EC Number   |
General Information |
Reference |
|---|
   3.4.21.B43 | malfunction |
knockdown of KLK12 results in a significant downregulation of autophagy and apoptosis in Mycobacterium bovis infected bone marrow derived macrophages |
753228 |
| 3.4.21.B43 | metabolism |
PDGF-B is probably one of the molecules linking the interaction between enzyme-induced endothelial cells and fibroblasts. Expression of both KLK12 and PDGFB genes is regulated by hypoxia in the lung tumor microenvironment |
731781 |
| 3.4.21.B43 | more |
KLK12 is a trypsin-like kallikrein-related peptidase that is abundant in a variety of human tissues |
731781 |
| 3.4.21.B43 | physiological function |
cleavage of the influenza hemagglutinin precursor by host proteases, e.g. kallikrein-related peptidase 12, is a critical step in the virus life cycle. Cleavage activation of influenza hemagglutinin enables fusion with the host endosome, allowing for release of the viral genome into the host cel |
732105 |
| 3.4.21.B43 | physiological function |
expression profile of the splice variants KLK12sv3 and KLK12sv1/KLK12sv2 of kallikrein-related peptidase 12 in breast cancer patients and their clinical significance, overview. Positive KLK12sv3 expression is associated with longer patient disease-free survival and higher progesterone receptor concentration. KLK12sv1/KLK12sv2 expression is statistically associated with KLK12sv3 expression |
732958 |
| 3.4.21.B43 | physiological function |
fragmentation of CCN1 or CCN5 by KLK12 prevents vascular endothelial growth factor165 binding, whereas it also triggers the release of intact vascular endothelial growth factor and bone morphogenetic protein 2 from the CCN protein complexes. The KLK12-mediated release of transforming growth factor-beta1 and fibroblast growth factor-2 is concentration-dependent. KLK12 may indirectly regulate the bioavailability and activity of several growth factors through processing of their CCN binding partners |
717833 |
| 3.4.21.B43 | physiological function |
implicated in the cancer progression |
753295 |
| 3.4.21.B43 | physiological function |
proangiogenic activity of the enzyme in lung endothelial cells. The enzyme may interfere with kininostatin-related antiangiogenic activity by cleaving the D5 domain |
731400 |
| 3.4.21.B43 | physiological function |
the enzyme induces the formation of pulmonary endothelial cell tubule-like structures. The enzyme converts the extracellular matrix- or membrane-bound precursor of platelet-derived growth factor B (PDGF-B) into a soluble active form. Both PDGF-B and vascular endothelial growth factor A (VEGF-A) take part in the induction of angiogenesis by enzyme KLK12 in a coculture model of angiogenesis that mimics endothelial tubule formation. Release of mature PDGF-B by enzyme KLK12 leads to the fibroblast-mediated secretion of VEGF-A, which stimulates endothelial cell differentiation and the formation of capillary tube-like structures. PDGF-B signaling ultimately results in cell growth, migration, and protection against apoptosis, overview |
731781 |
| 3.4.21.B43 | physiological function |
the enzyme regulates innate resistance of murine macrophages against Mycobacterium bovis infection by modulating autophagy and apoptosis |
753228 |
