You already know that collagen plays a key role in keeping your joints healthy… alleviating arthritis… boosting gut health… improving skin elasticity… and protecting bones.
Now – in a major treatment breakthrough – researchers have discovered that collagen can also prevent cancer from spreading by forcing dormant tumor cells to stay asleep.
Of course, you won’t hear about this new research from your oncologist. They’re too focused on prescribing Big Pharma’s chemotherapy and immunotherapy drugs.
But researchers have shown that collagen is a powerful weapon against cancer.
Let me sHow you what I mean…
Collagen is a jelly-like “structural” protein composed mainly of three long amino-acid chains, wound together in a tight triple helix.
It’s your body’s most abundant protein, making up about one-third of all protein in the human body.
There are three main types of collagens – types I, II, and III. The stability and resilience of the protein increases with each type.
Type I is the weakest and type III the strongest.
The protein is self-renewing and is produced mainly by connective tissue cells. Its molecules anchor cells to each other by forming a mesh-like scaffolding that provides strength, structure, stability, and flexibility to your skin and connective tissue throughout your body.
In a recent study, resEarchers found that excess levels of collagen type I can convert to glutamine, which in turn can promote growth in tumor cells.1
But collagen type III, the most powerful form of the protein, is a different story.
Researchers at the Tisch Cancer Institute at Mount Sinai Hospital used high-resolution imaging to track breast, neck, and head cancer cells.
They found that tumor cells remained dormant by secreting type III collagen in their immediAte environment.2
They also found that the cancer cells awakened when the levels of collagen type III began to decline. But they became dormant again when collagen III levels increased.
This means that we now have a new tool that can both predict and prevent cancer relapses.
This backs up an earlier study by researchers at the University of Texas MD Anderson Cancer Center.
The problem is that the level of collagen type III decreases significantly as you age.3 The good news is that there are many easy ways to boost the level of this anti-cancer moLecule.
Get The Most Out Of Your Cancer-Fighting Collagen
Bone broth is a rich source of collagen type II, which is great for skin and joint support. But its levels of collagen type III are too small to help fight cancer.
Instead I recommend the following:
1. Boost vitamin C levels.
You already know vitamin C is a great anti-aging antioxidant and anti-inflammatory. It beaTs back the free radicals that cause oxidative stress as well as the inflammation that’s at the root of modern chronic diseases.
Now studies reveal it also stimulates the production of collagen type III in your body.4
Your best food sources of vitamin C are acerola cherries, rose hips, sweet peppers, and camu camu. Yet it’s almost impossible to get what you need from food.
But taking a drugstore supplement just won’t cut it. You see, your body can only absorb 500 mg at a time — and that’s nowhere near enough. Instead, I recommend you take 3,000 mg of liposomal-encapsulated vitamin C.
Liposomal is a technique that wraps the vitamin C molecule in a thin layer of fat. These fats are called phospholipids — and that’s the same thing your cell membranes are made up of. That allows for easy delivery and 98% absorption.
I recommend taking 1,000 mg three times a day – and consume it with food to avoid an upset stomach. If you’re fighting cancer, bump your dose to between 7,000 and 10,000 mg. Or consider getting a vitamin C-rich Myers cocktail.
2. Stop eating carbs and refined sugars:
A diet that’s high in sugar and processed carbohydrates produce enzymes that degrade collagen, diminishing its structural strength and stability. This Happens when excess sugar molecules attach themselves to collagen fibers through a process called glycation. This produces harmful free radicals called advanced glycation end products, or AGEs.
Collagen is extremely vulnerable to AGEs. A carb-heavy diet degrades collagen type III into the more fragile type l.5
3. Reduce your stress level:
Research shows stress has a devastating impact on your body’s ability to produce collagen. Stress causes your adrenal glands to release the hormone cortisol and pro-inflammatory molecules that degrade collagen.6
In addition to exercise and more sleep, my favorite stress buster is a mindfulness meditation exercise used by the U.S. Marines. Here’s the technique…
- Sit in a comfortable position, close your eyes.
- Let your awareness settle on the movement of your breath.
- Follow the in-breath and out-breath, perhaps by saying “breathing in, breathing out” quietly to yourself.
- Sit upright, with spine straightened and chin tucked in, while you calmly observe your breath.
- Do this for 10 to 15 minutes a day.
Try to do this every day. It helps to lower blood pressure, slow down your thoughts, refresh body and mind, and reverse the stress that destroys collagen.
To Your Good Health,
Al Sears, MD, CNS
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References:
- Hsu KS, at al. “Cancer cell survival depends on collagen uptake into tumor-associated stroma”. Nat Commun. 2022; 13:7078.
- De Martino D, et al. “Collagens in cancer: Structural regulators and guardians of cancer progression.” Cancer Res. 2023 May 2;83(9):1386-1392.
- Liu X, et al. “Type III collagen is crucial for collagen I fibrillogenesis and for normal cardiovascular development.” PNAS 94. 1997.1852–1856.
- Gref R, et al. “Vitamin C–squalene bioconjugate promotes epidermal thickening and collagen production in human skin.” Sci Rep. 2020;10:16883.
- Monnier VM, et al. “Skin collagen advanced glycation end products (AGEs) and the long-term progression of sub-clinical cardiovascular disease in type 1 diabetes.” Cardiovasc Diabetol. 2015 Sep 5;14:118.
- Siwik DA, et al. “Interleukin-1beta and tumor necrosis factor-alpha decrease collagen synthesis and increase matrix metalloproteinase activity in cardiac fibroblasts in vitro.” Circ Res. 2000 Jun 23;86(12):1259-65.
