ironjustice

This study shows the effects of ferritin.
Ferritin is a storage site of iron .. and this storage site is argued
to be not .. needed .. because once one has red blood cells of proper
amount .. one doesn't need any **storage** iron of consequence.

This is evidenced in diabetes when the iron is lowered into .. "near
iron deficiency" .. the diabetes improves.

The ferritin is targeted by the .. milieu / inflammation ..
surrounding .. it .. DURING .. disease / inflammation .. and sooo ..
logically IF .. it / ferritin .. doesn't EXIST / near iron
deficiency / vegetarian / young bleeding women .. it couldn't BE ..
targeted.

<<snip>>
exacerbating the tissue damage
<<snip>>

http://www.pubmedcentral.nih.gov/art...?artid=1147255

Xanthine oxidase is able to mobilize iron from ferritin. This
mobilization can be blocked by 70% by superoxide dismutase, indicating
that part of its action is mediated by superoxide (O2-). Uric acid
induced the release of ferritin iron at concentrations normally found
in serum. The O2(-)-independent mobilization of ferritin iron by
xanthine oxidase cannot be attributed to uric acid, because uricase
did not influence the O2(-)-independent part and acetaldehyde, a
substrate for xanthine oxidase, also revealed an O2(-)-independent
part, although no uric acid was produced. Presumably the amount of
uric acid produced by xanthine oxidase and xanthine is insufficient to
release a measurable amount of iron from ferritin. The liberation of
iron from ferritin by xanthine oxidase has important consequences in
ischaemia and inflammation. In these circumstances xanthine oxidase,
formed from xanthine dehydrogenase, will stimulate the formation of a
non-protein-bound iron pool, and the O2(-)-produced by xanthine
oxidase, or granulocytes, will be converted by 'free' iron into much
more highly toxic oxygen species such as hydroxyl radicals (OH.),
exacerbating the tissue damage.


Who loves ya.
Tom


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