Treatments With Tumor Dissolving Potential

[Obi-wan]

@Travis said " Without enzymes such as fatty acid synthase the body is incapable of creating excessive lipids even if it could" and we all know niacinamide and aspirin inhibit FAS!

 

[Inaut]

My head just exploded

:)

Thanks everyone!

 

[Catcream]

I’m about to start taking diamox , an anahydrase inhibitor , in an attempt to manage my bone metastases . Also co2 baths . Both suggestions of RP. Will update.

 

[Amazoniac]

Curcumin and cancer: An "old-age" disease with an "age-old" solution

 

[raypeatclips]

Curcumin and cancer: An "old-age" disease with an "age-old" solution

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Sorry. We can't find the page you're looking for.

http://www.cancer.cytoluminator.com/cancer-photodynamic-therapy/curcumin.pdf

 

[Amazoniac]

Page Not Found
Sorry. We can't find the page you're looking for.

Page Found
But the title was there!

 

[Obi-wan]

@Travis stated "Without enzymes such as fatty acid synthase the body is incapable of creating excessive lipids even if it could, having lowered plasma glucose, and thus has no need to uncouple the mitochondria to commandeer its acetyl-CoA. In such a situation, with the cell operating under a more respirational suite of enzymes: the Warburg Effect evaporates, lactic acid decreases, and methylglyoxal in increased"


ACV/BS turns to acetate and is used as acetyl-CoA to couple mitochondria and evaporate the Warburg Effect. Aspirin would stop FAS, COX 1 & 2. Ubiquniol would aid in ECT. Thoughts?

 

[Travis]

@Travis stated "Without enzymes such as fatty acid synthase the body is incapable of creating excessive lipids even if it could, having lowered plasma glucose, and thus has no need to uncouple the mitochondria to commandeer its acetyl-CoA. In such a situation, with the cell operating under a more respirational suite of enzymes: the Warburg Effect evaporates, lactic acid decreases, and methylglyoxal in increased"


ACV/BS turns to acetate and is used as acetyl-CoA to couple mitochondria and evaporate the Warburg Effect. Aspirin would stop FAS, COX 1 & 2. Ubiquniol would aid in ECT. Thoughts?

Acetate is a very common cellular product, yet less often found in the extracellular space. There's some reason to believe that a larger percentage of extracellular acetate would affiliate with potassium over sodium, entering the cell as potassium acetate while displacing the latter. An increased intracellular K⁺/Na⁺ ratio translates into a greater absolute membrane potential, perhaps the single macroscopic parameter most highly correlated with mitotic rate. Alpha-tocopherol acetate does something similar yet chaperones calcium, an intracellular ion having other functions besides. Although osmotic balance is certainly a prime factor in cellular proliferation, this is no less a determinant than polyamine and glyoxylase systems. So from time to time, a brief mention of other natural ancillaries is still called-for—lest the should be forgotten: baicalein, lapachol, and selenomethionine have all been shown highly effective in slowing and preventing the proliferation of carcinogenic cells.

 

[Inaut]

slightly off topic but how do you recommend we take pau d'arco @Travis ? tea, extract, raw powder etc..? thanks

 

[Travis]

slightly off topic but how do you recommend we take pau d'arco @Travis ? tea, extract, raw powder etc..? thanks

Personally, I'd would add the bark to coffee grounds in a French press—medium roast ground course. I have actually done this and it tastes good, just as pleasant had cinnamon bark been used instead. Yet baicalein is certainly no kitten and this can be purchased in purified form. Baicalein is indisputably the most powerful natural glyoxylase inhibitor among flavanoids, an observation demonstrated repeatedly through direct binding and inferred by its effect on cells. Baicalein has been shown to inhibit the translocation of both the androgen and the estrogen receptor in multiple studies, despite not binding them directly, and it has been confirmed repeatedly to catalyze the rate of carbonic anhydrase. These functions can be achieved by methylglyoxal acting through arginine ➝ hydroimidizalone signalling. I have confirmed that both the androgen and estrogen receptors have key arginine residues, the loss of which corresponds to loss of activity (i.e. androgen insensitivity). A key arginine binds the 3-keto group of DHT in the androgen receptor, in a manner completely analogous to how the ERα binds the 3-hydroxy group of estradiol. Carbonic anhydrase has many arginines, and the substitution* of one of them in particular translates into a 250-fold reduction in enzyme activity. The transformation of this arginine into a hydroimidizalone, by methylglyoxal, would be expected to enhance the transmission of the 'proton wire' leading out of the catalytic domain. Carbonic anhydrase has free access to its substrates carbon dioxide and water, and it's rate is limited only by the removal of its two products: the bicarbonate ion (HCO₃⁻) and protons (H⁺). It has been proven by enzyme kineticists that proton transfer is indeed the rate limiting step, perhaps the reason why adding pyrroles to solution always increases the enzyme's rate: A small planar dibasic molecule having a pKa ≈ 15.7 would be an ideal catalyst of rapid proton transmission in aqueous solution. Pyrrole has a pKa = 16.5 and has been shown to increase the rate of carbonic anhydrase. The pKa of imidazole is 14.9.

