. H2O2 + Fe2+ = OH + H) + Fe3+.
So we must dispose of the H202 before it gives rise to hydroxyl radicals.
There is no enzymatic protection mechanism against hydroxyl radicals, once made. Catalase is important in destroying H2O2. It is a heme enzyme which catalysis the reaction: 2H202 � 0 (with a slash thru it) 2H20 +O2.
Now...talk about speed...catalase, which is made in the LIVER, works in something like 1/400,000th of a second. (And SOD is faster!).
The 3rd antioxidant enzyme is glutathione.
``Most cells contain excess of sulfhydryl compounds such as the tripeptide glutathione.
This consists of glutamate, cysteine and glyceine linked by peptide bonds....
.Glutathione and other -SH compounds act as scavengers for superoxides, peroxides and free radicals being oxidized themselves to the disulfides. Disulfides are then reduced the sulfhydryl derivatives by glutathione reductase, which uses NADPH.''
So...glutathione looks to be the last ``resort'' so to speak. It is not surprising that this antioxidant enzyme drops a LOT in lyme patients.
We know Bb is H2O2 ``resistant''. It possess SOD which eliminates superoxide , but this -> H2O2 which has to be broken down.
In the back of your mind, make note of this:
``Cu,Zn-SOD is also subject to inactivation by H202.''
And ``catalase and glutathion peroxydase are NOT co-upregulated with MnSOD. If NFkB (oxidative stress signaling enzyme) upregulates MnSOD the resultant H2O2 may speed up aging.
So what makes Bb resistant to H2O2?
``To confirm these findings, Dr. Skare showed that B burgdorferi containing an active form of the BB0647 gene was indeed able to resist hydrogen peroxide, around 3000 times better than a strain containing a mutated form of the gene.''
But what's happening to catalase? It is our most abundant anti-oxidant. It is produced in the LIVER and works incredibly fast...reducing H2O2 to H2O and O in 1/400,000th of a second! Where the heck is it? Why is glutathione, the ``last resort'' being utilized?
``Each molecule of catalase is a tetramer of four polypeptide chains. Each chain is composed of more than 500 amino acids.
Catalase has one of the highest turnover rates for all enzymes: one molecule of catalase can convert 6 million molecules of hydrogen peroxide to water and oxygen each minute.
Catalase uses the iron atom to help it break the bonds in the two molecules of hydrogen peroxide, shifting the atoms around to release two molecules of water and a molecule of oxygen gas.
``Until the Columbia paper, animal cells were thought to have only peroxisomal catalase, though cytosolic catalase had been seen in both plants and yeast.
The new catalase just identified, the first such enzyme found in animals, resides in the cell fluid, not within a specific compartment.
In this more general location, the cytosolic catalase could act as a kind of surveillance system, removing harmful peroxides from throughout the cell.
The research team dubbed the catalase CTL-1, and named the gene that produces it ctl-l.''
So, it should come as no surprise that the body is forced to turn to glutathione (glutamate, cysteine and glyceine requirements go up) to try to combat the extreme oxidative stress situation.
The most important question is why lyme disease becomes chronic. I recently came across a website that indicates the activation of a particular enzyme is responsible, but more importantly, it indicates how we might INactivate this enzyme.
The enzyme is NFkB. It is the ``oxidative stress-responsive nuclear factor kB (NFkB). This is the MAIN regulator of immune-related functions.''
Activation of human monocytic cells by Treponema pallidum and Borrelia burgdorferi lipoproteins and synthetic lipopeptides proceeds via a pathway distinct from that of lipopolysaccharide but involves the transcriptional activator NF-kappa B.
Ebnet K, Brown KD, Siebenlist UK, Simon MM, Shaw S.
Borrelia burgdorferi activates nuclear factor-kappa B and is a potent inducer of chemokine and adhesion molecule gene expression in endothelial cells and fibroblasts.
All of these events, cumulatively known as ``oxidative stress,'' lead to increased production of free radicals inside the cell, with the activation of tiny messengers called transcription factors such as AP-1 and nuclear factor kappa B, or NfkB for short.
When NfkB detects oxidative stress, it translocates to the nucleus of the cell, which contains the DNA (which in turn contains the master instructions of the cell).
NfkB attaches to a portion of the DNA and instructs the cell to make inflammatory chemicals such as interleukins 1 and 6 and tumor necrosis factor, types of cytokines (intercellular chemical messenger proteins released by white blood cells as well as other cells) that create further inflammation and damage.
