Dietician
Karolina Dobrowolska-Zrałka
Collagen This is a key structural protein that builds the scaffolding of our connective tissues. It accounts for up to 30 % of the total mass of proteins in the human body. His unique triple Helisa gives the skin elasticity and firmness, and the joints and bones - strength and depreciation of loads. In the skin, collagen fibers intertwine with elastin, forming a dense network that protects against water loss and is responsible for regeneration after microdamages. In tendons and ligaments, collagen gives tissue high stretch resistance, and in the bones it acts as a scaffolding for hydroxyapatite crystals, while ensuring flexibility and fracture resistance.
The synthesis of collagen takes place in fibroblasts, where preprocolagen is created from the amino acids of glycine, prolina and lysine. After numerous post -translational modifications and the creation of a triple heliisa, Prokolagen is transported to extracellular space, where enzymes remove the tips, and lysinoxydase creates covalent cross bonds, stabilizing fibers. At the same time, metaloproteinase (MMP) constantly degrade damaged fragments, ensuring the renewal of the network.
From around 25-30. The year of lifestyle collagen slows down - fibroblasts produce less molecules, and MMP activity increases. The skin becomes thinner and less elastic, wrinkles appear, and the joints lose depreciation, which intensifies degenerative ailments. External factors, such as UV radiation, environmental pollution, oxidative stress and low diet in cofactors (vitamin C, copper, zinc) and precursor amino acids, additionally accelerate degradation.
Fortunately, there are many ways to support the natural production of collagen and minimize its loss. A diet rich in protein, vegetables and fruits with vitamin C, regular physical activity, avoiding smoking and excessive exposure to the sun, as well as supplementation with hydrolyzed collagen peptides can significantly improve the condition of the skin, joints and bones. In recent years, the popularity of cosmetic procedures that stimulate fibroblasts - micro -gear, mesotherapy or fractional laser.
In this article, we will discuss in detail: what collagen is and how it is built, the main types and their functions, the role of collagen in the skin, connective tissues, joints and bones, causes of deficiency and symptoms of degradation, the process of synthesis and degradation, and practical support methods - from diet and supplementation, to lifestyle and treatments. Thanks to this, the acquired knowledge will allow you to consciously take care of your health and beauty every day.
What is collagen?
Collagen is a fibrillary protein, in which three polypeptide chains roll into a triple helisa with unique stability. Each chain consists of a repeated Gly -X -Y motif - glycine in every third position allows strictly adjacent laying of chains, and prolines and hydroxyprolins stabilize helisa through hydrogen bonds. Fibrillary collagen structure allows you to form a fibril with a diameter of 50-500 Nm, which then connect into larger fibers that build extracellular matrix connective tissues.
At least 28 types of collagen are distinguished in the human body, but the most important are types I, II and III. Type I collagen is responsible for tensile strength - it is found in the skin, tendons, ligaments, bones and teeth. Type II builds articular cartilage, thanks to which this tissue has depreciation properties and compressive resistance. Type III coexists with the type and in the skin, walls of vessels and parenchymal organs, increasing tissue elasticity.
Collagen functions are extremely diverse: it is responsible for tissue mechanical strength (stretching, breaking resistance), elasticity (return to its original shape), structural integrity (maintenance of cells in the matrix) and regeneration (wound healing). In extracellular matrix, he cooperates with elastin, fibrillin and laminin, creating a network that regulates cell migration, their proliferation and mechanotransduction.
Understanding the basic role of collagen is the foundation for further analysis: how it is chemically built, what are the main types and what functions they perform in different tissues. Without this knowledge, it is difficult to develop effective diet, supplementation or cosmetic strategies to support synthesis and protect collagen fibers against degradation.
Chemical construction of collagen
At the molecular level, collagen is a fibrillary protein with a molecular weight of several hundred kDa. His triple Helisa is formed of three identical or similar α chains. The characteristic Gly -X -Y motif is repeated every three amino acids, which is an absolute condition for stability - glycine, the smallest amino acid, allows the tight arrangement of Helisa, and X and Y are mostly proline and hydroxyproline.
Hydroxyization of proline and lysine is a key post -translational stage, taking place in the endoplasmic reticulum of fibroblasts. Enzymes Prolyl- and Lysyl-Hydroxylase catalyze these reactions, and the cofactor is vitamin C. The lack of vitamin C leads to the formation of incorrectly Jydrooksized Helis, which is observed in a scoring deficiency.
After throwing prokolagen into extracellular space, propeptide fragments of N- and C-end are removed by procololagenase, creating tropocolagen. Tropocolagens spontaneously aggregate into regular fibrils with a shift of every 67 Nm (so -called Drinking D). Then lysinoxydase catalyzes the creation of covalent cross bonds between tropocolagen molecules, which gives the network unique mechanical strength.
Each α chain has over 1000 amino acids, and the sequence dedicated to specific types of collagen determines the mechanical properties: the long sequence of numerous GLY-X-Y motifs gives fibers stiffness and stretching resistance, while the presence of non-hellial domains (so-called teleopeptides) will conditions cross-linking.
Higher -order structure - from fiber to macrofibril and macro - determines the unique properties of tissues: thin type III fibrils form loose networks in soft tissues, thick type I fibers strengthen the tendons, and the type II structure with proteoglycans absorbs joints.
Detailed knowledge of collagen chemical structure is the basis for the development of regenerative therapy and biomaterial design - collagen hydrogeles, tissue engineering scaffolding or carrier nanoparticles that may provide growth factors.
