Vitamin D, Calcium and mineral metabolism with Dr Ray Peat and Kate Deering

md_a

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We’ve had Dr. Peat on the podcast before, and it actually ended up being our most downloaded WinAtLife podcast. So, we brought him back again to discuss vitamin D, calcium and mineral metabolism.

There’s so much good information in this one! Dr. Peat offers up a lot of clarity when it comes to the great vitamin D debate. So, should you supplement vitamin D? Should you not? What else should you know when it comes to vitamin D and your metabolic health?

As a reminder Vitamin D has many names
The three most mentioned in this podcast are
Cholecalciferol also known as D3 (what is in food or supplements)
"Stored D" also know as calcidiol / 25OHD /hydroxycholecalciferol
"Active D" also know as calcitriol / 1,25D

Dr. Peat uses the references of 25OHD /hydroxycholecalciferol (stored) and 1,25D (active)

In this episode we talk about...
➡️ The purpose of Vitamin D
➡️ How is vitamin D metabolised and stored
➡️ How much D is too much?
➡️ The difference between Active and Stored Vitamin D
➡️ Can "stored D" have active properties?
➡️ Is elevated Active D (1,25D) a good thing?
➡️ Do Vitamin D supplements suppress the immune system?
➡️ The Vitamin D "receptor" theory-is it correct?
➡️ Are blood levels of stored D (25OHD) correct?
➡️ What are optimal stored Vitamin D levels?
➡️ The relationship between D and Ca
➡️ Understanding the importance of parathyroid hormone (PTH)
➡️ What can affect PTH besides Calcium and Vitamin D
➡️ What causes calcified tissue
➡️ Understanding the calcium -magnesium connection
➡️ What ratios, if any, are optimal for minerals?
➡️ Understanding Hair Tissue Mineral Analysis? Are they accurate?

Check out the entire podcast episode on Apple Podcasts, Spotify, Google Podcast, Stitcher, and iHeart Radio by searching for The Winatlife Podcast.

At the end of the podcast, Ray was asked about a study involving Vitamin D supplements and Bone density.

Here is the study and his answer:

Effect of High-Dose Vitamin D Supplementation on Volumetric Bone Density and Bone Strength

A Randomized Clinical Trial.

https://jamanetwork.com/journals/jama/fullarticle/2748796--i

"They didn’t control their phosphate intake, so it’s possible that the high dose D was now and then increasing the 1,25-dihydroxy D, taking some calcium out of the bone. A problem with judging bone mineral content with x-rays is that, in stress, the fat in bone is reduced, and replaced by water, causing more of the x-rays to be absorbed, making the bone seem denser.

High-dose vitamin D without extra calcium supplementation has been associated with increased levels of the active vitamin D metabolite 1, 25(OH)2 vitamin D (calcitriol), and an increase in CTx."
-
Check out the entire podcast episode on Apple Podcasts, Spotify, Google Podcast, Stitcher, and iHeart Radio by searching for The Winatlife Podcast.

 

Amazoniac

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40:45 - Dietary medium-chain triglycerides promote oral allergic sensitization and orally induced anaphylaxis to peanut protein in mice ?

It's a sensitizing agent to a dangerous toxin, whose exposure should be regulated as drugs. Fortunately it is: the liver hydroxylates killciol to killcidiol and then can conjugate the garbage.

However, if you think of it, it's only a tiny amount of fat in question. Oil floats on water, a drop should be less than 0.05 g. People are probably not taking the supplement on empty stomach, the fats of a meal would make such amount insignificant, if not add more of the fatty acids that are being blamed. Even when there's no meal, the lipids that recirculate combine with what's ingested, and since venom D isn't bound to vehicle oils, the others will prevail.

Soon we'll be witnessing Raj recommending venom D for hypervenomosis D, and if there's deterioration, it's due to some impurity in the product. Nevertheless, it would be interesting for our vendors to try a batch using clarified butter instead of olive oil as vehicle, there are no risks involved.

Might explain this:
- Be Wary Of Vitamin D Supplementation
 

Inaut

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Such a good interview. Kate, if you are reading this——you are awesome !!!!!!! :) :) :)
 

Amazoniac

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Katherines, don't mind the criticisms, it's so that Raj's claims aren't taken at facing the values, but the guy is a walking encyclopeatia; the same goes for Jorge. Just as impressive is the amount of killcium that he appears to consume and not be bothered by additional venom D in the presence of modest quantities of antidotes.


