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A Collagen for Every Situation

A Collagen for Every Situation

Chett Binning is both a Nutrition and Health Coach and former competitive athlete. He finished his hockey career with Carleton University, where he also completed an Honours BA in Psychology. After this, he completed a Masters in Neuroscience (MSc) from Western University, and started his own company known as Brain Ignition. Chett offers health and nutrition consulting services to athletes and everyday people and is also the Scientific Specialist and Educator with ATP Labs, helping educate about ATPs unique formulations. You can find him online at www.brainignition.ca or on Instagram @brainignition 

 

Collagen is the most abundant protein in the body and makes up roughly 30% of total body protein. It’s most concentrated in skin, hair, connective tissue, and bones. In this article, we are going to focus mainly on the ‘non-skin’ benefits but first, we will review some basics. 

Does Supplementing Collagen Do Anything?

The short answer is yes. Pharmacological studies clearly show that collagen is either degraded to form free amino acids, or the peptides themselves (from hydrolyzed collagen peptides) are directly absorbed (1, 2, 3). Regardless, these reach the circulation after being absorbed in the intestine and eventually reach target tissues including dermis, cartilage, bone, and so on. Human intervention studies also show benefits of supplementing collagen (we’ll get into a few of these in this article).

The answer to whether it will be beneficial for the individual is dependent on one's diet. Technically you can get plenty of collagen from diet. It’s quite easy, just make sure you eat these foods every week:

  • Skin from chicken and fish
  • Bone marrow
  • Broths made from hocks, drumsticks, and turkey necks
  • And make sure you munch the ends off any meat bones you consume too

…………

Is anyone eating this? Probably 0.1% of people at the most. So, if you care about overall health then you should consider supplementing collagen.

The main reason is that collagenous protein has a few unique properties that “balance” other sources of protein. One of the most important being its high amount of the amino acid glycine, which is required for:

  • Making your own collagen
  • Making creatine
  • Making glutathione
  • Involved in bile conjugation
  • Functions as a neurotransmitter
  • And more…

Glycine also reduces inflammation, improves sleep, lowers advanced glycation end products (AGEs), functions as a neurotransmitter and more. (4)

Research strongly suggests that we need to consume AT LEAST 10g of glycine per day just to meet basic requirements. But as I mentioned unless you’re consuming these above food sources (or supplementing collagen) then you’re nowhere near 10g per day because it’s not found in ‘typical’ protein sources.

Arguably, Glycine also balances high intakes of the amino acid methionine which is concentrated in ‘typical’ protein rich foods (chicken breast, eggs, lean beef etc.). Excess methionine (unbalanced) may increase homocysteine which is a risk factor for cardiovascular illness.

Glycine is not the only unique and important quality of collagen but it’s the only one that we have time to discuss in this article.

Collagen As a Pre workout?

Research shows that intake of essential amino acids is more effective when taken pre workout vs post workout. One of the reasons is because exercise increases blood flow to working muscles by up to 324%.

There may be a similar benefit to pre workout collagen because of this.

“But collagen is not a complete protein. Why would I take it pre workout?”

You’re not taking collagen for muscle protein synthesis, you’re taking it for connective tissue health (injuries, joint health etc.)

So, let’s say you have a nagging injury. You’d probably want to drive resources to that area that are required for recovery, such as collagen. What’s the best way to get these resources there? Probably with enhanced blood flow via training.

Shaw and Gregory et al., found that pre workout supplementation with gelatin increased collagen synthesis after exercise in a dose dependent manner. This is one question that needs more research but, in the meantime, I’d say you have a lot to potentially gain and nothing to lose by trying it (5).

Shouldn’t I Add Tryptophan?

I’ve heard people argue that collagen must be “complete” for it to be absorbed and therefore supplements are “junk” if they don’t add it.

This would render all other incomplete amino acid supplements useless such as:

  • Supplemental glutamine
  • Glycine
  • BCAAs
  • Collagen

This would also mean that you don’t absorb protein from incomplete food sources.

But here’s the real kicker:

Studies that find a benefit of supplementing collagen do not add tryptophan.

For instance, the review in The Open Nutraceuticals Journal, 2015, 8, 29-42 reviewed at least 12 studies and concluded that:

  • Collagen has reliable absorption,
  • Collagen has consistent benefits in randomized clinical trials.

None of these studies added tryptophan when testing collagen.

Adding TRP Makes it More Beneficial for Workout Performance and Recovery

Research shows that it’s total protein intake (throughout the course of the day) that determines muscle protein synthesis, not what you’re consuming at each individual meal (6). So, unless you’re ONLY consuming collagenous protein it doesn’t matter.

Is It Actually Useless for Muscle Growth and Strength?

