44 SKIN CARE
A
B
Mass
Mass
Figure 1: Matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry (MS) analysis of the biopeptide complex. A: The majority of the peptides are below 500Da. B: Zoom in on the small molecular weight peptides
Proteoglycans as signaling proteins Proteoglycans are composed of a heavily glycosylated protein core linked to one or more unbranched glycosaminoglycan side chains. In the skin, PGs like Decorin and Lumican are key signaling proteins in collagen metabolism interacting with collagen to regulate collagen fibril formation.13-16 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.15,17
The
presence of Decorin ensures that collagen fibrils are correctly assembled, contributing to the skin‘s structural integrity. Lumican ensures that collagen fibrils grow
at a controlled rate, preventing abnormalities in their size and structure.18
Lumican-deficient
mice exhibit thinner skin, skin laxity, disoriented collagen fibrils, and delayed wound healing compared to wild-type mice.16,19
By controlling
the growth of collagen fibrils, Lumican plays a critical role in maintaining the proper structure and function of tissues. Proteoglycans also play key roles in
20 15 10 5 0
maintaining water and ion homeostasis in the ECM6 and stimulating fibroblast and keratinocyte differentiation and proliferation through versican20-21
and perlecan22
connective tissues. Research has demonstrated that Fibulin-
respectively.
Additionally, proteoglycans sequester growth factors and create growth factor gradients within the ECM, which can modulate immune cell trafficking, control growth factor bioavailability, and prevent premature growth factor degradation.6,8,23
Glycoproteins in tissue stability and elasticity Glycoproteins differ from proteoglycans in that they have short, branched oligosaccharide side chains attached to their protein core. Examples like laminin and fibronectin bind to collagen IV, helping to stabilize the epidermal basement membrane.6,24
monomers (tropoelastin) to regulate and cross-link elastic fibre assembly.25
Fibulin-4 and fibulin-5 interact with elastin Cells secrete
Fibulin-4 to support copper ion transfer, which is a critical step in the elastin-collagen cross- linking process.26
This cross-linking is vital for the formation of strong and elastic fibres in Control ■ Treatment ■ *** *** *** *** ***
4-deficient mice often die of artery and diaphragmatic rupture due to disrupted collagen and elastic fibre formation.27
our cells produce less Fibulin-5, and acute UVB irradiation can further reduce its levels.28
As we age, The
decreased production of Fibulin proteins with age underscores its role in maintaining tissue elasticity and structural integrity. Additionally, glycoproteins serve as ligands for
nearby cell receptors. For instance, keratinocytes produce laminin-332, which acts on integrin α6 receptors on melanocytes, promoting their migration and adhesion.29
After UV exposure,
human skin induces the cellular form of fibronectin at the dermis and dermal-epidermal junction.30
This cellular fibronectin preferentially
binds to the β1 integrin receptor, likely signaling infiltrating CD11b+ monocytes/macrophages and triggering their IL-10 production.
Elastic Fibres as connective tissue components of the skin Elastic fibres consist primarily of an elastin core surrounded by fibrillin microfibrils.31-32
These
fibres allow our skin to stretch and recoil. The elasticity of the skin depends on the relative amounts of elastin, microfibrils, and other molecules like fibulins, as well as the orientation of the elastic fibres.31-32 One major cause of wrinkles and loose skin
with ageing is the gradual damage to elastin from repeated physical and environmental stress over a lifetime. Fibrillin microfibrils serve as a scaffold to ensure proper alignment of elastic fibres.31-32
and humans can lead to various skin conditions, ranging from thin and hyperextensible skin to stiff, thick, and fibrotic skin.32
COL4A1 CTGF HBEGF TGFA ITGA1
Figure 2: Gene expressions of human keratinocytes after treatment with biopeptide complex. Asterisks indicate statistical significance (t-test; p < 0.001) between treatment and control
PERSONAL CARE May 2025
The crucial role of growth factors in collagen metabolism and ECM regulation Collagen and other ECM molecules have the ability to self-organize into fibrils. However,
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Mutations in fibrillin genes in both mice
Relative expression
% Intensity
% Intensity
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