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Journal articles on the topic 'Hsp31'

Author: Grafiati
Published: 6 September 2023

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1

Rasouly, Aviram, Yotam Shenhar, and Eliora Z. Ron. "Thermoregulation of Escherichia coli hchA Transcript Stability." Journal of Bacteriology 189, no. 15 (May 25, 2007): 5779–81. http://dx.doi.org/10.1128/jb.00453-07.

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ABSTRACT The conserved chaperone Hsp31 of Escherichia coli is transcribed at low temperatures by σS and repressed by H-NS, whereas at high temperature, transcription is by σ70 independently of both σS and H-NS. Here we present evidence for an additional, novel, temperature-dependent control of Hsp31 expression by increased transcript stability.
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Mujacic, Mirna, and Fran�ois Baneyx. "Chaperone Hsp31 Contributes to Acid Resistance in Stationary-Phase Escherichia coli." Applied and Environmental Microbiology 73, no. 3 (December 8, 2006): 1014–18. http://dx.doi.org/10.1128/aem.02429-06.

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ABSTRACT Hsp31, the product of the σS- and σD-dependent hchA gene, is a heat-inducible chaperone implicated in the management of protein misfolding at high temperatures. We show here that Hsp31 plays an important role in the acid resistance of starved Escherichia coli but that it has little influence on oxidative-stress survival.
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3

Subedi, Krishna P., Dongwook Choi, Insook Kim, Bumchan Min, and Chankyu Park. "Hsp31 of Escherichia coli K-12 is glyoxalase III." Molecular Microbiology 81, no. 4 (July 6, 2011): 926–36. http://dx.doi.org/10.1111/j.1365-2958.2011.07736.x.

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4

Hansberg, Wilhelm, Teresa Nava-Ramírez, Pablo Rangel-Silva, Adelaida Díaz-Vilchis, and Aydé Mendoza-Oliva. "Large-Size Subunit Catalases Are Chimeric Proteins: A H2O2 Selecting Domain with Catalase Activity Fused to a Hsp31-Derived Domain Conferring Protein Stability and Chaperone Activity." Antioxidants 11, no. 5 (May 17, 2022): 979. http://dx.doi.org/10.3390/antiox11050979.

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Bacterial and fungal large-size subunit catalases (LSCs) are like small-size subunit catalases (SSCs) but have an additional C-terminal domain (CT). The catalytic domain is conserved at both primary sequence and structural levels and its amino acid composition is optimized to select H2O2 over water. The CT is structurally conserved, has an amino acid composition similar to very stable proteins, confers high stability to LSCs, and has independent molecular chaperone activity. While heat and denaturing agents increased Neurospora crassa catalase-1 (CAT-1) activity, a CAT-1 version lacking the CT (C63) was no longer activated by these agents. The addition of catalase-3 (CAT-3) CT to the CAT-1 or CAT-3 catalase domains prevented their heat denaturation in vitro. Protein structural alignments indicated CT similarity with members of the DJ-1/PfpI superfamily and the CT dimers present in LSCs constitute a new type of symmetric dimer within this superfamily. However, only the bacterial Hsp31 proteins show sequence similarity to the bacterial and fungal catalase mobile coil (MC) and are phylogenetically related to MC_CT sequences. LSCs might have originated by fusion of SSC and Hsp31 encoding genes during early bacterial diversification, conferring at the same time great stability and molecular chaperone activity to the novel catalases.
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Zhang, Kai, Kuikui Jiang, Ruoxi Hong, Fei Xu, Wen Xia, Ge Qin, Kaping Lee, et al. "Identification and characterization of critical genes associated with tamoxifen resistance in breast cancer." PeerJ 8 (December 4, 2020): e10468. http://dx.doi.org/10.7717/peerj.10468.

