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Journal articles on the topic 'High temperature requirement A (HtrA) protease'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

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1

NIE, Gui-Ying, Anne HAMPTON, Ying LI, Jock K. FINDLAY, and Lois A. SALAMONSEN. "Identification and cloning of two isoforms of human high-temperature requirement factor A3 (HtrA3), characterization of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2." Biochemical Journal 371, no. 1 (2003): 39–48. http://dx.doi.org/10.1042/bj20021569.

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In the present study, we identified an additional member of the human high-temperature requirement factor A (HtrA) protein family, called pregnancy-related serine protease or HtrA3, which was most highly expressed in the heart and placenta. We cloned the full-length sequences of two forms (long and short) of human HtrA3 mRNA, located the gene on chromosome 4p16.1, determined its genomic structure and revealed how the two mRNA variants are produced through alternative splicing. The alternative splicing was also verified by Northern blotting. Four distinct domains were found for the long form Ht

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Bowden, M. A., L. A. Di Nezza, T. Jobling, L. A. Salamonsen, and G. Nie. "284.Expression of HtrA1, 2 and 3 in human endometrial cancer." Reproduction, Fertility and Development 16, no. 9 (2004): 284. http://dx.doi.org/10.1071/srb04abs284.

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The mammalian HtrA family consists of serine proteases with distinct domains homologous to the bacterial high temperature requirement factor (HtrA). Three human HtrA members have been reported: HtrA1 (PRSS11 or L56), HtrA2 (OMI) and HtrA3 (PRSP). The function of HtrA1 is not well characterised, but it has been shown to be downregulated in malignant tissues (1–3) indicating that the downregulation of HtrA1 is associated with cancer progression. HtrA2 regulates apoptosis by interacting with X-linked inhibitors of apoptosis (XIAP) thus preventing the caspase-inhibitory function of XIAP (4). The f

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Bæk, Kristoffer T., Christina S. Vegge, Joanna Skórko-Glonek, and Lone Brøndsted. "Different Contributions of HtrA Protease and Chaperone Activities toCampylobacter jejuniStress Tolerance and Physiology." Applied and Environmental Microbiology 77, no. 1 (2010): 57–66. http://dx.doi.org/10.1128/aem.01603-10.

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ABSTRACTThe microaerophilic bacteriumCampylobacter jejuniis the most common cause of bacterial food-borne infections in the developed world. Tolerance to environmental stress relies on proteases and chaperones in the cell envelope, such as HtrA and SurA. HtrA displays both chaperone and protease activities, but little is known about how each of these activities contributes to stress tolerance in bacteria.In vitroexperiments showed temperature-dependent protease and chaperone activities ofC. jejuniHtrA. AC. jejunimutant lacking only the protease activity of HtrA was used to show that the HtrA c

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Singh, Khundrakpam Herojit, Savita Yadav, Deepak Kumar, and Bichitra Kumar Biswal. "The crystal structure of an essential high-temperature requirement protein HtrA1 (Rv1223) from Mycobacterium tuberculosis reveals its unique features." Acta Crystallographica Section D Structural Biology 74, no. 9 (2018): 906–21. http://dx.doi.org/10.1107/s205979831800952x.

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High-temperature requirement A (HtrA) proteins, which are members of the heat-shock-induced serine protease family, are involved in extracytoplasmic protein quality control and bacterial survival strategies under stress conditions, and are associated with the virulence of several pathogens; they are therefore major drug targets. Mycobacterium tuberculosis possesses three putative HtrAs: HtrA1 (Rv1223), HtrA2 (Rv0983) and HtrA3 (Rv0125). Each has a cytoplasmic region, a transmembrane helix and a periplasmic region. Here, the crystal structure of the periplasmic region consisting of a protease d

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Bernegger, Sabine, Evelyn Hutterer, Urszula Zarzecka, et al. "E-Cadherin Orthologues as Substrates for the Serine Protease High Temperature Requirement A (HtrA)." Biomolecules 12, no. 3 (2022): 356. http://dx.doi.org/10.3390/biom12030356.

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Helicobacter pylori (H. pylori) expresses the serine protease and chaperone High temperature requirement A (HtrA) that is involved in periplasmic unfolded protein stress response. Additionally, H. pylori-secreted HtrA directly cleaves the human cell adhesion molecule E-cadherin leading to a local disruption of intercellular adhesions during pathogenesis. HtrA-mediated E-cadherin cleavage has been observed in response to a broad range of pathogens, implying that it is a prevalent mechanism in humans. However, less is known whether E-cadherin orthologues serve as substrates for bacterial HtrA. H

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Padmanabhan, Nirmala, Lars Fichtner, Achim Dickmanns, Ralf Ficner, Jörg B. Schulz, and Gerhard H. Braus. "The Yeast HtrA Orthologue Ynm3 Is a Protease with Chaperone Activity that Aids Survival Under Heat Stress." Molecular Biology of the Cell 20, no. 1 (2009): 68–77. http://dx.doi.org/10.1091/mbc.e08-02-0178.