Four years before it's ability to inhibit glyoxylase had been discovered, baicalein had been shown to inhibit 12-lipoxygenase. This is still what the molecule is best known for, and you will in fact often see it listed as 12-lipoxygenase inhibitor. The arginine leading into 12-lipoxygenase is so important that it's called the 'Hornung determinant' and is responsible for binding the carboxy-end of fatty acids, swinging them into it's oxidizing catalytic domain. The arginine ➝ hydroimidizalone transformation of Hornung determinant—induced by methylgyoxal—would be expected to abrogate lipid binding.

[*] I think arginine had been replaced by valine, yet would expect a histidine substitution to effect a lesser change in kinetic rate. Since the carbonic anhydrase enzyme had been expressed and purified from yeast cells normally have high intracellular methylglyoxal concentrations, it could be presumed that particular carbonic anhydrase enzymes used in the abovementioned kinetic study did in fact had their exposed arginines pre-converted into hydroimidizalone..​

 

[Obi-wan]

Personally, I'd would add the bark to coffee grounds in a French press—medium roast ground course. I have actually done this and it tastes good, just as pleasant had cinnamon bark been used instead. Yet baicalein is certainly no kitten and this can be purchased in purified form. Baicalein is indisputably the most powerful natural glyoxylase inhibitor among flavanoids, an observation demonstrated repeatedly through direct binding and inferred by its effect on cells. Baicalein has been shown to inhibit the translocation of both the androgen and the estrogen receptor in multiple studies, despite not binding them directly, and it has been confirmed repeatedly to catalyze the rate of carbonic anhydrase. These functions can be achieved by methylglyoxal acting through arginine ➝ hydroimidizalone signalling. I have confirmed that both the androgen and estrogen receptors have key arginine residues, the loss of which corresponds to loss of activity (i.e. androgen insensitivity). A key arginine binds the 3-keto group of DHT in the androgen receptor, in a manner completely analogous to how the ERα binds the 3-hydroxy group of estradiol. Carbonic anhydrase has many arginines, and the substitution* of one of them in particular translates into a 250-fold reduction in enzyme activity. The transformation of this arginine into a hydroimidizalone, by methylglyoxal, would be expected to enhance the transmission of the 'proton wire' leading out of the catalytic domain. Carbonic anhydrase has free access to its substrates carbon dioxide and water, and it's rate is limited only by the removal of its two products: the bicarbonate ion (HCO₃⁻) and protons (H⁺). It has been proven by enzyme kineticists that proton transfer is indeed the rate limiting step, perhaps the reason why adding pyrroles to solution always increases the enzyme's rate: A small planar dibasic molecule having a pKa ≈ 15.7 would be an ideal catalyst of rapid proton transmission in aqueous solution. Pyrrole has a pKa = 16.5 and has been shown to increase the rate of carbonic anhydrase. The pKa of imidazole is 14.9.

Four years before it's ability to inhibit glyoxylase had been discovered, baicalein had been shown to inhibit 12-lipoxygenase. This is still what the molecule is best known for, and you will in fact often see it listed as 12-lipoxygenase inhibitor. The arginine leading into 12-lipoxygenase is so important that it's called the 'Hornung determinant' and is responsible for binding the carboxy-end of fatty acids, swinging them into it's oxidizing catalytic domain. The arginine ➝ hydroimidizalone transformation of Hornung determinant—induced by methylgyoxal—would be expected to abrogate lipid binding.

