Type I collagen is the most abundant in the skin and alone accounts for 60 to 80% of the collagens in the dermis, followed by type III collagen (15 to 25%). The combination of these two collagens forms the basis of the structural fibers that make up the dermis. Type IV collagen forms a network and is specific to the dermal-epidermal junction (DEJ) and the walls of blood vessels. It plays a key role in the DEJ, where it cooperates with type VII fibrillar collagen to ensure the cohesion and structure of the DEJ5. For its part, type XVII transmembrane collagen allows optimal connection between the intracellular and extracellular structures involved in the adhesion of the epidermis to the DEJ.6 Similarly, type VI collagen allows binding between the various components of the extracellular matrix of the dermis and the DEJ7, ensuring its consistency with the dermis (Figure 2).
Why is collagen severely affected by aging?
In intrinsic ageing, collagen production slows down from the age of 30. As a result, the dermis, which structures the entire skin, is less dense, leading to a weakening of superficial structures such as the epidermis. With age, there is also a loss of elasticity, an increase in skin thickness and eventually the appearance of wrinkles.
In addition to the decline in their synthesis, collagen fibers also undergo numerous changes that radically alter their physical properties. These changes increase with age and can be exacerbated by extrinsic ageing caused by UV rays, pollution, smoking and an unbalanced diet. This leads to increased production and activity of enzymes responsible for the breakdown of collagens, called matrix metalloproteinases (MMPs). At the same time, the synthesis and activity of the metalloproteinase inhibitors, the so-called TIMPs (tissue inhibitors of metalloproteinases), decreases.
In addition, collagens, due to their long life span, are a preferred target for slow enzymatic reactions such as glycation. This glycation acts like caramelization, making collagen fibers stiff and leading to loss of elasticity and sagging, which are typical features of aged skin5. Finally, with age there is an accumulation of reactive oxygen species that triggers oxidation reactions. In collagens, this leads to carbonylation of the amino acids lysine and arginine.8 This carbonylation radically changes the viscoelastic properties of the collagens.9
Seppic active ingredients that act on collagens
To protect collagens from aging, three approaches can be considered. The first is to stimulate the synthesis of these proteins to counteract the decline observed with age. The second approach is to protect the existing collagens from degradation or structural alteration leading to the loss of their physicochemical properties. And thirdly, it is possible to stimulate the contractile abilities of fibroblasts on collagen fibers, thus obtaining a local stretching effect. We offer several active ingredients that act on one or more approaches.
SEPILIFT™ DPHP, the preferred wrinkle correction product on the Aminovector™ tree, contains hydroxyproline, one of the most important amino acids found in tri-peptide base units. Hydroxyproline is the main component of the polypeptide chains of collagens.
It is an all-encompassing anti-aging ingredient that also moisturizes and has a triple firming effect at the same time. In vitro, we have demonstrated the following modes of action, among others: +14% contraction of collagen fibers, +26% stimulation of pro-collagen I, +94% MMP-2 inhibition and +46% TIMP-2 stimulation at the same time.
KALPARIANE™ is a natural, multifunctional skin care ingredient based on the brown algae Alaria esculenta. It helps protect the skin's firmness and elasticity while stimulating the synthesis of collagen and hyaluronic acid. Skin is plumped up and looks firmer and smoother. In vitro, we have demonstrated the following modes of action, among others: Reduction by -20% of collagenase (collagen-degrading enzyme) and stimulation of the synthesis of +24% collagen III, +28% collagen IV and +20% collagen VII.
AMBIATY EXTRACT is an anti-aging ingredient, derived from a Madagascan native plant, which stimulates the activation and protection of the dermis. With an action on the synthesis of GAGs, collagen and key elements of DEJ, this dermis protector is perfect for a firming effect. It also reduces glycation. In vitro, we have demonstrated the following modes of action, among others: Reduction of MMP-1 (-22%) and reduction of glycation (-37%). It also stimulates collagen IV synthesis (ex-vivo: +24%).
