KLK14: Difference between revisions
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Latest revision as of 16:28, 17 March 2025
KLK13
KLK13 (Kallikrein-related peptidase 13) is a member of the kallikrein subfamily of serine proteases, which are enzymes that cleave peptide bonds in proteins. KLK13 is encoded by the KLK13 gene located on chromosome 19q13.3-13.4, a region that contains a cluster of 15 kallikrein genes. This enzyme is involved in various physiological processes and has been implicated in several pathological conditions.
Structure[edit]
KLK13 is synthesized as a preproenzyme, which undergoes post-translational modifications to become an active enzyme. The mature form of KLK13 consists of a single polypeptide chain with a molecular weight of approximately 28 kDa. Like other serine proteases, KLK13 contains a catalytic triad composed of histidine, aspartate, and serine residues, which are essential for its proteolytic activity.
Function[edit]
KLK13 is expressed in various tissues, including the skin, prostate, and salivary glands. It is involved in the degradation of extracellular matrix components, regulation of cell proliferation, and modulation of inflammatory responses. KLK13 has been shown to activate other proteases and growth factors, thereby influencing cellular signaling pathways.
Clinical Significance[edit]
KLK13 has been studied for its potential role as a biomarker in cancer diagnosis and prognosis. Elevated levels of KLK13 expression have been observed in certain types of cancers, such as prostate and ovarian cancer. Research is ongoing to determine the utility of KLK13 as a therapeutic target or a diagnostic marker in oncology.
Research and Applications[edit]
The study of KLK13 and other kallikreins is an active area of research, with implications for understanding cancer biology, skin disorders, and other diseases. KLK13 inhibitors are being explored as potential therapeutic agents to modulate its activity in pathological conditions.
Also see[edit]
Template:Kallikrein-related peptidases