* When NfkB is activated in skin cells along with another transcription factor called AP-1, it can lead to wrinkles in the skin. (That sounds like normal aging!)
* When NfkB is activated in the brain, it can lead to Alzheimer's disease, and activated in other organs it can lead to cancer.
* When NfkB is activated in the pancreas, it can lead to the destruction of the B-cells of the pancreas, which are the sole source of insulin, resulting in diabetes.
* NfkB blocks the ability to utilize insulin effectively, which leads to the storage of body fat, causing us to gain weight and have great difficulty shedding the pounds.
With NF-kB activated, even thin animals develop insulin resistance and diabetes as though they were obese. Perhaps more importantly, with NF-kB inhibited, obese animals do not develop insulin resistance or diabetes.
Higher levels of Mg - 'cause LOW levels ACTIVATE NFkB
Choline - 'cause a fatty liver (choline deficient) flips on NFkB
Ibuprofen
ASA...actually....salicylates
High NFkB is inversely correlated with the hemaglobin level
Insulin (acidic)...Bb prefers sugar to insulin..but ongoing insulin not possible, not healthy...glucagon steps in to downregulate.
Let's look at this from another perspective:
Bb is locking onto OUR DNA. DNA is a chain of amino acids (proteins) that is WEAKLY held together by hydrogen bonds...like a ladder, with hydrogen being a rung on the ladder.
When the DNA chain is broken, this would theoretically release hydrogen.
Now when there is too much hydrogen IN the cells...
``Under acidosis hydrogen ions enter the cell and potassium and free magnesium leave the cell.''
Now with excess hydrogen IN the cell this signals metabolic acidosis and the need for the bicarbonates.
In steps melatonin which contains an indole...a hydrogen double bonded to nitrogen. Nitrogen stimulates bicarbonate release in the intestines.
Bicarbonates remove excess hydrogen.
The pain from inflammation and the fatigue are very early signs of this disease.
Very early on (at the rash stage) there is a ``significant'' loss of magnesium which we know from a Romanian Cancer Hospital abstract titled: ``Lyme disease and magnesium deficiency''.
The amt. of loss, that which has left the cells (Mg-ATP) appears far greater than one would expect if released from only infected cells.
One would logically assume the magnesium was released from one of the body's storage areas, the major ``detox'' organ of the body, the liver.
The reasons why the body chose to release this mineral into the blood stream in addition to that which left the infected cells are many.
Magnesium looks to INactivate PFK and INactivate HMG CoA reductase...effectively putting the brakes on the glycolysis and cholesterol pathways simultaneously.
Along with calcium, it is needed to make healthy antibodies. It is needed to make all proteins, including enzymes and hormones. It is an anti-inflammatory and anti-histamine. It is a natural calcium channel blocker.
Magnesium, in large doses can displace zinc. Magnesium can block the loss of protein kinase C (Bb contains a protein kinase C inhibitor). It raises HDL which in turn reduces inflammation. It stimulates DNA repair.
And high levels of Mg INactivate NFkB.
Now...there is one thing that has been bothering me. Bb has a Mg transporter protein. Now what is the function of this protein? It would seem Bb wouldn't want Mg present if it can INactivate PFK, block the loss of protein kinase C, etc.
But...this protein apparently is essential to cell replication.
``Riboswitches are a recently discovered class of gene expression regulators. They control gene expression through a segment of messenger RNA (mRNA)--the copy of a gene that is used to produce a protein--that interacts with a target molecule to regulate its own translation into protein.
Usually, the protein regulated by the riboswitch is part of the cellular machinery that regulates the levels of the target molecule.
When the switch detects that magnesium has dropped to too low a level, it can boost the translation of the RNA--meaning the cell produces more of the transporter protein, thereby correcting the magnesium deficiency.
Every energy-producing reaction in the cell depends on magnesium as an accompanying cofactor for the cell's main energy molecule, ATP. Magnesium is also essential for the stability of the cell's membranes and its protein-producing ribosomes.
Groisman noted. ``And they will likely be involved in similar sensing mechanisms.''
The proteins that transport magnesium into the cell--MgtA and MgtB--had been know for decades, Groisman said.
And he and his colleagues discovered a decade ago that a regulatory system they called PhoP/PhoQ switches the genes for the transporters on or off in response to changing magnesium levels.
``But before this work, it wasn't suspected at all that a riboswitch might sense magnesium levels in the cell,'' Groisman said.
``Although there was no reason to think there should be any additional regulation, we found evidence that there was, indeed, an independent magnesium sensor in the cell,'' he said.
