CONTENTS:

• What is collagen?
• Types of collagen
• The role of collagen in the body
• Consequences of a collagen deficiency
• What influences the synthesis and amount of collagen?
• Collagen sources

Everyone probably knows collagen, but do you know what it's made of and what it's used for? The term collagen doesn't define a single "substance," but rather a series of complex structures with slightly different properties. Read the article to learn more.

What is collagen?

Glue fiber forms. It makes up about 25-30% of all body proteins. The name itself comes from two Greek words: colla - to stick and gennao - to give birth. Collagen synthesis is a complex process in which the intermediate product is, among others, procollagen, formed from connective tissue cells - fibroblasts. In addition to amino acids, collagen also contains saccharides (about 0.5-10%), e.g. glucose, galactose and, in smaller amounts, mannose, fructose, arabiose, xylose and ribose. Currently, 29 genetically different collagen types have been described. A characteristic feature of all types is the tissue-specific occurrence and unique structure. Collagen consists of three left-handed α-polypeptide chains, each of which contains about 1050 amino acids. These chains are twisted to the right around their axis and form a superhelix. It contains acidic amino acids (glutamic acid – Glu, aspartic acid – Asp) and basic amino acids (lysine – Lys, arginine – Arg) in equimolar amounts. The characteristics described above apply to fibrillar collagens, but nonfibrillar collagens can also be distinguished, whose structure does not resemble a helix but forms network systems. Nonfibrillar collagens include anchor collagens, transmembrane collagens, multiplexins, and FACIT collagens. However, they only account for 10% of the total collagen content in the body.

Types of collagen

There are 29 types of collagen that can be divided according to their structural properties and functions:

• fibrillar collagens: I, II, III, V, XI, XXIV, XXVII,
• Basement membrane collagen: IV,
• Collagen-forming “anchor fibers”: VII,
• Multiplexins: XV, XVIII, collagen-forming microfibers: VI,
• Collagens that form hexagonal network systems: VIII, X,
• FACITs Collagens (Fibril-associated collagens with interrupted triple helices): IX, XII, XIV, XVI, XIX, XX, XXI, XXII, XXVI,
• Transmembrane domains: XIII, XVII, XXIII, XXV

Among the fibrillar collagens, which were the first discovered and are encoded by 11 genes, there are types I, II, III, V, XI, XXIV and XXVII. In mammals, they make up 90% of all collagen proteins. The best known collagen protein is collagen type I. Most of it is found in bones, ligaments, tendons, skin and cornea. The double helix of this collagen is usually composed of two identical α1[I] chains and one α2[I] chain, forming a heterotrimer or three α1[I] chains. It is mainly responsible for the tensile strength of the tissues in which it occurs and for the stiffness of bones.

If we consider the collagen types in terms of their location, they can be divided into the following groups: 2 groups:

• localized in the skin: I, III, V, VI, VII, VIII, XII, XIII, XIV, XVI, XVII, XIX, XXIX
• Joints (ligaments, cartilage): I, II, VI, VIII, IX, X, XI, XIV, XXVII,

The exact location of each collagen type and a brief description of its functions can be found in the table below.

Legend: Fibrous collagens are marked in bold.

The role of collagen in the body

Collagen is the most important protein in connective tissue and the building block of the extracellular matrix. The properties of collagen vary slightly depending on the type, but overall, collagen influences the function of the entire body, especially the skin, hair, bone and joint system, and the immune system. It participates in the regeneration process—accelerating wound healing, creating scars, reducing the activity of enzymes that cause inflammation and rheumatic pain, and promoting the rebuilding of connective tissue. Thanks to its ability to bind water, it ensures proper hydration, elasticity, and firmness of the skin. It provides essential amino acids that nourish hair follicles and ensure their proper growth and revitalization. Together with calcium, magnesium, and phosphorus, it makes up 90% of the bone skeleton. Collagen is also responsible for the production of synovial fluid and the condition of cartilage—it is responsible for its elastic properties and maintains its shape. Collagen supports the immune system's immune function. It reduces fibrosis and the spread of pathogenic microorganisms, cancer cells, and toxins. Furthermore, collagen fibers are carriers of some medications, such as interferon.

Consequences of a collagen deficiency

From the age of 25, the amount of collagen begins to decline physiologically. During menopause, the process of reduced synthesis of this protein accelerates significantly due to a decrease in estrogen levels, which affect collagen synthesis. By the age of 60, the body no longer produces any collagen at all. This process, along with the frequent collagen deficiency, can have serious health consequences. Symptoms of a deficiency include: visual disturbances, changes in the function of internal organs, weakening of the hair, deterioration of the condition, firmness, and elasticity of the skin, as well as the appearance of wrinkles (one of the first symptoms), hair weakness and brittleness, and, in the long term, premature hair loss.

What influences the synthesis and amount of collagen?

Many factors influence collagen status, including:

• Age – With increasing age, collagen synthesis decreases, resulting in a deterioration in the condition of the skin. Collagen changes its structure and physical and chemical properties with age. This leads, for example, to excessive dryness of the skin, loss of firmness and elasticity, which in turn leads to wrinkles and furrows. With increasing age, the levels of vitamins (A, C, E) and minerals (copper), which support the natural regeneration of collagen, also decrease.
• external factors: sunlight, excessive temperatures, free radicals and toxins,
• genetic and hormonal diseases – the reason for this may be a decrease in the concentration of this protein in young people,
• emphasize,
• Excessively intense physical exertion has a negative effect on collagen synthesis, but physical exertion itself supports both concentration and collagen synthesis and the entire skeleton.
• To promote natural collagen synthesis or to support supplementation, it is important that the diet is rich in vitamins and minerals, with particular emphasis on vitamins A, C, E and copper.

Collagen sources

Natural sources of collagen are products of animal origin. Previously, beef, pork, and, to a lesser extent, poultry have played the main role, but there are suggestions that collagen derived from such sources has low absorption and may have a significant impact on collagen growth in the body. Currently, evidence suggests that collagen from fish is better absorbed. However, the structure of these collagens is quite similar, so the final decision remains controversial.

It is also possible to use collagen in the form of supplements. The largest role in this group is played by collagen obtained by hydrolysis or hydration. However, regular use is of great importance for the supplement itself, so you don't have to worry about, for example, taking liquid, as we prefer capsules, where it is important to approach it systematically. Supplementing with collagen and most supplements will not bring the same effect as regular use of the preparation. An additional indicator of the effectiveness of the supplement used is the composition of the supplement, i.e., the absence of harmful and/or unnecessary additives. An additional advantage is the presence of vitamin C in the preparation, which directly affects collagen synthesis. In addition, it should be noted that jelly and gelatin cannot replace dietary supplements, as they are absorbed by only a few percent compared to dietary supplements, whose absorption is much higher.