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Ynm3 is the only budding yeast protein possessing a combination of serine protease and postsynaptic density 95/disc-large/zona occludens domains, a defining feature of the high temperature requirement A (HtrA) protein family. The bacterial HtrA/DegP is involved in protective stress response to aid survival at higher temperatures. The role of mammalian mitochondrial HtrA2/Omi in protein quality control is unclear, although loss of its protease activity results in susceptibility toward Parkinson's disease, in which mitochondrial dysfunction and impairment of protein folding and degradation are k

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Gupta, Arvind Kumar, Debashree Behera, and Balasubramanian Gopal. "The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism." Acta Crystallographica Section F Structural Biology Communications 74, no. 12 (2018): 803–9. http://dx.doi.org/10.1107/s2053230x18016217.

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The crystal structure of Mycobacterium tuberculosis high-temperature requirement A (HtrA) protein was determined at 1.83 Å resolution. This membrane-associated protease is essential for the survival of M. tuberculosis. The crystal structure reveals that interactions between the PDZ domain and the catalytic domain in HtrA lead to an inactive conformation. This finding is consistent with its proposed role as a regulatory protease that is conditionally activated upon appropriate environmental triggers. The structure provides a basis for directed studies to evaluate the role of this essential prot

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8

Ye, Meiping, Kavita Sharma, Meghna Thakur, et al. "HtrA, a Temperature- and Stationary Phase-Activated Protease Involved in Maturation of a Key Microbial Virulence Determinant, Facilitates Borrelia burgdorferi Infection in Mammalian Hosts." Infection and Immunity 84, no. 8 (2016): 2372–81. http://dx.doi.org/10.1128/iai.00360-16.

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High-temperature requirement protease A (HtrA) represents a family of serine proteases that play important roles in microbial biology. Unlike the genomes of most organisms, that ofBorrelia burgdorferinotably encodes a single HtrA gene product, termed BbHtrA. Previous studies identified a few substrates of BbHtrA; however, their physiological relevance could not be ascertained, as targeted deletion of the gene has not been successful. Here we show that BbhtrAtranscripts are induced during spirochete growth either in the stationary phase or at elevated temperature. Successful generation of a Bbh

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Kummari, Raghupathi, Shubhankar Dutta, Lalith K. Chaganti, and Kakoli Bose. "Discerning the mechanism of action of HtrA4: a serine protease implicated in the cell death pathway." Biochemical Journal 476, no. 10 (2019): 1445–63. http://dx.doi.org/10.1042/bcj20190224.

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Abstract High-temperature requirement protease A4 (HtrA4) is a secretary serine protease whose expression is up-regulated in pre-eclampsia (PE) and hence is a possible biomarker of PE. It has also been altered in cancers such as glioblastoma, breast carcinoma, and prostate cancer making it an emerging therapeutic target. Among the human HtrAs, HtrA4 is the least characterized protease pertaining to both structure and its functions. Although the members of human HtrA family share a significant structural and functional conservation, subtle structural changes have been associated with certain di

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Wang, Yao, and Guiying Nie. "Overview of Human HtrA Family Proteases and Their Distinctive Physiological Roles and Unique Involvement in Diseases, Especially Cancer and Pregnancy Complications." International Journal of Molecular Sciences 22, no. 19 (2021): 10756. http://dx.doi.org/10.3390/ijms221910756.

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The mammalian high temperature requirement A (HtrA) proteins are a family of evolutionarily conserved serine proteases, consisting of four homologs (HtrA1-4) that are involved in many cellular processes such as growth, unfolded protein stress response and programmed cell death. In humans, while HtrA1, 2 and 3 are widely expressed in multiple tissues with variable levels, HtrA4 expression is largely restricted to the placenta with the protein released into maternal circulation during pregnancy. This limited expression sets HtrA4 apart from the rest of the family. All four HtrAs are active prote

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Zhang, Luhua, Ying Li, Yiping Wen, et al. "HtrA Is Important for Stress Resistance and Virulence in Haemophilus parasuis." Infection and Immunity 84, no. 8 (2016): 2209–19. http://dx.doi.org/10.1128/iai.00147-16.

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Haemophilus parasuisis an opportunistic pathogen that causes Glässer's disease in swine, with polyserositis, meningitis, and arthritis. The high-temperature requirement A (HtrA)-like protease, which is involved in protein quality control, has been reported to be a virulence factor in many pathogens. In this study, we showed that HtrA ofH. parasuis(HpHtrA) exhibited both chaperone and protease activities. Finally, nickel import ATP-binding protein (NikE), periplasmic dipeptide transport protein (DppA), and outer membrane protein A (OmpA) were identified as proteolytic substrates for HpHtrA. The

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Bakker, Dennis, Anthony M. Buckley, Anne de Jong, et al. "The HtrA-Like Protease CD3284 Modulates Virulence of Clostridium difficile." Infection and Immunity 82, no. 10 (2014): 4222–32. http://dx.doi.org/10.1128/iai.02336-14.

