And if selenium causes oxidative stress that means it would never lower it, which we know is not true (depending in the type you take).
That makes logical sense.
I am wondering if someone has high blood levels of selenium maybe their body isn't able to put it where it is needed. Two things I am going to look at are genetic issue and rate limiting precursor. Does that make sense?
Similar to copper being such a necessary metal but causing so many problems by being biounavailable due to lack of ceruloplasmin.
Also, I am thinking that seleno-cysteine might be the type I would want.
From Linus Pauling Institute:
Twenty-five genes coding for selenoproteins have been identified in humans
(3). The insertion of selenocysteine into selenoproteins during
translation is directed by the presence of a selenocysteine-insertion sequence (SECIS) within selenoprotein
mRNAs. Briefly, the recognition of SECIS by the translational machinery results in the recruitment of specific translational factors that decode in-frame UGA codons by inserting selenocysteine into elongating selenoproteins
(4).
Research is gradually uncovering the metabolic functions of all human selenoproteins, including splicing variants
(3). Some of the selenoproteins with an identified function include:
mce-anchorGlutathione peroxidases
Five selenium-containing glutathione peroxidases (GPx1-4 and GPx6) have been identified: GPx1 (cytosolic GPx), GPx2 (epithelial cell-specific GPx expressed in intestinal lining and lungs), GPx3 (highly expressed in thyroid gland and kidneys), GPx4 (phospholipid-hydroperoxide GPx; PHGPx), and GPx6 (expressed in the olfactory epithelium)
(4). GPx isoenzymes are all
antioxidant enzymes that reduce potentially damaging
reactive oxygen species (ROS), such as hydrogen peroxide and lipid hydroperoxides, to harmless products like water and alcohols by coupling their
reduction with the
oxidation of
glutathione.