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Background Tamoxifen resistance in breast cancer is an unsolved problem in clinical practice. The aim of this study was to determine the potential mechanisms of tamoxifen resistance through bioinformatics analysis. Methods Gene expression profiles of tamoxifen-resistant MCF-7/TR and MCF-7 cells were acquired from the Gene Expression Omnibus dataset GSE26459, and differentially expressed genes (DEGs) were detected with R software. We conducted Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes pathway enrichment analyses using Database for Annotation, Visualization and Integrated Discovery. A protein–protein interaction (PPI) network was generated, and we analyzed hub genes in the network with the Search Tool for the Retrieval of Interacting Genes database. Finally, we used siRNAs to silence the target genes and conducted the MTS assay. Results We identified 865 DEGs, 399 of which were upregulated. GO analysis indicated that most genes are related to telomere organization, extracellular exosomes, and binding-related items for protein heterodimerization. PPI network construction revealed that the top 10 hub genes—ACLY, HSPD1, PFAS, GART, TXN, HSPH1, HSPE1, IRAS, TRAP1, and ATIC—might be associated with tamoxifen resistance. Consistently, RT-qPCR analysis indicated that the expression of these 10 genes was increased in MCF-7/TR cells comparing with MCF-7 cells. Four hub genes (TXN, HSPD1, HSPH1 and ATIC) were related to overall survival in patients who accepted tamoxifen. In addition, knockdown of HSPH1 by siRNA may lead to reduced growth of MCF-7/TR cell with a trend close to significance (P = 0.07), indicating that upregulation of HSPH1 may play a role in tamoxifen resistance. Conclusion This study revealed a number of critical hub genes that might serve as therapeutic targets in breast cancer resistant to tamoxifen and provided potential directions for uncovering the mechanisms of tamoxifen resistance.
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Kim, Jihong, Dongwook Choi, Chankyu Park, and Kyoung-Seok Ryu. "Backbone resonance assignments of the Escherichia coli 62 kDa protein, Hsp31." Biomolecular NMR Assignments 11, no. 2 (March 3, 2017): 159–63. http://dx.doi.org/10.1007/s12104-017-9739-6.

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Kim, Jihong, Dongwook Choi, So-Young Cha, Young-Mee Oh, Eunha Hwang, Chankyu Park, and Kyoung-Seok Ryu. "Zinc-mediated Reversible Multimerization of Hsp31 Enhances the Activity of Holding Chaperone." Journal of Molecular Biology 430, no. 12 (June 2018): 1760–72. http://dx.doi.org/10.1016/j.jmb.2018.04.029.

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8

Choi, Dongwook, Kyoung-Seok Ryu, and Chankyu Park. "Structural alteration of Escherichia coli Hsp31 by thermal unfolding increases chaperone activity." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834, no. 2 (February 2013): 621–28. http://dx.doi.org/10.1016/j.bbapap.2012.11.006.

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9

Hasim, Sahar, Nur Ahmad Hussin, Fadhel Alomar, Keshore R. Bidasee, Kenneth W. Nickerson, and Mark A. Wilson. "A Glutathione-independent Glyoxalase of the DJ-1 Superfamily Plays an Important Role in Managing Metabolically Generated Methylglyoxal in Candida albicans." Journal of Biological Chemistry 289, no. 3 (December 3, 2013): 1662–74. http://dx.doi.org/10.1074/jbc.m113.505784.

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Methylglyoxal is a cytotoxic reactive carbonyl compound produced by central metabolism. Dedicated glyoxalases convert methylglyoxal to d-lactate using multiple catalytic strategies. In this study, the DJ-1 superfamily member ORF 19.251/GLX3 from Candida albicans is shown to possess glyoxalase activity, making this the first demonstrated glutathione-independent glyoxalase in fungi. The crystal structure of Glx3p indicates that the protein is a monomer containing the catalytic triad Cys136-His137-Glu168. Purified Glx3p has an in vitro methylglyoxalase activity (Km = 5.5 mm and kcat = 7.8 s−1) that is significantly greater than that of more distantly related members of the DJ-1 superfamily. A close Glx3p homolog from Saccharomyces cerevisiae (YDR533C/Hsp31) also has glyoxalase activity, suggesting that fungal members of the Hsp31 clade of the DJ-1 superfamily are all probable glutathione-independent glyoxalases. A homozygous glx3 null mutant in C. albicans strain SC5314 displays greater sensitivity to millimolar levels of exogenous methylglyoxal, elevated levels of intracellular methylglyoxal, and carbon source-dependent growth defects, especially when grown on glycerol. These phenotypic defects are complemented by restoration of the wild-type GLX3 locus. The growth defect of Glx3-deficient cells in glycerol is also partially complemented by added inorganic phosphate, which is not observed for wild-type or glucose-grown cells. Therefore, C. albicans Glx3 and its fungal homologs are physiologically relevant glutathione-independent glyoxalases that are not redundant with the previously characterized glutathione-dependent GLO1/GLO2 system. In addition to its role in detoxifying glyoxals, Glx3 and its close homologs may have other important roles in stress response.
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Nava-Ramírez, Teresa, Sammy Gutiérrez-Terrazas, and Wilhelm Hansberg. "The Molecular Chaperone Mechanism of the C-Terminal Domain of Large-Size Subunit Catalases." Antioxidants 12, no. 4 (March 30, 2023): 839. http://dx.doi.org/10.3390/antiox12040839.