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ABSTRACTIn the past decade,Clostridium difficilehas emerged as an important gut pathogen. Symptoms ofC. difficileinfection range from mild diarrhea to pseudomembranous colitis. Besides the two main virulence factors toxin A and toxin B, other virulence factors are likely to play a role in the pathogenesis of the disease. In other Gram-positive and Gram-negative pathogenic bacteria, conserved high-temperature requirement A (HtrA)-like proteases have been shown to have a role in protein homeostasis and quality control. This affects the functionality of virulence factors and the resistance of bac

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Zhang, Zhemin, Qi Huang, Xuan Tao, et al. "The unique trimeric assembly of the virulence factor HtrA from Helicobacter pylori occurs via N-terminal domain swapping." Journal of Biological Chemistry 294, no. 20 (2019): 7990–8000. http://dx.doi.org/10.1074/jbc.ra119.007387.

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Knowledge of the molecular mechanisms of specific bacterial virulence factors can significantly contribute to antibacterial drug discovery. Helicobacter pylori is a Gram-negative microaerophilic bacterium that infects almost half of the world's population, leading to gastric disorders and even gastric cancer. H. pylori expresses a series of virulence factors in the host, among which high-temperature requirement A (HpHtrA) is a newly identified serine protease secreted by H. pylori. HpHtrA cleaves the extracellular domain of the epithelial cell surface adhesion protein E-cadherin and disrupts g

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Fahrenkrog, Birthe. "Nma111p, the pro-apoptotic HtrA-like nuclear serine protease in Saccharomyces cerevisiae: a short survey." Biochemical Society Transactions 39, no. 5 (2011): 1499–501. http://dx.doi.org/10.1042/bst0391499.

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The baker's yeast, Saccharomyces cerevisiae, is also capable of undergoing programmed cell death or apoptosis, for example in response to viral infection as well as during chronological and replicative aging. Intrinsically, programmed cell death in yeast can be induced by, for example, H2O2, acetic acid or the mating-type pheromone. A number of evolutionarily conserved apoptosis-regulatory proteins have been identified in yeast, one of which is the HtrA (high-temperature requirement A)-like serine protease Nma111p (Nma is nuclear mediator of apoptosis). Nma111p is a nuclear serine protease of

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15

Huesgen, Pitter F., Helder Miranda, XuanTam Lam, et al. "Recombinant Deg/HtrA proteases from Synechocystis sp. PCC 6803 differ in substrate specificity, biochemical characteristics and mechanism." Biochemical Journal 435, no. 3 (2011): 733–42. http://dx.doi.org/10.1042/bj20102131.

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Cyanobacteria require efficient protein-quality-control mechanisms to survive under dynamic, often stressful, environmental conditions. It was reported that three serine proteases, HtrA (high temperature requirement A), HhoA (HtrA homologue A) and HhoB (HtrA homologue B), are important for survival of Synechocystis sp. PCC 6803 under high light and temperature stresses and might have redundant physiological functions. In the present paper, we show that all three proteases can degrade unfolded model substrates, but differ with respect to cleavage sites, temperature and pH optima. For recombinan

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Canadas-Ortega, Marina, Iris Mühlbacher, Gernot Posselt, et al. "HtrA-Dependent E-Cadherin Shedding Impairs the Epithelial Barrier Function in Primary Gastric Epithelial Cells and Gastric Organoids." International Journal of Molecular Sciences 25, no. 13 (2024): 7083. http://dx.doi.org/10.3390/ijms25137083.

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Impaired E-cadherin (Cdh1) functions are closely associated with cellular dedifferentiation, infiltrative tumor growth and metastasis, particularly in gastric cancer. The class-I carcinogen Helicobacter pylori (H. pylori) colonizes gastric epithelial cells and induces Cdh1 shedding, which is primarily mediated by the secreted bacterial protease high temperature requirement A (HtrA). In this study, we used human primary epithelial cell lines derived from gastroids and mucosoids from different healthy donors to investigate HtrA-mediated Cdh1 cleavage and the subsequent impact on bacterial pathog

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Zaide, Galia, Uri Elia, Inbar Cohen-Gihon, et al. "Comparative Analysis of the Global Transcriptomic Response to Oxidative Stress of Bacillus anthracis htrA-Disrupted and Parental Wild Type Strains." Microorganisms 8, no. 12 (2020): 1896. http://dx.doi.org/10.3390/microorganisms8121896.

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We previously demonstrated that the HtrA (High Temperature Requirement A) protease/chaperone active in the quality control of protein synthesis, represents an important virulence determinant of Bacillus anthracis. Virulence attenuation of htrA-disrupted Bacillus anthracis strains was attributed to susceptibility of ΔhtrA strains to stress insults, as evidenced by affected growth under various stress conditions. Here, we report a comparative RNA-seq transcriptomic study generating a database of differentially expressed genes in the B. anthracis htrA-disrupted and wild type parental strains unde

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Sharafutdinov, Irshad, Nicole Tegtmeyer, Mathias Müsken, and Steffen Backert. "Campylobacter jejuni Serine Protease HtrA Induces Paracellular Transmigration of Microbiota across Polarized Intestinal Epithelial Cells." Biomolecules 12, no. 4 (2022): 521. http://dx.doi.org/10.3390/biom12040521.

