The latest research has shown that there are at least 29 different types of collagen. The four main collagen types are types I, II, III and IV, which form almost 90 % of all the collagen in the body. The type I collagen is by far the most common of these. The types I-III are so called fibrillar collagens and the type IV is the so called sheet-forming collagen.
The main collagen types and their role in the body are:
- Type I: 300 nm long fibrillars which exist in the skin, tendons, bones, ligaments, dentins and other connective tissues
- Type II: 300 nm long fibrillars which exist in cartilage and vitreous humour
- Type III: 300 nm long fibrillars (usually with the type I) which exist in the skin, muscles and blood vessels
- Type IV: forms basal lamina, the epithelium-secreted layer of the basement membrane
Collagen proteins form three-dimensional or so called triple helix shapes which make the connective tissues very durable, tolerating all movement patterns. The ability of the collagen proteins to get organized into these shapes weakens with age. The amount of collagen is also reduced in the body with aging. This can be seen externally especially on the skin which loses its elasticity and firmness. Excessive UV radiation also accelerates the reduction and damage of collagen.
The amount of type I collagen is reduced by almost 70 % between the ages of 30 and 80. This deterioration related to aging can however be significantly prevented and slowed down by ensuring the sufficient intake of collagen from nutrition. Based on a test made by aging mice, the aging of skin can significantly be slowed down by taking bovine (beef) collagen peptides. Based on a randomized, placebo-controlled double blind test published in 2018, collagen peptides significantly improved the moisture and elasticity of skin and reduced wrinkles over the course of 12 weeks.
Which lifestyle factors cause damage to collagen?
Nutrition plays a key role in the functioning of collagen in the body. Environmental factors are also known to affect collagen both internally and externally.
The following factors cause collagen damage:
- Excessive UV radiation and the burning of skin.
- Smoking reduces the production of collagen and damages collagen
- Sugar and processed carbohydrates prevent the repairing mechanisms of collagen due to the so called advanced glycation end products
- Oxidative stress and low-grade inflammation also damage skin and collagen
- Certain autoimmune diseases such as lupus erytematosus (SLE) and other connective tissue disorders damage collagen. These include Ehlers-Danlos, scleroderma, osteogenesis imperfecta, Sjögren syndrome and Marfan syndrome)
Nutritional factors that support the formation and repairing of collagen
The formation of collagen depends on many different nutritional factors. The actual collagen protein is produced from the precursor of collagen, procollagen. Procollagen is formed from two amino acids, glycine and proline. The intake of glycine and proline are typically insufficient for many people.
Glycine is a conditionally necessary proteinogenic amino acid. Glycine has a very simple chemical formula which enables its extensive use in the body. We need glycine from nutrition even though the body also produces it from serine and tetrahydrofolate (bioactive vitamin B9). Glycine functions in the central nervous system as an important inhibitory neurotransmitter. It also has an important role in the DNA, phospholipid and collagen syntheses as well as in the energy production.
The majority of people consume only the muscle tissue from all animal proteins. Muscle tissue however contains very little glycine amino acid which is important for the body. Glycine can be found in other animal parts containing collagen such as connective tissues, bone marrow and skin. Minced meat also contains a bit of connective tissue containing glycine.
Based on one research, people consume 4.5–6 g/day of glycine, of which the body produces 3 g and 1.5–3 g are consumed from nutrition. However, the recommendation for glycine intake is 10 g/day to maintain optimal collagen synthesis. This means that to maintain the wellbeing of connective tissues, special attention should be paid for the intake of glycine. The most high-quality source of glycine is hydrolyzed collagen protein powder, such as all Arctic Pure collagen supplements. From foodstuff, the most important sources of glycine are bone broth, fish soup (made from fish paring), gelatin, chicken, lamb, oysters and other shellfish, spirulina, chuck of game and generally edible animal parts containing connective tissue.