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Large-size subunit catalases (LSCs) have an additional C-terminal domain (CT) that is structurally similar to Hsp31 and DJ-1 proteins, which have molecular chaperone activity. The CT of LSCs derives from a bacterial Hsp31 protein. There are two CT dimers with inverted symmetry in LSCs, one dimer in each pole of the homotetrameric structure. We previously demonstrated the molecular chaperone activity of the CT of LSCs. Like other chaperones, LSCs are abundant proteins that are induced under stress conditions and during cell differentiation in bacteria and fungi. Here, we analyze the mechanism of the CT of LSCs as an unfolding enzyme. The dimeric form of catalase-3 (CAT-3) CT (TDC3) of Neurospora crassa presented the highest activity as compared to its monomeric form. A variant of the CAT-3 CT lacking the last 17 amino acid residues (TDC3Δ17aa), a loop containing hydrophobic and charged amino acid residues only, lost most of its unfolding activity. Substituting charged for hydrophobic residues or vice versa in this C-terminal loop diminished the molecular chaperone activity in all the mutant variants analyzed, indicating that these amino acid residues play a relevant role in its unfolding activity. These data suggest that the general unfolding mechanism of CAT-3 CT involves a dimer with an inverted symmetry, and hydrophobic and charged amino acid residues. Each tetramer has four sites of interaction with partially unfolded or misfolded proteins. LSCs preserve their catalase activity under different stress conditions and, at the same time, function as unfolding enzymes.
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11

Mujacic, Mirna, and Francois Baneyx. "Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31." Molecular Microbiology 60, no. 6 (June 2006): 1576–89. http://dx.doi.org/10.1111/j.1365-2958.2006.05207.x.

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12

Tsai, Chai-jui, Kiran Aslam, Holli M. Drendel, Josephat M. Asiago, Kourtney M. Goode, Lake N. Paul, Jean-Christophe Rochet, and Tony R. Hazbun. "Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process." Journal of Biological Chemistry 290, no. 41 (August 25, 2015): 24816–34. http://dx.doi.org/10.1074/jbc.m115.678367.

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Aslam, Kiran, Chai-jui Tsai, and Tony R. Hazbun. "The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation." Prion 10, no. 6 (October 3, 2016): 444–65. http://dx.doi.org/10.1080/19336896.2016.1234574.

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Mihoub, Mouadh, Jad Abdallah, Brigitte Gontero, Julien Dairou, and Gilbert Richarme. "The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal." Biochemical and Biophysical Research Communications 463, no. 4 (August 2015): 1305–10. http://dx.doi.org/10.1016/j.bbrc.2015.06.111.

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Kim, Jihong, Dongwook Choi, Chankyu Park, and Kyoung-Seok Ryu. "Per-deuteration and NMR experiments for the backbone assignment of 62 kDa protein, Hsp31." Journal of the Korean Magnetic Resonance Society 19, no. 3 (December 20, 2015): 112–18. http://dx.doi.org/10.6564/jkmrs.2015.19.3.112.

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Sastry, M. S. R., Weibin Zhou, and François Baneyx. "Integrity of N- and C-termini is important for E. coli Hsp31 chaperone activity." Protein Science 18, no. 7 (May 13, 2009): 1439–47. http://dx.doi.org/10.1002/pro.158.

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Aslam, Kiran, and Tony R. Hazbun. "Hsp31, a member of the DJ-1 superfamily, is a multitasking stress responder with chaperone activity." Prion 10, no. 2 (March 3, 2016): 103–11. http://dx.doi.org/10.1080/19336896.2016.1141858.

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18

Graille, Marc, Sophie Quevillon-Cheruel, Nicolas Leulliot, Cong-Zhao Zhou, Ines Li de La Sierra Gallay, Lilian Jacquamet, Jean-Luc Ferrer, et al. "Crystal Structure of the YDR533c S. cerevisiae Protein, a Class II Member of the Hsp31 Family." Structure 12, no. 5 (May 2004): 839–47. http://dx.doi.org/10.1016/j.str.2004.02.030.