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Campylobacter jejuni represents an eminent zoonotic germ responsible for foodborne infections causing campylobacteriosis. In addition, infections with C. jejuni constitute a risk factor for the occurrence of inflammatory bowel disease (IBD). In the latter case, patients show inflammatory reactions not only against C. jejuni, but also against the non-infectious microbiota. However, the involved mechanisms and molecular basis are still largely unclear. We recently reported that C. jejuni breaches the intestinal epithelial barrier by secretion of serine protease HtrA (high temperature requirement

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Colomer-Winter, Cristina, Adeline M. H. Yong, Kelvin K. L. Chong, et al. "The HtrA chaperone monitors sortase-assembled pilus biogenesis in Enterococcus faecalis." PLOS Genetics 20, no. 8 (2024): e1011071. http://dx.doi.org/10.1371/journal.pgen.1011071.

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Sortase-assembled pili contribute to virulence in many Gram-positive bacteria. In Enterococcus faecalis, the endocarditis and biofilm-associated pilus (Ebp) is polymerized on the membrane by sortase C (SrtC) and attached to the cell wall by sortase A (SrtA). In the absence of SrtA, polymerized pili remain anchored to the membrane (i.e. off-pathway). Here we show that the high temperature requirement A (HtrA) bifunctional chaperone/protease of E. faecalis is a quality control system that clears aberrant off-pathway pili from the cell membrane. In the absence of HtrA and SrtA, accumulation of me

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Chen, Yan, Jianfeng Yang, Hangbin Jin, et al. "HtrA3: a promising prognostic biomarker and therapeutic target for head and neck squamous cell carcinoma." PeerJ 11 (October 10, 2023): e16237. http://dx.doi.org/10.7717/peerj.16237.

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Objective The dysregulation of the human high-temperature requirement A (HtrA) family of serine proteases is associated with many malignancies. However, there are few reports on HtrAs in head and neck squamous cell carcinoma (HNSCC). The aim of this study was to investigate the expression, prognostic value, and biological functions of HtrAs in HNSCC. Methods The RNA-sequencing data and clinical data of HNSCC were downloaded from The Cancer Genome Atlas (TCGA) database. The GSE30784 and GSE31056 datasets from the Gene Expression Omnibus (GEO) database were used for further verification. This st

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Renke, Joanna, Eliza Wasilewska, Sabina Kędzierska-Mieszkowska, et al. "Tumor Suppressors—HTRA Proteases and Interleukin-12—in Pediatric Asthma and Allergic Rhinitis Patients." Medicina 56, no. 6 (2020): 298. http://dx.doi.org/10.3390/medicina56060298.

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Background and objective: Allergy belongs to a group of mast cell-related disorders and is one of the most common diseases of childhood. It was shown that asthma and allergic rhinitis diminish the risk of various cancers, including colon cancer and acute lymphoblastic leukemia. On the other hand, asthma augments the risk of lung cancer and an increased risk of breast cancer in patients with allergy has been observed. Thus, the relation between allergy and cancer is not straightforward and furthermore, its biological mechanism is unknown. The HTRA (high temperature requirement A) proteases prom

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Wahlberg, Patrik, Åsa Nylander, Nina Ahlskog, Kui Liu, and Tor Ny. "Expression and Localization of the Serine Proteases High-Temperature Requirement Factor A1, Serine Protease 23, and Serine Protease 35 in the Mouse Ovary." Endocrinology 149, no. 10 (2008): 5070–77. http://dx.doi.org/10.1210/en.2007-1736.

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Proteolytic degradation of extracellular matrix components has been suggested to play an essential role in the occurrence of ovulation. Recent studies in our laboratory have indicated that the plasminogen activator and matrix metalloproteinase systems, which were previously believed to be crucial for ovulation, are not required in this process. In this study we have used a microarray approach to identify new proteases that are involved in ovulation. We found three serine proteases that were relatively highly expressed during ovulation: high-temperature requirement factor A1 (HtrA1), which was

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Sun, Hongyu, Luyan Shen, Ping Zhang, et al. "Inhibition of High-Temperature Requirement Protein A2 Protease Activity Represses Myogenic Differentiation via UPRmt." International Journal of Molecular Sciences 23, no. 19 (2022): 11761. http://dx.doi.org/10.3390/ijms231911761.

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Skeletal muscles require muscle satellite cell (MuSC) differentiation to facilitate the replenishment and repair of muscle fibers. A key step in this process is called myogenic differentiation. The differentiation ability of MuSCs decreases with age and can result in sarcopenia. Although mitochondria have been reported to be involved in myogenic differentiation by promoting a bioenergetic remodeling, little is known about the interplay of mitochondrial proteostasis and myogenic differentiation. High-temperature-requirement protein A2 (HtrA2/Omi) is a protease that regulates proteostasis in the

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Ciferri, Claudio, Michael T. Lipari, Wei-Ching Liang, et al. "The trimeric serine protease HtrA1 forms a cage-like inhibition complex with an anti-HtrA1 antibody." Biochemical Journal 472, no. 2 (2015): 169–81. http://dx.doi.org/10.1042/bj20150601.