One piece of evidence came in the form of a mutation in the Salmonella bacterium that the researchers studied. That mutation in the PhoQ protein should have rendered the cell unable to respond to low magnesium levels, but the transporter genes remained sensitive to fluctuations in the mineral, said Groisman.
So, the researchers decided to analyze in detail how the mRNA molecule for mgtA responded to magnesium, in hopes of discovering a basis for magnesium-sensing. To do so, they dissected the function of the components of the Salmonella bacterium's mRNA for mgtA by systematically altering those parts' function and observing the results.
Their studies revealed that a region at one end of the mRNA molecule--which is not translated into the MgtA protein--responded to levels of magnesium.
A specific structure in this untranslated region, they showed, adopted different shapes depending on the level of magnesium in the bacterium.
Their studies revealed that a region at one end of the mRNA molecule--which is not translated into the MgtA protein--responded to levels of magnesium.
A specific structure in this untranslated region, they showed, adopted different shapes depending on the level of magnesium in the bacterium.
``Although we still have much work to do to understand the system, our analysis indicates that, in response to different magnesium levels, these different structures either allow or prevent the full-length messenger RNA from being translated,'' said Groisman.
He noted that the sequence of the untranslated region is conserved across many organisms, which indicates that it has a critical regulatory role.
In further studies, Groisman and his colleagues hope to understand in greater structural detail how the riboswitch senses magnesium levels--pinpointing the particular part of the molecule influenced by magnesium.
Also, he said, the researchers will seek to understand how this magnesium sensor applies the brakes on translation of the mRNA into the magnesium transporter protein, MgtA.
Researchers from Children's Hospital and Regional Medical Center in Seattle and the University of Washington School of Medicine have identified a magnesium transport protein that is essential to cell replication.
The research results, published today in the July 25 issue of Cell, show that tumor cells containing the protein divide rapidly, while cells lacking the protein become magnesium deficient and unable to divide.
"Our results indicated that this magnesium transport protein has a role in mediating magnesium uptake into cells. Special properties of the protein include forming a pore in the cell wall for magnesium to move through and an enzyme, which modifies other cellular proteins," said Dr. Scharenberg.
If this transporter protein is too abundant (in mice so far) it looks like there is an increased Mg and Ca LOSS via the urine:
``Insulin administration completely corrected the hyperglycemia-associated hypercalciuria and hypermagnesiuria, and reversed the increase of calcium and magnesium transporter abundance.''
Kidney International (2006) 69, 1786-1791. doi:10.1038/sj.ki.5000344; published online 22 March 2006
But we know that insulin shock doesn't work to cure lyme. It was tried by a doctor in Atlanta.
Salmonella (also have a Mg transporter protein):
``The influx of Mg2+ in Salmonella typhimurium LT-2 was studied by both kinetic and genetic techniques.
Wild-type cells grown in a high MgSO4 concentration (10 mM) exhibited a Km of 15 microM for Mg2+ influx, with a Vmax of 0.25 nmol of Mg2+ per min per 10(8) cells.
The apparent Km decreased to 3 microM, and the Vmax increased 60% after growth in a low MgSO4 concentration (10 microM).
Co2+ was a simple competitive *inhibitor* (Ki = 30 microM) of Mg2+ influx in cells grown in high Mg2+ concentrations but blocked only a portion of the Mg2+ influx in cells grown in low Mg2+ concentrations.''
If Mg levels drop ``significantly'' at the onset of lyme disease and if the pathogen and even the beneficial bacteria (and yeast) are taking whatever Mg is consumed, then it appears the lyme patient would be continuously low in Mg levels which then might impact Bb's protein expression.
``Movement through the carbonic acid system is fluid and constant. What this means is that water (H2O) can combine with CO2 and form carbonic acid. If necessary, carbonic acid (H2CO3) can then break up to form hydrogen ions (H+) and bicarbonate (HCO3).''
If there is a low level of CO2 in the blood in metabolic acidosis then there would be less carbonic acid (H2CO3) formed which can break up to form hydrogen ions (H+) and bicarbonate (HCO3).
This would indicate a bicarbonate loss...and need for additional to raise the pH.
Is it carbonic acid? Supply a bicarbonate + hydrogen -> carbonic acid.
Mg bicarbonate?
I do find it interesting that melatonin, NFkB and Magnesium transporter proteins are being researched by cancer specialists. My research indicates there are a number of pathogens (bacterial and viral) as well as situations (toxic exposure) that damage the DNA and lead to cancer.