[*] I think arginine had been replaced by valine, yet would expect a histidine substitution to effect a lesser change in kinetic rate. Since the carbonic anhydrase enzyme had been expressed and purified from yeast cells normally have high intracellular methylglyoxal concentrations, it could be presumed that particular carbonic anhydrase enzymes used in the abovementioned kinetic study did in fact had their exposed arginines pre-converted into hydroimidizalone..​

Baicalein is an inhibitor of CYP2C9,[16] an enzyme of the cytochrome P450 system that metabolizes drugs in the body.-Wikipedia. This would interfere with Xtandi (Enzalutamide), which I am currently taking...

Enzalutamide is a moderate to strong inducer of multiple cytochrome P450 enzymes including CYP3A4, CYP2C9, and CYP2C19 and hence has a high potential for clinically relevant drug interactions.[2] Circulating concentrations of enzalutamide may be altered by inhibitors and inducers of CYP2C8 and CYP3A4, and should be avoided if possible.

Enzalutamide acts as a selective silent antagonist of the androgen receptor (AR), the biological target of androgens like testosterone and dihydrotestosterone (DHT). Unlike the first-generation NSAA bicalutamide, enzalutamide does not promote translocation of AR to the cell nucleus and in addition prevents binding of AR to deoxyribonucleic acid (DNA) and AR to coactivator proteins.[37] As such, it has been described as an AR signaling inhibitor in addition to antagonist.

 

[Obi-wan]

Acetate is a very common cellular product, yet less often found in the extracellular space. There's some reason to believe that a larger percentage of extracellular acetate would affiliate with potassium over sodium, entering the cell as potassium acetate while displacing the latter. An increased intracellular K⁺/Na⁺ ratio translates into a greater absolute membrane potential, perhaps the single macroscopic parameter most highly correlated with mitotic rate. Alpha-tocopherol acetate does something similar yet chaperones calcium, an intracellular ion having other functions besides. Although osmotic balance is certainly a prime factor in cellular proliferation, this is no less a determinant than polyamine and glyoxylase systems. So from time to time, a brief mention of other natural ancillaries is still called-for—lest the should be forgotten: baicalein, lapachol, and selenomethionine have all been shown highly effective in slowing and preventing the proliferation of carcinogenic cells.

I have ordered potassium bicarbonate and will try it with ACV...

 

[Obi-wan]

@Travis said "Acetate is a very common cellular product" but in cancer Pyruvate will not convert to acetyl-CoA due to Pyruvate kinase...instead it converts into Lactic acid. No acetyl-CoA no Krebs cycle no Krebs cycle no ECT no ECT no oxidative phosphorylation...end result fermentation...Warburg effect...

Acetate is a common anion in biology. It is mainly utilized by organisms in the form of acetyl coenzyme A.[5] -Wikipedia

Once the machinery is re coupled in aerobic organisms the energy needed to fuel biological functions is produced in the mitochondria via the electron transport chain. In addition to energy, reactive oxygen species (ROS) with the potential to cause cellular damage are produced. ROS can damage lipid, DNA, RNA, and proteins.

Cancer[edit]
ROS are constantly generated and eliminated in the biological system and are required to drive regulatory pathways.[30] Under normal physiological conditions, cells control ROS levels by balancing the generation of ROS with their elimination by scavenging system. But under oxidative stress conditions, excessive ROS can damage cellular proteins, lipids and DNA, leading to fatal lesions in cell that contribute to carcinogenesis.

Cancer cells exhibit greater ROS stress than normal cells do, partly due to oncogenic stimulation, increased metabolic activity and mitochondrial malfunction. ROS is a double-edged sword. On one hand, at low levels, ROS facilitates cancer cell survival since cell-cycle progression driven by growth factors and receptor tyrosine kinases (RTK) require ROS for activation[31] and chronic inflammation, a major mediator of cancer, is regulated by ROS. On the other hand, a high level of ROS can suppress tumor growth through the sustained activation of cell-cycle inhibitor[32][33] and induction of cell death as well as senescence by damaging macromolecules. In fact, most of the chemotherapeutic and radiotherapeutic agents kill cancer cells by augmenting ROS stress.[34][35] The ability of cancer cells to distinguish between ROS as a survival or apoptotic signal is controlled by the dosage, duration, type, and site of ROS production. Modest levels of ROS are required for cancer cells to survive, whereas excessive levels kill them.

