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The more Poison/"Vitamin A", the faster the body tries (TRIES) to get rid of it!

Here's a question for you.

If the body wants MORE of something, what would it do to the breakdown/metabolism pathways of that thing?  It would SLOW them down to conserve it, correct?

If they body wants LESS of something (toxic), what would it do to the breakdown/metabolism pathways of that thing?  It would SPEED THEM UP to get rid of it, correct?

The more retinoic acids (aka Poison/"Vitamin A") that the body has in it, the FASTER it ramps up the cytochrome systems in the liver to GET RID OF IT.  More explanation below the abstract.  This is called "self-induction", or "being induced by oneself/itself".

Induction of CYP26A1 by Metabolites of Retinoic Acid: Evidence That CYP26A1 Is an Important Enzyme in the Elimination of Active Retinoids

All-trans-retinoic acid (atRA), the active metabolite of vitamin A, induces gene transcription via binding to nuclear retinoic acid receptors (RARs). The primary hydroxylated metabolites formed from atRA by CYP26A1, and the subsequent metabolite 4-oxo-atRA, bind to RARs and potentially have biologic activity. Hence, CYP26A1, the main atRA hydroxylase, may function either to deplete bioactive retinoids or to form active metabolites. This study aimed to determine the role of CYP26A1 in modulating RAR activation via formation and elimination of active retinoids. After treatment of HepG2 cells with atRA, (4S)-OH-atRA, (4R)-OH-atRA, 4-oxo-atRA, and 18-OH-atRA, mRNAs of CYP26A1 and RARβ were increased 300- to 3000-fold, with 4-oxo-atRA and atRA being the most potent inducers. However, >60% of the 4-OH-atRA enantiomers were converted to 4-oxo-atRA in the first 12 hours of treatment, suggesting that the activity of the 4-OH-atRA was due to 4-oxo-atRA. In human hepatocytes, atRA, 4-OH-atRA, and 4-oxo-atRA induced CYP26A1 and 4-oxo-atRA formation was observed from 4-OH-atRA. In HepG2 cells, 4-oxo-atRA formation was observed even in the absence of CYP26A1 activity and this formation was not inhibited by ketoconazole. In human liver microsomes, 4-oxo-atRA formation was supported by NAD+, suggesting that 4-oxo-atRA formation is mediated by a microsomal alcohol dehydrogenase. Although 4-oxo-atRA was not formed by CYP26A1, it was depleted by CYP26A1 (Km = 63 nM and intrinsic clearance = 90 μl/min per pmol). Similarly, CYP26A1 depleted 18-OH-atRA and the 4-OH-atRA enantiomers. These data support the role of CYP26A1 to clear bioactive retinoids, and suggest that the enzyme forming active 4-oxo-atRA may be important in modulating retinoid action.

Induce (induction) = to cause something to happen.

What does the CYP (cytochrome P450) system do?

Basic Review of the Cytochrome P450 System

As the primary site of drug metabolism, the liver functions to detoxify and facilitate excretion of xenobiotics (foreign drugs or chemicals) by enzymatically converting lipid-soluble compounds to more water-soluble compounds. Drug metabolism is achieved through phase I reactions, phase II reactions, or both. The most common phase I reaction is oxidation, which is catalyzed by the CYP system (Gibson & Skett, 2001).

When a compound is put into the body, and the body then immediately ramps up the detoxification pathways of said compound, you can be QUITE sure that the body believes that compound is a POISON, and definitely not a vitamin!  The body itself is telling us it wants this poison OUT, not in.

Think about it.  What if every time you consumed a certain nutrient, your body greatly increased its speed of getting rid of it.  You would always be deficient! If you believe we are "wonderfully made" or "intelligently designed", why in the world would our system be set up to try to cause deficiency?  Doesn't make sense, does it?

We address both the Phase I (cytochrome) and Phase II detoxification pathways--as they specifically relate to both Poison/"Vitamin A" and glyphosate--in the Poison/"Vitamin A" and Glyphosate Detox Program.

Dr. Garrett Smith, the "Nutrition Detective"
Licensed Naturopathic Physician (NMD) in Arizona
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