Personally...I'd take lecithin (for choline and phosphorus)
Personally...I might try a little L-tyrosine
Personally, I'd take (not on the list) d-ribose and CoQ10
Personally, I'd take Pharmanex vits (esp. for the ginkgo)
I would EAT dark berries...YUM!
By now you should know me well enough ;-) that you know I am not talking about "once a day".
I believe small doses more often is really important.
For pain, MY choice is Bufferin or if not strong enough...Advil.
But FIRST...I'd restore the health of my gut with loading doses of good probiotics...and then maintenance.
There are other supplements that can indeed help and might be nec. depending on the pathogen load and the length of infection. Example: if digestive problems, might need help by supp. digestive enzymes for awhile.
Incidentally...I do understand pain and inflammation. I do not have much of a disc left between L4-L5...2 surgeries. I use ice packs often at night when sitting and reading/watching TV and I just keep going...keep moving throughout the day. I try not to give in to the pain.
Bet you are not surprised I'm a "fighter". LOL.
Posted by 6t5frlane (Member # 8628) on :
OK Marnie......I'm sure many of us here are not at your scientific level so....I read on the Arthritis board someone touting SOD Suoperoxide Dismutase. Also Wobenzyme N. would they be helpful for us or those with autoimmune issues. They also talk about SOD as maybe having an effect for ALS.Thanks
Posted by Marnie (Member # 773) on :
Corrected Juvenon ingredients...Thanks "Welcome" for catching my mistake...I have to stop posting at 4:30 am...
Bb and many, many other pathogens come "prepared"...with their own SOD.
SOD looks to rid the really bad superoxides.
Then what's left over is H2O2 which has to be reduced, so in steps the other 2 antioxidant enzymes: catalase and glutathione.
Posted by 6t5frlane (Member # 8628) on :
Marnie, I'm sorry My Lyme brain just does not get it. Could you comment again on SOD and WobenzymeN...for auto immune issues as well as Lyme and even ALS......
Posted by 6t5frlane (Member # 8628) on :
Marnie??? Thanks,can youanswer my post when you get a chance ref...SOD
Posted by Marnie (Member # 773) on :
I need an "undo last move"...I just erased all I had typed.
Starting over...
You can take all the antioxidants in the world to try to prevent DNA damage, but to knock out Bb which is CAUSING the DNA damage, we have to understand exactly what it is doing.
More importantly we must look closely at clues our body gives us as to how the body thinks it can destroy Bb. What are all the backup routes it takes to keep us alive? What goes up, what drops? Why?
Bb wiggles its way into the cells and makes the inside of the cells very acidic.
Now...the command center of the cell says to Miss Magnesium, "This cell is under attack and needs to be very acidic to destroy bad boy Borris that is in here and you are going to be destroyed too, so take a hike. Go instead into general circulation... to help make antibodies (with your friend-competitor Charlie Calcium), to help keep inflammation under control to the best of your ability, to quickly shut down angiotensin II and stop excess cholesterol production, and to INactivate PFK. Do your job(s). HURRY!"
Now from a slightly more technical standpoint, but one I hope you will understand:
To me, it looks like Bb locks onto our DNA strands INSIDE the cells. It looks like a ladder with hydrogen as the "rungs". The vertical strands are chains of amino acids...proteins.
Hydogen DNA bonds are really weak...the weakest in the body.
So, it looks like those bonds are broken = up goes the amt. of free floating hydrogen IN the cells and this might trigger Mg to leave the cells. Now the inside of the cell is acidic.
But Bb has a Mg transporter protein, so it can call for as much or as little Mg as it wants....enough to survive, but not enough to bond to our ATP as Mg-ATP to supply energy to that cell.
Bb makes its own ATP via the "glycolysis"/sugar route. We make it primarily thru the oxygen route although we can use both routes. ATP needs phosphate/phosphorus via either route!
(Too many hydrogens IN the cells = fewer outside = lower pH = metabolic acidosis.)Blood CO2 levels drop.
The Mg-ATP...to make energy... bond is broken. Now we make less energy in that cell. ATP is an energy carrier...but it needs Mg to work.
Inside the cells one is likely to see: (1)broken DNA strands (proteins - chains of amino acids)with Bb attached sucking away at the amino acids and (2) hydrogen...and (3) ATP with no Mg.
