Exercise Intervention: Collagen Supplementation for the Elderly

In elderly people, there are many physiological changes that make living a healthy lifestyle difficult. Changes such as sarcopenia, decreased skin elasticity, osteoarthritis (OA) and osteoporosis limit an individual’s ability to function on a daily basis. Sarcopenia is a slow deterioration of muscle that occurs as people age. This decreases one’s ability to safely and effectively complete daily activities. Osteoarthritis (OA) symptoms are also very common in the elderly. OA occurs when the articular cartilage, that cushions our synovial joints degrades and becomes thin. This results in muscle atrophy, inflammation, decrease joint function and range of motion. Even though symptoms of OA may not be noticeable until later in life, 90% of adults show signs of OA by the time they are 40 (Williamson, 2019, p. 254). Another result of aging that is evident in the musculoskeletal system is osteoporosis.  Osteoporosis occurs when our bones loose more calcium than they build up. As a result, one’s bones become cavernous, weak and prone to fracturing. A bone fracture in an elderly person can be devastating to their long-term range of motion and muscular fitness. Often times, osteoporosis develops due to a diet lacking in vitamin D and calcium. As bone health wanes in the elderly, one’s ability to produce collagen also decreases. This is significant because collagen is an ingredient necessary for a supple and durable bone (Williamson, 2019, p. 116). As muscle atrophy and osteoporosis occur, ligaments, cartilage and tendons lack collagen fibers which is essential for elasticity. Without this elasticity, muscle sprains and strains become common (Williamson, 2019, p. 118).

A little on collagen…

               In many of these disorders, one’s collagen levels may not be where they are supposed to be. By weight, collagen is the most abundant protein in the human body making up a major part of tendons, ligaments, bones and connective tissue.  The structure of collagen consists of three intertwined chains of amino acids. While there can be a variety of amino acids within these chains, the main composition is glycine, proline and hydroxyproline. Since collagen is made up of amino acid, the machinery within the cell uses the mRNA transcripts to craft the protein into a triple helix shape. Surprisingly, there are 20 different collagen types in the body. These collagen types are isolated, or combined with other types throughout the body to give elasticity and structural support to different types of tissue. For example, collagen types I and III are both abundant in the skin. However, both of these types can be found in other tissues such as the ligaments, arteries, nerves etc. Another example is type II collagen and type XI collagen are found to make up the majority of collagen in cartilaginous tissue (joints, discs etc.) (Patino et al., 2002). Overall collagen is essential for the structure and the function of the human body. It is the lack of collagen that results in stiff, wrinkly skin, unstable joints and defective extracellular matrixes. The degradation or loss of collagen can cause undesirable inflammatory responses, osteoarthritis, osteoporosis and other disorders. However, when isolating collagen from its natural source, there is a process that is essential to improve its strength. While naturally ingested collagen (e.g., from bone broth) has a high amount of strength, its durability drops when collagen is hydrolyzed (broken down by enzymes, water, acids etc.) because its strong triple helix shape is lost. In this state, it is extremely sensitive to degradation/denaturation. In order to fix this issue, the isolated collagen must be chemically cross-linked. Chemical cross-linking involves a multi-step reaction where a functional groups from one polymer (amino acid chain) is covalently bonded to another polymer. When this is done, the strength of collagen is increased as its sensitivity to the environment decreases (Ryglova et al., 2017). Chemically cross-linked collagen is often used to synthesize edible film that is used in meat production while hydrolyzed collagen is found to be the most effective form for supplementation.

