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Re: dopamine oxidation » Larry Hoover

Posted by raybakes on November 26, 2004, at 13:00:09

In reply to Re: dopamine oxidation » raybakes, posted by Larry Hoover on November 25, 2004, at 5:23:14

>
> > I see the oxidative stress as the root, and acidosis as the outcome.
> >
> > I can go with that!
>
> So, it still is oxidative stress that needs controlling, to avoid the acidotic response.

I agree, but find 'oxidative stress' too vague and feel I need to know the specific pattern of oxidative stress for each condition, and what gets oxidised!


>
> I've been using inosine, and it certainly doesn't seem to have any adverse effects. It's totally inexpensive, and readily scavenges peroxynitrite. I'll leave the superoxide to my dismutase enzymes, which work best with lots of alphalipoic backing them up.

Think I might try inosine to see how it feels - my only concern was if it raises adenosine, could it affect the adenosine receptor? Also does xanthine oxidase have any negative effects.
>
> > The balance of arginine/NOS/biopterin/methylation seems important. Low biopterin or low arginine can switch NOS to produce superoxide instead of nitric oxide. Arginine without methyl factors can increase homocysteine.

> how?

'Interactions of peroxynitrite, tetrahydrobiopterin, ascorbic acid, and thiols: implications for uncoupling endothelial nitric-oxide synthase.'


http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12692136

"Recent evidence also indicates that iNOS-induced pathophysiological effects involve substrate deficiency. Thus, at low concentrations of L-arginine iNOS produces both NO and superoxide anions, which results in the increased synthesis of the highly reactive, detrimental oxidant peroxynitrite"

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12967769

"Both endothelial NO synthase (eNOS) and inducible NO synthase (iNOS) isoforms are expressed in the atherothrombotic vasculature and, owing to a loss of substrate or reducing cofactors required for NO synthesis, undergo enzymatic "uncoupling" leading to both a loss of NO production and an increase in superoxide anion generation."

"Owing to the sizeable methylation stress created by supplemental L-arginine in these animals (creatine synthesis accounts for 70% of the total utilization of labile methyl groups in mammals under normal circumstances16), the remethylation of homocysteine to methionine would be limited. Thus, transsulfuration, which is localized principally to the liver, is likely to have been the principal metabolic mechanism for eliminating the increase in homocysteine"

http://atvb.ahajournals.org/cgi/content/full/23/1/3


> MSM takes the load off of methionine for sulphation. How are you with methionine?
>

I'm fine with methionine as long as I take methyl factors - otherwise, I'm awful! Do even better with it if I take a little lysine too - think carnitine is very important for me. Interesting that homocysteine is linked with apoptosis.


> Yes, me too. In then end, it's what makes you feel better, not whether you can explain why it does so.

Yes, I tend to try things first - if it feels good, I try to find out why - but frequently the first few attempts to understand can be misguided!

Ray


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