As we grow older, the collagen fibrils in our skin—the tiny, cylindrical structures made of collagen molecules—start to break down and become disorganized, contributing to the aging of our skin. Therefore, maintaining healthy collagen production is crucial for preserving youthful skin.

Collagen is a protein produced by animal cells, rich in specific amino acids such as glycine, proline, hydroxyproline, and arginine. These collagen molecules assemble into fibrils, which range in diameter from 10 to 500 nanometers. The structure of these fibrils can vary widely: they may be thin and transparent, as found in the cornea, or thick and bundled, as seen in tendons. The arrangement and properties of these fibrils play a crucial role in their function, whether forming a gel-like structure or contributing to the mechanical strength of tissues.

Collagen molecules have the ability to self-organize into fibrils. However, without guidance from the cell, this formation process results in a random gel, lacking the specific orientation and structure necessary for functional tissues. To produce useful fibrils and tissues, cells secrete not just collagen but also various signaling proteins to guide the formation process.

Signaling proteins are vital for healthy collagen metabolism. They facilitate the production, organization, and maintenance of collagen fibrils, which are crucial for the skin's structural integrity. These proteins ensure that collagen production aligns with the body's needs, maintaining the balance necessary for healthy skin, connective tissues, and overall tissue function. Examples of signaling proteins important for skin health include but are not limited to, Decorin, Fibulin, Lumican, and Connective Tissue Growth Factor.

One of the key signaling proteins in collagen metabolism is Decorin. Cells produce Decorin to aid in the assembly of collagen fibrils. Decorin binds to collagen fibrils, promoting their proper alignment and organization. Studies have shown that Decorin-deficient mice suffer from fragile skin, highlighting its importance in maintaining skin strength and resilience. The presence of Decorin ensures that collagen fibrils are correctly assembled, contributing to the skin's structural integrity.

Fibulin is another essential signaling protein involved in collagen metabolism. Cells secrete Fibulin to support copper ion transfer, which is a critical step in the elastin-collagen cross-linking process. This cross-linking is vital for the formation of strong and elastic fibers in connective tissues. Research has demonstrated that Fibulin-deficient mice often die of artery and diaphragmatic rupture due to disrupted collagen and elastic fiber formation. As we age, our cells produce less Fibulin, and acute UVB irradiation can further reduce its levels. The decreased production of Fibulin with age underscores its role in maintaining tissue elasticity and structural integrity.

Lumican is a signalling protein that cells produce to regulate collagen fibril assembly. It ensures that collagen fibrils grow at a controlled rate, preventing abnormalities in their size and structure. Lumican-deficient mice exhibit skin laxity and corneal opacity, conditions arising from deregulated growth of collagen fibrils that result in abnormally thick collagen fibrils. By controlling the growth of collagen fibrils, Lumican plays a critical role in maintaining the proper structure and function of tissues.

CTGF is another signaling protein that cells secrete to promote collagen production. CTGF stimulates fibroblasts to produce collagen, supporting tissue repair and regeneration. The balanced secretion of CTGF ensures that collagen production is sufficient for tissue maintenance and repair without leading to adverse effects.

These signaling proteins are produced by cells in precise amounts to ensure proper function. If we could replicate these proteins and turn them into smaller peptides that the skin can absorb, they could support collagen formation in our skin.

While these proteins aren't available from plants and are challenging to extract from animal tissues, advances in biotechnology have made it possible to produce them by replicating the cell biological process. The Zellulin® BioPlatform, for instance, uses patented technology to cultivate cells from a single fish, producing these signaling proteins in a sustainable and traceable manner. These proteins are then transformed into biopeptide complexes that can significantly improve skin hydration, elasticity, and firmness.

Produced by the Zellulin® BioPlatform, ZelluGEN™ is a biopeptide complex that encourages skin cells to produce more of the extracellular matrix, the structural foundation of the skin. ZelluGEN™ is proven to help renew, protect, and maintain youthful skin and is suitable for use in advanced anti-aging formulations.

ZelluGEN™ not only contains the aforementioned signaling peptides but also includes Copper tripeptide (GHK) and peptides derived from collagen. GHK, composed of the amino acids glycine, histidine, and lysine, is typically found in ECM proteins. It is released through the breakdown of cells or the ECM following injury and may play a role in wound healing.

Analysis shows that the Zellulin® Bioplatform’s hydrolysis process produces GHK peptides from cultivated fish cells. Notably, ZelluGEN™ contains GHK peptides originating from ECM proteins such as collagen and SPARC, alongside other cell-identical multiple peptides.

In human skin cells, both ZelluGEN™ and hydrolyzed collagen stimulate the cells and increase the production of proteins responsible for healthy skin metabolism. However, ZelluGEN™ demonstrated a more significant and broader effect compared to hydrolyzed collagen.