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The high temperature requirement A1 (HtrA1) protease is implicated in many pathological processes, including the age-related macular degeneration (AMD). We identified a blocking antibody binding to the HTRA1 complex trimer and were able to elucidate an unusual inhibitory mechanism by structural and biochemical experiments.

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Tennstaedt, Annette, Simon Pöpsel, Linda Truebestein, et al. "Human High Temperature Requirement Serine Protease A1 (HTRA1) Degrades Tau Protein Aggregates." Journal of Biological Chemistry 287, no. 25 (2012): 20931–41. http://dx.doi.org/10.1074/jbc.m111.316232.

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Campbell, Robert A., Mark Cody, Yasuhiro Kosaka, Heather D. Campbell, and Christian Yost. "Placental HTRA1 Protease Cleaves Alpha-1-Antitrypsin and Generates Neonatal NET-Inhibitory Factor." Blood 132, Supplement 1 (2018): 273. http://dx.doi.org/10.1182/blood-2018-99-111195.

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Abstract BACKGROUND: Neutrophil extracellular traps (NET) are extracellular lattices of decondensed chromatin associated with anti-microbial proteins and degradative enzymes released by polymorphonuclear leukocytes (PMN) to trap and kill invading microbes. Dysregulated NET formation, however, contributes to inflammatory tissue damage. We have identified a novel NET-inhibitory peptide, neonatal NET-Inhibitory Factor (nNIF), present in the fetal circulation. nNIF is formed as a carboxy-terminus cleavage fragment of alpha-1 antitrypsin (AAT), an abundant, circulating protease inhibitor with homol

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Zhang, Dingwa, Deyong He, Xiaoliang Pan, Yaping Xu, and Lijun Liu. "Molecular design of orthogonal stacking system at the complex interface of HtrA PDZ domain with its peptide ligands." Journal of the Serbian Chemical Society 84, no. 12 (2019): 1367–79. http://dx.doi.org/10.2298/jsc181221029z.

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The high temperature requirement A (HtrA) protease plays a crucial role in protein quality control and cell fate. The enzyme contains a catalytic protease domain and a regulatory PDZ domain; the latter determines the substrate specificity of the former by specifically binding to the C-terminal hydrophobic stretch of its partner proteins. Previously, a pentapeptide ligand H3C1 was identified as the potential binder of HtrA PDZ domain using phage display technique. Here, an orthogonal ??cation?? stacking system at the crystal domain?peptide complex interface was analysed by integrating theoretic

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Acharya, Saujanya, Shubhankar Dutta, and Kakoli Bose. "A distinct concerted mechanism of structural dynamism defines activity of human serine protease HtrA3." Biochemical Journal 477, no. 2 (2020): 407–29. http://dx.doi.org/10.1042/bcj20190706.

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Human HtrA3 (high-temperature requirement protease A3) is a trimeric multitasking propapoptotic serine protease associated with critical cellular functions and pathogenicity. Implicated in diseases including cancer and pre-eclampsia, its role as a tumor suppressor and potential therapeutic target cannot be ignored. Therefore, elucidating its mode of activation and regulatory switch becomes indispensable towards modulating its functions with desired effects for disease intervention. Using computational, biochemical and biophysical tools, we delineated the role of all domains, their combinations

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Dynon, K., and G. Nie. "309. DEVELOPMENT AND VALIDATION OF AN ELISA FOR HIGH TEMPERATURE REQUIREMENT FACTOR A3 (HtrA3): EARLY DETECTION OF PREECLAMPSIA." Reproduction, Fertility and Development 22, no. 9 (2010): 109. http://dx.doi.org/10.1071/srb10abs309.

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Preeclampsia (PE) is a multisystemic condition in pregnant women that can be life threatening for both mother and baby. PE is a hypertensive disorder that develops concurrently with proteinuria after 20 weeks of gestation. Abnormal placental development during early pregnancy precedes the onset of PE later in gestation. Early diagnosis of PE is essential to reduce PE-related mortality and morbidity. To date there is no clinically useful biochemical diagnostic method that can detect PE during early pregnancy. Our laboratory discovered and cloned the serine protease HtrA3 and has shown that HtrA

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Spiers, Alison, Heather K. Lamb, Simon Cocklin, et al. "PDZ Domains Facilitate Binding of High Temperature Requirement Protease A (HtrA) and Tail-specific Protease (Tsp) to Heterologous Substrates through Recognition of the Small Stable RNA A (ssrA)-encoded Peptide." Journal of Biological Chemistry 277, no. 42 (2002): 39443–49. http://dx.doi.org/10.1074/jbc.m202790200.

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Hwang, Jimin, Sonya Mros, Allan B. Gamble, Joel D. A. Tyndall, and Arlene McDowell. "Improving Antibacterial Activity of a HtrA Protease Inhibitor JO146 against Helicobacter pylori: A Novel Approach Using Microfluidics-Engineered PLGA Nanoparticles." Pharmaceutics 14, no. 2 (2022): 348. http://dx.doi.org/10.3390/pharmaceutics14020348.

