COLSWINE does not contain fats, sugars, sweeteners, colorings, preservatives or allergens. It is a food supplement that does not present intolerances, side effects or incompatibility with diets.
Collagen is the most abundant protein in the human body, it forms the tissue structure of the musculoskeletal system (bones, cartilage, muscles, tendons, ligaments), the protective and supportive tissues (skin and subcutaneous tissue), but also of some other specific tissues (gums, dentin ...).
The percentage of protein content in the various tissues is as follows:
Dosage form: 30 sachets of 15.5 g of soluble powder, cocoa taste
How to use: 1 sachet a day dissolved in a liquid food (water, liquid yogurt, milk, milk shakes, fruit juices, etc.) At room temperature or warm, preferably in the evening, at least 1 hour after dinner, for the stimulus that exerts on the production of GH and collagen.
Warnings: do not exceed the recommended daily dose. Keep out of reach of children under three years. The product should not be understood as a substitute for a balanced diet and a healthy lifestyle. Keep in a cool and dry place. Do not consume the product beyond the declaration data reported on the box and in each sachet. The product is contraindicated alone in patients suffering from phenylketonuria and the reason is easily understandable: the recommended daily dose brings 230 mg of phenylalanine, an essential amino acid present in nature in collagen. Finally, like all protein products, people on a low-protein diet and a cause of kidney problems or severe hepatitis can only take it under strict medical supervision.
COLSWINE is a food supplement with:
The triple helix of collagen is made compact and stable by a particular sequence of amino acids: one amino acid every three is Glycine and most of the remaining amino acids are Proline and Hydroxyproline:
The HYDROLYZED PIG COLLAGEN contained in COLSWINE is easily used by humans: the pig genome is very similar to the human one and this makes this type of collagen extremely histocompatible with humans. Hydrolyzed collagen has the following nutritional characteristics:
In its hydrolyzed form, pig collagen has an average molecular weight particularly low, and is characterized by a high food absorption.
Bioavailability studies show that absorption at intestinal level of ingested CH rises to 82% in the first 6 hours after ingestion (1) and to 95% in 12 hours (2):
In rats, 12 hours after the administration of a hydrolysed collagen dose with the C14 isotope marker in the rat cartilage (C), twice as much radioactivity is accumulated than that which accumulates when only the marked proline is ingested. Furthermore, in cartilage (C), the radioactive signal is maintained in the 96 hours, which indicates a considerable concentration of the hydrolyzed collagen in the cartilage tissue. This effect is not detected in plasma (P) or in other tissues (2).
STUDIES IN VITRO
On the cartilaginous tissue
Studies on the cultivation of animal and human chondrocytes show that the presence of Hydrolyzed Collagen stimulates these cells to synthesize collagen, as well as the other components of the extracellular matrix of cartilaginous tissue (proteoglycans) (3,4,5). This effect occurs as much if hydrolyzed collagen is obtained from type I collagen as from type II (4). Furthermore, it is dose-dependent (3,4) and is not produced with non-hydrolyzed collagen, nor with hydrolyzed proteins other than collagen (4).
On the bone tissue
Studies on osteoblast and osteoclast cultures have shown that the presence of hydrolyzed collagen stimulates collagen synthesis and the osteogenic activity of the former and inhibits the re-absorbing activity of the latter, in a dose-dependent manner (6,7). Other studies done on osteoblasts and bone marrow cells show that the presence of a type I collagen matrix induces the differentiation and maturation of osteoblasts and the uniform mineralization of that matrix (8,9,10). This effect is dose-dependent (9).
BAMBOO, ORTICA, VITAMIN C: bamboo contains the highest percentage of organic silicon; the nettle contains a fair amount and favors its absorption.
The triple helix of collagen is made compact and stable by a particular sequence of amino acids. One amino acid every three is glycine, and most of the remaining amino acids consist of proline and hydroxyproline. The body produces its own collagen every day, but as production decreases with age, the available amount of collagen quickly becomes insufficient and the different parts of the body gradually deteriorate. Hydroxyproline, which is critical for collagen stability, is synthesized by hydroxylation of the amino acid proline; the reaction requires organic silicon and vitamin C to allow the addition of oxygen:
Collagen synthesis is therefore dependent on silicon, which influences the hydroxylation process of proline in hydroxy-proline. Silicon is a structural element of the 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 correlated with the optimal conditions of the skin, such as the rate of hydration, elasticity, the absence of wrinkles and expression lines, the ability to heal and regenerate. Furthermore, silicon plays an important role in bone metabolism: it prevents osteoporosis by inhibiting the activity of osteoclasts and stimulating that of osteoblasts.
