The science behind the physical processes and the resulting benefits to the use of collagen supplements has been researched for many years, and is now quite well understood.
Below, and in the related pages, you will find a range of information on the key ingredients and their function and value to the human body. Please feel free to read and learn for yourself as to why you should include an S·ONE·S product as a natural part of your personal care program.
To see and learn about actual results based on documented, scientific research, see our CLINICAL STUDIES page.
From the inside
S·ONE·S and S·ONE·S G Plus, like other collagen supplements available, were developed to address the needs of the body as we grow older, to counteract the aging process, improving both the skin’s beauty and the body’s overall health from within.
Former Osaka Medical College president Dr. Motoki Yamanaka was one of the first to highlight the use of porcine based collagen for internal consumption, in 1990 noting ‘the composition of the amino acid is the nearest to a human being’. Dr. Yamanaka’s work is the basis for the S·ONE·S family, which carries the Japanese Society of Clinical Anti-Aging Medicine (JSCAM) mark. The JSCAM is the only society of clinical anti-aging medicine in Japan recognized throughout the world.
Unlike many skin creams or serums, which have limited ability to penetrate the outer layers of skin, S·ONE·S products work from the inside.
S·ONE·S and S·ONE·S G Plus provides the key building blocks for the development of both collagen and elastin in the skin, as well as essential components for health and maintenance of the joints. Further, they serve to naturally increase the levels of hyaluronic acid in the skin.
This total body, holistic approach, can only be achieved by working from the inside out.
The result is naturally smoother, more beautifully hydrated skin, hair, finger and toenails, enhanced joint maintenance and function, and an improved overall quality of life.
How it works
S·ONE·S and S·ONE·S G Plus are a composite of hydrolyzed collagen and key ingredients, designed to act from within. The physical processes themselves and the resulting benefits to the use of a collagen supplement are summarized in 3 basic steps:
- When consumed internally, hydrolyzed collagen is broken down in to its components and essential amino acids during digestion, where they are subsequently absorbed into the blood steam.
- These components and amino acids are then transferred throughout the body, including the dermal layer of the skin.
- In the dermal layer, these components provide the foundation for the formation of collagen and elastin, as well as stimulating the body’s own production of collagen and hyaluronic acid.
In more detailed terms, the collagen components, or peptides, delivered to the skin through the bloodstream stimulate fibroplast cells. Fibroplasts are the most common type of cell found in connective tissue, and synthesizes the extracellular matrix and collagen1.
The extracellular matrix is composed of an interlocking mesh of proteins and molecular components, some of which include:
- Collagen, the most abundant protein in the human body2,3, which provides structure and strength to cells, tissues, tendons, bones, ligaments, cartilage and the skin. It forms in strong bundles and ropes called collagen fibers, which work alongside keratin to keep skin youthful and wrinkle-free, and keep joints cushioned and muscles strong.
- Elastin, which in contrast to collagen, gives elasticity to the skin, allowing it to stretch when needed and then return to its original state.
- Hyaluronic acid, or hyaluronan, which provides the skin and joints the ability to resist compression, providing a counteracting force by absorbing significant amounts of water.
- Chondroitin sulfate, which contributes to the tensile strength of cartilage, tendons and ligaments.
For an exceptional scientific summary of the collagen synthesis process, please see an excerpt from some of Dr. Ananya Mandal’s presentation material on collagen4, by clicking here .
1 – http://ghr.nlm.nih.gov/
2 – Di Lullo GA, Sweeney SM, Korkko J, Ala-Kokko L, San Antonio JD (2002). “Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen”. J. Biol. Chem. 277 (6): 4223–31.
3 – Karsenty G, Park RW (1995). “Regulation of type I collagen genes expression”. Int. Rev. Immunol. 12 (2–4): 177–85.
4 – Mandal A. “Collagen Synthesis”. http://www.news-medical.net/health/Collagen-Synthesis.aspx