TIMECODE™ , incorporates the anti-aging experience of PalGly, known as the body's own happiness molecule. The PalGly molecule is available to your skin because it is composed of an amphiphilic amino acid vector consisting of glycine and palmitic acid. Glycine is a key amino acid of collagen. This Aminovector - Solution provides an additional source of glycine, contributing to skin firmness. TIMECODE™ is a highly effective wrinkle corrector for deep wrinkles. It helps alleviate chronic silent inflammation, also known as inflamm'aging, increases microcirculation due to poor oxygenation and nutrient deficiency, and helps with deficient collagen organization and synthesis. In vitro, we have demonstrated the following modes of action, among others: Reduction by -100% of collagenase activity, MMP-1 inhibition (-56%), +29% TIMP-2 stimulation, and stimulation of pro-collagen I synthesis (+21%).
ANTILEUKINE™ 6 is extracted from the brown algae Laminaria ochroleuca, also known as golden algae. The algae produces secondary metabolites that are resistant to UV radiation, which gives ANTILEUKINE™ 6 its anti-photoaging property, it is also a DNA protector after UVA/UVB exposure. It has long-term anti-photoaging properties with a reduction in wrinkles and a moisturizing effect. In vitro, we have demonstrated the following modes of action, among others: Reduction of -31% MMP-1, -28% MMP-2, -31% MMP-3 and -35% MMP-9 and stimulation of +30% collagens.
CELTOSOME™ Eryngium Maritimum is an exclusive marine, pure & plant-derived stem cell culture from beach thistle designed to promote the regeneration of aging skin. Its specific activity targeting the epidermis-dermal junction helps to increase elastin and collagen synthesis and regulate epidermal renewal for plumper, firmer and more radiant looking skin. It has more than 100 million cells/g of active ingredient: formulated in a cream with 0.05% EC, that's about 50,000 cells in 1g of cream. In vitro, we have demonstrated the following modes of action, among others: Collagen IV + VII synthesis (+16%) stimulated and also collagen IV is protected from UVA/UVB exposure.
All active ingredients have additional in-vitro and in-vivo tests. Do not hesitate to ask us for more detailed product information.
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2J.H. Mortensen and Morten A. Karsdal. Chapter 7 - Type VII Collagen. Biochemistry of Collagens, Laminins and Elastin. Structure, Function and Biomarkers. (2016), Pages 57-60
3Dorothy M. Supp, Jennifer M. Hahn, Kelly A. Combs, Kevin L. McFarland, Ann Schwentker, Raymond E. Boissy, Steven T. Boyce, Heather M. Powell, and Anne W. Lucky. Collagen VII Expression Is Required in Both Keratinocytes and Fibroblasts for Anchoring Fibril Formation in bilayer Engineered Skin Substitutes. Cell Transplantation (2019), Vol. 28(9-10) 1242–1256
4Marion K. Gordon and Rita A. Hahn. Collagens. Cell Tissue Res. (2010) January 339(1): 247–257. doi:10.1007/s00441-009-0844-4.
5Sylvie Ricard-Blum. The Collagen Family. Cold Spring Harb Perspect Biol (2011);3:a004978
6Eva Roig-Rosello and Patricia Rousselle. The Human Epidermal Basement Membrane: A Shaped and Cell Instructive Platform That Aging Slowly Alters. Biomolecules (2020), 10, 1607; doi:10.3390/biom10121607
7Matilde Cescon, Francesca Gattazzo, Peiwen Chen and Paolo Bonaldo. Collagen VI at a glance.Journal of Cell Science (2015) 128, 3525-3531 doi:10.1242/jcs.169748
8Sugiura K, Koike S, Suzuki T, Ogasawara Y. Carbonylation of skin collagen induced by reaction with methylglyoxal. Biochem Biophys Res Commun. (2021) May 25;562:100-104. doi: 10.1016/j.bbrc.2021.05.044. Epub ahead of print. PMID: 34049202.
9Morimoto, H.; Gu, L.; Zeng, H.; Maeda, K. Amino Carbonylation of Epidermal Basement Membrane Inhibits Epidermal Cell Function and Is Suppressed by Methylparaben. Cosmetics (2017), 4, 38. https://doi.org/10.3390/cosmetics4040038