               Fortunately, there are interventions that can be put into place to significantly improve the situations of many elderly people.  One of these interventions is collagen supplementation. Collagen supplementation has been studied extensively in humans. A study titled “Collagen supplementation as a complementary therapy for the prevention and treatment of osteoporosis and osteoarthritis: A systematic review,” looked at the effect of collagen hydrolysate (designed to be absorbed and restore depleted collagen levels) on osteoarthritis and osteoporosis. The researchers observed a protective effect on the articular cartilage, alleviation in subject pain levels as well as a potential increase in bone mineral density. The researches even found this intervention to have a protective effect on the cardiovascular system and show anti-hypertensive properties (Porfirio & Fanaro, 2016). Research conducted in part by Philips et al., (2016) found that in elderly adults who supplemented with 15g of collagen peptides three times per week, experienced increased creatine synthesis and significant improvement in body composition due to fat loss. Another study sought to find ways to mitigate the common disorder among the elderly, sarcopenia. This study included 46 participants with sarcopenia, 30 of which took 46g of collagen peptides each day in combination with resistance training for 12 weeks. The results showed a statistically significant decrease in fat mass, an increase in muscular strength as well as a significant increase in bone mass in both groups. However, for these metrics, the results were significantly more pronounced in the group supplementing with collagen compared with the placebo group. This study shows 60 minutes of resistance training 3 days a week can be effective in staving off sarcopenia (Zdzieblik et al., 2015). A systematic review titled “The effects of collagen peptide supplementation on body composition, collagen synthesis, and recovery from joint injury and exercise: a systematic review” focused on the impact that hydrolyzed collagen supplements had on joint function, joint injury recovery, muscle synthesis and collagen synthesis. The results showed positive outcomes for reducing joint discomfort and knee pain. Ankle and knee functionality were improved and Achilles’ tendinopathy recovery was enhanced after collagen supplementation. This review also found enhanced markers indicating collagen synthesis following 5 to 15g of collagen paired with vitamin D (in one study) every day (Khatri et al., 2021). Finally, another study took a comprehensive view of the topic and stated that “The intake of hydrolyzed collagen leads to a significant increase in bone mass and the reduction of fractures for osteoporosis sufferers,” also indicating that osteoblasts were activated after collagen supplementation (Pluvinat & Taffin, 2008). These studies are just a sample of the amount of research supporting the supplementation of collagen.

Many experiments have paired collagen supplementation with resistance training. Undoubtedly, resistance training is an outstanding intervention that we can amalgamate with collagen supplementation in order to get the best results for our clients. A practical application for an elderly population who will be struggling with osteoporosis, sarcopenia, painful joints and other disorders is to not only consider implementing collagen supplementation, but to include resistance training in training cycles. Even though not every person who tries these types of supplements will have significant results, the potential benefits to be experienced in the muscle, bone and connective tissue far outweigh any cost.

References

Khatri, M., Naughton, R., Cliford, T., Harper, L., Corr, L. (2021). The effects of collagen peptide supplementation on body composition, collagen synthesis, and recovery from joint injury and exercise: A systematic review. Amino Acids (2021) 53:1493–1506 https://doi.org/10.1007/s00726-021-03072-x

Patino, M. G., Neiders M. E., Sebastiano, A., Noble, B., Cohen, R. (2002) Collagen: An overview. Implant Dentistry, 11(3), 280-285. https://journals.lww.com/implantdent/Fulltext/2002/07000/Collagen__An_Overview.14.aspx

Phillips, S. M., Tipton, K. D., Van Loon, L. J. C., Verdijk, L. B., Paddon-Jones, D., Close, G. L. (2016). Exceptional body composition changes attributed to collagen peptide supplementation and resistance training in older sarcopenic men. British Journal of Nutrition (2016), 116, 569–570. https://doi:10.1017/S000711451600221X 

Pluvinet, R., Taffin, A. (2008). Hydrolyzed collagen. Nutraceutical Business & Technology; Leatherhead (4)6, 26-29. http://search.proquest.com.ezproxy.gvsu.edu/trade-journals/hydrolyzed-collagen/docview/207662670/se-2?accountid=39473

Porfirio, E. & Fanaro, G. B. (2016). Collagen supplementation as a complementary therapy for the prevention and treatment of osteoporosis and osteoarthritis: A systematic review. Revista Brasileira de Geriatria e Gerontologia. (19)1. https://doi.org/10.1590/1809-9823.2016.14145 

Ry´glová, S., Braun, M. & Suchy, T. (2017). Collagen and it’s modifications—Crucial aspect with concern to its processing and analysis. Macromolecular Materials and Engineering. 302, 1600460. https://doi:10.1002/mame.201600460

Williamson, P. L., (2019. Exercise for special populations (2^nd ed.). Wolters Kluwer.

Zdzieblik, D., Oesser, S., Baumstark, M. W., Gollhofer, A., König, D. (2015). Collagen peptide supplementation in combination with resistance training improves body composition and increases muscle strength in elderly sarcopenic men: A randomized controlled trial. British Journal of Nutrition (2015), 114, 1237–1245. https://doi:10.1017/S0007114515002810