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Nanoparticle drug delivery systems have emerged as a promising strategy for overcoming limitations of antimicrobial drugs such as stability, bioavailability, and insufficient exposure to the hard-to-reach bacterial drug targets. Although size is a vital colloidal feature of nanoparticles that governs biological interactions, the absence of well-defined size control technology has hampered the investigation of optimal nanoparticle size for targeting bacterial cells. Previously, we identified a lead antichlamydial compound JO146 against the high temperature requirement A (HtrA) protease, a promi

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M’Angale, P. Githure, and Brian E. Staveley. "The HtrA2 Drosophila model of Parkinson’s disease is suppressed by the pro-survival Bcl-2 Buffy." Genome 60, no. 1 (2017): 1–7. http://dx.doi.org/10.1139/gen-2016-0069.

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Mutations in High temperature requirement A2 (HtrA2), also designated PARK13, which lead to the loss of its protease activity, have been associated with Parkinson’s disease (PD). HtrA2 is a mitochondrial protease that translocates to the cytosol upon the initiation of apoptosis where it participates in the abrogation of inhibitors of apoptosis (IAP) inhibition of caspases. Here, we demonstrate that the loss of the HtrA2 function in the dopaminergic neurons of Drosophila melanogaster results in PD-like phenotypes, and we attempt to restore the age-dependent loss in locomotor ability by co-expre

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Yamauchi, Shota, Yan Yan Hou, Alvin Kunyao Guo, et al. "p53-mediated activation of the mitochondrial protease HtrA2/Omi prevents cell invasion." Journal of Cell Biology 204, no. 7 (2014): 1191–207. http://dx.doi.org/10.1083/jcb.201309107.

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Oncogenic Ras induces cell transformation and promotes an invasive phenotype. The tumor suppressor p53 has a suppressive role in Ras-driven invasion. However, its mechanism remains poorly understood. Here we show that p53 induces activation of the mitochondrial protease high-temperature requirement A2 (HtrA2; also known as Omi) and prevents Ras-driven invasion by modulating the actin cytoskeleton. Oncogenic Ras increases accumulation of p53 in the cytoplasm, which promotes the translocation of p38 mitogen-activated protein kinase (MAPK) into mitochondria and induces phosphorylation of HtrA2/Om

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Vierkotten, Sascha, та Victoria Korinek. "HTRA1 enhance signaling pathway of uveitis via modulation of the TGF-β signaling cascade". American Journal of BioMedicine 4, № 3 (2016): 276–88. http://dx.doi.org/10.18081/2333-5106/016-276-288.

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High temperature requirement protein A1 (HtrA1) is a serine protease that is mostly secreted to degrade numerous extracellular matrix proteins, They are involved in the development and progression of several pathological processes such as cancer, neurodegenerative disorders and arthritic diseases, but it also exists within cells for some partially understood. The purpose of this study was to investigate the role of HTRA1 in the uveitis, and the possible mechanisms involved. Interphotoreceptor retinoid-binding protein peptide R14 to induced uveitis in rat model. A recombinant lentiviral vector

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Frochaux, Violette, Diana Hildebrand, Anja Talke, Michael W. Linscheid, and Hartmut Schlüter. "Alpha-1-Antitrypsin: A Novel Human High Temperature Requirement Protease A1 (HTRA1) Substrate in Human Placental Tissue." PLoS ONE 9, no. 10 (2014): e109483. http://dx.doi.org/10.1371/journal.pone.0109483.

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Canfield, A. E., K. D. Hadfield, C. F. Rock, E. C. Wylie, and F. L. Wilkinson. "HtrA1: a novel regulator of physiological and pathological matrix mineralization?" Biochemical Society Transactions 35, no. 4 (2007): 669–71. http://dx.doi.org/10.1042/bst0350669.

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HtrA1 (high-temperature requirement protein A1) is a secreted multidomain protein with proven serine protease activity and the ability to regulate TGF-β (transforming growth factor-β)/BMP (bone morphogenetic protein) signalling. There is increasing evidence that HtrA1 regulates several pathological processes, including tumour development, Alzheimer's disease, age-related macular degeneration and osteoarthritis, although the mechanism(s) by which it regulates these processes have not been fully elucidated. Using overexpression and knock-down strategies, we have evidence demonstrating that HtrA1

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Catalano, V., A. Baldi, V. Shridhar, et al. "HtrA1 expression as a predictive factor of response to cisplatin-based regimen in patients with advanced gastric cancer." Journal of Clinical Oncology 24, no. 18_suppl (2006): 4077. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.4077.

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4077 Background: Human HtrA1 is a member of the HtrA (High temperature requirement) family of serine proteases. Recent reports suggest that htrA1 plays a protective role in varous malignancies due to its tumour suppressive properties. This study was performed to estimate HtrA1 expression as a predictor of the response to chemotherapy of patients with gastric cancer. Methods: HtrA1 was measured immunohistochemically on archival specimens of primary gastric cancer from 51 patients treated consecutively at our institution with a weekly chemotherapy including cisplatin 40 mg/m2, epirubicin 35 mg/m

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Kummari, Raghupathi, Shubhankar Dutta, Shubhangi Patil, Snehal Pandav Mudrale, and Kakoli Bose. "Elucidating the role of GRIM-19 as a substrate and allosteric activator of pro-apoptotic serine protease HtrA2." Biochemical Journal 478, no. 6 (2021): 1241–59. http://dx.doi.org/10.1042/bcj20200923.