Now...meanwhile, it looks like when this happens, when the inside of the cell becomes too acidic, this triggers the cell command center to activate an enzyme (NFkB) to START the immune response. Since it takes a few DAYS for antibodies to be made...TNF alpha will go up first. Ouch. "I ache all over."
This response goes on and on and on...too much TNF alpha triggers angiotensin II (cholesterol is released...actually it's VLDL...very low density kind) from the liver. VLDL is very much like LDL...the "lousy" cholesterol.
This is what Bb wants. VLDL looks like it might contain what Bb is really after...choline.
All gram negative pathogens are missing acids. They need ours.
That's not to say Bb isn't sapping us of other nutrients too!
"Choline is needed to make VLDL."
If we can stop/lower TNF alpha, we theoretically should be able to stop the "cholesterol" pathway that Bb is taking...stop TNF alpha from triggering angiotensin II from triggering the release of VLDL...very low density lipoprotein. Think of it as "baby cholesterol".
But, this isn't the best/safest approach as blocking TNF alpha "side effect" is STILL cancer (DNA damage). We need to work "backwards".
IMO... this is the real problem:
Mg drops, Ca tries to go into the cells, TNF alpha kicks up, angiotensin II kicks in.
If we go back to the beginning (Mg drops)..and give a LOT more Mg (the right kind), we have a fighting chance. I don't think we had enough, fast enough, to counter the severe toxicity this pathogen triggers...from multiple pathways all at once.
From the Romanian abstracts...a LOT, a HUGE amt., of Mg was released to try to fight. There was a "significant" Mg loss right at the outset (the time of the rash).
But...to maintain the pH balance...the kidneys will dump "excess" Mg within a 2 hour time frame.
Since Bb does seem to need Mg...why not attach it to something it doesn't want...a bicarbonate? Citrates convert to bicarbonates. That makes Mg citrate/Mg bicarbonate "attractive".
If we can get that INTO the cells, if Bb takes it up...the bicarbonate theoretically should counter any excess hydrogen in the cells and make the INSIDE OF the cell more alkaline and...at the same time INactivate PFK.
Looks like Bb is perfectly happy hanging around in an acidic environment.
The oxygen connection...
We need oxygen, but it also is toxic to us in "excess" and to pathogens) because excess -> "superoxides" -> hydrogen peroxide.
Now both superoxides and hydrogen peroxide can cause cell death and the death of most pathogens.
We can't have this happen, so we have (3)antioxidant enzymes to protect us...to breakdown that superoxide and hydrogen peroxide.
They are: superoxide dismutase (SOD), glutathione peroxidase and catalase.
The problem is...so do many of our worse pathogens. They can breakdown superoxides and H2O2...which helps them survive.
Repeat...the really bad germs contain antioxidant enzymes to prevent their own destruction by superoxides and H2O2.
If superoxide and hydrogen peroxide breakdown too fast or if a pathogen can breakdown these toxic oxygen compounds to "save its own skin", our 1st level defense system is kapoot.
Interjecting something: it would appear that hyperbaric oxygen would generate more superoxides than Bb can handle. It appears ozone saunas work differently by depleting the antioxidant enzymes that breakdown superoxide and hydrogen peroxide. In both cases -> an increase in superoxide and hydrogen peroxide.
Pick your poison.
There is a 3rd antioxidant enzyme that WE have, but Bb does NOT. It is our most abundant anti-oxidant enzyme...catalase...and why it is not kicking in maybe related to what is happening in the liver even though our cells throughout appear to contain some of this antioxidant enzyme (catalase).
If Bb is using our SOD and our glutathione ie., the nutrients we need to make these enzymes, then the body will call for help...the fat stored vitamins A and E...which we KNOW drop in lyme to help out.
Vitamin E (esp.) looks to be very important...esp. from a liver, pancreas and brain protection viewpoint.
Vitamin A...is a 2-edged sword. While it does seem to downregulate eye damaging TNF alpha, it UPregulates choline acetyltransferase. This maybe because all our cells must have cholesterol for their outer cell walls...including the cells of our eyes.
Bb looks to be using many of our nutrients, many of our proteins, many of our enzymes to survive.
Bb looks to ACTIVATE a number of our defensive enzymes:
1. NFkB - tiggers inflammation response
2. HMG CoA reductase - triggers cholesterol production
3. PFK - triggers sugar, in a round-about way
and maybe:
4. PKC...protein kinase C (because Bb has a "PKC inhibitor"...there are many, many kinds)...we'll talk about this another time.
We need to INactivate all of the above.