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Lee, Sun-Joo, So Jung Kim, In-Kwon Kim, Junsang Ko, Chang-Sook Jeong, Gyung-Hwa Kim, Chankyu Park, et al. "Crystal Structures of Human DJ-1 and Escherichia coli Hsp31, Which Share an Evolutionarily Conserved Domain." Journal of Biological Chemistry 278, no. 45 (August 25, 2003): 44552–59. http://dx.doi.org/10.1074/jbc.m304517200.

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de Miguel, N., P. C. Echeverria, and S. O. Angel. "Differential Subcellular Localization of Members of the Toxoplasma gondii Small Heat Shock Protein Family." Eukaryotic Cell 4, no. 12 (December 2005): 1990–97. http://dx.doi.org/10.1128/ec.4.12.1990-1997.2005.

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ABSTRACT The results of this study describe the identification and characterization of the Toxoplasma gondii α-crystallin/small heat shock protein (sHsp) family. By database (www.toxodb.org ) search, five parasite sHsps (Hsp20, Hsp21, Hsp28, Hsp29, and the previously characterized Hsp30/Bag1) were identified. As expected, they share the homologous α-crystallin domain, which is the key characteristic of sHsps. However, the N-terminal segment of each protein contains unique characteristics in size and sequence. Most T. gondii sHsps are constitutively expressed in tachyzoites and fully differentiated bradyzoites, with the exception of Hsp30/Bag1. Interestingly, by subcellular localization we observed that T. gondii sHsps are located in different compartments. Hsp20 is located at the apical end of the cell, Hsp28 is located inside the mitochondrion, Hsp29 showed a membrane-associated labeling, and Hsp21 appeared throughout the cytosol of the parasites. These particular differences in the immunostaining patterns suggest that their targets and functions might be different.
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Das, Samir, Sanghati Roy Chowdhury, Sanjay Dey, and Udayaditya Sen. "Structural and biochemical studies on Vibrio cholerae Hsp31 reveals a novel dimeric form and Glutathione-independent Glyoxalase activity." PLOS ONE 12, no. 2 (February 24, 2017): e0172629. http://dx.doi.org/10.1371/journal.pone.0172629.

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Sastry, M. S. R., Konstantin Korotkov, Yan Brodsky, and François Baneyx. "Hsp31, theEscherichia coli yedUGene Product, Is a Molecular Chaperone Whose Activity Is Inhibited by ATP at High Temperatures." Journal of Biological Chemistry 277, no. 48 (September 15, 2002): 46026–34. http://dx.doi.org/10.1074/jbc.m205800200.

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Padilla, C. A., J. A. Bárcena, M. J. López-Grueso, and R. Requejo-Aguilar. "The regulation of TORC1 pathway by the yeast chaperones Hsp31 is mediated by SFP1 and affects proteasomal activity." Biochimica et Biophysica Acta (BBA) - General Subjects 1863, no. 3 (March 2019): 534–46. http://dx.doi.org/10.1016/j.bbagen.2018.12.011.

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Graf, Paul C. F., Maria Martinez-Yamout, Stephen VanHaerents, Hauke Lilie, H. Jane Dyson, and Ursula Jakob. "Activation of the Redox-regulated Chaperone Hsp33 by Domain Unfolding." Journal of Biological Chemistry 279, no. 19 (March 15, 2004): 20529–38. http://dx.doi.org/10.1074/jbc.m401764200.

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The molecular chaperone Hsp33 inEscherichia coliresponds to oxidative stress conditions with the rapid activation of its chaperone function. On its activation pathway, Hsp33 progresses through three major conformations, starting as a reduced, zinc-bound inactive monomer, proceeding through an oxidized zinc-free monomer, and ending as a fully active oxidized dimer. While it is known that Hsp33 senses oxidative stress through its C-terminal four-cysteine zinc center, the nature of the conformational changes in Hsp33 that must take place to accommodate this activation process is largely unknown. To investigate these conformational rearrangements, we constructed constitutively monomeric Hsp33 variants as well as fragments consisting of the redox regulatory C-terminal domain of Hsp33. These proteins were studied by a combination of biochemical and NMR spectroscopic techniques. We found that in the reduced, monomeric conformation, zinc binding stabilizes the C terminus of Hsp33 in a highly compact, α-helical structure. This appears to conceal both the substrate-binding site as well as the dimerization interface. Zinc release without formation of the two native disulfide bonds causes the partial unfolding of the C terminus of Hsp33. This is sufficient to unmask the substrate-binding site, but not the dimerization interface, rendering reduced zinc-free Hsp33 partially active yet monomeric. Critical for the dimerization is disulfide bond formation, which causes the further unfolding of the C terminus of Hsp3 and allows the association of two oxidized Hsp33 monomers. This then leads to the formation of active Hsp33 dimers, which are capable of protecting cells against the severe consequences of oxidative heat stress.
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Quigley, P. M., K. Korotkov, F. Baneyx, and W. G. J. Hol. "The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad." Proceedings of the National Academy of Sciences 100, no. 6 (March 5, 2003): 3137–42. http://dx.doi.org/10.1073/pnas.0530312100.

