KLK15

Kallikrein-related peptidase 14 (KLK14) is a member of the kallikrein family of serine proteases, which are enzymes that cleave peptide bonds in proteins. KLK14 is encoded by the KLK14 gene located on chromosome 19q13.3, a region known for containing a cluster of kallikrein genes.

Structure

The KLK14 gene is composed of several exons and introns, and its expression is regulated by various promoters and enhancers. The protein product of KLK14 is synthesized as an inactive zymogen, which is activated by proteolytic cleavage. The active enzyme has a typical serine protease structure, with a catalytic triad consisting of histidine, aspartate, and serine residues.

Function

KLK14 is involved in a variety of physiological processes, including skin desquamation, semen liquefaction, and the regulation of extracellular matrix components. It is expressed in several tissues, including the skin, prostate, and central nervous system. KLK14 has been implicated in the degradation of extracellular matrix proteins, which is important for tissue remodeling and repair.

Clinical Significance

KLK14 has been studied for its potential role in cancer progression, particularly in prostate cancer and ovarian cancer. Elevated levels of KLK14 have been observed in certain cancer tissues, suggesting it may serve as a biomarker for diagnosis or prognosis. Additionally, KLK14 may be involved in the pathogenesis of skin disorders such as psoriasis and atopic dermatitis.

Research

Ongoing research is focused on understanding the precise biological functions of KLK14 and its interactions with other proteins. Studies are also exploring the potential of KLK14 as a therapeutic target, particularly in cancer treatment. Inhibitors of KLK14 are being investigated for their ability to modulate its activity in disease contexts.

Also see

• Kallikrein
• Serine protease
• Prostate cancer
• Ovarian cancer
• Extracellular matrix