Collagen - The Protein Of Youth: How To Choose And Take It Correctly

Collagen is one of the main components of connective tissue and, undoubtedly, the most popular (along with omega-3 polyunsaturated fatty acids) dietary supplement. It is called the protein of youth - and this, as we will demonstrate a little later, is very reasonable.

However, sometimes the pursuit of beauty can turn into very unpleasant consequences: after all, an incomplete understanding of the processes of biochemical transformation does not exempt from responsibility. So, in particular, one should be aware that there is a huge number of different types of collagen - their number has long exceeded two dozen - each of which has its own specific localization, and therefore, certain functions. So what to choose and how to stimulate the formation of your own protein? Let's figure it out.

Collagen and its structure

Collagen has an interesting spatial structure that largely determines its properties: it consists of three intertwined chains. However, from the point of view of understanding the processes leading to its insufficient production, it is its amino acid composition that is much more important - those working bricks that create the initial framework.

Three amino acids are needed to build the correct collagen polypeptide sequences: glycine, proline, and lysine. The first is replaceable: our body is able to independently reproduce its synthesis in cellular factories. In particular, this is also observed in the brain: after all, as you know, glycine acts as one of the neurotransmitters - chemical compounds that contribute to the transmission of a nerve impulse from one neuron to another.

And if proline, another amino acid in the composition of collagen, is also capable of endogenous formation, then lysine should only come with biologically active additives or food components. So, let's say they are rich:

• beef and veal;

• chicken, turkey, rabbit meat;

• herring, tuna and shrimp;

• eggs;

• soybeans and beans.

In addition, in the process of collagen synthesis, a number of important transformations occur, the key of which is undoubtedly the transformation of proline and lysine into hydroxyproline and hydroxylysine under the action of a specific enzyme (hydroxylase). The functioning of this enzyme is impossible without copper, as well as the participation of vitamin C.

So, in particular, one of the most striking signs indicating hypovitaminosis of ascorbic acid and requiring targeted attention from nutritionists and doctors - gum bleeding - develops due to increased vascular fragility observed in the absence of hydroxylation reactions of the corresponding amino acids in the composition of the collagen fiber. .

Recent studies also indicate that this process is significantly suppressed by homocysteine, the most significant marker of cardiovascular pathologies. Thus, we can draw a logical conclusion: without monitoring the dynamics of this indicator and without providing proper support for methylation reactions, in which homocysteine ​​is converted, one can forget about the production of high-quality collagen. We will talk about this a little below.

Types of Collagen

The number of currently known types of collagen approaches three dozen, and each of them has its own localization. The appearance of one type or another in the wrong place indicates, just like a change in the amino acid composition, systemic diseases of the connective tissue - collagenoses.

Causes of lack of own collagen

1. Given that collagen is a protein, its structural building blocks are amino acids, the insufficient intake of which, together with food components, will also lead to a decrease in endogenous synthesis.

2. Violation of the digestion and breakdown of protein in the stomach, observed with a decrease in the secretion of hydrochloric acid by the cells of the mucous membrane, is usually manifested by a complex of characteristic complaints:

   • heaviness in the abdomen;

   • heartburn and belching;

   • bloating and gas formation;

   • unstable chair.

   A decrease in the total protein index in a biochemical blood test is characteristic, and a compensatory increase in the albumin fraction is also possible.

    

   Hypoacidity is also associated with a lower resistance of the organism to various kinds of infections, in particular, parasitic ones. The reason for this decrease in the secretion of hydrochloric acid may be:

   • distribution of H.pylori along the entire perimeter of the stomach;

   • frequent exposure to stress factors: the hormones secreted by the adrenal cortex lead to vasospasm and, thus, worsen the blood supply to the mucosa;

   • the formation of antibodies to one's own cells is characteristic of autoimmune gastritis;

   • reverse reflux of bile;

   • violation of methylation processes.

   Any of the above factors, leading to a decrease in acidity, also inhibits the activation of proteolytic enzymes under the action of hydrochloric acid - the cleavage of bonds in polypeptide chains is disturbed.

    

3. Exocrine pancreatic insufficiency, the enzymes produced by which carry out the final enzymatic cleavage in the intestinal cavity and on the villi of its epithelial lining.