Metabolic adaptation in tumors balances the cells' need for energy with equally important need for macromolecular building blocks and tighter control of redox balance. As a result, production of NADPH is greatly enhanced, which functions as a cofactor to provide reducing power in many enzymatic reactions for macromolecular biosynthesis and at the same time rescuing the cells from excessive ROS produced during rapid proliferation. Cells counterbalance the detrimental effects of ROS by producing antioxidant molecules, such as reduced glutathione (GSH) and thioredoxin (TRX), which rely on the reducing power of NADPH to maintain their activities.[36]

As I mentioned on another thread I stopped taking Vit E

Most risk factors associated with cancer interact with cells through the generation of ROS. ROS then activate various transcription factors such as nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), activator protein-1 (AP-1), hypoxia-inducible factor-1α and signal transducer and activator of transcription 3 (STAT3), leading to expression of proteins that control inflammation; cellular transformation; tumor cell survival; tumor cell proliferation; and invasion, agiogenesis as well as metastasis. And ROS also control the expression of various tumor suppressor genes such as p53, retinoblastoma gene (Rb), and phosphatase and tensin homolog (PTEN).[37]

Carcinogenesis[edit]
ROS-related oxidation of DNA is one of the main causes of mutations, which can produce several types of DNA damage, including non-bulky (8-oxoguanine and formamidopyrimidine) and bulky (cyclopurine and etheno adducts) base modifications, abasic sites, non-conventional single-strand breaks, protein-DNA adducts, and intra/interstrand DNA crosslinks.[38] It has been estimated that endogenous ROS produced via normal cell metabolism modify approximately 20,000 bases of DNA per day in a single cell. 8-oxoguanine is the most abundant among various oxidized nitrogeneous bases observed. During DNA replication, DNA polymerase mispairs 8-oxoguanine with adenine, leading to a G→T transversion mutation. The resulting genomic instability directly contributes to carcinogenesis. Cellular transformation leads to cancer and interaction of atypical PKC-ζ isoform with p47phox controls ROS production and transformation from apoptotic cancer stem cells through blebbishield emergency program,.[39][40]

Cell proliferation[edit]
Uncontrolled proliferation is a hallmark of cancer cells. Both exogenous and endogenous ROS have been shown to enhance proliferation of cancer cells. The role of ROS in promoting tumor proliferation is further supported by the observation that agents with potential to inhibit ROS generation can also inhibit cancer cell proliferation.[37] Although ROS can promote tumor cell proliferation, a great increase in ROS has been associated with reduced cancer cell proliferation by induction of G2/M cell cycle arrest; increased phosphorylation of ataxia telangiectasia mutated (ATM), checkpoint kinase 1 (Chk 1), Chk 2; and reduced cell division cycle 25 homolog c (CDC25).[41]

Cell death[edit]
A cancer cell can die in three ways: apoptosis, necrosis, and autophagy. Excessive ROS can induce apoptosis through both the extrinsic and intrinsic pathways.[42] In the extrinsic pathway of apoptosis, ROS are generated by Fas ligand as an upstream event for Fas activation via phosphorylation, which is necessary for subsequent recruitment of Fas-associated protein with death domain and caspase 8 as well as apoptosis induction.[37] In the intrinsic pathway, ROS function to facilitate cytochrome c release by activating pore-stabilizing proteins (Bcl-2 and Bcl-xL) as well as inhibiting pore-destabilizing proteins (Bcl-2-associated X protein, Bcl-2 homologous antagonist/killer).[43] The intrinsic pathway is also known as the caspase cascade and is induced through mitochondrial damage which triggers the release of cytochrome c. DNA damage, oxidative stress, and loss of mitochondrial membrane potential lead to the release of the pro-apoptotic proteins mentioned above stimulating apoptosis.[44] Mitochondrial damage is closely linked to apoptosis and since mitochondria are easily targeted there is potential for cancer therapy.[45]

The cytotoxic nature of ROS is a driving force behind apoptosis, but in even higher amounts, ROS can result in both apoptosis and necrosis, a form of uncontrolled cell death, in cancer cells.[46]

