Kallikrein-7 is a serine protease that is primarily expressed in the skin, particularly by keratinocytes in the epidermis . The full-length human Kallikrein-7 consists of 253 amino acids, including a signal peptide (residues 1-22), a short pro peptide (residues 23-29), and the mature chain (residues 30-252) . The enzyme is known for its chymotryptic activity, meaning it preferentially cleaves peptide bonds at the carboxyl side of aromatic amino acids .
Kallikrein-7 plays a crucial role in the process of skin desquamation, which is the shedding of the outermost layer of the skin. It achieves this by degrading corneodesmosomes, the structures that hold corneocytes together in the stratum corneum . This activity is essential for maintaining skin homeostasis and barrier function.
In addition to its role in skin physiology, Kallikrein-7 is also implicated in various pathological conditions. For instance, it is upregulated in certain types of cancer, including ovarian carcinoma, where its expression is associated with poor prognosis and cancer progression . Elevated levels of Kallikrein-7 have also been observed in inflammatory skin diseases such as atopic dermatitis and psoriasis .
Recombinant human Kallikrein-7 is produced using various expression systems, including bacterial, yeast, and mammalian cells. The recombinant protein is often tagged with a His-tag to facilitate purification and detection . It is used in various research applications, including enzyme activity assays, structural studies, and drug screening.
The recombinant form of Kallikrein-7 retains its enzymatic activity and can cleave specific peptide substrates. For example, it can cleave the fluorogenic peptide substrate Mca-RPKPVE-Nval-WRK (Dnp)-NH2, with a specific activity of over 150 pmol/min/µg . This activity is measured under specific conditions, including the presence of activation and assay buffers .
Recombinant Kallikrein-7 is widely used in research to study its role in skin physiology and pathology. It is also used to screen potential inhibitors that could be developed into therapeutic agents for conditions such as cancer and inflammatory skin diseases . Additionally, structural studies of Kallikrein-7 help in understanding its substrate specificity and mechanism of action, which can aid in the design of specific inhibitors .