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The Benefits of Using Collagen for Joint Pain

Authored by Kristyen Tomcik, PhD • 
November 12, 2019
 • 8 min read
supplementsrecoveryresearchnutrition

Our body is like a house. 

And like a house, as we get older, our body will require some maintenance. The foundation (bones) needs reinforcing. Squeaky hinges (joints) will need greasing.

What’s the body’s natural tool to help fix a few of these problems? That might be collagen. 

Along with its reported benefit for skin, hair and nail health,1 collagen is a vital protein used for maintaining the structural integrity of our body’s connective tissues. With roughly 12% of the population being affected by osteoarthritic (bone and joint) ailments2 and around 69% of those taking some sort of supplement to help manage lingering bone- and joint-related issues,3 collagen’s therapeutic benefits becomes an important factor in helping to relieve structural issues.

Before getting into all the benefits of collagen, let’s look at where it comes from and how the body uses it.

This will help us lay the framework for the joint- and bone-maintenance benefits of collagen supplementation, and equip you with information on how to optimize your body’s natural collagen-making machinery.

Collagen Basics

Etymology

Collagen is the main structural protein of various connective tissues found within the body, including skin, tendons, muscles, ligaments, and cartilage (joints).4

The term “collagen” actually originates from the Greek word “kólla” and the suffix “gen,” whose literal translation ends up being "glue-producing.” This is in reference to the ancient process of boiling down the skin and tendons of horses and other animals in order to obtain a glue-like substance.5

Collagen Sources

The skin, tendons, muscles, ligaments, and cartilage tissue of various animals such as poultry, fish, and livestock are a good source of dietary collagen. Foods such as beans, nuts, seeds, grains, or dietary supplements like collagen are also great alternative sources of collagen.

Have you ever wondered why some soups have a viscous, umami thickness to them? Don’t worry, it's not glue.

This is caused because of the use of animal bones to make the stock or broth (hence the term “bone broth”). The collagen found naturally in the bones seeps out during the cooking process to give the broth or soup more flavor and thickness.

Another form of collagen you may have heard of is gelatin, a denatured form of collagen that is a natural mix of protein and short amino acid chains (the “building blocks” of protein) called peptides that are extracted from animal matter like skin, bone, and connective tissue.6 Gelatin is often used in certain culinary processes to make a jelly-like consistency (think Jell-O).

Breakdown and Absorption

In order for the body to absorb animal-derived or supplemented forms of collagen, it needs to be broken down, or hydrolyzed (using a water molecule to break apart a chemical bond), into its amino acid components.

Once in the bloodstream, those amino acids become bioavailable for collagen synthesis within the body.7 In the case of gelatin formation, collagen is hydrolyzed by acid, alkali, or enzymatic methods, allowing the peptide chains that make up collagen to be rearranged and broken down easier. This is also why gelatin is sometimes referred to as hydrolyzed collagen or collagen peptides.

Synthesis

The body is also able to create collagen on its own.

It’s a complex metabolic process but, in a nutshell, collagen-forming genes are “turned on” and will cause the formation of peptide chains made up mainly of the amino acids proline, arginine, and glycine. Its specific amino acid order, namely having every third amino acid be a glycine residue, is responsible for collagen’s tightly bound, triple helix shape. These chains then undergo multiple chemical modifications that is aided by necessary co-factors vitamin C, copper, and zinc, culminating in the formation of a collagen molecule.8

As we age, however, the machinery behind synthesizing our own collagen slows down.

This reduces the amount of collagen that’s produced, thus increasing our need for supplementing it in our diet. A decline in collagen generally begins to occur in our 20s and 30s and has a noticeable effect on different parts of the body, including skin, hair, nails, and even bone and muscle (collagen is a protein after all).9

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Types of Collagen

Collagen is, in fact, the most abundant protein found in mammals, making up 25% to 35% of whole-body protein content (skin, muscle, tendons, etc.).10

To date, there have been over 28 different types of collagen that have been identified.11 In this article, we will only highlight the three most common types: type I (over >90% of body collagen), followed by types II and III.

Type I

Nearly 90% - 95% of your body’s collagen stores come in the form of type I collagen.12 This should come as no surprise since type I collagen is a key competent of your body’s structural machinery (tendons, and bones) as well as your skin (the human body’s largest “organ”). As such, may beauty products use type

I collagen to prevent wrinkles and maintain skin elasticity and hydration.13 It is also found in your eyes (corneas) and teeth.