He mentioned something about indecent lamp, not just ultraviolent light, being capable of contaminating the body with more venom D. How does it work? It must be in speeding up the 'thermal isomerization' of existing prevenom to venom D. If you search for '7-dehydroatherosclerol absorption spectrum', the range doesn't coincide with that of the lamps.


On excess poisonol somehow competing with thyrotoxine in transthyretin/prealbumin to the point of displacing it, and that this explains the metabolic impairment upon intoxication with poisonol, does it really occur? Transthyretin is not a major transporter of T4 in the body. Just like he mentioned that hindering the cells' ability to interact with killcitriol makes them responsive to killcidiol, the principle would have to apply here as well, others means to transport it could kick in.

- Retinol-Binding Protein Interferes with Transthyretin-Mediated β-Amyloid Aggregation Inhibition

"TTR is a homotetrameric soluble protein (55 kDa) that is synthesized in both the liver and the choroid plexus and circulates in blood (3–7 μM) and CSF (0.1–0.4 μM).[28,29] The protein consists of four identical 127-residue subunits, each with two four-stranded antiparallel β-sheets and a short α-helix (Figure 1).[30,31] Extensive hydrogen bonding between β-strands H and F of two monomers forms the dimer. The packing of two dimers produces a hydrophobic channel in which the thyroid hormone thyroxine (T4) coordinates to residues in the inner β- sheet.[32] Two T4 molecules may bind per TTR tetramer. The first T4 binds with high affinity (Kd ~ 10 nM) to TTR, but the second has lower affinity due to negative cooperativity; the TTR-T4 complex predominantly exists with a 1:1 stoichiometry in vivo.[33] TTR serves as the primary carrier of T4 in CSF and as a minor carrier in blood.[31,34] TTR also facilitates the delivery of retinol from blood to peripheral tissue through its interaction with retinol-binding protein (RBP; 21 kDa; 2–4 μM).[35] Most RBP (~95%) in circulation is complexed with TTR to prevent glomerular filtration and renal catabolism of RBP.[36] Holo-RBP (hRBP) coordinates with three subunits of TTR, making contact with the EF helix loop, AB loop, and GH loop in subunits B and C as well as the FG loop in subunit A (Figure 1).[37,38] Although two hRBPs can bind per TTR tetramer, the predominant species in vivo is a 1:1 complex.[39] The affinity of hRBP for TTR (Kd ~ 0.20–0.35 μM)[37,40,41] decreases upon loss of retinol.[40] In human serum, approximately half of TTR is complexed with hRBP and 10–20% with T4. The RBP-binding sites on TTR are orthogonally positioned to the nonoverlapping thyroxine-binding sites;[32,37,38] no competition has been observed.[42]"​

- Thyroid Hormone Transport Proteins: Thyroxine-Binding Globulin, Transthyretin, and Albumin

"The presence of RBP does not interfere with T4 binding and vice versa."

"Despite the 20-fold higher concentration of TTR in serum relative to that of TBG, it plays a lesser role in iodothyronine transport. TTR is responsible for the transport of 15%–20% of T4. The first T4 molecule binds to TTR with a Ka that is approximately 100-fold higher than that for HSA and approximately 100-fold less than that for TBG (Table 1). Relative to T4, T3 has lower affinity and tetraiodoacetic acid has higher affinity for TTR. Among the drugs that compete with T4 binding to TTR are ethacrynic acid, salicylates, 2,4-dinitrophenol, and penicillin.

The average concentration of TTR in serum is 25 mg/dL and corresponds to a maximal binding capacity of 300 μg T4. Changes in TTR concentration have relatively little effect on the concentration of serum iodothyronines. Only 0.5% of the circulating TTR is occupied by T4."​
 

SOMO

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Among the drugs that compete with T4 binding to TTR are ethacrynic acid, salicylates, 2,4-dinitrophenol, and penicillin.
The average concentration of TTR in serum is 25 mg/dL and corresponds to a maximal binding capacity of 300 μg T4. Changes in TTR concentration have relatively little effect on the concentration of serum iodothyronines. Only 0.5% of the circulating TTR is occupied by T4."​
Do you think Aspirin/SA/Acetylsalicylic Acid can indirectly reduce T4->T3 conversion by competitively binding to TTR?
 

Hans

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Do you think Aspirin/SA/Acetylsalicylic Acid can indirectly reduce T4->T3 conversion by competitively binding to TTR?
I haven't seen studies showing that. On the contrary, aspirin increases fT3 and T3 uptake into cells. It basically has a pro-thyroid effect.
 
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