MSM (Methyl Sulfonyl Methane) is a biologically active form of sulfur, in practice organic sulfur in its natural form, naturally present in many varieties of fruit and vegetables, but in the cooking and food preparation phases it is easily degraded.
It can be easily integrated into the body without causing allergic side effects. Sulfur is present in keratins, fundamental proteins for the formation of nails and hair. It is also physiologically present in the joints, forming part of the chondroitin sulfate, a precious molecule of cartilage.
Vitamin E, together with vitamin C, contributes to the protection of cells from oxidative stress; Vitamin C also contributes to the normal formation of collagen for the normal function of bones, blood vessels, cartilage, skin, teeth and gums.
OPC (ProCyanidine Oligomers) extracted from the bark of Maritime Pine and Vitis Vitifera both with an antioxidant action. OPCs have a high affinity with the hydroxyproline amino acid, present in collagen and elastin and selectively bind these two proteins, protecting them from enzymatic degradation and damage caused by free radicals. Collagen and elastin also contribute to building the vessel walls and keep them resistant and elastic.
Vitis Vinifera, properties:
- function of the microcirculation (heaviness of the legs)
- antioxidant action
-regular functionality of the cardiovascular system
- integrity and functionality of cell membranes
-trophy and functionality of the skin
- contrast of menstrual cycle disorders
- articular function
1. Zeijdner E. E. "Digestibility of collagen hydrolysate during passage through a dynamic gastric and small intestinal model (TIM-1) ". TNO Nutrition and food Research Report. 24 June 2002.
2. Oesser S., Adam M., Babel W. and Seifert J. "Oral Administration of 14C Labelled Gelatin Hydrolysate Leads to an Accumulation of Radioactivity in Cartilage of Mice (C57/BL)" American Society for Nutritional Sciences.1999:1891-1895.
3. Benito P., Monfort J., Nacher M. "Effect of Hydrolyzed Collagen on human chondrocytes cultures". Sept 2002
4. Oesser S. and Seifert J. "Stimulation of type II collagen biosynthesis and secretion in bovine chondrocytes cultured with degraded collagen". Cell Tissue Research. 2003; 311 (3): 393-399.
5. Oesser S., Haggenmuller D., Schulze, C.H. "Collagen hydrolysate modulates the extracellula matrix metabolism of human chondrocytes". Ann. Rheum. Dis. 2006; 65 (suppl. II): 401.
6. Guillerminet F, Beaupied H, Fabien-Soulè V, Tomé D, Benhamou CL, Roux C, Blais A. "Hydrolyzed collagen improves bone metabolism and biomechanical parameters in ovariectomized mice: an in vitro and in vivo study" Bone. 2010 Mar; 46(3):827-34.
7. Takada Y., Aoe S. , Kato K , Toba Y., Yamamura J. "Collagen containin preparations for strengthening bone". European Patent Application n° EP 0 798 001 A2 (1.10.1997).
8. Lynch MP Stein JL, Stein GS, Lian JB. "The influence of type I collagen on the development and maintenance of the osteoblast phenotype in primary and passaged rat calvarial osteoblasts: modification of expression of genes supporting cell growth, adhesion, and extracellular matrix mineralization". Exp Cell Res. 1995 Jan;216(1):35-45.
9. Mizuno M, Fujisawa R, Kuboki Y. "Type I collagen-induced osteoblastic differentiation of bone-marrow cells mediated by collagen-alpha2beta1 integrin interaction". J Cell Physiol. 2000 Aug;184(2):207-13.
10. Mizuno M, Kuboki Y. "Osteoblast-related gene expression of bone marrow cells during the osteoblastic differentiation induced by type I collagen" J Biochem. 2001 Jan;129(1):133-8.