Unveiling the Molecular Culprit: Carbonylation of Skin Proteins and the Unwanted Side Effect of Skin Yellowing in Aging
Skin aging is an intricate process influenced by various factors, with the carbonylation of skin proteins emerging as a key contributor to the unwelcome phenomenon of skin yellowing. This article explores the mechanisms behind protein carbonylation, examines whether certain phenotypes are more susceptible, delves into preventive measures, and highlights the role of ascorbic acid, particularly stabilized forms like Ascorbyl-2 glucoside (AA2G™), in mitigating protein carbonylation.
Aging is an inevitable biological process that manifests in numerous ways, and one of the less-discussed outcomes is skin yellowing attributed to protein carbonylation. This chemical modification, often a result of oxidative stress, alters skin proteins, leading to changes in pigmentation and tone.
What is Carbonylation?
Carbonylation is a chemical process in which a carbonyl group (a carbon atom double-bonded to an oxygen atom) is introduced into a compound or molecule. In the context of biological systems, carbonylation often refers to the modification of proteins by the addition of a carbonyl group to specific amino acid residues, typically lysine, arginine, proline, and threonine.
Protein carbonylation is a form of oxidative damage that occurs when proteins are exposed to reactive oxygen species (ROS) or reactive nitrogen species (RNS). These reactive species can be generated during normal cellular metabolism or in response to external factors such as exposure to ultraviolet (UV) radiation, pollution, or other environmental stressors.
The addition of carbonyl groups to proteins can lead to structural and functional changes in the affected proteins. This modification is often considered a marker of oxidative stress and is associated with various pathological conditions, including aging and age-related diseases. Carbonylated proteins can exhibit altered enzymatic activity, impaired function, and increased susceptibility to degradation.
In the context of skin aging, carbonylation of skin proteins can contribute to the development of wrinkles, loss of elasticity, and changes in pigmentation, such as skin yellowing. This process is influenced by the cumulative effects of oxidative stress over time.
Understanding and studying protein carbonylation is important in the field of aging research and related health issues, as it provides insights into the molecular mechanisms underlying cellular damage and dysfunction associated with various physiological processes. Researchers often investigate ways to mitigate protein carbonylation as a strategy to promote healthier aging and address age-related conditions.
Susceptibility Across Phenotypes
Research on the susceptibility of different phenotypes—whites, blacks, and Asians—to skin yellowing through protein carbonylation is limited. However, studies suggest that factors like melanin distribution, collagen composition, and genetic variations contribute to the diverse aging experiences among individuals with different skin types. It is crucial to approach this topic with a recognition of the uniqueness of each person's skin biology and the multifaceted nature of skin aging.
Preventing skin yellowing associated with protein carbonylation involves a comprehensive approach. A balanced, antioxidant-rich diet, meticulous UV protection, and adequate hydration are fundamental. Research towards carbonylation and what preventive measures may be effective is currently an active field of study by independent scientists and groups around the world.
Ascorbic Acid: A Guardian Against Carbonylation
Ascorbic acid, commonly known as vitamin C, emerges as a formidable ally in the battle against skin protein carbonylation. As a potent antioxidant, vitamin C plays a crucial role in neutralizing free radicals and reducing oxidative stress, thus minimizing the risk of protein carbonylation. A study published in the peer-reviewed journal Clinical, Cosmetic and Investigational Dermatology illuminates the pivotal role of antioxidants such as ascorbic acid in supporting skin health.
The quest for effective prevention has led to the exploration of stabilized forms of vitamin C, such as Ascorbyl-2 glucoside. This stable derivative exhibits enhanced resistance to oxidation, ensuring a prolonged shelf life and improved efficacy when applied topically. An interesting unique feature of AA2G™ is its excellent stability both while in the product formula and when applied to the skin. Once absorbed into the skin, the stabilized Ascorbyl-2-glucoside form of the molecule is cleaved by alpha-glucosidase into the active L-ascorbic acid form. This means that the active vitamin C participates only in the desired physiological mechanisms instead of being oxidized by atmospheric oxygen.
DKSH has been a long-time partner with Hayashibara, a Nagase company who is the innovator behind the genius of AA2G™. Visit DKSH Discover to learn more about AA2G™, download documentation, and request samples to accelerate your formulations of products and solutions to counteract carbonylation.
The carbonylation of skin proteins and the ensuing skin yellowing pose challenges in the aging process, affecting individuals across different phenotypes. While research on phenotype susceptibility is evolving, preventive measures rooted in a holistic approach to skincare are essential. Ascorbic acid, particularly stabilized forms like AA2G™ (Ascorbyl-2 glucoside), emerges as a promising avenue for preventing protein carbonylation and preserving skin health. The scientific community's ongoing efforts in this field promise a deeper understanding of skin aging and innovative solutions for maintaining skin vitality.
- Benoit I, Burty-Valin E, Radman M. A Proteome-Centric View of Ageing, including that of the Skin and Age-Related Diseases: Considerations of a Common Cause and Common Preventative and Curative Interventions. Clin Cosmet Investig Dermatol. 2023;16:79-85 https://doi.org/10.2147/CCID.S397751
- Kregel, K. C. and Zhang, H. J. (2007). An integrated view of oxidative stress in aging: basic mechanisms, functional effects, and pathological considerations. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 292(1), R18-R36. https://doi.org/10.1152/ajpregu.00327.2006
- Baraibar, Martin & Ladouce, Romain & Friguet, Bertrand. (2013). Proteomic quantification and identification of carbonylated proteins upon oxidative stress and during cellular aging. Journal of proteomics. 92. 10.1016/j.jprot.2013.05.008.