Kallikrein-6
Kallikrein-6 (also known as KLK6, Protease M, or Neurosin) is a serine protease enzyme that is encoded by the KLK6 gene in humans. It is part of the kallikrein family of enzymes, which are known for their physiological importance in processes such as blood coagulation, tissue remodeling, and the inflammatory response.
Structure[edit | edit source]
Kallikrein-6 is a trypsin-like serine protease, meaning it cleaves peptide bonds in proteins. It is composed of two chains, A and B, which are held together by disulfide bonds. The A chain contains the catalytic triad of the enzyme, which is composed of the amino acids histidine, aspartate, and serine.
Function[edit | edit source]
Kallikrein-6 is expressed in a variety of tissues, including the central nervous system, salivary glands, and skin. In the central nervous system, it is thought to play a role in the degradation of amyloid plaques, which are associated with Alzheimer's disease. In the skin, it is involved in the process of desquamation, or the shedding of dead skin cells.
Clinical significance[edit | edit source]
Alterations in the expression of kallikrein-6 have been associated with a number of diseases, including cancer, neurodegenerative diseases, and inflammatory diseases. For example, increased levels of kallikrein-6 have been found in the cerebrospinal fluid of patients with Alzheimer's disease, suggesting that it may be a potential biomarker for this condition.
See also[edit | edit source]
References[edit | edit source]
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