Collagen is the most plentiful fibrillary protein of the body that conforms the conjunctive and connective tissues in the human body, essentially skin, joints, and bones. It holds all the living tissues together and ensures the integrity, elasticity, regeneration of the skin, cartilages and bones and maintenance of tonicity of the skin thanks to the serum proteins, the hydroxyproline, cystine and silicon amino acids. Collagen accounts for 80% of our connective tissues and 30% of proteins in our body. There are 28 different types of collagen in the literature depending on the tissue in which it is found: type I is more expressed in the skin, tendons and bones; cartilage is rich in type II. What changes is only the three-dimensional organization that collagen takes in space, influenced by the “cross-linking” induced by a specific amino acid: hydroxyproline. This is the reason why we find it elastic in the skin, hard and consistent in nails, filamentous and flexible in the fibrils of the bone. The human organism does not absorb collagen as such, but it is digested through the action of the gastric enzymes, in the constituent components, represented by more or less long chains of amino acids; it is superfluous for exogenous collagen, to speak of “different types”, since the protein must necessarily be decomposed into fragments in order to “enter” the body and thus performs its precious physiological properties: the variation of the amino acid sequence of collagen, whatever it is, does not reflect changes in its physiological properties, but only a different conformational orientation in space. The daily integration of collagen should amount to about 1 gram per 10 kg of body mass1.
Hydrolized Pork Collagen is produced from fresh skin or food grade gelatin products. Is an effective food aid for the regeneration and protection of collagen, provides 16% of essential amino acids, 60% of conditionally essential amino acids, contains glycine, arginine and methionine, the 3 amino acids precursors of synthesis of creatine (regenerating ATP, the source of muscular energy). In its hydrolyzed form, porcine collagen is characterized by a high food absorption: bioavailability studies show that the intestinal absorption of the pork hydrolyzed collagen ingested rises to 82% in the first 6 hours after ingestion and to 95% in 12 hours.
Silicon from Equisetum arvense is a structural element of connective tissue and enters the constitution of the main macromolecules such as elastin, collagen, proteoglycans and glycoproteins, promoting their regeneration. The silicon content is closely related to the optimal skin conditions, such as the rate of hydration, elasticity, the absence of wrinkles and expression lines, the ability to heal and regenerate. It also acts as a metabolic protector, acting at different levels: it opposes the lipid peroxidation responsible for the liberation of free radicals, it counteracts the cross-linking and non-enzymatic glycosylation of the connective tissue proteins that cause stiffness and sclerosis, it regulates and stimulates the mitosis of fibroblasts and for this property, it plays an essential role in the process of dermal and epidermal cells regeneration, and lastly it is a cofactor of the elastin synthesis. Collagen synthesis is silicon-dependent, which influences the hydroxylation process of proline in hydroxyproline.
MSM (Methylsulfonylmethane) is a biologically active form of organic sulphur with anti-inflammatory, antioxidant and pain-relieving properties. It restores the formation of cross-links in collagen, preserving its elasticity, and is considered a synergistic element in stimulating collagen synthesis for the amino acids cystine, glycine, hydroxyproline, ornithine and silicon. MSM is a potent antioxidant, which can have positive effects on joints, help protect cells from oxidative stress and has a positive impact on the health of the skin and subcutaneous tissue.
Vitamin C: essential for the formation of collagen, it helps to maintain the integrity of substances of mesenchymal origin (connective tissue, osteoid tissue and dentin). It is a potent reducing agent which in the body is oxidized and reduced, functioning as a cellular redox system. In the absence of vitamin C, cells cannot hydrogenate proline in y positions, resulting in an instability of the collagen leading to scurvy.
Maritime pine extract. Collagen is degraded by proteolytic enzymes, called metalloproteinases. They break the long protein chains that make up collagen, forming shorter fragments with no mechanical properties. MMPs are a family of molecules similar in chemical structure, with different specificities for a wide variety of substrates, capable of degrading all the components of the extracellular matrix (collagen, elastin, laminins, proteoglycans). The MMPs most involved with skin aging processes are MMP1, which begins the degradation of type I and III collagen; MMP9, which operates a further fragmentation into smaller peptides; while MMP2 attacks type IV collagen, contributing to the formation of wrinkles. In young skin that is not exposed to sunlight, the synthesis of collagen by fibroblasts and its degradation by MMPs are in constant equilibrium, so as to guarantee the physiological replacement of structural macromolecules, keeping their content and functionality unchanged, and preserving the integrity of the skin. With increasing age there is a progressive imbalance of this equilibrium and there is a gradual reduction in the synthesis of collagen precursor peptides, associated with an increase in the degradation of mature collagen. The consequence of this degenerative phenomenon is a general disorganization of the collagen fibers, which partially lose their supporting role, causing a partial atrophy of the extracellular matrix, which becomes soft and lacking in tone. The maritime pine bark has excellent radical scavenging properties2. The extract act as inhibitor of metalloproteinases, resulting in proteolytic tissue damage or remodeling in pathophysiological conditions.
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