Discovery of haemoglobin in epidermis throws light on skin's protective features: Study

CALIFORNIA: Researchers have discovered that haemoglobin, a protein found in red blood cells that binds oxygen, is also present in the epidermis, our skin's outermost bodily tissue.

The study, which appeared in Elsevier's Journal of Investigative Dermatology, sheds light on the qualities of our skin's protective outermost layer.

The curiosity about how the epidermis protects our sensitive body from the environment and what unexpected substances are expressed in the epidermis drove this research.

The haemoglobin protein was identified in epidermal keratinocytes and hair follicles by researchers. This unexpected evidence adds a new dimension to our understanding of how our skin's defence mechanisms work.

Lead investigator of the study Masayuki Amagai, MD, PhD, Department of Dermatology, Keio University School of Medicine, Tokyo, and Laboratory for Skin Homeostasis, RIKEN Center for Integrative Medical Sciences, Yokohama, explained, "The epidermis consists of keratinized stratified squamous epithelium, which is primarily composed of keratinocytes."

"Previous studies have identified the expression of various genes with protective functions in keratinocytes during their differentiation and formation of the outer skin barrier. However, other barrier-related genes escaped prior detection because of difficulties obtaining adequate amounts of isolated terminally differentiated keratinocytes for transcriptome analysis."

Haemoglobin binds gases such as oxygen, carbon dioxide, and nitric oxide, and it is an iron carrier via the heme complex. These properties make epidermal haemoglobin a prime candidate for antioxidant activity and potentially other roles in barrier function.

Professor Amagai continued, "We conducted a comparative transcriptome analysis of the whole and upper epidermis, both of which were enzymatically separated as cell sheets from human and mouse skin. We discovered that the genes responsible for producing haemoglobin were highly active in the upper part of the epidermis. To confirm our findings, we used immunostaining to visualize the presence of haemoglobin a protein in keratinocytes of the upper epidermis."

Professor Amagai concluded, "Our study showed that epidermal haemoglobin was upregulated by oxidative stress and inhibited the production of reactive oxygen species in human keratinocyte cell cultures. Our findings suggest that haemoglobin a protects keratinocytes from oxidative stress derived from external or internal sources such as UV irradiation and impaired mitochondrial function, respectively. Therefore, the expression of haemoglobin by keratinocytes represents an endogenous defence mechanism against skin aging and skin cancer."