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<hr />Natalia Velichko, Ph.D., medical consultant at the representative office of Guna Italy in Ukraine (Ukraine)<hr /> Aging gracefully is a worthy goal. Sophia Loren In the field of aesthetic medicine, one of the priority trends in the last 30–40 years is the solution to the problems of correcting age-related changes in the dermis using biotechnologies aimed at rejuvenation by activating one’s own renewal processes. This direction is based on the ability of skin fibroblasts to repair themselves. The most physiological method of stimulating fibroblasts and their production of collagen at present is the introduction of a complex of amino acids in the form of nutritional supplements. Let&#39;s talk about this Fibroblasts are the main cells of connective tissue that originate from mesenchymal stem cells (germ tissue of humans and animals). Their function is to synthesize the intercellular matrix of connective tissue, which provides transport of chemical elements and mechanical support of cells. The main components of the matrix are glycoproteins, among which collagen predominates. Skin fibroblasts are located in its middle layer. They are responsible for the synthesis of proteins such as:<ul><li> tinascin – is involved in regulating the normal distribution of collagen and elastin in tissue;</li><li> nidogen and laminin are peptides that are part of the basement membrane of the skin and are its building material;</li><li> proteoglycans – play a role in cell interaction,</li></ul> and others. Fibroblasts are also indispensable for the regeneration of epithelial cells, producing many cell growth factors (tissue protein hormones), including:<ul><li> epidermal - accelerates tissue growth through cell division and the movement of keratinocytes synthesizing keratin (pigment);</li><li> main – enhances the growth of all skin cells, the production of fibronectin, which is involved in the body’s defense reactions, collagen and elastin;</li><li> keratinocyte growth factor – promotes epithelization and healing of damaged skin areas;</li><li> transforming (various types) – promotes the formation of small vessels, the movement of phagocytes to a foreign element, as well as stimulation of the synthesis of elastin and collagen.</li></ul> From a biological point of view, skin aging is a process of reducing the number of fibroblasts responsible for the synthesis and reproduction of collagen. It has been scientifically proven that normal human fibroblasts can multiply only a limited number of times - approximately 50 (Hayflick limit), and the functional activity of old cells decreases. Age-related changes in the structure of collagen are caused not only by genetic reasons: they are also associated with spontaneous structural modification of collagen molecules under the influence of certain agents (bad habits, strict diets, smoking, excessive physical activity, UV radiation), leading to the formation of cross-links. Normally, collagen forms intramolecular and intermolecular cross-links. This reaction is carried out due to the activity of the enzyme lysyl oxidase. The main structural unit of collagen is tropocollagen, which consists of three polypeptide chains rich in glycine, proline, hydroxyproline, lysine and hydroxylysine residues. Intramolecular cross- links are formed between lysine residues, intermolecular cross-links are formed from lysine and two hydroxylysine residues. During life, products of non-enzymatic glycation of proteins and their receptors accumulate in tissues, promoting the formation of cross- links between collagen fibers. In this case, collagen of connective tissue fibers is glycosylated at lysine and oxylysine residues, which interferes with the formation of normal inter- and intramolecular cross-links between fibers. In addition, it is known that the structure of collagen includes helical sections and so-called telopeptides - special sections of the protein that are used in the synthesis and acquisition of the required conformation by the protein, after which they are proteolytically removed over time. Normally, lysyl oxidase forms cross-links only between the helical sections of collagen, and with aging, telopeptides also begin to “cross-link.” All these processes cause disruption of collagen architecture and lead to loss of its elastic properties . To all of the above, it should be added that an increase in the number of cross-links leads to a deterioration in the penetration of nutrients and regulatory substances through the collagen network - this is also the reason for the dysfunction of the dermis with age (collagen maturation processes begin to slow down between 25 and 30 years of life). The “unlinking” of cross-links between collagen fibers is carried out by a special enzyme, collagenase. However, under the influence of a number of factors, the enzyme is not able to break down these structures, so the process of collagen renewal in the skin is inhibited. As a result, collagen threads accumulate in the intercellular space and cause wrinkles. From what has been said, it is clear that the main task of anti-aging agents is to inhibit the formation and destroy existing collagen cross-links and increase the production of the latter by fibroblasts. And modern aesthetic cosmetology constantly works with this task, stimulating the processes of neocollagenesis by:<ul><li> the use of hardware techniques, such as ultrasonic, acid and diamond peeling, fractional thermolysis and laser dermabrasion, ultrasonic phonophoresis, myostimulation, thermolifting, microcurrent therapy (electroporation, iontophoresis, etc.), ridolysis, thermage, collagenarium;</li><li> conducting mesotherapy and contouring sessions using injections of hyaluronic acid, vitamin and protein complexes;</li><li> carrying out microneedling procedures (using a mesoscooter) both in a cosmetology clinic and at home.