4. Violation of the outflow of bile, which acts as an activator of pancreatic enzymes, is observed when stones are blocked with excretory ducts, with helminthic invasion, a decrease in the fluidity of bile due to an increase in the content of cholesterol in its composition.

1. Malabsorption syndrome, celiac disease and other pathologies in which, to a significant extent, the process of absorption of nutrients on the intestinal villi is inhibited.

2. An increase in the concentration of the amino acid homocysteine, which disrupts the formation of the correct structure of collagen protein, is noted with deficiencies of vitamins B2, B6, B9, B12, as well as with a lack of zinc in the body and mutations in the most important genes that control the entire methylation process: MTRR, MTHFR. MTR.

3. Hypovitaminosis of ascorbic acid.

4. Copper deficiency, a mineral also needed to convert the amino acid lysine to hydroxylysine.

Signs of a lack of collagen

Given that the formation of collagen in the body is significantly reduced not only with age, but also under certain previously described conditions, we strongly recommend that you pay attention to the clearly visible signs of a deficiency of this connective tissue protein:

• bone fragility - collagen is a kind of framework to which the minerals involved in bone formation are attached;

• early wrinkles;

• pain in the joints;

• problems with intervertebral discs;

• loosening of teeth;

• glaucoma.

Separately, I would like to add about hypovitaminosis of ascorbic acid - after all, as already mentioned, in conditions of its deficiency, the conversion of lysine and proline is impossible. You can focus on the indicators of organic acids and amino acids in the urine - in particular, to increase:

Symptoms of vitamin C deficiency include:

1. Frequent colds due to a decrease in the activity of the immune system and a decrease in the formation of protective proteins by neutrophils.

2. Iron deficiency due to a violation of its absorption in the gastrointestinal tract - up to anemia.

3. Prolonged healing of wounds - especially well seen on scratches, damage from pimples.

4. Bleeding from the nose and gums.

Violations in the formation of collagen fibers also occur with an excessive concentration of the amino acid homocysteine ​​in the blood, which, as a rule, is observed in conditions of a lack of folic acid, vitamin B6 or cobalamin, as well as mutations in the corresponding genes. Thus, the measurement of homocysteine ​​levels can be a diagnostically important parameter.

1. Definition of deficiency of folic acid (vitamin B9):

   ↑ MCV (mean volume of erythrocytes) in the general blood test;

   ↑ homocysteine;

   ↑Forminoglutamic acid in organic acids in urine;

    

2. B12 deficiency is indicated by:

   ↑ MCV (mean volume of erythrocytes) in the general blood test;

   ↑ homocysteine;

   ↑ methylmalonic acid in organic acids in urine;

    

3. Folate cycle genetics: MTHFR, MTR, MTRR.

Which collagen to choose

Previously, mammalian collagen was widely used, especially in regenerative medicine. It was used as a scaffold material in the restoration of damaged or diseased tissue.

However, now, after revealing a sufficiently high risk of infection with infectious diseases (in particular, incurable, invariably fatal spongiform encephalopathy, bird and swine flu), its use has gradually been abandoned in favor of marine collagen, extracted from the scales, skin and bones of fish. The latter has, in addition, biocompatibility, low antigenicity (in other words, caused less reactions from the immune system), and also had good biodegradability.

As a nutritional supplement, marine collagen also occupies a leading position, although it is somewhat inferior to collagen peptides, which have positively proven themselves in the context of wound healing, reducing pain in the joints and tendons.

Since the first study was published on the ability of collagen hydrolysates - heterogeneous (i.e., heterogeneous) mixtures of its peptides obtained during the enzymatic cleavage of tissues containing this protein - to stimulate the formation of collagen by cartilage cells, their use has become widespread. Today, they are considered as a safe method (or a component of the main therapy) for the treatment of osteoarthritis, the most common joint disease that affects more than 60% of elderly patients and has a progressive nature.

However, given the close relationship between the transformation of amino acids in the composition of collagen and vitamin C, we want to emphasize once again: to achieve a greater effect, make sure that the supplements you buy contain ascorbic acid (or, in case of its absence, take it separately).

Supplements That Stimulate Collagen Synthesis

Recently, more and more studies have begun to be carried out on the effect of precursors (precursors) of amino acids that make up collagen on the endogenous formation, that is, directly in the cells of the human body, of this connective tissue protein.