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Amm, Ingo, Derrick Norell, and Dieter H. Wolf. "Absence of the Yeast Hsp31 Chaperones of the DJ-1 Superfamily Perturbs Cytoplasmic Protein Quality Control in Late Growth Phase." PLOS ONE 10, no. 10 (October 14, 2015): e0140363. http://dx.doi.org/10.1371/journal.pone.0140363.

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Carlin, Aaron F., Sinem Beyhan, Jesús F. Peña, Jason E. Stajich, Suganya Viriyakosol, Joshua Fierer, and Theo N. Kirkland. "Transcriptional Analysis of Coccidioides immitis Mycelia and Spherules by RNA Sequencing." Journal of Fungi 7, no. 5 (May 7, 2021): 366. http://dx.doi.org/10.3390/jof7050366.

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Coccidioides immitis and C. posadasii are dimorphic fungi that transform from mycelia with internal arthroconidia in the soil to a tissue form known as a spherule in mammals. This process can be recapitulated in vitro by increasing the temperature, CO2 and changing other culture conditions. In this study, we have analyzed changes in gene expression in mycelia and young and mature spherules. Genes that were highly upregulated in young spherules include a spherule surface protein and iron and copper membrane transporters. Genes that are unique to Coccidioides spp. are also overrepresented in this group, suggesting that they may be important for spherule differentiation. Enriched GO terms in young spherule upregulated genes include oxidation-reduction, response to stress and membrane proteins. Downregulated genes are enriched for transcription factors, especially helix–loop–helix and C2H2 type zinc finger domain-containing proteins, which is consistent with the dramatic change in transcriptional profile. Almost all genes that are upregulated in young spherules remain upregulated in mature spherules, but a small number of genes are differentially expressed in those two stages of spherule development. Mature spherules express more Hsp31 and amylase and less tyrosinase than young spherules. Some expression of transposons was detected and most of the differentially expressed transposons were upregulated in spherules.
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Hansberg, Wilhelm. "Monofunctional Heme-Catalases." Antioxidants 11, no. 11 (November 2, 2022): 2173. http://dx.doi.org/10.3390/antiox11112173.

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The review focuses on four issues that are critical for the understanding of monofunctional catalases. How hydrogen peroxide (H2O2) reaches the active site and outcompetes water molecules to be able to function at a very high rate is one of the issues examined. Part of the answer is a gate valve system that is instrumental to drive out solvent molecules from the final section of the main channel. A second issue relates to how the enzyme deals with an unproductive reactive compound I (Cpd I) intermediate. Peroxidatic two and one electron donors and the transfer of electrons to the active site from NADPH and other compounds are reviewed. The new ascribed catalase reactions are revised, indicating possible measurement pitfalls. A third issue concerns the heme b to heme d oxidation, why this reaction occurs only in some large-size subunit catalases (LSCs), and the possible role of singlet oxygen in this and other modifications. The formation of a covalent bond between the proximal tyrosine with the vicinal residue is analyzed. The last issue refers to the origin and function of the additional C-terminal domain (TD) of LSCs. The TD has a molecular chaperone activity that is traced to a gene fusion between a Hsp31-type chaperone and a small-size subunit catalase (SSC).
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Boudreault, Julien, Ni Wang, Gang Yan, Meiou Dai, Sophie Poulet, Girija Daliah, and Jean-Jacques Lebrun. "Abstract 3938: In vivo genome-wide CRISPR screen in pancreatic ductal adenocarcinoma defines HSPE1 as a potential oncogene by acting through G2/M cell cycle arrest." Cancer Research 83, no. 7_Supplement (April 4, 2023): 3938. http://dx.doi.org/10.1158/1538-7445.am2023-3938.

