EC Number   |
General Information |
Reference |
|---|
   3.4.21.B12 | malfunction |
KLK4 dysfunction causes some types of developmental defect in enamel |
752672 |
| 3.4.21.B12 | metabolism |
coincidence of KLK4 and dipeptidyl-peptidase I distribution in ameloblasts strongly suggests that dipeptidyl-peptidase I activates KLK4 |
753881 |
| 3.4.21.B12 | metabolism |
KLK4 activates matrix metalloproteinase-1, a protease that promotes prostate tumor growth and metastasis. It is a potential multifunctional regulator of prostate cancer progression |
754486 |
| 3.4.21.B12 | physiological function |
kallikrein-related peptidase-4 (KLK4) initiates tumor-stroma interactions in prostate cancer through protease-activated receptor-1 (PAR-1). KLK4 triggers transmembrane signaling and upregulates interleukin-6 in WPMY-1 cells through PAR-1. Cancer epithelium produces KLK4 to activate PAR-1 in the surrounding stroma, which in-turn releases cytokines (interleukin-6) that stimulate cancer cells to proliferate and increase production of kallikreins |
717674 |
| 3.4.21.B12 | physiological function |
KLK4 most likely plays a proteolytic role in degeneration of enamel organ |
753881 |
| 3.4.21.B12 | physiological function |
the enzyme activates the hepatocyte growth factor, a multifunctional growth factor that plays an important role in cancer progression via its specific receptor tyrosine kinase MET, a c-met proto-oncogene product. Correlation between phospho-MET, MET, KLK4 expression and clinicopathological parameters, overview |
731893 |
| 3.4.21.B12 | physiological function |
the enzyme plays a pivotal role during dental enamel formation by degrading the major enamel protein, amelogenin, prior to the final steps of enamel hardening. KLK4 binds hydroxyapatite directly |
752672 |
| 3.4.21.B12 | physiological function |
the enzyme serves vital functions in dental enamel formation. KLK4 is involved in degradation of extracellular matrix proteins and it is thought that this proteolytic activity can also promote tumor invasion and metastasis. KLK4 expression is stronger in primary tumors that later either recurred or developed metastases, suggesting that its preferential expression in OSCC might contribute to individual tumor biology |
752500 |
| 3.4.21.B12 | physiological function |
the enzyme substrate murine ephrin-B2 is glycosylated and this post-translational modification may regulate the enzyme cleavage activity |
731763 |
