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Generalities

The structure is found in the human psoriasin, also called S100A7. This protein belongs to the family of S100 proteins. It is a family of 21 proteins of low molecular weights. Those proteins are found in cells as homo and heterodimers. One of their main properties is their ability to bind the calcium. They share some common structures such as two helix-loop-helix structures which are calcium-binding domains. All the S100 proteins have different functions in many various cell types. They have significant roles in calcium-associated signal transduction. They play the roles of calcium sensors proteins that regulate the function or distribution of specific target proteins.

Human Psoriasin

The protein S100A7 is found in the cytoplasm of keratinocytes. The expression of the psoriasin is regulated by different agents. An increase of the cellular amount of calcium also increases the cellular level of S100A7. The UV light increases the expression of the protein. The level of the protein is thought to increase in keratinocytes in response to inflammatory stress. Some studies show that the target protein of the psoriasin could be E-FABP, the epidermal fatty acid binding protein. They proved that immunoprecipitation of E-FABP resulted in co-immunoprecipitation of S100A7. Fatty acid binding proteins are involved in cellular transports and in the regulation of the solubility of fatty acids. Generaly they can be found in the cytoplasm or in the nucleus.

Disease

Some S100 proteins such as S100A7 are clearly overexpressed in psoriasis, wound healing, skin cancer, inflammation, cellular stress and other skin conditions. Human psoriasin is highly expressed in hyperproliferative skin conditions such as Atopic_dermatitis and Psoriasis which causes a disruption of the skin barrier. This one is a genetic disease that disrupts cell division in skin cells. The study of S100A7 as well as S100 is therefore of great interest in the search for treatments for certain epidermal diseases.

Utility

Human psoriasin can be used has antimicrobial petide agaisnt E-coli. Some mutant of S100A7 are capable of decrease the survival rate of E. coli mainly. Mutation of the conserved carboxyl-terminal EF-hand calcium-binding motif or heat denaturation slightly reduces S100A7 antibacterial activity.

Relevance

Structural highlights

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