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Abstract Superior knowledge of cancer biology has enabled unprecedented innovations in therapies targeting mutated driver genes. Despite the attempt of targeting cancer-inducing genes such as KRAS, the life expectancy of patients diagnosed with pancreatic ductal adenocarcinoma (PDAC) has poorly improved. We performed an unbiased genome wide in-vivo loss-of-function CRISPR screen to discover novel oncogenes and identified heat-shock protein HSPE1, whose function is still unknown in PDAC. By decreasing HSPE1 expression with shRNA and CRISPR technology, we detected a slowdown in cell growth of PDAC cancer cells. HSPE1 knock-out cells injected in mice displayed a drastic reduction in tumor volume. We exploited this vulnerability by disrupting HSPE1 function by using KHS101, a validated HSPD1-HSPE1 complex inhibitor. Several PDAC cell lines cultured in vitro were sensitive upon KHS101 treatment and in vivo administration of KHS101 reduced tumorigenesis. Compiling the negative fitness scores from DepMap database revealed a co-dependency between HSPE1 and PLK1, a protein involved in regulating G2/M checkpoint. Indeed, we detected a protein-level decrease of PLK1 in our experimental model of PDAC cells having either a drug-induced HSPE1 deficiency by KHS101 exposure or a HSPE1 gene-expression reduction by shRNA. We found that the cell cycle was disrupted through G2/M arrest in PDAC cells treated with KHS101. Our findings highlight a new role underlying PDAC tumorigenesis for HSPE1 and could unlock a new area of research towards precision medicine. Citation Format: Julien Boudreault, Ni Wang, Gang Yan, Meiou Dai, Sophie Poulet, Girija Daliah, Jean-Jacques Lebrun. In vivo genome-wide CRISPR screen in pancreatic ductal adenocarcinoma defines HSPE1 as a potential oncogene by acting through G2/M cell cycle arrest. [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2023; Part 1 (Regular and Invited Abstracts); 2023 Apr 14-19; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2023;83(7_Suppl):Abstract nr 3938.
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Galai, Geut, Hila Ben-David, Liron Levin, Martin F. Orth, Thomas G. P. Grünewald, Shai Pilosof, Shimon Bershtein, and Barak Rotblat. "Pan-Cancer Analysis of Mitochondria Chaperone-Client Co-Expression Reveals Chaperone Functional Partitioning." Cancers 12, no. 4 (March 30, 2020): 825. http://dx.doi.org/10.3390/cancers12040825.

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Metabolic reprogramming is a hallmark of cancer. Such reprogramming entails the up-regulation of the expression of specific mitochondrial proteins, thus increasing the burden on the mitochondrial protein quality control. However, very little is known about the specificity of interactions between mitochondrial chaperones and their clients, or to what extent the mitochondrial chaperone–client co-expression is coordinated. We hypothesized that a physical interaction between a chaperone and its client in mitochondria ought to be manifested in the co-expression pattern of both transcripts. Using The Cancer Genome Atlas (TCGA) gene expression data from 13 tumor entities, we constructed the mitochondrial chaperone-client co-expression network. We determined that the network is comprised of three distinct modules, each populated with unique chaperone-clients co-expression pairs belonging to distinct functional groups. Surprisingly, chaperonins HSPD1 and HSPE1, which are known to comprise a functional complex, each occupied a different module: HSPD1 co-expressed with tricarboxylic acid cycle cycle enzymes, while HSPE1 co-expressed with proteins involved in oxidative phosphorylation. Importantly, we found that the genes in each module were enriched for discrete transcription factor binding sites, suggesting the mechanism for the coordinated co-expression. We propose that our mitochondrial chaperone–client interactome can facilitate the identification of chaperones supporting specific mitochondrial pathways and bring forth a fundamental principle in metabolic adaptation.
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Scieglinska, Dorota, Zdzisław Krawczyk, Damian Robert Sojka, and Agnieszka Gogler-Pigłowska. "Heat shock proteins in the physiology and pathophysiology of epidermal keratinocytes." Cell Stress and Chaperones 24, no. 6 (November 2019): 1027–44. http://dx.doi.org/10.1007/s12192-019-01044-5.

