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- Table of Contents
Facts about Serine protease HTRA2, mitochondrial.
Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 appears to be proteolytically inactive.
Human | |
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Gene Name: | HTRA2 |
Uniprot: | O43464 |
Entrez: | 27429 |
Belongs to: |
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peptidase S1C family |
High temperature requirement protein A2; HtrA serine peptidase 2; HTRA2; HtrA-like serine protease; Omi; OMIOmi stress-regulated endoprotease; PARK13EC 3.4.21.108; PRSS25; PRSS25serine, 25; Serine protease 25; serine protease HTRA2, mitochondrial; Serine proteinase OMI
Mass (kDA):
48.841 kDA
Human | |
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Location: | 2p13.1 |
Sequence: | 2; NC_000002.12 (74529405..74533556) |
Isoform 1 is ubiquitous. Isoform 2 is expressed predominantly in the kidney, colon and thyroid.
Mitochondrion intermembrane space. Mitochondrion membrane; Single-pass membrane protein. Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 truncated BID/tBID.
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The current study of the HTRA2 marker is aimed at determining the status of this gene in Chinese populations. This genetic variant was found in mitochondrial proteins FPD and ETPD mice. It was associated to high levels protein synthesis. This mutation has not been linked to familial Parkinson's. However, its multitasking potential has made it a promising therapeutic target for the treatment of various neurological conditions, including Alzheimer's disease.
The HTRA2 marker, also known as OMI, is a nuclear-encoded serine protease. The protein is produced in the nucleus as a precursor, which contains its mitochondrial target sequence. The protein undergoes further processing before it emerges in the mitochondria as the mature version. The protein is then released by the mitochondria after it enters the cell and interacts avec caspase inhibitor proteins.
OMI/HTRA2 was found to be associated with APP gene activity, which may indicate a link between cholinergic deficits and APP processing. Ab peptides are also known to have an effect on acetylcholinesterase activities and homeostasis. These peptides are found to preferentially accumulate within cholinergic neuronal cells, suggesting that they play a biological role in the cholinergic systems.
The current study shows OMI/HTRA2 level correlates with other biomarkers. Although further studies are needed, the OMI/HTRA2 protein level is associated with cholinergic signaling and may serve as a stress response in AD. This study may help in the development and validation of a diagnostic tool for Alzheimer's. These studies also suggest that HTRA2 is an important marker in the treatment of this disease.
The HTRA2 gene is a mitochondrial serine protease. It is controlled by a protein known PINK1 that contributes to the risk for developing Parkinson's disease. Recent work by Beaudette KN, Wang JH, and Beaudette KN have shown that HTRA2 in Parkinson's disease is a target of PINK1. Future plans for the HTRA2 marker include identifying whether it plays a role in the onset of the disease, as well as determining its role in the development of the disease.
PMID: 10644717 by Faccio L., et al. Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia.
PMID: 10971580 by Gray C.W., et al. Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response.