Thus, in particular, the use of the amino acids arginine and ornithine (which are involved in the neutralization of toxic for our tissues - especially nervous - ammonia) was studied as the initial substrate for the production of proline - one of the main building blocks in the polypeptide chains of collagen.

Arginine, unlike ornithine, is much more common in protein products, and is also produced in sufficient quantities in the human body to maintain and normal functioning of muscle and connective tissue, but, most likely, its formation still does not satisfy the need for adequate collagen biosynthesis during wound healing followed by scarring of the injury site.

Scientists were very interested in the work carried out for the first time on laboratory animals: for example, they, adhering to an arginine-deficient diet for 4-6 weeks, were characterized by a higher mortality rate and increased weight loss after they were subjected to a minor injury in the form of an incision on the back. Subsequently, experiments were also carried out on healthy volunteers, the results of which showed that the use of arginine supplements did not affect the rate of formation of epithelial tissue at the site of skin injury, but significantly affected the deposition of collagen in the wound - this was also observed in mice who additionally received the amino acid ornithine.

Arginine, in addition, is involved in the formation of nitric oxide, which promotes vasodilation and is critical in the context of wound healing. This amino acid (along with ornithine) stimulates the secretion of growth hormone, and also activates the cellular link of immunity - in particular, T-lymphocytes.

In addition to arginine and ornithine, information is also provided on citrulline, another chess piece in the urea cycle, which provides ammonia detoxification. This amino acid is a direct precursor of arginine, and its use has been associated with an increase in plasma concentrations of the latter in animals with a short digestive tract. However, at the moment, there is no other indirect effect of citrulline on collagen formation.

Collagen Boosting Foods

To strengthen the skin, maintain its turgor and elasticity, prevent the development of wrinkles and preserve youth, we recommend that you pay attention to the following foods and dishes:

1. Bouillons are modern rejuvenating apples. Obtained from decoctions of meat on the bones (especially beef), they are excellent sources of collagen and a wide range of amino acids.

2. Oily fish is an excellent source of omega-3 polyunsaturated fatty acids, which have pro-inflammatory effects, as well as certain minerals, in particular zinc, which is necessary for the folate cycle reactions.

3. Eggs are rich in amino acids that make up collagen. To reduce the risk of developing food intolerances (due to the high degree of immunization of chicken protein), we recommend focusing on quail rather than chicken.

4. Leafy vegetables: spinach, arugula, lettuce. They are rich in folic acid, which is involved in the reactions of methylation and neutralization of homocysteine.

5. Sources of vitamin C, which provides the conversion of the amino acids proline and lysine:

   • rose hip;

   • sea ​​​​buckthorn;

   • bell pepper;

   • kiwi;

   • citrus;

   • Rowan;

   • currant;

   • strawberry;

   • broccoli;

   • cauliflower;

   • guava;

   • thyme;

   • parsley;

   • litchi;

   • Strawberry.

    

1. Products containing copper:

   • oysters;

   • squids;

   • offal;

   • black chocolate;

   • almond;

   • sesame and sunflower seeds.

    

How to stimulate your own collagen production

1. With a healthy gastric mucosa, you can start working on increasing acidity - the key to good protein absorption.

   We recommend that you consider taking the following dietary supplements:

   • Trimethylglycine.

   • Vitamin B2.

   • Iodine, chlorine and zinc.

    

2. For work with bile outflow (again, only after the preliminary restoration of the integrity of the intestinal epithelium and in the absence of calculi) are perfect:

   • phospholipids;

   • bitterness: tincture of wormwood and dandelion root;

   • ursodeoxycholic acid;

   • eating warm, high-fat foods;

   • duodenal sounding;

   • preparations containing animal bile.

    

3. With a decrease in the enzymatic activity of the pancreas, it is necessary to individually select suitable enzymes (of plant or protein origin).

4. Reducing the intake of fast carbohydrates and trans fats to prevent an increase in the concentration of cholesterol and, thus, a decrease in the flow of bile.

1. Working with the folate cycle - taking vitamins in their active forms and donors of methyl groups:

   • methylcobalamin;

   • pyridoxal-5-phosphate;

   • methyltetrahydrofolate;

   • S-adenosylmethionine;

   • trimethylglycine (betaine) - in the absence of damage to the gastric mucosa.

    

2. Vitamin C intake - no more than 2000 mg / day for adults.

3. Eliminate or minimize stressors.