Disease relevance of KLK12

• Preliminary studies suggest that KLK12 is differentially expressed in breast cancer and may have potential use as a cancer biomarker [1].
• Our preliminary results indicate that the expression of KLK12 is down-regulated at the mRNA level in breast cancer tissues and is up-regulated by steroid hormones in breast and prostate cancer cell lines [2].
• In this study, we examined 50 non-cancerous tissues from Japanese patients with primary gastric cancer to determine the presence of genetic polymorphisms in the KLK12 gene using polymerase chain reaction (PCR)-single-strand conformation polymorphism and sequencing [3].

High impact information on KLK12

• Antibodies against the relevant kallikreins on normal endothelial cells revealed that while kallikreins 9, 11, and 12 induced cell growth, only kallikrein 12 regulated invasion and capillary morphogenesis [4].
• In situ hybridization revealed intense expression of all KLK mRNA studied except KLK12 mRNA in the stratum granulosum of normal epidermis, where SPINK5 mRNA coexisted [5].
• KLK12 is a novel serine protease and a new member of the human kallikrein gene family-differential expression in breast cancer [2].
• By using the positional candidate approach, we were able to identify a new kallikrein-like gene, tentatively named KLK12 (for kallikrein gene 12) [2].
• KLK12 is expressed in a variety of tissues including salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, breast, thyroid, and trachea [2].

Biological context of KLK12

• Here, we report the production of recombinant KLK12 and analyses of its enzymatic characteristics, including zymogen activation, substrate specificity, and regulation of its activity [1].

Associations of KLK12 with chemical compounds

• It has been predicted that KLK12 is a secreted serine protease [1].
• Through screening of a panel of fluorogenic and chromogenic peptide substrates, we establish that active KLK12 possesses trypsin-like activity, cleaving peptide bonds after both arginine and lysine [1].

Regulatory relationships of KLK12

• Furthermore, we demonstrate that KLK12 is able to activate KLK11 zymogen in vitro [1].

References