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AbstractHeat shock proteins (HSPs), a large group of highly evolutionary conserved proteins, are considered to be main elements of the cellular proteoprotection system. HSPs are encoded by genes activated during the exposure of cells to proteotoxic factors, as well as by genes that are expressed constitutively under physiological conditions. HSPs, having properties of molecular chaperones, are involved in controlling/modulation of multiple cellular and physiological processes. In the presented review, we summarize the current knowledge on HSPs in the biology of epidermis, the outer skin layer composed of stratified squamous epithelium. This tissue has a vital barrier function preventing from dehydratation due to passive diffusion of water out of the skin, and protecting from infection and other environmental insults. We focused on HSPB1 (HSP27), HSPA1 (HSP70), HSPA2, and HSPC (HSP90), because only these HSPs have been studied in the context of physiology and pathophysiology of the epidermis. The analysis of literature data shows that HSPB1 plays a role in the regulation of final steps of keratinization; HSPA1 is involved in the cytoprotection, HSPA2 contributes to the early steps of keratinocyte differentiation, while HSPC is essential in the re-epithelialization process. Since HSPs have diverse functions in various types of somatic tissues, in spite of multiple investigations, open questions still remain about detailed roles of a particular HSP isoform in the biology of epidermal keratinocytes.
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Bankapalli, Kondalarao, SreeDivya Saladi, Sahezeel S. Awadia, Arvind Vittal Goswami, Madhuja Samaddar, and Patrick D'Silva. "Robust Glyoxalase activity of Hsp31, a ThiJ/DJ-1/PfpI Family Member Protein, Is Critical for Oxidative Stress Resistance inSaccharomyces cerevisiae." Journal of Biological Chemistry 290, no. 44 (September 14, 2015): 26491–507. http://dx.doi.org/10.1074/jbc.m115.673624.

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Seibert, Jacob T., Malavika K. Adur, Ronald B. Schultz, Porsha Q. Thomas, Zoe E. Kiefer, Aileen F. Keating, Lance H. Baumgard, and Jason W. Ross. "Differentiating between the effects of heat stress and lipopolysaccharide on the porcine ovarian heat shock protein response1." Journal of Animal Science 97, no. 12 (November 29, 2019): 4965–73. http://dx.doi.org/10.1093/jas/skz343.

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Abstract Heat stress (HS) negatively affects both human and farm-animal health and undermines efficiency in a variety of economically important agricultural variables, including reproduction. HS impairs the intestinal barrier, allowing for translocation of the resident microflora and endotoxins, such as lipopolysaccharide (LPS), from the gastrointestinal lumen into systemic circulation. While much is known about the cellular function of heat shock proteins (HSPs) in most tissues, the in vivo ovarian HSP response to stressful stimuli remains ill-defined. The purpose of this study was to compare the effects of HS or LPS on ovarian HSP expression in pigs. We hypothesized that ovarian HSPs are responsive to both HS and LPS. Altrenogest (15 mg/d) was administered per os for estrus synchronization (14 d) prior to treatment and three animal paradigms were used: (i) gilts were exposed to cyclical HS (31 ± 1.4 °C) or thermoneutral (TN; 20 ± 0.5 °C) conditions immediately following altrenogest withdrawal for 5 d during follicular development; (ii) gilts were subjected to repeated (4×/d) saline (CON) or LPS (0.1 μg/kg BW) i.v. infusion immediately following altrenogest withdrawal for 5 d; and (iii) gilts were subjected to TN (20 ± 1 °C) or cyclical HS (31 to 35 °C) conditions 2 d post estrus (dpe) until 12 dpe during the luteal phase. While no differences were detected for transcript abundances of the assessed ovarian HSP, the protein abundance of specific HSP was influenced by stressors during the follicular and luteal phases. HS during the follicular phase tended (P < 0.1) to increase ovarian protein abundance of HSP90AA1 and HSPA1A, and increased (P ≤ 0.05) HSF1, HSPD1, and HSPB1 compared with TN controls, while HS decreased HSP90AB1 (P = 0.01). Exposure to LPS increased (P < 0.05) HSP90AA1 and HSPA1A and tended (P < 0.1) to increase HSF1 and HSPB1 compared with CON gilts, while HSP90AB1 and HSPD1 were not affected by LPS. HS during the luteal phase increased (P < 0.05) abundance of HSPB1 in corpora lutea (CL), decreased (P < 0.05) CL HSP90AB1, but did not impact HSF1, HSPD1, HSP90AA1, or HSPA1A abundance. Thus, these data support that HS and LPS similarly regulate expression of specific ovarian HSP, which suggest that HS effects on the ovary are in part mediated by LPS.
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Sastry, M. S. R., P. M. Quigley, W. G. J. Hol, and F. Baneyx. "The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures." Proceedings of the National Academy of Sciences 101, no. 23 (June 1, 2004): 8587–92. http://dx.doi.org/10.1073/pnas.0403033101.

