EC Number   |
General Information |
Reference |
|---|
   3.4.21.108 | physiological function |
cytosolic HtrA2 decreases ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) protein level and its hydrolase activity through HtrA2-mediated cleavage of UCH-L1 under apoptotic conditions. HtrA2-mediated cleavage of UCH-L1 plays important roles in regulating the fine balance between cell growth and cell death |
717200 |
| 3.4.21.108 | malfunction |
decreased enzyme function damages mitochondrial quality in the heterozygous mouse brain cortex, leading to more brain ischemia/reperfusion injury. HtrA2-heterozygous mice show decreased mitochondrial quality control and reduced mitochondrial function after ischemia/reperfusion injury, decreased anti-damage ability and increased apoptosis after middle cerebral artery occlusion |
771822 |
| 3.4.21.108 | physiological function |
during thermal activation, the PDZ domain changes its position versus the protease domain inside a subunit, including a prominent change affecting the L3 regulatory loop of the protease domain, and also changes its interactions with the protease domain of the adjacent subunit, specifically with its L1* regulatory loop containing the active site serine. The alpha5 helix of PDZ is involved in both, the intra- and intersubunit changes of interactions and seems to play an important role in HtrA2 activation |
752820 |
| 3.4.21.108 | malfunction |
endogenous levels of Parkin are significantly decreased in wild-type (HtrA2+/+) mouse embryonic fibroblasts compared with those in HtrA2-knockout (HtrA2-/-) mouse embryonic fibroblasts under the same stress conditions |
707374 |
| 3.4.21.108 | malfunction |
enzyme inactivation leads to the growth retardation of adipocytes, thereby delaying the hair cycle of mnd2 mice |
769073 |
| 3.4.21.108 | malfunction |
fewer and abnormal mitochondria are found in HtrA2/Omi knockout mice photoreceptors and pigment epithelial cells |
708821 |
| 3.4.21.108 | physiological function |
HtrA2 acts as an apoptotic factor which targets inhibitors of apoptosis during apoptosis, and thereby enhances caspase activation and caspase-mediated cell death |
717632 |
| 3.4.21.108 | physiological function |
HtrA2 has a moderate ability to delay the aggregation of citrate synthase in vitro. Additionally, using electron microscopy and nuclear magnetic resonance analyses, it is observed that HtrA2 significantly delays the aggregation of the Abeta1-42 peptide. The protease activity of HtrA2 and its PDZ domain are not essential for the delay of Abeta1-42 peptide aggregation |
708862 |
| 3.4.21.108 | physiological function |
HtrA2 under several different stress conditions induces cleavage of vimentin in wild-type as well as SH-SY5Y cells transfected with amyloid precursor protein with the Alzheimer disease-associated Swedish mutation. After stress treatment, inhibition of HtrA2 protease activity by the specific inhibitor, Ucf-101, reduces the cleavage of vimentin in wild-type cells |
754775 |
| 3.4.21.108 | physiological function |
HtrA2/Omi cleave Wilms'tumor suppressor protein WT1 which causes the removal of WT1 from its binding sites at gene promoters, leading to alterations in gene regulation that enhance apoptosis |
709955 |
