What is collagen?
Collagen is the most abundant protein in the human body and plays a structural role. It is mainly found in connective tissues (skin, bone, cartilage, muscles, vessel walls …). There are 28 types of collagen in our body. All are composed of 3 α chains that form a helix, but each type of collagen has particular α chains. The common point between all the α chains is the helical part in the middle, mainly comprising a succession of amino acids (elements making up the proteins) Glycine-XY. X and Y are most often a Proline and a Hydroxyproline, but other amino acids (such as Hydroxylysine) in X or Y allows to have a less perfect helix, and therefore more flexible.
The various structures of different collagen allow them to perform distinct functions. Their specific properties make them essential elements for different tissues. For example, the cartilage is composed of fibrils mixing collagen II and III, while those of the skin mix collagen I and III. The assemblies between the molecules (eg in fibrils or fillets) also depend on the tissue, giving them specific properties.1,2
The issue: collagen destruction
Collagen can be degraded by enzymes called matrix metalloproteases (MMPs). It is a process that can be important during the growth or healing of a tissue, but it can also be pathological (cancer, rheumatoid arthritis, nephrosis, encephalomyelitis, chronic ulcers, fibrosis …) when these proteins expression becomes too important. The presence of inflammatory cytokines, free radicals, hormones and growth factors, UV radiation, chemical derivatives (cigarette, pesticides, etc.) can cause the overactivation of these MMP proteins. During aging, collagen becomes more sensitive and more easily changed (by some processes of mineralization, by glycation products and by the loss of glycosaminoglycans), which affects the stability of collagen fibers and increases their susceptibility to degradation. In addition, collagen synthesis is reduced because of defective stimulation and cell aging. The tissues regenerate more slowly, allowing for a greater accumulation of abnormalities in the cells, which affects the proper functioning of certain processes. These abnormalities can promote an inflammatory environment and oxidative stress, which will further increase collagen degradation and tissue aging.3-7
A solution: A selection of specific collagens with ExtraCellMatrix
Fortunately, taking collagen peptides (or hydrolysates) has many virtues against articular, bone, muscle and skin diseases. It’s also reinforces connective tissue. Peptides are small bits of protein that have been cut by the water molecules action. Peptides have been shown to be better digested and easily absorbed than whole proteins, while being better incorporated and available in tissues. With approximately 10g (10,000 mg) of collagen hydrolysates in our products, we exceed the 30 mg that is needed to have a lasting and effective effect.8-12
How does it work scientifically?
Many studies have pointed out that taking oral collagen is beneficial for collagen synthesis and tissue regeneration. The collagen peptides are absorbed in the intestine, and are found, along with their constituents (amino acids), in the blood and in the tissues concerned (for example, ligaments, cartilage, skin, muscles). And it changes their composition. A study *13 using collagen incorporating radioactive carbon atoms showed that 95% of collagen was absorbed during the first 12 hours, then it was distributed in all tissues, with a pronounced presence (2x more) and lasting in the body cartilage.
It has been shown that a physiological regulation process makes possible the collagen production increasing, so it doesn’t come running out: the presence of degraded endogenous collagen can stimulate chondrocytes (cartilage cells) and amplify fiber biosynthesis of collagen. Many studies have shown that the ingestion of collagen peptides can induce the production of collagen, probably by mimicry of this regulatory mechanism.14-20
The many benefits of taking collagen
Taking oral collagen peptides can:
- Stimulate chondrocytes and their production of collagen fibers in cartilage
- Change the behavior of bone cells, decreasing bone loss by reducing osteoclast activation and stimulating osteoblast growth to reshape bone and remineralize bone matrix.
- Increase the density of dermal cells (fibroblasts) and extracellular fibrils (collagen) to firm and maintain the elasticity and hydration of the skin.21,22
Thus, collagen can be beneficial in osteoarthritis, arthritis, osteoporosis, skin aging, cellulite, or for the healing of wounds, among many other applications whose studies are detailed here !
However, not all forms of collagen have the same benefits. That’s why we have always focused on creating the best and most complete formulations for your health. #ExtraCellMatrix #EtraCellWoman #BeautyCollagenMatrix
- Ricard-Blum, S. The Collagen Family. Cold Spring Harbor Perspectives in Biology 3, 1–19 (2011).
