KLK11
| Kallikrein-related peptidase 10 | |||||||
|---|---|---|---|---|---|---|---|
| Script error: No such module "InfoboxImage". | |||||||
| Identifiers | |||||||
| Symbol | ? | ||||||
| NCBI gene | 5655 | ||||||
| HGNC | 6355 | ||||||
| OMIM | 603129 | ||||||
| RefSeq | NM_002776 | ||||||
| UniProt | Q9UBX1 | ||||||
| |||||||
Kallikrein-related peptidase 10 (KLK10) is a member of the kallikrein family of serine proteases, which are involved in various physiological processes. KLK10 is encoded by the KLK10 gene located on chromosome 19q13.3, a region known for containing a cluster of kallikrein genes.
Structure[edit | edit source]
The KLK10 gene spans approximately 5.5 kb and consists of 5 exons and 4 introns. The protein product is initially synthesized as a preproenzyme, which undergoes post-translational modifications to become an active enzyme. The mature KLK10 protein is composed of 276 amino acids and has a molecular weight of approximately 30 kDa.
Function[edit | edit source]
KLK10 is involved in the regulation of various physiological processes, including skin desquamation, semen liquefaction, and the activation of other proteases. It is also implicated in the degradation of extracellular matrix components, which is crucial for tissue remodeling and repair.
Clinical Significance[edit | edit source]
KLK10 has been studied for its potential role as a biomarker in various cancers, including breast cancer, ovarian cancer, and prostate cancer. Altered expression levels of KLK10 have been associated with tumor progression and metastasis. In breast cancer, for instance, KLK10 expression is often downregulated, and its loss is correlated with poor prognosis.
Regulation[edit | edit source]
The expression of KLK10 is regulated by steroid hormones, including androgens and estrogens. It is also subject to epigenetic modifications, such as DNA methylation, which can lead to its silencing in certain cancer types.
Research[edit | edit source]
Ongoing research is focused on understanding the precise biological functions of KLK10 and its interactions with other kallikreins and proteases. Studies are also exploring its potential as a therapeutic target and its role in the tumor microenvironment.
Also see[edit | edit source]
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Contributors: Prab R. Tumpati, MD