Proline is a conditionally necessary cyclic proteinogenic amino acid. The body can synthesize it from glutamic acid but for optimal health, proline also needs to be acquired from nutrition. Collagen contains plenty of proline (such as glycine), nearly one third of the protein.
In the gut, proline is needed for the functioning of normal mucosa-associated lymphoid tissue (so called GALT tissue) and for maintaining mucous membrane. The role of proline is critical especially in the production of the antibody IgA (immunoglobulin A). Proline is also needed in the production of the proline-rich polypeptides in the immune system. They have an important role in the regulation of the immune system, management of inflammations and protection against toxins especially in the gut and the brain. Colostrum contains a high amount of proline-rich polypeptides. The use of proline-rich polypeptides can be useful in the treatment of Alzheimer’s disease as they may reduce the formation of the so called amyloid plaques.
The best sources of proline are almost identical to glycine: bone broth, fish soup (made from fish paring), gelatin, chicken, lamb, oysters and other shellfish, spirulina, chuck of game and generally edible animal parts containing connective tissue. As a supplement, the best source of proline is hydrolyzed collagen protein.
Other nutrients that support the collagen protein synthesis include:
- Vitamin C advances collagen synthesis and through that strengthens the supportive tissue such as the bones, ligaments and joints.
- Sufficient intake of vitamin C is a critical factor in the formation and the regulation of collagen.
- Copper is needed in the connective tissues for the functioning of lysyl oxidase which strengthens collagen and elastin in the connective tissues.
- Pi participates in the activation of the proline-4-hydroxylase-enzyme which has an important role in the formation of collagen and for example the healing of wounds.
- Lysine is needed for the absorption of calcium and it also helps in the formation of collagen.
- Threonine has an important role in the protein synthesis in the supportive tissues (and their protein structures) such as enamel, collagen and elastin.
Is the use of collagen protein supplements backed up by research?
Collagen is mainly used in two different forms in supplements: hydrolyzed collagen protein (from fish or bovine) and gelatine. Gelatine is formed when collagen is cooked. Out of these two, hydrolyzed collagen protein has better bioavailability and therefore it has more significant effects in the body. It doesn’t however mean that gelatine from natural sources wouldn’t be nutritionally useful.
In the beginning of 2019, an extensive review was published on the use of oral collagen supplements for dermatological purposes. It was found in the review that both short-term and long-term use of collagen for advancing the healing of wounds and delaying the skin’s aging process is beneficial. Collagen supplements have also been discovered to improve the elasticity, moisture level and the density of collagen in the skin. No side effects with the use of collagen supplements have been found.
A randomized, placebo-controlled double-blind experiment focusing on the wellbeing of joints was published in 2018. It was discovered that using collagen protein together with chondroitin sulfate, glucosamine, L-carnitine and certain vitamins and minerals (see above) significantly improves the function of joints and slows down the aging of the body. In the same study the use of collagen was discovered to increase the subjects’ energy levels and the general physical wellbeing. It was discovered in another study published during the same year that collagen improves the performance of the subjects who suffered from osteoarthritis (hip or knee) as well as reduces pain.
Collagen can also be useful with the prevention of sarcopenia (the loss of muscle mass). Based on a research done on male subjects in their 70s published in 2015, the use of collagen showed significant benefit in the increasing of muscle mass and strength when its use was combined with strength training.
As a summary, the use of collagen protein supplements is beneficial especially with slowing down the aging of the skin, maintaining the general condition and structure of the skin and maintaining the wellbeing of joints and other connective tissues. The recommendation is to use high-quality and well-absorbing hydrolyzed collagen protein from fish or bovine. Fish collagen, such as the Arctic Pure collagen powder, is absorbed to the body even more efficiently than bovine collagen. Collagen protein supplements are available even for vegetarians which have been made primarily of egg whites and egg shells. In addition to type I, these do not however include the other important types of collagen (II, III and IV). There are currently no collagen supplements suitable for vegans.
P.S. Explore the selection of collagen supplements at our webshop!