Numerous studies have shown the pathways and associations between ROS levels and apoptosis, but a newer line of study has connected ROS levels and autophagy.[47] ROS can also induce cell death through autophagy, which is a self-catabolic process involving sequestration of cytoplasmic contents (exhausted or damaged organelles and protein aggregates) for degradation in lysosomes.[48] Therefore, autophagy can also regulate the cell’s health in times of oxidative stress. Autophagy can be induced by ROS levels through many different pathways in the cell in an attempt to dispose of harmful organelles and prevent damage, such as carcinogens, without inducing apoptosis.[49] Autophagic cell death can be prompted by the over expression of autophagy where the cell digests too much of itself in an attempt to minimize the damage and can no longer survive. When this type of cell death occurs, an increase or loss of control of autophagy regulating genes is commonly co-observed.[50] Thus, once a more in-depth understanding of autophagic cell death is attained and its relation to ROS, this form of programmed cell death may serve as a future cancer therapy. Autophagy and apoptosis are two different cell death mechanisms brought on by high levels of ROS in the cells, however; autophagy and apoptosis rarely act through strictly independent pathways. There is a clear connection between ROS and autophagy and a correlation seen between excessive amounts of ROS leading to apoptosis.[49] The depolarization of the mitochondrial membrane is also characteristic of the initiation of autophagy. When mitochondria are damaged and begin to release ROS, autophagy is initiated to dispose of the damaging organelle. If a drug targets mitochondria and creates ROS, autophagy may dispose of so many mitochondria and other damaged organelles that the cell is no longer viable. The extensive amount of ROS and mitochondrial damage may also signal for apoptosis. The balance of autophagy within the cell and the crosstalk between autophagy and apoptosis mediated by ROS is crucial for a cell’s survival. This crosstalk and connection between autophagy and apoptosis could be a mechanism targeted by cancer therapies or used in combination therapies for highly resistant cancers.

Tumor cell invasion, angiogenesis and metastasis[edit]
After growth factor stimulation of RTKs, ROS can trigger activation of signaling pathways involved in cell migration and invasion such as members of the mitogen activated protein kinase (MAPK) family – extracellular regulated kinase (ERK), c-jun NH-2 terminal kinase (JNK) and p38 MAPK. ROS can also promote migration by augmenting phosphorylation of the focal adhesion kinase (FAK) p130Cas and paxilin.[51]

Both in vitro and in vivo, ROS have been shown to induce transcription factors and modulate signaling molecules involved in angiogenesis (MMP, VEGF) and metastasis (upregulation of AP-1, CXCR4, AKT and downregulation of PTEN).[37]

Chronic inflammation and cancer[edit]
Experimental and epidemiologic research over the past several years has indicated close associations among ROS, chronic inflammation, and cancer.[37] ROS induces chronic inflammation by the induction of COX-2, inflammatory cytokines (TNFα, interleukin 1 (IL-1), IL-6), chemokines (IL-8, CXCR4) and pro-inflammatory transcription factors (NF-κB).[37] These chemokines and chemokine receptors, in turn, promote invasion and metastasis of various tumor types.

But Aspirin stops Cox 1&2

Cancer therapy[edit]
Both ROS-elevating and ROS-eliminating strategies have been developed with the former being predominantly used. Cancer cells with elevated ROS levels depend heavily on the antioxidant defense system. ROS-elevating drugs further increase cellular ROS stress level, either by direct ROS-generation (e.g. motexafin gadolinium, elesclomol) or by agents that abrogate the inherent antioxidant system such as SOD inhibitor (e.g. ATN-224, 2-methoxyestradiol) and GSH inhibitor (e.g. PEITC, buthionine sulfoximine (BSO)). The result is an overall increase in endogenous ROS, which when above a cellular tolerability threshold, may induce cell death.[52][53] On the other hand, normal cells appear to have, under lower basal stress and reserve, a higher capacity to cope with additional ROS-generating insults than cancer cells do.[52][54] Therefore, the elevation of ROS in all cells can be used to achieve the selective killing of cancer cells.