<a name="_GoBack"></a></li></ul> However, the cosmetic procedures listed above provoke only a short-term release of fibroblast growth factors in the skin. Only a sufficient supply (qualitative and quantitative) of amino acids as a building material for the protein of youth can provide a long-term and increasing rejuvenating effect based on self-healing of the skin, along with periodically repeated procedures for stimulating neocollagenesis. <img alt="" src="https://pro.bhub.com.ua/cosmetology/upload/files/%D0%BA%D0%BE%D0%BB%D0%B0%D0%B3%D0%B5%D0%BD.png" style="width: 450px; height: 272px;" /> It is known that collagen is rich in essential amino acids such as glycine, tyrosine, methionine, proline, leucine, lysine. Moreover, the last two are present only in this protein. Fibroblasts that synthesize collagen “use” these amino acids to enzymatically hydroxylate the finished collagen chain. When at least one essential amino acid is missing, collagen formation stops. As a result, the skin becomes thinner and cannot retain water. This leads to another way to combat collagen aging - providing the dermis with the necessary amino acids. Almost all amino acids found in nature contain an asymmetric carbon atom, therefore they are optically active compounds and are capable of rotating the plane of polarization either to the right or to the left (D- and L-isomers). Physiologically, their meaning is different. Mostly L-amino acids are found in animal and human proteins, which is why they are called natural. D-series amino acids are not absorbed by the body at all, since enzymatic systems are not adapted to their breakdown. Fibroblasts require essential amino acids to maintain collagen synthesis. Moreover, it is necessary that these are left-handed isomers of amino acids (L-form). Only in this case can one count on a positive result - an increase in the number of fibroblasts, stabilization of collagen synthesis, formation of stable tertiary and quaternary bonds and ordered deposition of fibrils. Another interesting feature of collagen synthesis is that all amino acids that will be contained in the new dermal protein must be present in sufficient quantities and in a certain proportion at the site of its synthesis. To do this, you can eat more food rich in proteins, but this method very often turns out to be ineffective. Why? Firstly, proteins that enter the body along with natural daily nutrition are for the most part not broken down (in a healthy person - up to 70%). All those nutritional proteins that consist of long chains of amino acids have problems with absorption in the small intestine. This is where the roots of the eternal dietary problem of effectively renewing collagen in the body lie. Long amino acid chains (poly- and oligopeptides) should usually be split into fragments built from 2-3 amino acids (dipeptides and tripeptides), or even into free amino acids. The division of proteins is catalyzed by specific digestive enzymes - proteases. After absorption into the blood, they are transported to the liver, where plasma proteins and enzyme proteins undergo synthesis. Amino acids that do not participate in the synthesis of new protein molecules undergo a catabolic process of deamination in the liver. The remaining amino acids containing nitrogen are reformed into urea and excreted in the urine. Particles of amino acid molecules that do not contain nitrogen are reformed into fats or carbohydrates and are oxidized to produce energy or create a reserve in the form of fat. There are no reserves of protein in our body. Only blood plasma albumins serve as a mobile reserve of amino acids to meet the necessary life needs. The second reason is a monotonous, monotonous menu, which is constantly lacking essential amino acids. Thus, strict vegetarians are susceptible to nervous tension, which is a consequence of a lack of protein in food, which supports brain function. It is no coincidence that the culture of meditation, “calming down,” “turning off” the mind was born in a society that, for religious reasons, denies proteins from animal meat. Thirdly , in the whirlwind of a continuously flowing life, it is really difficult to balance a diet in such a way, to compare a set of different products so that they completely cover our body’s needs for amino acids. Fourthly , diseases of the body such as impaired gastric acidity, pancreatitis, pancreatopathies or hepatobiliary problems, dysbiosis, cause disturbances in the process of dissimilation or transport of nutritional elements of proteins in the intestine. The fifth reason is common overeating. Excessive amounts of proteins can be just as dangerous (except during adolescence or, for example, increased sports activity) as their lack. In medicine and biology, the “path of life” is the intestine. The sixth reason is the influence of neurotransmitting factors of the brain on the functioning of fibroblasts. For example, when a pregnant woman eats optimally, the brain sends signals to fibroblasts. These signals are intended to stimulate skin growth in connection with the expected growth of the fetus. If, however, during pregnancy a woman eats food depleted in essential amino acids, then the signals become weak, the production cells do not work “overtime”, as a result of which the skin does not grow, the number of keratinocytes does not increase, and the fetus, stretching the skin, also stretches the epidermis , causing unsightly and unwanted stretch marks. The seventh reason is processes directly related to intoxication caused by a cancerous tumor (a deficiency of complete proteins in food can only