- Nov 16, 2012
That's more Eskin and Ghent stuff. Can you find a study by authors that don't have patents in iodine treatment??
This is a blatant conflict of interest.
There are some here: chemistry_trall
But ultimately the research on the subject seems limited.
I found studies that suggest different uptake mechanisms for I2 and I-:
This study shows the ability of cancerous prostate to take up I− and I2. NIS expression and the inhibition of I− uptake by ClO4− (specific inhibitor of NIS symporter) in normal and cancerous prostate confirm that iodide uptake is NIS dependent. ...
With regard to I2 uptake, no significant blockade by ClO4− was observed in any group, corroborating an NIS-independent mechanism. These data agree with studies in human cell lines of prostate and breast cancer (8,25). There is evidence that I2 uptake depends on protein synthesis, independent of ATP and Na+/K− ATPase (8). A NIS-independent mechanism for I2 uptake has also been demonstrated in sea urchin larvae and seaweeds (7,35), suggesting that this mechanism could be widespread in nature.
(Iodine Uptake and Prostate Cancer in the TRAMP Mouse Model)
A large body of data has demonstrated that several tissues share with the thyroid gland the capacity to actively accumulate iodide, including salivary glands, gastric mucosa, lactating mammary gland, the choroid plexus, ciliary body of the eye, lacrimal gland, thymus, skin, placenta, ovary, uterus, prostate and so on, and may either maintain or lose this ability under pathological conditions. The iodide transport system in these extrathyroidal tissues reveals several functional similarities to its thyroid counterpart, suchas inhibition by thiocyanate and perchlorate (KClO4), suggesting the presence of the specific iodine transporter called the sodium iodine symporter (NIS). However, only some of these organs express the enzymatic machinery to oxidize I-to I2, which is bound to cell components and exhibits physiological effects.
In thyroid and lactating mammary gland, I2 uptake is three times less than thyroid, and only about half of this I2 capture is inhibited by KClO4. In contrast, in nubile animals, mammary tissue and prostate captured 300 times less iodine than thyroid and four times less than lactating mammary gland, and NIS does not participate in their internalization. These findings strongly support previous data showing that this chemical form of iodine contributes to the maintenance of the normal integrity of the mammary gland.
The importance of I 2 as an oxidized chemical form of iodine agrees with our recent demonstration ( Alfaro-Hernandez, 2004 ) that the addition of I 2 , but not potassium iodide (KI), to mammary gland homogenates from virgin rats significantly decreases lipoperoxidation measured by the thiobarbituric acid reaction and expressed as malondialdehyde. The inability of I - to decrease lipoperoxidation may be explained by the absence of lactoperoxidase (LPO) in mammary glands from virgin rats, which is only present during pregnancy and lactation ( Strum, 1978 ).
Thus, we hypothesize that iodine generated by LPO activity is bound to an abundant and specific protein (e.g., thyroglobulin in the thyroid and casein in lactating mammary gland), whereas I2 or another oxidized form of iodine, obtained by deiodination or in the diet, binds to lipids and/or other membrane or nuclear components, and acts as an antioxidant and/or antiproliferative agent ( Aceves et al. , 2005 ). This notion is supported by our finding that in the tumoral mammary cell line MCF-7, I 2 but not I- supplement, is accompanied by antiproliferative effects and the appearance of iodinated proteins and lipids ( Arroyo-Helguera et al. , 2006 )