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HtrA2 (high-temperature requirement A2) and GRIM-19 (gene associated with retinoic and interferon-induced mortality 19 protein) are involved in various biological functions with their deregulation leading to multiple diseases. Although it is known that the interaction between GRIM-19 with HtrA2 promotes the pro-apoptotic activity of the latter, the mechanistic details remained elusive till date. Moreover, designing allosteric modulators of HtrA2 remains obscure due to lack of adequate information on the mode of interaction with its natural substrates cum binding partners. Therefore, in this st

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Tom, Irene, Victoria C. Pham, Kenneth J. Katschke, et al. "Development of a therapeutic anti-HtrA1 antibody and the identification of DKK3 as a pharmacodynamic biomarker in geographic atrophy." Proceedings of the National Academy of Sciences 117, no. 18 (2020): 9952–63. http://dx.doi.org/10.1073/pnas.1917608117.

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Genetic polymorphisms in the region of the trimeric serine hydrolase high-temperature requirement 1 (HTRA1) are associated with increased risk of age-related macular degeneration (AMD) and disease progression, but the precise biological function of HtrA1 in the eye and its contribution to disease etiologies remain undefined. In this study, we have developed an HtrA1-blocking Fab fragment to test the therapeutic hypothesis that HtrA1 protease activity is involved in the progression of AMD. Next, we generated an activity-based small-molecule probe (ABP) to track target engagement in vivo. In add

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Tiaden, André N., Marina Klawitter, Vanda Lux, et al. "Detrimental Role for Human High Temperature Requirement Serine Protease A1 (HTRA1) in the Pathogenesis of Intervertebral Disc (IVD) Degeneration." Journal of Biological Chemistry 287, no. 25 (2012): 21335–45. http://dx.doi.org/10.1074/jbc.m112.341032.

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Toyama, Yuki, Robert W. Harkness, Tim Y. T. Lee, Jason T. Maynes, and Lewis E. Kay. "Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR." Proceedings of the National Academy of Sciences 118, no. 11 (2021): e2025022118. http://dx.doi.org/10.1073/pnas.2025022118.

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Human High temperature requirement A2 (HtrA2) is a mitochondrial protease chaperone that plays an important role in cellular proteostasis and in regulating cell-signaling events, with aberrant HtrA2 function leading to neurodegeneration and parkinsonian phenotypes. Structural studies of the enzyme have established a trimeric architecture, comprising three identical protomers in which the active sites of each protease domain are sequestered to form a catalytically inactive complex. The mechanism by which enzyme function is regulated is not well understood. Using methyl transverse relaxation opt

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Campbell, Robert A., Heather D. Campbell, J. Samuel Bircher та ін. "Placental HTRA1 cleaves α1-antitrypsin to generate a NET-inhibitory peptide". Blood 138, № 11 (2021): 977–88. http://dx.doi.org/10.1182/blood.2020009021.

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Abstract Neutrophil extracellular traps (NETs) are important components of innate immunity. Neonatal neutrophils (polymorphonuclear leukocytes [PMNs]) fail to form NETs due to circulating NET-inhibitory peptides (NIPs), cleavage fragments of α1-antitrypsin (A1AT). How fetal and neonatal blood NIPs are generated remains unknown, however. The placenta expresses high-temperature requirement serine protease A1 (HTRA1) during fetal development, which can cleave A1AT. We hypothesized that placentally expressed HTRA1 regulates the formation of NIPs and that NET competency changed in PMNs isolated fro

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Bowden, Marissa A., Ann E. Drummond, Peter J. Fuller, Lois A. Salamonsen, Jock K. Findlay, and Guiying Nie. "High-temperature requirement factor A3 (Htra3): A novel serine protease and its potential role in ovarian function and ovarian cancers." Molecular and Cellular Endocrinology 327, no. 1-2 (2010): 13–18. http://dx.doi.org/10.1016/j.mce.2010.06.001.

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Li, Dapeng, Jiawei Yue, Lu Jiang, Yonghui Huang, Jifu Sun, and Yan Wu. "Correlation Between Expression of High Temperature Requirement Serine Protease A1 (HtrA1) in Nucleus Pulposus and T2 Value of Magnetic Resonance Imaging." Medical Science Monitor 23 (April 22, 2017): 1940–46. http://dx.doi.org/10.12659/msm.904018.

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Hur, Kang, Kim, et al. "Serine Protease HtrA2/Omi Deficiency Impairs Mitochondrial Homeostasis and Promotes Hepatic Fibrogenesis via Activation of Hepatic Stellate Cells." Cells 8, no. 10 (2019): 1119. http://dx.doi.org/10.3390/cells8101119.

