Marnie
Frequent Contributor (5K+ posts)
Member # 773
posted
Yes, I know that Bb is utilizing OUR manganese and it would be logical we shouldn't take extra...or should we?
OR is Bb actually depleting our Mn stores?
A lack of this nutrient might be disasterous to our mitochondria, the powerhouses of our cells. Here is why:
"In humans, three forms of superoxide dismutase are present. SOD1 is located in the cytoplasm, SOD2 in the mitochondria and SOD3 is extracellular.
SOD1 and SOD3 contain copper and zinc, while SOD2 has manganese in its reactive centre. The genes are located on chromosomes 21, 6 and 4, respectively (21q22.1, 6q25.3 and 4p15.3-p15.1)."
Above from a dictionary definition.
The Sod2 gene for Mn−superoxide dismutase (MnSOD),
an intramitochondrial free radical scavenging enzyme
that is the first line of defense against superoxide produced as a
byproduct of oxidative phosphorylation,
was inactivated by homologous recombination. Homozygous mutant mice die within the first 10 days of life with a dilated cardiomyopathy, accumulation of lipid in liver and skeletal muscle, and metabolic acidosis.
Cytochemical analysis revealed a severe reduction in succinate dehydrogenase (complex II) and aconitase (a TCA cycle enzyme) activities in the heart and, to a lesser extent, in other organs.
These findings indicate that MnSOD is required for normal biological function of tissues by maintaining the integrity of mitochondrial enzymes susceptible to direct inactivation by superoxide.
If Bb is "forcing" the glycolysis pathway (via tyrosine) rather than the "oxygen" route to make ATP (oxidative phosphorylation) it looks like less of this enzyme, MnSOD would be produced leading to damage of the powerhouses of the cells.
Are we "upregulating" the other SOD enzymes and does this lead to less Cu and Zn?
We KNOW that prostate cancer cells contain LESS zinc. Since zinc is so important for immune function, that would be disasterous.
Also,
Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine.
F Yamakura, H Taka, T Fujimura, K Murayama Department of Chemistry, Juntendo University School of Medicine, Inba, Chiba 270-16, Japan.
Peroxynitrite has recently been implicated in the inactivation of many enzymes.
However, little has been reported on the structural basis of the inactivation reaction.
This study proposes that nitration of a specific
tyrosine residue
is responsible for inactivation of recombinant human mitochondrial manganese-superoxide dismutase (Mn-SOD) by peroxynitrite."
To counter this (too much peroxynitrite, too little MnSOD), it looks like the body calls for vitamin E (specifically the gamma portion of that vitamin) to help prevent the damage done by peroxynitrite.
Vitamin C may play a role also. It looks to impact nitrates->nitrites. (Halt the conversion.) Unfortunately we don't STORE that water soluable antioxidant.
Side note: SOD1 is "implicated" in ALS.
Simply "food for thought".
To complicate matters further ;-(
Indeed, studies using rabbit aortas or bovine coronary arteries have shown that
inhibition of vascular SOD activity results in a rapid impairment of endothelium-dependent, NO�-mediated vasodilation,
suggesting that SOD levels are critical for the ability of NO� to modulate vascular tone.6,7
Furthermore, reduced vascular SOD activity induced by dietary copper restriction was associated with an impaired endothelium-dependent vasodilation due to increased inactivation of NO�.8
Moreover, recombinant ecSOD was shown to be effective in protecting NO� bioactivity against the detrimental effects of O2�-.9
Given these observations, several recent studies have focused on the regulation of vascular ecSOD expression and activity.
Interestingly, NO� itself was identified as one of the major regulators of vascular ecSOD expression. NO� donors potently induced ecSOD expression in vascular smooth muscle cells, while lack of endothelial NO� production in eNOS knockout mice dramatically reduced vascular ecSOD levels.10
This could represent an important "feed-forward" mechanism whereby NO� enhances its biological effects.10 In addition, ecSOD expression in vascular smooth muscle cells was found to be downregulated by the inflammatory cytokine TNF 11 and homocysteine.12
Rapid inactivation of Ile58Thr MnSOD at the elevated temperatures associated with fever and inflammation could provide an early advantage by killing infected cells, but also would increase superoxide-mediated oxidative damage and perhaps contribute to late-onset diseases.
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