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Mitochondrial serine protease HtrA2 (zeige F2 Proteine)/Omi is an important mediator of germ cell death.
Data show the presence of apoptosis at the cellular level in both ade2 (zeige PAICS Proteine) and Prat (zeige PPAT Proteine) mutants, and the upregulated gene HtrA2, which encodes an apoptosis effector and is thus a candidate for initiating apoptosis in response to purine depletion.
Drosophila Omi (dOmi), a fly homologue of the serine protease Omi/HtrA2, alleviates th/DIAP1 (zeige DIAPH1 Proteine) inhibition of all caspases by proteolytically degrading th/DIAP1 (zeige DIAPH1 Proteine) and induces apoptosis both in cultured cells and in the developing fly eye.
The binding of DIAP1 (zeige DIAPH1 Proteine) to dOmi resulted in DIAP1 (zeige DIAPH1 Proteine)-mediated polyubiquitination of dOmi, suggesting that DIAP1 (zeige DIAPH1 Proteine) could target dOmi for proteasomal degradation.
found that Rhomboid-7, a mitochondrial protease not previously implicated in PD, acts as an upstream component of this pathway, and showed that it is required to cleave the precursor forms of both Pink1 (zeige PINK1 Proteine) and Omi
HtrA2 was shown to be phosphorylated in a PINK1 (zeige PINK1 Proteine)-dependent manner, suggesting it might act in the PINK1 (zeige PINK1 Proteine) pathway.
The important functions for HTRA2 in programmed cell death.
A pathogenic role of serine protease HtrA2 (zeige F2 Proteine) in Parkinson's and Alzheimer's diseases has been described. (Review)
The first report of recessive deleterious mutations in HTRA2 in human. Absence of HTRA2/Omi is associated with severe neurodegenerative disorder of infancy, abnormal mitochondria, 3-methylglutaconic aciduria and increased sensitivity to apoptosis.
HTRA2 and ANO3 (zeige ANO3 Proteine) mutations are not common causes of essential tremor
HtrA2 under stress conditions induces vimentin (zeige VIM Proteine) cleavage in wild-type and SH-SY5Y cells transfected with ABP (zeige ABP1 Proteine) with the Alzheimer disease-associated Swedish mutation. Interplay between Omi/HtrA2 and vimentin (zeige VIM Proteine) affects mitochondrial distribution in neurons.
The a5 helix of PDZ was involved in both, the intra- and intersubunit changes of interactions and thus seems to play an important role in HtrA2 activation.
study examined the association of HTRA2 p.G399S mutation with essential tremor(ET) and Parkinson disease (PD) in Asians and found that HTRA2 p.G399S is rare and does not appear to play a major role in subjects with coexistent ET and PD nor in those with pure ET or PD phenotype
The NG2 (zeige MCSP Proteine) proteoglycan (zeige Vcan Proteine) protects oligodendrocyte precursor cells against oxidative stress via interaction with OMI/HtrA2.
Omi/HtrA2 overexpression promotes hepatocellular carcinoma cell apoptosis and the ped/pea-15 expression level causes this difference of the Omi/HtrA2 pro-apoptotic marker in the various hepatocellular carcinoma cell lines
HtrA2 might promote the apoptosis of non-small cell lung cancer cells, and serve as a target for NSCLC's treatment.
Mice overexpressing wild-type or G399S mutant HtrA2 have mitochondrial defects resulting in neurodegeneration.
Protease Omi facilitates neurite outgrowth by cleaving the transcription factor E2F1 (zeige E2F1 Proteine) in differentiated neuroblastoma (zeige ARHGEF16 Proteine) cells; E2F1 (zeige E2F1 Proteine) is a substrate of Omi.
Protease Omi impairs mitochondrial function by cleaving Hax-1 (zeige HAX1 Proteine), which induces apoptosis in oxygen-glucose deprivation and reoxygenation -treated N2a cells and causes reperfusion injury in middle cerebral artery occlusion mice.
The NG2 (zeige Vcan Proteine) proteoglycan (zeige Vcan Proteine) protects oligodendrocyte precursor cells against oxidative stress via interaction with OMI/HtrA2.
Loss of Omi protease activity results in an abnormal increase of GSK3b, leading to the degradation of PGC (zeige PGC Proteine)-1a, which causes an impairment of mitochondrial biogenesis and induces neurodegeneration.
Neural-specific deletion of Htra2 causes cerebellar neurodegeneration and defective processing of mitochondrial OPA1.
Inactivation of Omi/HtrA2 protease leads to the deregulation of mitochondrial Mulan E3 ubiquitin ligase (zeige MUL1 Proteine) and increased mitophagy.
Phosphorylated HtrA2/Omi cleaves beta-actin and decreases the amount of filamentous actin (F-actin) in the cytosol.
The proteases HtrA2/Omi and UCH-L1 (zeige UCHL1 Proteine) regulate TNF (zeige TNF Proteine)-induced necroptosis.
Downregulation of PARL (zeige PARL Proteine) after ischemia is a key step in ischemic neuronal injury, and that it decreases HtrA2 processing and increases neuronal vulnerability.
This gene encodes a serine protease. The protein has been localized in the endoplasmic reticulum and interacts with an alternatively spliced form of mitogen-activated protein kinase 14. The protein has also been localized to the mitochondria with release to the cytosol following apoptotic stimulus. The protein is thought to induce apoptosis by binding the apoptosis inhibitory protein baculoviral IAP repeat-containing 4. Nuclear localization of this protein has also been observed. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Additional transcript variants have been described, but their full-length sequences have not been determined.
, HtrA serine peptidase 2
, protease, serine, 25
, serine protease HTRA2, mitochondrial-like
, HtrA-like serine protease
, Omi stress-regulated endoprotease
, high temperature requirement protein A2
, serine protease 25
, serine protease HTRA2, mitochondrial
, serine proteinase OMI
, motor neuron degeneration 2
, omi stress-regulated endoprotease
, serine protease OMI
, protease serine 25