Balance the skin microbiome to boost skin barrier function
SYN-UP™ - our skin microbiome active for better skin barrier
Two serine proteases have a crucial role to play in the development of good skin resilience: plasmin and urokinase.
In normal skin, plasminogen, the precursor of plasmin, lies in the basal layer of the epidermis only. But if the skin loses its resilience, through stress for example, urokinase activates plasmin out of plasminogen. This release of plasmin can lead to inflammation and dryness. Our scientists have found a good correlation between plasmin activity and transepidermal water loss – a marker of skin barrier function.
Plasmin activity is also affected by one of the most common bacteria in the skin microbiome: S. aureus. When there is an imbalance in the skin microbiome, S. aureous affects skin barrier function via bacterial proteases that eventually trigger inflammation processes. This inflammation leads to an additional release of plasmin in the epidermis, further weakening the skin barrier and setting a vicious cycle in motion.
Rebalancing plasmin the Epibiotic way
Thanks to its mode of action, SYN-UP™ breaks the plasmin cycle in two ways. At microbe level, it has been shown in-vitro to act directly on S. aureous by reducing levels of the bacteria. At molecule level, it has been shown to reversibly inhibit the serine proteases urokinase and plasmin, boosting skin barrier strength.
In-vivo studies back up the benefits of this action: after 29 days of using SYN-UP®, volunteers showed a significant improvement in skin resilience, smoothness and hydration and reported reduced skin sensitivity.
Because of its capacity to rebalance S. aureous, urokinase and plasmin symbiotically, SYN-UP™ improves skin resilience and protects it against external stress. This means consumers can have confidence in achieving smoother, better hydrated and visibly less irritated skin, and a stronger skin barrier.
1 Increased basal transepidermal water loss leads to elevation of some but not all stratum corneum serine proteases. (R Voegeli et al. DSM, IJCS 2008)