Type I collagen has also been shown to strengthen nails and support hair thickness / prevent hair loss. But one of the biggest benefactors of collagen is muscle. Taken as a post-workout supplement after a hard training session, type I collagen helps in training recovery by helping provide the necessary protein components to rebuild muscle fiber.4

Type II

Sometimes referred to as collagen hydrolysate, type II collagen is the most abundant protein found in the make up of cartilage — an elastic tissue that provides “padding” between bones at the joints.

Type II collagen is produced in the cartilage matrix by chondrocytes, which are specialized stem cells that have “clumped” together to form a cushion, and makes up roughly 50% - 60% of the protein found in healthy cartilage.14

Interestingly enough, collagen is also found in high concentrations in your eyes and in spinal discs.4 Supplementation with type II collagen has been shown to reduce inflammation, lessen symptoms of rheumatoid arthritis, and alleviate joint pain as cartilage deteriorates with age.15 We will cover more on this in the next section.

Type III

Type III is the second most abundant type of collagen found in your body and is most abundantly found as a structural component in blood vessels, uterus, and bowels / intestines.

Type III and type I collagen are often found in concentrations together (almost 40% of bone is made up of type I and III collagen) and have seen use in gut-healing remedies.16

Because 19 of the amino acids that are found in type I and III collagen are produced in fibroblasts and osteoblasts (cells found in connective tissue and bone matrices, respectively), type III collagen has the potential to offer protective properties in several human disease states, including liver and kidney fibrosis.11

Collagen’s Joint Benefits

With all that background in mind, you may be asking yourself, “If the body creates its own collagen, why do I need to supplement with it?”

This is where supplements like grass-fed collagen protein powders can come in handy.

Through daily activity, collagen fibers break down from repeated use and the older we get, the less our cartilage is unable to be repaired or regenerated. This is an especially important consideration for many athletes or those who exercise regularly.

Unfortunately, in the case of cartilage, once it’s gone, it’s gone.

Some medical procedures and surgically invasive “gels” can help restore / mimic its activity in joints but the body’s natural ability to produce collagen dissipates, leading to a rise in osteoarthritic issues in individuals.

A review of the literature available suggests that the building up of collagen may help improve anti-inflammatory markers, thereby reducing incidences of pain and ability to continue performing daily activities - including exercising.17

A 2008 trial found that college athletes who took Type II collagen (collagen hydrolysate) improved joint pain parameters compared to a placebo treated group over the course of six months of supplementation.15 The authors highlight that athletes are at high risk of developing joint pain due repeated strenuous workouts.

The implementation of collagen supplementation may, therefore, be a promising dietary tool to help support athletic performance by aiding in joint-related pain relief following physical activity.

Decreases Functional Movement Pain

The reduction of type II collagen often tends to go unnoticed. Symptoms of osteoarthritis—the most common form of arthritis which occurs when cartilage in joints is significantly worn away - don’t often appear until later in life. At this point, it may be too late to slow the degenerative process.18

As age increases, so does our risk of bone-related injuries.

A two-cohort, placebo-controlled clinical study carried out in 2016 sought to determine whether age was a determining factor in osteoarthritic pain.

Athletes (average age = 24) with activity-related knee pain were compared with more elderly adults (average age = 50) with functional knee or hip pain following supplementation with collagen peptides. Both cohorts showed that collagen supplementation significantly improved pain parameters compared to placebo.19

The study stated: “The data suggests that a [collagen peptide] treatment over a longer period of time is effective in individuals putting their joints under stress, or individuals with a certain risk of developing a degenerative joint disease in the foreseeable future.”

What must be noted, however, was that both athlete and elderly groups once again showed around 25% placebo-effect “improvements” in individuals NOT supplemented with collagen. This suggests that either more research needs to be done on the type of collagen supplemented, the rigor and physiologically applicable assessment of pain, or diet of individuals tested.

Improves Pain Management

As stated earlier, the connective tissue of animals (skin, tendons, muscles, ligaments, and cartilage) are primary dietary sources of collagen. But what about people who choose to limit their intake of meat?

