Posted by Larry Hoover on September 5, 2003, at 8:30:19
In reply to Lar, Re:thyroid replacement , posted by tealady on September 2, 2003, at 22:52:47
I've been pondering this thyroid issue for a while. There's another line of inquiry to consider.
The deiodinase enzyme (generically) that converts T4 to T3 depends on adequate selenium, as we've discussed. Your lack of response to selenium would pretty much suggest that is dead end. However, there is a still unidentified cofactor for the enzyme that is a sulphur-bearing molecule.
Every time the deiodinase pulls an iodine off T4, it has to be restored to activity by a subsequent reaction with the sulphur molecule. This leads to what is known as ping-pong kinetics. It's like firing and reloading a gun.
The problem right now is that even the state of the art, cutting edge research has not further characterized that sulphur molecule, beyond the fact that it is a sulhydryl (thiol) structure. That's a hydrogen on a sulphur (S-H), analogous to an alcohol group.
So, it may be something to try, to load up on sulphur-containing foods. The obvious amino-acid supplement would be cysteine, or N-acectyl-cysteine (it has a sulfhydryl group). Foods would be egg yolk, onion, garlic (side-effects may be malodorous flatus). There's a conversion pathway in our bodies that requires adequate methionine, so maybe B12/folate/B6, and/or TMG (trimethylglycine, also known as betaine) would ensure that you're processing homocysteine adequately. MSM (methylsulfonylmethane) also takes a little burden off the sulfhydryl processes, so it may contribute.
I'm just brainstorming. Deiodinase is also permanently disable by exposure to a chemical known as PTU. I'll see if I can find out how that is regulated.
Lar
poster:Larry Hoover
thread:255272
URL: http://www.dr-bob.org/babble/20030902/msgs/257234.html