I know Mg will INactivate PFK and HMG CoA reductase. I KNOW Mg is also capable of stimulating DNA REPAIR (so is another nutrient helpful in protecting DNA).
It appears IF we can get enough Mg back INTO the cells, this might solve the problem from a LOT of aspects.
(But HOW...normally ATP pumps Mg into the cells.)
Since Hydrogen is one thing that normally INactivates PFK (brakes on the sugar-to-make ATP route)...this is odd. One would logically think, if Bb is "PFK dependent" how could it survive in that hydrogen rich acidic environment?
The other things that INactivate PFK include: H2O2. Now...if Bb is breaking down superoxides via the antioxidant SOD and then breaking down H2O2 (utilizing another antioxidant enzyme - glutathione peroxidase)...H2O2 -> H2O and O...which maybe reacting with some of the H = OH or HO? Not good!
Now Bb needs a LITTLE oxygen, not much, to survive. It has to have some, but too much maybe overwhelming to its defense. Because too much looks to -> a LOT of superoxides.
What else INactivates PFK? Citrates. Citrates convert to bicarbonates. Make the cell more alkaline...turn off glycolysis, "force" the oxygen route.
What is our body's response? Melatonin, to trigger *bicarbonate* release from the intestine. When coming down with a disease -> "Im tired. I need to sleep. I don't feel good."
So...it looks to me that Mg citrate/bicarbonate maybe the primary nutrient to change the INTRAcellular acidosis.
Now..we can reduce inflammation (TNF alpha) via Humira, etc. and it looks like antibiotics do alter the immune response too, but...
If we don't get Mg levels back up, cancer will happen...in time. Pathogen triggers DNA damage triggers cancer. Cells go wild.
Cancer ONLY happens in an acidic environment. If Mg-ATP remains low, Ca will continue to be pulled out of storage (bones) and this will trigger TNF alpha (acidic protein)...ongoing.
We MUST get the inside of the cells less acidic.
We HAVE to get Mg and the nutrients to make ATP back IN.
So...what is absolutely critical as far as nutrients go if you're broke?
1. Heal the gut first. You will get NOWHERE if your gut isn't healthy. The beneficial bacteria make many B vitamins for us...more than we consume AND they (lactobacillus) help bind zinc. Keep your digestive system healthy (!)...maintenance doses.
2. Mg citrate/bicarbonate...yes, I know about the latter...keep looking, it's there.
3. Lecithin. Need to restore choline and phosphorus.
4. B vitamins.
5. Vitamin E.
Now...this will NOT WORK if you continue to destroy the beneficial bacteria via abx. and further deplete various nutrients via abx.
And...many will say, "You want me to take the nutrients that Bb wants?! Are you nuts?"
Mg is needed to MAKE all proteins...these include immunoglobulins (antibodies), all the hormones and enzymes. It is absolutely critical to making energy...it, and only it, is attached to ATP.
Mg + phosphorus...ATP. Now...
Choline...
"A choline-deficient diet increased DNA damage in humans."
B vitamins work in harmony with Mg. We need the beneficial bacteria to make a LOT of B vitamins for us.
Restore the balance to heal. This will NOT happen overnight (!) and do not expect that as your own immune system kicks in...as you replenish the nutrients, the dormant forms will not emerge, they will.
Finally...when I have those not so cute teeny tiny ants in my kitchen, I put a little honey on a small square of aluminum foil and sprinkle a tiny amt. of boric acid on the honey and mix it with a toothpick, carefully, because boric acid is a powerful poison. I "lure" the ants with the honey, the boric acid does them in.
We can and WILL outsmart Bb.
Mg to INactivate HMG CoA reductase. Mg to INactivate PFK Mg to reduce inflammation (Mg is an anti-inflammatory, Ca triggers) Mg (along with Ca) to make HEALTHY antibodies..your OWN "antibiotics". Mg to stimulate DNA repair. Mg to displace Zn.
Mg attached to what...citrate/bicarbonate.
Small doses of the above nutrients more often is the key. Not massive doses all at once!!!
How did Dr. Valletta manage to cure RA, ulcerative colitis and invasive cancer in 6 months (although he was able to "jumpstart" this with IV doses)? (Patent: "Magnesium for autoimmune".)
What did he use?
Magnesium pyrophosphate and sub (lingual - under the tongue) B6.
Mg and B6 work together -> CoQ10.
Phosphorus...ya mean like in ATP...or
Mg + phosphorus = Mg-ATP...Power the cells.
Catching on?
Posted by 6t5frlane (Member # 8628) on :