A person’s dietary habits was determined to be a significant factor, as determined in a multi-center study carried out in 2008.

Following a six-month collagen hydrolysate supplementation period in individuals around 60 years old, researchers from Spain found that, along with an observed improvement of knee joint comfort assessments in those taking collagen, subjects that previously had a lower intake of meat products were the ones who had the greatest perceived improvement in pain management.20

Investigation on a new, low molecular weight (or lower mass) hydrolyzed collagen supplement showed that 70 days of supplementation caused both the expected reduction in joint pain but also resulted in a greater ability to participate in physical activity compared to those who did not receive collagen.21

The ability to exercise in order to maintain both bone health as well as muscle integrity becomes a paramount concern as we age.

Maintains Muscle Mass

Muscle and bone work in tandem; meaning good muscle structure generally results in better bone support.

As we grow older, we naturally begin to lose muscle mass—a process known as sarcopenia.

We all know that protein is essential for maintaining muscle mass. But did you know that 1% - 10% muscle is composed of collagen?22 As we’ve covered, collagen is a protein and one that is essential for proper muscle maintenance.

A 2015 study from Germany showed that people with sarcopenia who supplemented with collagen peptides saw a significant reduction in the rate of age-related muscle loss. What was even more important was the finding that, compared to collagen alone, further improvements were found when adding in a resistance exercise program.23

More research is required, however, in order to accurately to compare the efficacy of collagen compared to standard protein intake.

Why Should You Take Collagen?

Collagen supplements have experienced a rise in popularity lately. However, just because a supplement is appealing doesn’t exempt it from the fact that it also needs to be backed by strong scientific evidence.

As we saw earlier, some collagen trials have showed a significantly high placebo effect in control groups, making it difficult to ascribe certain benefits to collagen supplementation alone. In terms of building up bone and muscle, more studies are definitely needed to nail this down collagen’s specific ergogenic effects.

However, collagen does have scientifically-backed holistic benefits—including aiding in the management of joint health and pain management—and can definitely be an alternative to protein supplementation with a number of additional benefits a typical protein supplement doesn’t offer.

The main goal for individuals when deciding to supplement with collagen should ultimately be optimizing the body’s natural collagen making machinery.

Adequate protein intake (meat, fish, poultry, or beans, nuts, seeds, and grains) can aid in this, not only for preserving strong bones / healthy joints but building up more muscle to support those bones.

Although collagen-rich food sources are always preferential, powders are often easier to consume and less thought intensive. You can just add some to your morning coffee or smoothie and you’re good to go!

As shown in the studies we’ve covered, the people who typically get the most benefit from collagen are those who don’t eat a lot of meat, which make collagen supplements and collagen protein powders a great way to incorporate collagen into your diet.

Although collagen isn’t a complete protein (lacks the amino acid tryptophan), it still is capable of supplying your body with some of the tools it needs, like amino acids, for building, maintaining, and repairing.

Collagen supplements not only help get you those amino acids essential for supporting bones, skin, hair, and nails but also helps you boost recovery for sore joints following intense workouts.

Give your body what it needs to help maintain structural integrity to carry you through all of life’s adventures.