Radiotherapy also relies on ROS toxicity to eradicate tumor cells. Radiotherapy uses X-rays, γ-rays as well as heavy particle radiation such as protons and neutrons to induce ROS-mediated cell death and mitotic failure.[37]

Due to the dual role of ROS, both prooxidant and antioxidant-based anticancer agents have been developed. However, modulation of ROS signaling alone seems not to be an ideal approach due to adaptation of cancer cells to ROS stress, redundant pathways for supporting cancer growth and toxicity from ROS-generating anticancer drugs. Combinations of ROS-generating drugs with pharmaceuticals that can break the redox adaptation could be a better strategy for enhancing cancer cell cytotoxicity.[37]

James Watson[55] and others[56] have proposed that lack of intracellular ROS due to a lack of physical exercise may contribute to the malignant progression of cancer, because spikes of ROS are needed to correctly fold proteins in the endoplasmatic reticulum and low ROS levels may thus aspecifically hamper the formation of tumor suppressor proteins.[56] Since physical exercise induces temporary spikes of ROS, this may explain why physical exercise is beneficial for cancer patient prognosis.[57] Moreover, high inducers of ROS such as 2-deoxy-D-glucose and carbohydrate-based inducers of cellular stress induce cancer cell death more potently because they exploit cancer cell high avidity for sugars.[58]

Cut and paste from Wikipedia with my comments.

 

[Amazoniac]

- Nature curing cancer – review on structural modification studies with natural active compounds having anti-tumor efficiency
- Essential Trace Elements and Cancer

 

[Obi-wan]

- Nature curing cancer – review on structural modification studies with natural active compounds having anti-tumor efficiency
- Essential Trace Elements and Cancer

The studies talk about immune response so lets look at ROS some more

More on ROS:

Pathogen response[edit]
When a plant recognizes an attacking pathogen, one of the first induced reactions is to rapidly produce superoxide (O−2) or hydrogen peroxide (H
2O2) to strengthen the cell wall. This prevents the spread of the pathogen to other parts of the plant, essentially forming a net around the pathogen to restrict movement and reproduction.

In the mammalian host, ROS is induced as an antimicrobial defense. To highlight the importance of this defense, individuals with chronic granulomatous disease who have deficiencies in generating ROS, are highly susceptible to infection by a broad range of microbes including Salmonella enterica, Staphylococcus aureus, Serratia marcescens, and Aspergillus spp.

The exact manner in which ROS defends the host from invading microbe is not fully understood. One of the more likely modes of defense is damage to microbial DNA. Studies using Salmonella demonstrated that DNA repair mechanisms were required to resist killing by ROS. More recently, a role for ROS in antiviral defense mechanisms has been demonstrated via Rig-like helicase-1 and mitochondrial antiviral signaling protein. Increased levels of ROS potentiate signaling through this mitochondria-associated antiviral receptor to activate interferon regulatory factor (IRF)-3, IRF-7, and nuclear factor kappa B (NF-κB), resulting in an antiviral state.[15] Respiratory epithelial cells were recently demonstrated to induce mitrochondrial ROS in response to influenza infection. This induction of ROS led to the induction of type III interferon and the induction of an antiviral state, limiting viral replication.[16] In host defense against mycobacteria, ROS play a role, although direct killing is likely not the key mechanism; rather, ROS likely affect ROS-dependent signalling controls, such as cytokine production, autophagy, and granuloma formation.[17] -Wikipedia

ROS are produced as a normal product of cellular metabolism. In particular, one major contributor to oxidative damage is hydrogen peroxide (H2O2).

Cells called phagocytes engulf pathogens and then use hydrogen peroxide to destroy them. The peroxide is toxic to both the cell and the pathogen and so is kept within a special compartment, called a phagosome

I found this interesting- Hydrogen peroxide is also used for tooth whitening. It can be found in most whitening toothpastes. Hydrogen peroxide has shown positive results involving teeth lightness and chroma shade parameters. It works by oxidizing colored pigments onto the enamel where the shade of the tooth can indeed become lighter. Hydrogen peroxide can be mixed with baking soda and salt to make a home-made toothpaste.[68]

So now I brush with 3% Hydrogen peroxide and BS 2x per day. My teeth are definitely whiter...but since this is done orally I wonder if I increase cellular ROS...