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The loss of mitochondrial function impairs intracellular energy production and potentially results in chronic liver disease. Increasing evidence suggests that mitochondrial dysfunction in hepatocytes contributes to the activation of hepatic stellate cells (HSCs), thereby resulting in hepatic fibrogenesis. High-temperature requirement protein A2 (HtrA2/Omi), a mitochondrial serine protease with various functions, is responsible for quality control in mitochondrial homeostasis. However, little information is available regarding its role in mitochondrial damage during the development of liver fib

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Tossetta, Giovanni, Sonia Fantone, Rosaria Gesuita, et al. "HtrA1 in Gestational Diabetes Mellitus: A Possible Biomarker?" Diagnostics 12, no. 11 (2022): 2705. http://dx.doi.org/10.3390/diagnostics12112705.

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Background: The high-temperature requirement A 1 (HtrA1) is a multidomain secretory protein with serine-protease activity, expressed in many tissues, including placenta, where its expression is higher in the first trimester, suggesting an association of this serine protease in early phases of human placenta development. In this study, we evaluated maternal serum HtrA1 levels in the first and third trimester of gestation. In particular, we evaluated a possible role of HtrA1 as an early marker of gestational diabetes mellitus (GDM) in the first trimester of gestation. Methods: We evaluated HtrA1

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Zheng, Jing, Xianhua Huang, Xian-e. Peng, and Yunli Wu. "Abstract 3790: HtrA3 promotes malignant progression of colorectal cancer via PI3K-AKT-FOXO1 signaling pathway." Cancer Research 84, no. 6_Supplement (2024): 3790. http://dx.doi.org/10.1158/1538-7445.am2024-3790.

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Abstract High-temperature requirement protease A3 (HtrA3) is known to contribute to the progression of various carcinomas through tissue-specific actions, yet its precise role in colorectal cancer (CRC) remains unclear. Our study revealed that HtrA3 is significantly upregulated in CRC at both mRNA and protein levels. TCGA database analysis showed that higher HtrA3 expression in colon adenocarcinoma is linked to poorer patient survival. Moreover, increased HtrA3 expression in HCT116 cells boosted their proliferation, migration, and invasion, while decreasing HtrA3 in SW480 cells had the reverse

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Williams, Brandi L., Nathan A. Seager, Jamie D. Gardiner, et al. "Chromosome 10q26–driven age-related macular degeneration is associated with reduced levels of HTRA1 in human retinal pigment epithelium." Proceedings of the National Academy of Sciences 118, no. 30 (2021): e2103617118. http://dx.doi.org/10.1073/pnas.2103617118.

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Genome-wide association studies have identified the chromosome 10q26 (Chr10) locus, which contains the age-related maculopathy susceptibility 2 (ARMS2) and high temperature requirement A serine peptidase 1 (HTRA1) genes, as the strongest genetic risk factor for age-related macular degeneration (AMD) [L.G. Fritsche et al., Annu. Rev. Genomics Hum. Genet. 15, 151–171, (2014)]. To date, it has been difficult to assign causality to any specific single nucleotide polymorphism (SNP), haplotype, or gene within this region because of high linkage disequilibrium among the disease-associated variants [J

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Morin, Gilles, Maria Nouri, Oliver Brandau, et al. "HTRA2 Defect: A Recognizable Inborn Error of Metabolism with 3-Methylglutaconic Aciduria as Discriminating Feature Characterized by Neonatal Movement Disorder and Epilepsy—Report of 11 Patients." Neuropediatrics 49, no. 06 (2018): 373–78. http://dx.doi.org/10.1055/s-0038-1667345.

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AbstractNeonatal-onset movement disorders, especially in combination with seizures, are rare and often related to mitochondrial disorders. 3-methylglutaconic aciduria (3-MGA-uria) is a marker for mitochondrial dysfunction. In particular, consistently elevated urinary excretion of 3-methylglutaconic acid is the hallmark of a small but growing group of inborn errors of metabolism (IEM) due to defective phospholipid remodeling or mitochondrial membrane-associated disorders (mutations in TAZ, SERAC1, OPA3, CLPB, DNAJC19, TMEM70, TIMM50). Exome/genome sequencing is a powerful tool for the diagnosis

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Hortmann, Marcus, Samuel Robinson, Moritz Mohr, et al. "The mitochondria-targeting peptide elamipretide diminishes circulating HtrA2 in ST-segment elevation myocardial infarction." European Heart Journal: Acute Cardiovascular Care 8, no. 8 (2017): 695–702. http://dx.doi.org/10.1177/2048872617710789.

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Background: The extent of myocardial damage in patients with ST-segment elevation myocardial infarction (STEMI) depends on both the time to reperfusion as well as injury induced by ischaemia–reperfusion resulting in a cascade of cellular and humoral reactions. As a consequence of ischaemia–reperfusion in the heart, the high-temperature requirement serine peptidase 2 (HtrA2) is translocated from the mitochondria to the cytosol, whereupon it induces protease activity-dependent apoptosis mediated via caspases. Myocardial damage induced by reperfusion cannot be monitored due to a current lack in s

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