From Purity to Performance: The Science Behind Collagen’s Effects on Muscles and Tendons

Description

The tradition of consuming bone broths for their nourishing benefits has been around for a long time. Many families pass down their broth recipes from one generation to the next, providing a time-tested home remedy for what ails you. To make a proper bone broth that provides all of the nourishing benefits takes time, effort, and love. 

One of the primary reasons we consume bone broth is to obtain the powerful ingredient, collagen. 

However, thanks to modern science, we can now consume collagen products that offer similar benefits but are more versatile and convenient, without all the work of making bone broth. 

In today’s article, we will take a look at some of the science behind collagen’s effects on muscles and tendons. 

However, before we delve into the science of collagen, let’s examine what collagen is and some of the modern versions available to consumers.

What exactly is collagen? 

Collagen is a protein that the body produces, playing an essential role in supporting the structure and function of hair, skin, nails, cartilage, bones, blood vessels, and connective tissue. It is the human body's most abundant protein, accounting for approximately 35% of its dry weight, and is composed of 19 essential and nonessential amino acids. It is composed of three chains wound into a tight helix, with each chain being approximately 1,400 amino acids long. 

Collagen is primarily made up of the amino acids Glycine (33% of total collagen), hydroxyproline and proline (22% of total collagen), and glutamate (derived from its precursor glutamine and an essential precursor for proline).  Bones, marrow, and connective tissue not only contain all the necessary materials needed to keep the structural foundation of our body strong and healthy, but also a litany of amino acids. Bone broth is one of the best natural sources of collagen. 

Collagen is the glue that holds your body together and has been classified into two prominent families: fibrillar and network-forming collagens.

• Fibril-associated collagens with interrupted triple helices (FACITs) are the most abundant in vertebrae and play a structural role in the tissue's shape and mechanical properties. Includes types I, II, III, V, XI, XXIV, XXVII)
• Membrane-associated collagens with interrupted triple helices (MACITs)
• Multi-triple-helix domains and interruptions (MULTIPLEXINS) include types XV(skeletal and cardiac tissue) and XVIII(liver)

While there are technically 28 types of collagen that differ by molecular assembly, added cell components, and their use in the body, there are five primary types. 

• Type I makes up 90% of your body’s collagen and is densely packed to provide structure for your skin, bones, tendons, and ligaments.
• Type II is found in elastic cartilage, which provides cartilage with both strength and elasticity, as well as joint support. It supports the binding process via fibronectin (a glycoprotein that plays an essential role in tissue repair) and other collagens. 
• Type III is a significant component of the extracellular matrix found in muscles, arteries, blood vessels, and organs. Specific to tissues with large portions of elastic fibers. Type III collagen also interacts with platelets in the blood clotting cascade and is an essential signaling molecule in wound healing. 
• Type IV is the primary component of basement membranes(thin layers of extracellular matrix that form supportive structures) found in layers of your skin, creating their backbone.
• Type V is a fibrillar collagen(essential for forming collagen fibers)of types I and III collagen, optimal for the formation and quality of tissue. Type V collagen contributes to the bone matrix, corneal stroma, and interstitial matrix of muscles, liver, lungs, and placenta. 

What is hydrolyzed collagen?

First, it is crucial to understand that hydrolyzed collagen may be referred to by several other names, including collagen hydrolysate and collagen peptides. Next, all collagen is technically hydrolyzed, but there are different levels of hydrolysis (partial and complete). 

For example, gelatin is partially hydrolyzed, and collagen peptides are fully hydrolyzed. Finally, hydrolyzed collagen is, by definition, a denatured protein. Now, to correctly answer the question of what hydrolyzed collagen is, it is also essential to understand the hydrolysis process. Hydrolyzed collagen is produced through hydrolysis, a process in which water molecules break the chemical bonds. 

Gelatin vs. Hydrolyzed Collagen

This comparison is not about which form is better; it is intended for clarification, so you understand the use and proper application of these raw materials. As mentioned earlier, there are two levels of hydrolysis: partially and fully hydrolyzed. Gelatin is a partially hydrolyzed collagen because it does not undergo the crucial step of enzymatic breakdown. 

Partially hydrolyzed gelatin also has a higher molecular weight, making it soluble only in hot water and solidifying in cold water. While this makes a superior thickening agent for soups, stews, and desserts, and is also excellent for making gummies, some might consider it less versatile. You may also know this raw material by its other name, JELLO. 

As your mother used to tell you, “There is always room for jello.” Fully hydrolyzed collagen (collagen peptides) is soluble in hot and cold liquids and highly versatile. In simple terms, gelatin is the cooked form of collagen, and hydrolyzed collagen is gelatin that has been more highly processed to break up the protein chain for better absorption. 

Essentially, we consume various forms of collagen to provide our bodies with the amino acids necessary to build collagen where it is needed.

Three primary sources of collagen

1) Chicken Collagen

Chicken contains Type II collagen, which is found in elastic cartilage and provides it with strength and elasticity, thereby supporting the joints. It also supports the binding process via fibronectin (a glycoprotein that plays an essential role in tissue repair) and other collagens. This type of collagen is derived from chicken sternum cartilage. In simple terms, type 2 collagen is a peptide and a component of joint cartilage. Type 2 collagen can be found in both hydrolyzed and undenatured forms.

2) Beef Collagen

A significant portion of the market's hydrolyzed peptide collagen products originates from beef bones (unless otherwise specified) and is a high-quality source of Types I and III collagen. As mentioned earlier in the article, 

• Type I makes up 90% of your body’s collagen and is densely packed to provide structure for your skin, bones, tendons, and ligaments.
• Type III is a significant extracellular matrix component found in muscles, arteries, blood vessels, and organs. Specific to tissues with large portions of elastic fibers. Type III collagen also interacts with platelets in the blood clotting cascade and is an essential signaling molecule in wound healing. 