 

[Amazoniac]

The studies talk about immune response so lets look at ROS some more

More on ROS:

Pathogen response[edit]
When a plant recognizes an attacking pathogen, one of the first induced reactions is to rapidly produce superoxide (O−2) or hydrogen peroxide (H
2O2) to strengthen the cell wall. This prevents the spread of the pathogen to other parts of the plant, essentially forming a net around the pathogen to restrict movement and reproduction.

In the mammalian host, ROS is induced as an antimicrobial defense. To highlight the importance of this defense, individuals with chronic granulomatous disease who have deficiencies in generating ROS, are highly susceptible to infection by a broad range of microbes including Salmonella enterica, Staphylococcus aureus, Serratia marcescens, and Aspergillus spp.

The exact manner in which ROS defends the host from invading microbe is not fully understood. One of the more likely modes of defense is damage to microbial DNA. Studies using Salmonella demonstrated that DNA repair mechanisms were required to resist killing by ROS. More recently, a role for ROS in antiviral defense mechanisms has been demonstrated via Rig-like helicase-1 and mitochondrial antiviral signaling protein. Increased levels of ROS potentiate signaling through this mitochondria-associated antiviral receptor to activate interferon regulatory factor (IRF)-3, IRF-7, and nuclear factor kappa B (NF-κB), resulting in an antiviral state.[15] Respiratory epithelial cells were recently demonstrated to induce mitrochondrial ROS in response to influenza infection. This induction of ROS led to the induction of type III interferon and the induction of an antiviral state, limiting viral replication.[16] In host defense against mycobacteria, ROS play a role, although direct killing is likely not the key mechanism; rather, ROS likely affect ROS-dependent signalling controls, such as cytokine production, autophagy, and granuloma formation.[17] -Wikipedia

ROS are produced as a normal product of cellular metabolism. In particular, one major contributor to oxidative damage is hydrogen peroxide (H2O2),

I found this interesting- Hydrogen peroxide is also used for tooth whitening. It can be found in most whitening toothpastes. Hydrogen peroxide has shown positive results involving teeth lightness and chroma shade parameters. It works by oxidizing colored pigments onto the enamel where the shade of the tooth can indeed become lighter. Hydrogen peroxide can be mixed with baking soda and salt to make a home-made toothpaste.[68]

So now I brush with 3% Hydrogen peroxide and BS 2x per day. My teeth are definitely whiter...but since this is done orally I wonder if I increase cellular ROS...

The idea of focusing on oxidative stress to recover seems to me just a milder version of the barbaric conventional approach. The goal must be to restore oxidation in the least stressful way.

 

[Obi-wan]

The idea of focusing on oxidative stress to recover seems to me just a milder version of the barbaric conventional approach. The goal must be to restore oxidation in the least stressful way.

But " On the other hand, normal cells appear to have, under lower basal stress and reserve, a higher capacity to cope with additional ROS-generating insults than cancer cells do.[52][54] Therefore, the elevation of ROS in all cells can be used to achieve the selective killing of cancer cells." -Wikipedia

 

[Obi-wan]

According to Warburg cancer is a disconnect to mitochondria metabolism which ACV/ BS restarts thus creating ROS again...the way a normal cell is engineered...

 

[Amazoniac]

But " On the other hand, normal cells appear to have, under lower basal stress and reserve, a higher capacity to cope with additional ROS-generating insults than cancer cells do.[52][54] Therefore, the elevation of ROS in all cells can be used to achieve the selective killing of cancer cells." -Wikipedia

But one can get caught up in the trees instead of looking at the forest. When the body has what it needs and is stimulated, it will control the amount of oxidative stress needed to take care of the problem. But when the focus is on stress, you tend to disturb more than needed and compromise other parts. Just an opinion.

 

[Obi-wan]

But one can get caught up in the trees instead of looking at the forest. When the body has what it needs and is stimulated, it will control the amount of oxidative stress needed to take care of the problem. But when the focus is on stress, you tend to disturb more than needed and compromise other parts. Just an opinion.

"When the body has what it needs and is stimulated, it will control the amount of oxidative stress needed to take care of the problem" Yes via:

Superoxide dismutase (SOD, EC 1.15.1.1) is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O2−) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage.[2] Hydrogen peroxide is also damaging and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen.-Wikipedia