Lastly, studies have shown that collagen supplementation (without the addition of tryptophan) can increase muscle thickness.

In one study, supplementation led to a significantly greater increase in tendon cross sectional area (CSA) (+11.0%) compared with the PLA group (+4.7%). There was also a greater increase in muscle thickness in the collagen group (+7.3%) compared with the PLA group (+2.7%) (7).

Another study found that supplementation during 12 weeks of resistance training led to a more pronounced increase in leg muscle strength compared to a placebo control group in women (8):

  • Great reduction in fat during the training plan
  • Greater gain in hand grip strength
  • Greater increase in lean muscle
  • Great increase in leg strength

The Best Type of Collagen for Joint Pain and Symptoms of Osteoarthritis is the Type That is Poorly Absorbed

Yes, you read that correctly. MOST collagen supplements are hydrolyzed collagen peptides composed primarily of type 1 and 3. MOST collagen supplements do not contain type 2. This is critical because joint cartilage is predominantly made from type 2 collagen synthesised by your chondrocyte cells.

A special type of collagen called Undenatured UC-2 is the gold standard for joint pain and even symptoms of osteoarthritis. And the reason it’s so effective is because it’s poorly absorbed.

Hydrolyzed collagen peptides are absorbed by the intestine.

UC2 is not. It resists digestion and retains the 3D-structure needed to interact with Peyer’s patches and induce oral tolerance.

HCPs help chondrocytes synthesise type 2 collagen.

UC2 “turns off” T cells immune response to type 2 collagen and thus reduces inflammatory cartilage damage. This action helps reduce joint inflammation and promotes cartilage repair.

 

You are now nearly an expert on why ATP Labs offers three high quality sources of collagen:

Supreme Beef Protein provides collagen and 24g of protein with 4.8g of glycine per scoop. Incredible for people who want the benefits of collagen, glycine, plus high protein.  Click the image to review this product.

Total Radiance Collagen contains 10g of hydrolyzed collagen peptides and is incredible for skin, also owing to the addition of the potent anti-aging Hawaiian plant Gotu Kola.  Click the link to review this product.

Lastly, Syner Collagen is the GOAT for joint health since it contains both hydrolyzed collagen as well as patented undenatured uc 2 collagen, plus the cofactors required for collagen to do its job throughout the body.  This product is not online but is available in store at many Popeye’s locations – click to see the Store Locator.

 

References

 

1- Oesser S, Adam M, Babel W, Seifert J. Oral administration of (14)C labeled gelatin hydrolysate leads to an accumulation of radioactivity in cartilage of mice (C57/BL). J Nutr 1999; 129(10): 1891-5.

 

2 - Iwai K, Hasegawa T, Taguchi Y, et al. Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates. J Agric Food Chem 2005; 53(16): 6531-6.

 

3 - Ohara H, Matsumoto H, Ito K, Iwai K, Sato K. Comparison of quantity and structures of hydroxyproline-containing peptides in human blood after oral ingestion of gelatin hydrolysates from different sources. J Agric Food Chem 2007; 55(4): 1532-5.

 

4 - Razak, Meerza Abdul et al. “Multifarious Beneficial Effect of Nonessential Amino Acid, Glycine: A Review.” Oxidative medicine and cellular longevity vol. 2017 (2017): 1716701. doi:10.1155/2017/1716701

 

5 - Shaw, Gregory et al. “Vitamin C-enriched gelatin supplementation before intermittent activity augments collagen synthesis.” The American journal of clinical nutrition vol. 105,1 (2017): 136-143. doi:10.3945/ajcn.116.138594

 

6 - Andrew M Holwerda , Luc J C van Loon, The impact of collagen protein ingestion on musculoskeletal connective tissue remodeling: a narrative review, Nutrition Reviews, Volume 80, Issue 6, June 2022, Pages 1497–1514, https://doi.org/10.1093/nutrit/nuab083

 

7 - Jerger, Simon et al. “Effects of specific collagen peptide supplementation combined with resistance training on Achilles tendon properties.” Scandinavian journal of medicine & science in sports vol. 32,7 (2022): 1131-1141. doi:10.1111/sms.14164

 

8 - Jendricke, Patrick et al. “Specific Collagen Peptides in Combination with Resistance Training Improve Body Composition and Regional Muscle Strength in Premenopausal Women: A Randomized Controlled Trial.” Nutrients vol. 11,4 892. 20 Apr. 2019, doi:10.3390/nu11040892

 

9 - Narayanan and Gandhi, “Understanding Collagen Supplements in Arthritis- Immunomodulation with Undenatured Collagen ll Versus Cartilage Building with Hydrolyzed Collagen ll.” Archives of Orthopedics and Rheumatology, ISSN: 2639-3654

Volume 2, Issue 2, 2019, PP: 04-11

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