accelerate this process, as well as the development of protein deficiency), radiation and other results of the influence of environmental factors. In any case, the above seven reasons lead to insufficient cell nutrition, disruption of the functioning of fibroblasts and regeneration of the dermis. <img alt="" src="https://pro.bhub.com.ua/cosmetology/upload/files/%D0%BA%D0%BE%D0%BB%D0%BB%D0%B0%D0%B3%D0%B5%D0%BD.png" style="width: 500px; height: 350px;" /> You can compensate for the deficiency of amino acids by giving the body a concentrated and pure form of a ready-made set of free amino acids with NNU (Net Nitrogen Utilization - the percentage of nitrogen utilization) equal to 99%, which in 99% of cases will be used in anabolic processes to recreate and reconstruct new collagen proteins. Such a nutraceutical is Gunamino Formula. An innovative and unique characteristic of Gunamino Formula Amino Acid Complex is that it produces NNU equivalent to 99%. This percentage of protein digestibility is without a doubt the highest compared to any other protein food or dietary product. Clinical studies have shown that NNU Gunamino Formula is approximately 34% higher than that of whole chicken eggs, previously considered a protein with high biological value. Thanks to its special amino acid composition, Gunamino Formula releases less than 1% of metabolic nitrogen, which is much less than other dietary proteins or dietary products, thereby not creating additional stress on the kidneys and liver. The amino acids in Gunamino Formula are derived from plants through extraction, fermentation, ultra-high purification and crystallization. The drug contains eight essential, so-called free amino acids , almost ready for absorption (isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine). The body of a person taking the drug does not need to waste time, digestive enzymes and energy on digestion. Free amino acids are able to enter the blood in the shortest possible time and, being delivered by it to places that require additional collagen synthesis, are immediately included in its formation. It is also of great importance that in GUNAMINO FORMULA all amino acids are in the L-form, since proteins of animal and plant organisms are created mainly by L-forms of amino acids (with the exception of phenylalanine, which is represented by D-, L-forms). Thus, dietary supplements containing L-amino acids are considered more suitable for the biochemical processes of the human body. GUNAMINO FORMULA after administration behaves like a pre-digested food protein and is rapidly absorbed in the first 100 cm of the small intestine within only 23 minutes, without any fecal residues, without causing allergic reactions. The drug can be given even to a very sick person, almost like a dropper, because it is absorbed directly into the blood and takes an active part in the processes of construction and restoration of proteins, including proteins that are most difficult to restore - collagens. Ten grams of GUNAMINO FORMULA provides protein synthesis equivalent to approximately 350 g of meat or fish, while only 50 kcal are consumed. Amino acid cofactors are vitamins, mineral salts or trace elements that help amino acids during metabolic processes in the human body. Thus, the formation of the most important amino acid for collagen, hydroxyproline, occurs exclusively with the help of the enzyme proline hydroxylase, and this enzyme is in active form only if it consists of divalent iron, and divalent iron is provided by vitamin C. A deficiency of this vitamin disrupts the hydroxylation process, thereby disrupting neocollagenesis, which is fraught with the formation of loose collagen, which underlies sagging, “tired” skin. A lack of vitamin B6 or copper leads to disruption of the structure and stability of collagen, since pyridoxine, in the presence of copper, strengthens the intra- and intermolecular cross-links of collagen. In the absence or insufficient intake of zinc into the body, the aging process of the dermis is accelerated, since zinc is present in the active center of the enzyme collagenase, which triggers the hydrolysis of collagen and ensures its constant renewal. Activation of collagenosis is also influenced by:<ul><li> vitamin A (retinol) – causes metabolic processes in cells to proceed more intensely, stimulating the activity of the cells themselves, which leads to the necessary tissue regeneration due to increased collagen production;</li><li> selenium – stimulates the activity of stem cells, enhances collagen synthesis, as a result of which the skin is renewed and regenerates faster;</li><li> methionine is an amino acid containing sulfur that firmly binds fibers to each other, ensuring collagen elasticity.</li></ul> All these substances in preventive doses (without causing hypervitaminosis) are contained in the Vit Formula preparation. In addition to the cofactors listed above, necessary for neocollagenesis, Vit Formula also contains biotin, choline and inositol. Biotin, or vitamin H, is essential for maintaining skin tone, moisture and hair strength. Choline and inositol take part in the metabolism of cholesterol, improve the flow of bile, and have a strengthening effect on hair. As can be seen from the composition, Vit Formula is indicated as an ideal supplement and complement to the use of Gunamino Formula to ensure optimal collagen synthesis. We hope that you read this article carefully and with interest and, like us, came to the conclusion that the key to success in correcting involutional skin changes is to carry out cosmetic biorevitalization procedures in combination with Gunamino Formula, Vit Formula. First published in Les Nouvelles Esthetiques 2015/№1

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