3) Marine Collagen: Type 1 collagen: The superstar of collagen from the sea

Type I collagen comprises 90% of your body’s collagen and is densely packed to provide structure for your skin, bones, tendons, and ligaments; this can be found in highly nourishing quantities in marine collagen. As a side note, type III collagen is another type of fibrillar collagen often associated with type I. Type III is thinner and present in high concentrations in the skin and blood vessels. While more human research is needed, Marine collagen has been shown in preliminary studies and some small clinical trials to support skin health. 

What Causes Collagen Depletion?

The foundation of the human structure is a perfect creation of bones, joints, ligaments, cartilage, tendons, and muscles. These moving parts have been strategically placed to support one another, optimizing movement, agility, and strength, while also protecting our anatomy and physiology. In simple terms, it is support for optimally surviving and thriving. Unfortunately, our natural collagen production begins to slow as we age, and these essential parts break down. This natural process begins to weaken the cell structures that support our structural foundation. 

While it is believed the group of enzymes called collagenases is responsible for collagen degradation, our lifestyle habits may be the most significant factor in accelerating this natural process. While excessive exposure to sunlight, smoking, and sugar play a direct role in this process, a diet lacking the essential ingredients for supporting healthy collagen levels is one of the top reasons for this process. Vitamin C and the amino acids proline, hydroxyproline, and glycine are essential components in supporting the process known as collagen synthesis. Collagen synthesis is a complex, multistep process that requires numerous structures within and outside collagen-producing cells, known as fibroblasts, within connective tissue. 

The science behind collagen

Various forms of collagen products have been building a substantial body of scientific evidence supporting their ability to support muscle, tendon, and joint health. Research on the effectiveness of collagen supplements is ongoing, but many studies suggest that various forms of collagen products have produced effective results for a wide range of structural conditions. Here are just a few examples. 

The following was stated in a randomized controlled study discussing the Efficacy and tolerability of an undenatured type II collagen supplement in modulating knee osteoarthritis symptoms of 191 volunteers, who were randomized into three groups: receiving a daily dose of UC-II (40 mg), GC (1500 mg G & 1200 mg C), or placebo, for 180 days.

• At day 180, the UC-II group demonstrated a significant reduction in overall WOMAC score compared to placebo (p = 0.002) and GC (p = 0.04). 
• Supplementation with UC-II also resulted in significant changes for all three WOMAC subscales: pain (p = 0.0003 vs. placebo; p = 0.016 vs. GC); stiffness (p = 0.004 vs. placebo; p = 0.044 vs. GC); physical function (p = 0.007 vs. placebo). 
• Safety outcomes did not differ among the groups.

Therefore, it was concluded that UC-II improved knee joint symptoms in subjects with knee OA and was well tolerated. 

• The following was also stated in a study examining how a daily dose of 10 grams of Collagen Peptide Supplementation given to 50 young, healthy men over 16 weeks enhances muscle-tendon stiffness and explosive strength. 
• The collagen peptide group exhibited significant increases in MG (medial gastrocnemius) stiffness (P < 0.001, Cohen's d = 0.594) and Achilles tendon stiffness (P < 0.001, Cohen's d = 0.378), while no significant changes occurred in the placebo group. 
• Similarly, the normalized rate of torque development increased significantly in the CP group (P < 0.001, Cohen's d = 0.525) but not in the placebo group. 
• Positive correlations were found between MG stiffness and normalized RTD in both groups before and after the intervention (P ≤ 0.033, r ≥ 0.427).

Finally, I don’t want to leave you hanging without explaining this research. 

So, how exactly does collagen enhance stiffness and strength? Essentially, there are five components of how this happens. 

• Because collagen peptides contain high levels of the key amino acids glycine, proline, and hydroxyproline that are essential for synthesizing new collagen, they provide the building blocks for stronger tendons and ligaments.
• Combining resistance training with collagen supplementation results in a greater increase in tendon cross-sectional area and stiffness. The mechanical loading created by resistance training signals the tendon cells to increase collagen synthesis.
• Consuming collagen supplements may support upregulation of ECM proteins, leading to higher collagen synthesis rates in muscle and tendon.
• Collagen peptides have been shown to modulate intramuscular connective tissue, which, in turn, supports muscle remodeling and hypertrophy by interacting with satellite stem cells. 
• Greater tendon stiffness and a stronger ECM (molecules that form the framework for tissues and organs) enable more efficient force transmission from muscle to bone, which is crucial for explosive movements and can increase the rate of torque development. 

Furthermore, preliminary studies have shown that collagen peptides may improve cardiometabolic parameters, including reducing fat mass and LDL cholesterol and lowering systolic blood pressure. 

In conclusion, while these studies are just the beginning of what we still need to learn about the short- and long-term effects of collagen consumption, consuming collagen daily is a great way to get the essential building blocks for the most significant type of protein in the human body. 

For more information about our Grass-Fed Hydrolyzed Collagen Peptides, go here:

Grass-Fed Hydrolyzed Collagen Peptides 

The Author’s Bio
Michael Stuchiner is a Master Herbalist and proud graduate of The School of Natural Healing, with over 25 years of experience in various aspects of the field. He is a retired elite-level powerlifter who competed for 27 years. As an avid international traveler, he is passionate about the use of medicinal and tonic herbs, as well as foods traditionally found in local markets in the 35 countries he has visited. Michael shares his years of experience as a Master Herbalist, traveler, and athlete through the hundreds of articles he has written and his YouTube channel, "A Master Herbalist Perspective." He is considered a true educator in this field. For more articles written by Mike, go here: Master Herbalist.