- Gordon, M. K. & Hahn, R. A. Collagens. Cell and Tissue Research 247–257 (2010). doi:10.1007/s00441-009-0844-4
- Borel, J.-P., Monboisse, J.-C. & Bellon, G. Inflammation, collagène et radicaux libres oxygénés. Médecine/sciences (1988).
- Jabłońska-Trypuć, A., Matejczyk, M. & Rosochacki, S. Matrix metalloproteinases (MMPs), the main extracellular matrix (ECM) enzymes in collagen degradation, as a target for anticancer drugs. Journal of Enzyme Inhibition and Medicinal Chemistry 31, 177–183 (2016).
- Panwar, P. et al. Aging-associated modifications of collagen affect its degradation by matrix metalloproteinases. Matrix biology : journal of the International Society for Matrix Biology 65, 30–44 (2018).
- Zhang, S. & Duan, E. Fighting against Skin Aging: The Way from Bench to Bedside. Cell Transplantation 27, 729–738 (2018).
- Varani, J. et al. Decreased collagen production in chronologically aged skin: Roles of age-dependent alteration in fibroblast function and defective mechanical stimulation. American Journal of Pathology 168, 1861–1868 (2006).
- Skov, K., Oxfeldt, M., Thøgersen, R., Hansen, M. & Bertram, H. C. Enzymatic hydrolysis of a collagen hydrolysate enhances postprandial absorption rate—a randomized controlled trial. Nutrients 11, (2019).
- 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 chemistry 159, 328–32 (2014).
- Koopman, R. et al. Ingestion of a protein hydrolysate is accompanied by an accelerated in vivo digestion and absorption rate when compared with its intact protein. American Journal of Clinical Nutrition 90, 106–115 (2009).
- Manninen, A. H. Protein hydrolysates in sports and exercise: A brief review. Journal of Sports Science and Medicine 3, 60–63 (2004).
- Calbet, J. A. L. & Holst, J. J. Gastric emptying, gastric secretion and enterogastrone response after administration of milk proteins or their peptide hydrolysates in humans. European journal of nutrition 43, 127–39 (2004).
- Oesser, S., Adam, M., Babel, W. & Seifert, J. Oral Administration of 14C Labeled Gelatin Hydrolysate Leads to an Accumulation of Radioactivity in Cartilage of Mice (C57/BL). The Journal of Nutrition 129, 1891–1895 (1999).
- Oesser, S. & Seifert, J. Stimulation of type II collagen biosynthesis and secretion in bovine chondrocytes cultured with degraded collagen. Cell and Tissue Research 311, 393–399 (2003).
- Wauquier, F. et al. Human enriched serum following hydrolysed collagen absorption modulates bone cell activity: From bedside to bench and vice versa. Nutrients 11, (2019).
- Elango, J. et al. Cross-talk between primary osteocytes and bone marrow macrophages for osteoclastogenesis upon collagen treatment. Scientific Reports 8, (2018).
- Liu, J. L. et al. Bovine collagen peptides compounds promote the proliferation and differentiation of MC3T3-E1 pre-osteoblasts. PLoS ONE 9, (2014).
- Yazaki, M. et al. Oral Ingestion of Collagen Hydrolysate Leads to the Transportation of Highly Concentrated Gly-Pro-Hyp and Its Hydrolyzed Form of Pro-Hyp into the Bloodstream and Skin. Journal of agricultural and food chemistry 65, 2315–2322 (2017).
- Shaw, G., Lee-Barthel, A., Ross, M. L. R., Wang, B. & Baar, K. Vitamin C-enriched gelatin supplementation before intermittent activity augments collagen synthesis. American Journal of Clinical Nutrition 105, 136–143 (2017).
- McAlindon, T. E. et al. Change in knee osteoarthritis cartilage detected by delayed gadolinium enhanced magnetic resonance imaging following treatment with collagen hydrolysate: a pilot randomized controlled trial. Osteoarthritis and cartilage 19, 399–405 (2011).
- Matsuda, N. et al. Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis. Journal of nutritional science and vitaminology 52, 211–5 (2006).
- Pyun, H. B. et al. Effects of collagen tripeptide supplement on photoaging and epidermal skin barrier in UVB-exposed hairless mice. Preventive Nutrition and Food Science 17, 245–253 (2012).