The synthesis of endogenous collagen is a fundamental aspect of health. Due to its nature, this structural protein is essential for the correct functioning of organs as diverse as the eye and bones. In this article we will discuss its importance and how to produce and preserve it.
Collagen
The most exact definition we can find is provided by the Linus Pauling Institute: “fibrous protein that is the basis for the structures of skin, tendons, bone, cartilage and all connective tissues”. Indeed, collagen provides support, strength and elasticity to expandable organs, such as the intestine.
It is the most abundant protein in the body, accounting for 25% of its weight. It is unevenly distributed in different tissues. Bone contains up to 90 % of this protein; tendons 80 %; in the skin it represents between 80 and 60 %, as does cartilage. In our body, 28 different types of collagen are synthesised, encoded by 42 genes, the most abundant being types I, II and III (1)
The distinctive feature of this molecule is that it is organised into fibrils and has a triple helix structure in at least part of it. Collagen synthesis takes place mainly in cells called osteoblasts in bone tissue, chondroblasts in cartilage and fibroblasts. It is then secreted and becomes part of the extracellular matrix. This term is used to define the substances that surround cells and make up tissues (2)
Effects and properties
The different types of collagen are networks of countless molecules. In addition to their structural functions and mechanical properties, they organise tissues and give them their shape. Moreover, they establish interactions with various cell types and regulate their differentiation, migration and proliferation (2)
Type I has high tensile and stretch strength and is found in bone tissue, tendons and the dermis. Type II, which is resistant to pressure, is present in cartilage and in the vitreous humour of the eyeball. Type III collagen is part of the lax connective tissue, which provides elasticity and support for blood vessels and glands.
Optimising endogenous collagen synthesis
Collagen loss occurs as part of the natural ageing process. Synthesis within the body slows down and its quality decreases. The result is musculoskeletal fragility with the possibility of fractures, joint wear and tear and skin sagging.
In addition, there are alterations in the nails and hair, causing them to become brittle. This process starts around the age of 45, but accelerates after the age of 60, leading to losses of up to 35% of their body content.
Supplements made from natural ingredients, such as plant extracts, amino acids, vitamins and minerals, modify this process by helping the body to reactivate protein synthesis and do not cause adverse reactions. The specific effects of each component are reviewed below.
Glycine, lysine and proline
When chondroblast and fibroblast culture media were enriched with these three amino acids, an acceleration in collagen synthesis was detected. This phenomenon was especially evident when the concentrations reached high physiological ranges. The conclusion was that supplementing the diet with these compounds would prevent the problems caused by the reduced production of the protein. (3)
Magnesium
This trace element is essential for the process of adenosine triphosphate, or ATP, synthesis. It is a molecule that provides energy in most metabolic processes, including collagen production. In fact, the mineral and the molecule form a complex called MgATP. (4)
L-arginine
Evidence suggests that L-arginine activates the expression of genes that control collagen synthesis. In addition, this amino acid may be an indirect precursor, because it acts as a source of proline. (5)
S-adenosyl-L-methionine or SAMe
This compound, which we use in the form of ademetionine, has shown efficacy in improving osteoarthritis when administered systemically. The evidence was obtained from two studies reviewed in 2002 which, in conclusion, demonstrated an effect similar to that of common anti-inflammatory drugs, but without their adverse effects. (6)
Iron
This mineral plays an important role in the proper activity of the enzymes lysyl hydroxylase and prolyl hydroxylase, which generate the collagen triple helix. Moreover, oral iron overload in mice demonstrated the activation of genes that regulate its production. (7)
Vitamin C
A randomised controlled study evaluated the effect of interventions that could increase collagen synthesis. A gelatin supplement containing vitamin C was administered to several athletes, with results suggesting its potential usefulness in sports injuries. (8)
Hyaluronic acid
The complex structure of articular cartilage requires the availability of many substances to achieve optimal levels. Several orally administered substances appear to improve tissue response in the presence of cartilage injury. In one trial, glucosamine, hyaluronic acid and vitamin C were shown to slow down chronic cartilage damage. (9)
L-citrulline
Citrulline-containing supplements provide a substrate that is converted to arginine in kidney tissue. Moreover, this amino acid functions as an inhibitor of the enzyme that breaks down arginine, which is an indirect way of increasing its availability. (10)
L-serine
This is a non-essential amino acid from which the body can synthesise glycine. . However, the availability of serine may not be sufficient, so providing it in a supplement indirectly increases glycine production. In addition, L-serine plays an essential role in protein synthesis and nerve impulse transmission. (11)
As we have seen, food supplements made with these components can alleviate age-related skin and musculoskeletal problems. The synthesis of endogenous collagen is essential for the functions of many organs and for maintaining the youthful appearance of the skin. Visit our website, because Mederi Nutrition always offers products with natural ingredients of the highest quality.
Bibliography:
- Gerhard Meisenberg & William H. Simmons. Principios de bioquímica médica, Editorial Elsevier, 4 edition, 03/2018
- Sylvie Ricard-Blum. «La familia del colágeno», Cold Spring Harb perspectiva Biol. 1 de enero de 2011;3(1).
- De Paz Lugo, P. Estimulación de la síntesis de colágeno: Posible tratamiento de enfermedades degenerativas mediante la dieta. Tesis doctoral. 2006. Universidad de Granada.
- Rude RK, Shils ME. Magnesium. In: Shils ME, Shike M, Ross AC, Caballero B, Cousins RJ, eds. Modern Nutrition in Health and Disease. 10th ed. Baltimore: Lippincott Williams & Wilkins; 2006:223-247.
- Souza, Adria do Prado Barros de. Influência da L-arginina na síntese de colágeno em cultura de fibroblastos dérmicos humanos. Tese (doutorado)—Universidade de Brasilia, 2016.
- Karen L Soeken 1, Wen-Lin Lee, R Barker Bausell, Maria Agelli, Brian M Berman. «Safety and efficacy of S-adenosylmethionine (SAMe) for osteoarthritis». J Fam Pract. 2002 May;51(5):425-30.
- H Ikeda, GYWu, CH Wu. «Evidencia de que un quelante de hierro regula la síntesis de colágeno al disminuir la estabilidad del ARNm de procolágeno». Hepatología. 1992 febrero; 15 (2):
- Gregory Shaw, Ann Lee-Barthel, Megan Lr Ross, Bing Wang, Keith Baar. «Vitamin C-enriched gelatin supplementation before intermittent activity augments collagen synthesis». Am J Clin Nutr. 2017 Jan;105(1):
- Dragos Apostu, Ondine Lucaciu, Alexandru Mester, Daniel Oltean-Dan, Mihaela Baciut, Grigore Baciut, Simion Bran, Florin Onisor, Andra Piciu, Roxana D Pasca, Andrei Maxim, Horea Benea. «Systemic drugs with impact on osteoarthritis». Drug Metab Rev. 2019 Nov;51(4):498-523.
- Gonzalez AM, Trexler ET. «Effects of Citrulline Supplementation on Exercise Performance in Humans: A Review of the Current Literature». J Strength Cond Res. 2020 May;34(5):1480-1495.
- Milan Holeček. «Serine Metabolism in Health and Disease and as a Conditionally Essential Amino Acid». Nutrients. 2022 May 9;14(9):1987