ArticleJournal of Alzheimer's disease : JAD2009
A new function of human HtrA2 as an amyloid-beta oligomerization inhibitor.
Article in Journal of Alzheimer's disease : JAD, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- HtrA2/Omi: potential therapeutic targets for neurodegenerative diseases.Frontiers in pharmacology · 2026Review
- Therapeutic potential of melatonin-induced mitophagy in the pathogenesis of Alzheimer's disease.Inflammopharmacology · 2025Review
- HTRA2/OMI-Mediated Mitochondrial Quality Control Alters Macrophage Polarization Affecting Systemic Chronic Inflammation.International journal of molecular sciences · 2024Review
- Protease-independent control of parthanatos by HtrA2/Omi.Cellular and molecular life sciences : CMLS · 2023Article
- The "mitochondrial stress responses": the "Dr. Jekyll and Mr. Hyde" of neuronal disorders.Neural regeneration research · 2022Review
- Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Mitochondrial Protein Homeostasis and Cardiomyopathy.International journal of molecular sciences · 2022Review
- Mitochondria dysfunction in the pathogenesis of Alzheimer's disease: recent advances.Molecular neurodegeneration · 2020Review
- Chaperone activity of serine protease HtrA of Helicobacter pylori as a crucial survival factor under stress conditions.Cell communication and signaling : CCS · 2019Article
- ER stress-induced aggresome trafficking of HtrA1 protects against proteotoxicity.Journal of molecular cell biology · 2017Article
- Distinct 3D Architecture and Dynamics of the Human HtrA2(Omi) Protease and Its Mutated Variants.PloS one · 2016Article
- Stress Conditions Increase Vimentin Cleavage by Omi/HtrA2 Protease in Human Primary Neurons and Differentiated Neuroblastoma Cells.Molecular neurobiology · 2015Article
- Mitochondria Retrograde Signaling and the UPR mt: Where Are We in Mammals?International journal of molecular sciences · 2015Review
- Molecular basis of etiological implications in Alzheimer's disease: focus on neuroinflammation.Molecular neurobiology · 2013Review
- Temperature-induced changes of HtrA2(Omi) protease activity and structure.Cell stress & chaperones · 2013Article
- Allosteric regulation of serine protease HtrA2 through novel non-canonical substrate binding pocket.PloS one · 2013Article
- Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration.Frontiers in aging neuroscience · 2012Article
- Altered enzymatic activity and allele frequency of OMI/HTRA2 in Alzheimer's disease.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
- Stoichiometry and affinity of the human serum albumin-Alzheimer's Aβ peptide interactions.Biophysical journal · 2011Article
- Escherichia coli DegP: a structure-driven functional model.Journal of bacteriology · 2009Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human HtrA2 is part of the HtrA family of ATP-independent serine proteases that are conserved in both prokaryotes and eukaryotes and localizes to the intermembrane space of the mitochondria. Several recent reports have suggested that HtrA2 is important for maintaining proper mitochondrial homeostasis and may play a role in Alzheimer's disease (AD), which is characterized by the presence of aggregates of the amyloid-beta peptide 1-42 (Abeta1-42). In this study, we analyzed the ability of HtrA2 to delay the aggregation of the model substrate citrate synthase (CS) and of the toxic Abeta1-42 peptide. We found that HtrA2 had a moderate ability to delay the aggregation of CS in vitro, and this activity was significantly enhanced when the PDZ domain was removed suggesting an inhibitory role for this domain on the activity. Additionally, using electron microscopy and nuclear magnetic resonance analyses, we observed that HtrA2 significantly delayed the aggregation of the Abeta1-42 peptide. Interestingly, the protease activity of HtrA2 and its PDZ domain were not essential for the delay of Abeta1-42 peptide aggregation. These results indicate that besides its protease activity, HtrA2 also performs a chaperone function and suggest a role for HtrA2 in the metabolism of intracellular Abeta and in AD.
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Registered trials
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