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Scientific Citations

1.Avila rodríguez MI, Rodríguez barroso LG, Sánchez ML. Collagen: A review on its sources and potential cosmetic applications. J Cosmet Dermatol. 2018;17(1):20-26.
2.Lawrence RC, Felson DT, Helmick CG, et al. Estimates of the prevalence of arthritis and other rheumatic conditions in the United States. Part II. Arthritis Rheum. 2008;58(1):26-35.
3.Basedow M, Runciman WB, March L, Esterman A. Australians with osteoarthritis; the use of and beliefs about complementary and alternative medicines. Complement Ther Clin Pract. 2014;20(4):237-42.
4.Lodish H, Berk A, Zipursky SL, et al. Molecular Cell Biology. 4th edition. New York: W. H. Freeman; 2000. Section 22.3, Collagen: The Fibrous Proteins of the Matrix. Available from: https://www.ncbi.nlm.nih.gov/books/NBK21582/
5.Müller WE. The origin of metazoan complexity: porifera as integrated animals. Integr Comp Biol. 2003;43(1):3-10.
6.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.
7.Shigemura Y, Kubomura D, Sato Y, Sato K. Dose-dependent changes in the levels of free and peptide forms of hydroxyproline in human plasma after collagen hydrolysate ingestion. Food Chem. 2014;159:328-32.
8.Wu M, Crane JS. Biochemistry, Collagen Synthesis. [Updated 2019 Apr 21]. In: StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2019 Jan-.
9.Marcos-garcés V, Molina aguilar P, Bea serrano C, et al. Age-related dermal collagen changes during development, maturation and ageing - a morphometric and comparative study. J Anat. 2014;225(1):98-108.
10.Di lullo GA, Sweeney SM, Korkko J, Ala-kokko L, San antonio JD. Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J Biol Chem. 2002;277(6):4223-31.
11.Ricard-blum S. The collagen family. Cold Spring Harb Perspect Biol. 2011;3(1):a004978.
12.Correlo V.M., Oliveira J.M., Mano J.F., Neves N.M., Reis R.L., CHAPTER 32 - Natural Origin Materials for Bone Tissue Engineering – Properties, Processing, and Performance, Editor(s): Anthony Atala, Robert Lanza, James A. Thomson, Robert Nerem, Principles of Regenerative Medicine (Second Edition), Academic Press, 2011, Pages 557-586, ISBN 9780123814227, https://doi.org/10.1016/B978-0-12-381422-7.10032-X.
13.Proksch E, Segger D, Degwert J, Schunck M, Zague V, Oesser S. Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo-controlled study. Skin Pharmacol Physiol. 2014;27(1):47-55.
14.Eyre D. Collagen of articular cartilage. Arthritis Res. 2002;4(1):30-5.
15.Clark KL, Sebastianelli W, Flechsenhar KR, et al. 24-Week study on the use of collagen hydrolysate as a dietary supplement in athletes with activity-related joint pain. Curr Med Res Opin. 2008;24(5):1485-96.
16.Karsdal M. Biochemistry of Collagens, Laminins and Elastin, Structure, Function and Biomarkers. Academic Press; 2016.
17.Bello AE, Oesser S. Collagen hydrolysate for the treatment of osteoarthritis and other joint disorders: a review of the literature. Curr Med Res Opin. 2006;22(11):2221-32.
18.Porfírio E, Fanaro G. Collagen supplementation as a complementary therapy for the prevention and treatment of osteoporosis and osteoarthritis: a systematic review. Revista Brasileira de Geriatria e Gerontologia. 2016;19;153-164. 10.1590/1809-9823.2016.14145.
19.Oessert S, Schulze CH, Zdzieblik D, König‖ D. Efficacy of specific bioactive collagen peptides in the treatment of joint pain. Osteoarthritis and Cartilage (2016). Volume 24, S189
20.Benito-ruiz P, Camacho-zambrano MM, Carrillo-arcentales JN, et al. A randomized controlled trial on the efficacy and safety of a food ingredient, collagen hydrolysate, for improving joint comfort. Int J Food Sci Nutr. 2009;60 Suppl 2:99-113.
21.Schauss AG, Stenehjem J, Park J, Endres JR, Clewell A. Effect of the novel low molecular weight hydrolyzed chicken sternal cartilage extract, BioCell Collagen, on improving osteoarthritis-related symptoms: a randomized, double-blind, placebo-controlled trial. J Agric Food Chem. 2012;60(16):4096-101.
22.Gillies AR, Lieber RL. Structure and function of the skeletal muscle extracellular matrix. Muscle Nerve. 2011;44(3):318–331. doi:10.1002/mus.22094
23.Zdzieblik D, Oesser S, Baumstark MW, Gollhofer A, König D. Collagen peptide supplementation in combination with resistance training improves body composition and increases muscle strength in elderly sarcopenic men: a randomised controlled trial. Br J Nutr. 2015;114(8):1237-45.
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These statements have not been evaluated by the FDA. Our products are not intended to diagnose, treat, cure, or prevent any disease.

© 2019 HVMN Inc. All Rights Reserved. H.V.M.N.®, Health Via Modern Nutrition™, Nootrobox®, Rise™, Sprint®, Yawn®, Kado™, and GO Cubes® are registered trademarks of HVMN Inc. ΔG® is a trademark of TΔS® and used under exclusive license by HVMN Inc.