Psoriasin

Psoriasin is a protein that in humans is encoded by the S100A7 gene. This protein is a member of the S100 family of proteins, which contain 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. Psoriasin has been found to play a critical role in the pathogenesis of psoriasis, a chronic inflammatory skin condition.

Function

Psoriasin is predominantly expressed in epidermis and is highly upregulated in psoriatic lesions. It is involved in the inflammatory response and helps in the defense against microbes. Psoriasin is also known to play a role in cell proliferation and differentiation, which are key aspects of the skin's response to injury and infection. Its antimicrobial properties are significant in the skin's innate immunity, providing protection against a variety of pathogens.

Clinical Significance

The overexpression of Psoriasin is closely associated with the development of psoriasis. It is considered a biomarker for the disease and is used in understanding the disease mechanism as well as in the development of therapeutic targets. Beyond psoriasis, Psoriasin has been implicated in various other conditions, including some forms of cancer, where its expression may influence tumor progression and metastasis.

Genetics

The S100A7 gene encoding Psoriasin is located on chromosome 1 (1q21), a region that is often associated with susceptibility to psoriasis. Variations in this gene are thought to affect the individual's risk of developing psoriasis, making it a subject of genetic studies related to the disease.

Research Directions

Research on Psoriasin encompasses its role in inflammation, immunity, and cell proliferation, aiming to uncover its potential as a therapeutic target not only for psoriasis but also for other inflammatory and neoplastic diseases. Understanding the regulation of Psoriasin expression and its interaction with other cellular proteins could provide insights into the pathophysiology of these conditions.