Tips to Maximize Collagen Production

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Collagen is found in almost every bodily tissue and is made up of amino acids—mainly glycine, proline, and hydroxyproline. Collagen consists of three long amino acid chains that are wound together like a strong rope. This tight, sturdy configuration helps it withstand stress and provides stability for connective tissues. As we age, the thickness and the strength of these chains can begin to deteriorate and not be replaced as quickly which can lead to many of the signs of aging humans experience.

Key Benefits of Healthy Collagen Production

Under healthy conditions, the collagen production pathway sustains optimal levels that afford the following benefits [3]:

  • Helps connective tissue cells for the different layers of the skin
  • Promotes new cell growth
  • Supports healthy blood clotting
  • Plays a role in replacing dead or weak cells
  • Provides a protective covering for vital tissues and organs
  • Gives structure, stability, elasticity, and strength to the skin, ligaments, muscles, and tissues

As with any biological pathway, there are various steps that must be precisely executed, regulated, and controlled to maintain collagen balance. However, issues (e.g., genetic mutations, environmental toxins) that disrupt any of the steps can lead to assembly errors that may cause low collagen production or weak collagen fibers.

Factors Influencing Collagen Production

There are internal and external factors that may influence the body’s natural ability to produce healthy levels of collagen. For instance, certain diseases, and nutritional deficiencies can lead to different types of collagen-related health issues.

Autoimmune diseases such as lupus, rheumatoid arthritis, scleroderma, and dermatomyositis can also weaken or damage collagen. In addition, nutritional deficiencies—particularly a vitamin C deficiency—can alter collagen production by disrupting the activity of hydroxylase, an enzyme involved in the collagen production pathway that needs vitamin C to function properly [3].

In addition, the human body produces less collagen with age, as the configuration of collagen fibers gradually changes from tightly woven fibers to loose, unorganized strands [6]. Unfortunately, external factors such as smoking, excess sun exposure, poor diet, and a lack of exercise can also cause collagen levels to drop, thus worsening age-related collagen loss.

It is important to avoid these factors to minimize their risk of blocking healthy collagen production:

  • Smoking – Various chemicals in cigarettes, including nicotine, damage elastin and collagen fibers. This loosens the fibers and leads to wrinkles as well as delayed wound healing. Nicotine also causes blood vessels near the surface of the skin to become narrow, which is an issue that can reduce the delivery of nutrients and oxygen to the skin. Proper nutrient delivery supports optimal collagen production [7].
  • Excess exposure to sunlight – Excess sunlight exposes the skin to high levels of ultraviolet (UV) rays. Prolonged exposure to UV rays disrupts collagen production, damages collagen fibers, and causes the fibers to unravel and break down rapidly—leading to wrinkles [8].
  • Eating large amounts of refined carbohydrates and sugar – These molecules bind to collagen protein and form advanced glycation end products (AGEs). AGEs damage collagen fibers, causing them to become brittle and dry. Large amounts of sugar also cause the fibers to tangle. Over time, this leads to skin dehydration, wrinkles, and abnormal levels of inflammation. AGEs also make it harder for connective tissue cells to produce collagen [9].

Although there are different factors that impact collagen production, the body’s ability to absorb collagen that is consumed through food or supplements also depends on various factors such as the source and form of collagen.

Factors Influencing Collagen Absorbtion

Collagen is naturally found in a variety of foods such as legumes, dairy, poultry, beef, fish, and soy. However, it is hard to measure or determine the body’s ability to absorb ideal amounts of collagen after eating these types of foods. This is where supplementation comes in, as adding a rich source of collagen in the form of collagen peptides can help ensure adequate levels of collagen are absorbed and used by the body in a consistent manner.

However, it is harder for the body to absorb large amounts of amino acids from pure collagen gelatin or native collagen from the human diet [10, 11]. This is because pure collagen gelatin and collagen in foods are made up of large amino acid chains that take extended time for the intestines to digest. In most cases, the intestinal tract simply can’t break down native collagen and collagen gelatin efficiently, leaving most of it undigested. The body can’t use undigested collagen and it gets eliminated as waste.

Collagen that is used to manufacture dietary supplements is commonly extracted from bovine (cow) tissues such as the skin or bones, as this is one of the most abundant sources. Furthermore, collagen peptides—also called collagen hydrolysate or hydrolyzed collagen—that are isolated from bovine sources are typically the ideal size for optimal digestion and absorption [10]. The peptides consist of small chains of amino acids that the intestines can easily absorb.

Collagen peptides contain these types of small amino acid chains that lead to rapid intestinal absorption, digestion, and transfer to the bloodstream, where they are transported to different parts of the body. Once single amino acids reach the targeted tissue, they are converted into bioactive proteins that regulate important processes, including heightened collagen production [3, 11].

To experience proper absorption, it is best to consume collagen peptides from bovine sources, which have been shown through research to boost the body’s natural production of collagen types I, II, and III [1, 12]. These are the most common forms found in the skin, hair, nails, bones, muscles, and joints [1, 12].


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  12. Leon-Lopez A, Morales-Penzloza A, Martinez-Juarez VM, et al. Hydrolyzed-collagen—Sources and applications. Molecules. 2019;24(22):4031-4047.

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