Collagen types (I, II, III ...)
According to the NIDCR classification, at least 28 types of collagen are distinguished, but the most important in the context of mechanical and medical functions are I- V types:
Type and - creates thick fibers with a diameter of up to 500 Nm, is responsible for tensile strength. Occurs in the skin, bones, tendons and ligaments.
Type II - builds thin fibrils in articular cartilage, which allows cushioning and compressive resistance.
Type III - co -occur with the type and in the skin, walls of vessels and parenchymal organs; The fibers are more flexible.
Type IV - creates a network in the basement membranes (e.g. epidermis, alveoli), it acts as a filter.
Type V - present in the placenta, microfibrillary skin structures, co -creates fibers with type I.
Mutations in the genes Col1A1 and COL1A2 (Type I) lead to Osteogenesis Imperfecta, and in COL3A1 (type III) to the Ehlers -Danlosa Type IV syndrome, which shows how key the specific construction of each type is.
The role of collagen in the skin and connective tissues
In the proper skin, collagen type I and III forms a network. In the papillary layer, the fibers are arranged irregularly, facilitating the replacement of the substance between the dermis and the epidermis. In the mesh layer, the fibers are thicker, arranged in parallel, which gives tensile strength.
Collagen maintains skin tension, and in combination with elastin is responsible for firmness and elasticity. Its deficiency results in flabby, wrinkles and loss of firmness.
In tendons and ligaments, the type I intertwines into parallel fibers, which ensures enormous strength with minimal stretching. Such an organization allows you to transfer loads from muscles to the bones.
Collagen also plays a role in healing - fibroblasts synthesize it at the place of damage, creating granulation, and in the remodeling phase the fibers are rebuilt, restoring mechanical functions.
The role of collagen in the joints and bones
In articular cartilage, collagen type II forms a network with a scottroket, which binds water and absorbs loads. Supplementation with type II collagen peptides stimulates ecm chondrocytes and reduces degenerative pain in clinical trials.
In bones, type I collagen is a scaffolding for hydroxyapatite crystals, which gives bones elasticity and fracture resistance. Collagen supplementation with calcium and vitamin D supports bone mineral density.
Collagen deficiency - symptoms and consequences
Collagen deficiency is manifested by the loss of skin elasticity, wrinkles and stretch marks, joint pain, stiffness and osteoporosis. Weakened tendons and ligaments are more susceptible to injuries, and slower wound healing testifies to the ECM deficit.
Causes of collagen loss
The main factors are UV radiation (activates MMP), free radicals (oxidative stress), advanced glycation products (AGE), smoking (nicotine strengthens ROS) and stress (cortisol inhibits fibroblasts). A diet low in amino acids and cofactors (vitamin C, copper, zinc) also weakens synthesis.
How does the body synthesize collagen?
Synthesis takes the stages: transcription and translation of preproprocolagen, post-translational hydroxylation of proline and lysine (cofactor: vitamin C), glycoslation, submission of a triple heliis, secretion of prokolagen, removing tips by prokolagenase, and then cross-linking by lysinoxidase. MMP control degradation, enabling renovation.
How to support natural collagen production?
It is worth combining a diet rich in protein (meat, fish, bone broth), vitamin C (citrus fruits, peppers), copper and zinc (nuts, seeds) with hydrolyzed supplementation with collagen peptides (5-10 g per day). Physical activity, UV avoidance and toxins and fibroblasts stimulating treatments (micro -gear, mesotherapy) bring the best results.
Sources
- Shoulders MD, Raines rt. Collagen Structure and Stability. Ann Rev Biochem. 2009.
- Prockop DJ, Kivirikko Ki. Collagens: Molecular Biology, Diseases, and Potentials for Therapy. Ann Rev Biochem. 1995.
- Ricard-Blum S. The Collagen Family. Cold spring harb perspect biol. 2011.
- EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA). Scientific Opinion on the Substantytion of Health Claims Related to Collagen Hydrolysate. EFSA Journal. 2017.
- Furukawa H. et al. The effect of collagen peptides ingestion on body composition and skin-aging parameters. J nutr sci vitaminol. 2017.
FAQ
What is collagen and what is the functions in the body?
Collagen is a fibrous structural protein forming a triple helisa. He builds a network in extracellular matrix, joints and bones, responsible for their endurance, elasticity and regeneration.
What are the main types of collagen and where do they occur?
Type I - skin, tendons, bones; Type II - articular cartilage; Type III - vessels, skin; Type IV - basal membranes; Type V - bearing and skin microfibrils.
Why does collagen production decrease with age?
After the age of 25, fibroblasts produce less preprocolagen, and degrading enzymes (MMP) are more active. External factors (UV, ROS, Age) intensify degradation.
How to support dietary collagen synthesis?
A diet rich in protein (glycine, prolina, lysine), vitamin C (citrus fruits), copper and zinc (nuts, seeds) and collagen peptide supplementation supports synthesis and fiber stabilization.
Is collagen supplementation safe?
Yes, hydrolyzed collagen peptides are safe at a dose of 5-10 g per day. Gastrointestinal discomfort or allergic reactions may occur rarely.
What cosmetic treatments support collagen production?
Micro -gear, mesotherapy and fractional laser stimulate fibroblasts through controlled microdamages, accelerating ecm remodeling.
How long do you need to use collagen to see the effects?
The first results are visible after 4-6 weeks, while full effects (skin firmness, reduction of joint pain) appear after about 10-12 weeks of regular treatment.
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