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Richarme, Gilbert, Jad Abdallah, Nicolas Mathas, Valérie Gautier, and Julien Dairou. "Further characterization of the Maillard deglycase DJ-1 and its prokaryotic homologs, deglycase 1/Hsp31, deglycase 2/YhbO, and deglycase 3/YajL." Biochemical and Biophysical Research Communications 503, no. 2 (September 2018): 703–9. http://dx.doi.org/10.1016/j.bbrc.2018.06.064.

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36

Andrade, Warne Pedro, Bryan Ôrtero Perez Gonçalves, Luciana Maria Silva, and Agnaldo Lopes Dasilva Filho. "Upregulation of HSPB1 heat shock gene and ERCC1 gene on serous ovarian cancer cell line in HIPEC in vitro model." Journal of Clinical Oncology 39, no. 15_suppl (May 20, 2021): e17559-e17559. http://dx.doi.org/10.1200/jco.2021.39.15_suppl.e17559.

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e17559 Background: Epithelial ovarian cancer (EOC) is the most lethal gynecological malignancy, with the presence of chemoresistance contributing to the poor prognosis. Approximately 80% of cases are diagnosed in stage III C and are treated with cytoreduction surgery followed by adjuvant chemotherapy. However, 70 percent of these patients have pelvic and peritoneal recurrences. Heat Shock Proteins are produced in response to pathophysiological stress and take part in several stages of carcinogenesis, acting primarily as anti-apoptotic agents. They are also implicated in resistance to chemotherapy in several types of tumors. In an attempt to improve oncological results, new therapeutic approaches such as intraperitoneal chemotherapy and HIPEC have been proposed in recent studies with gains in overall survival (OS). However, some questions have not yet been answered. Methods: in the study cultures of ovarian cancer cells were performed TOV-21G (clear cell carcinoma), SK-OV-3 (platinum-resistant serous carcinoma) and OV-90 (high-grade serous). Cell cytotoxicity (MTT) assay was performed. The ovarian cancer cells lines were treated with cisplatin in normothermia (37 degrees Celsius) and cisplatin in hyperthermia (41 degrees Celsius) and a control group treated with PBS saline solution at (37 degrees Celsius and 41 degrees Celsius) for 24 hours followed by new supplementation and a new 3-hours incubation. Clonogenic assay was performed. Then they were submitted to RNA extraction and reverse transcription. qRT-PCR was performed to compare the expression of TRAP1, HSPB1, HSPD1, HSPA1A, HSPA1L and ERCC1 in different treatments. Results: There was no statistical difference in relation to cytotoxicity between treatment with heated cisplatin compared to treatment with normothermia. It was not possible to evaluate the expression of the heat shock genes in the SK-OV3 lineage.The HSPB1, HSPD1, TRAP1 and ERCCC1 genes were positively regulated in OV-90 submitted to hyperthermia in relation to normothermia and there were no significant changes in expression in the TOV-21-G. Conclusions: In conclusion, we suggest that OV-90 Serous ovarian cancer cell line was more susceptibly at hyperthermia by cisplatin. The HSPA1A, HSPA1L, TRAP1 and HSPB1 heat shock genes and ERCC1 genes were upregulated in the heated cisplatin group and contribute to a poor prognosis related to resistance. The HSPB1 and ERCC1 genes had the greatest expression with 1000x higher.Thus, it is necessary to evaluate these genes in a clinical study of HIPEC.
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Zaitsev, M. S., T. N. Kiseleva, K. V. Lugovkina, N. V. Balatskaya, E. V. Jani, and K. E. Seliverstova. "Experimental assessment of the impact of high acoustic power ultrasound diagnostics on animal eyes." Russian Ophthalmological Journal 15, no. 3 (September 23, 2022): 92–98. http://dx.doi.org/10.21516/2072-0076-2022-15-3-92-98.

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Purpose: to study the impact of diagnostic ultrasound of high acoustic power on animal eye tissues in the experiment.Material and methods. 46 Chinchilla rabbits (92 eyes) were divided into the main group of 38 rabbits (76 eyes) and the control group of 8 rabbits (16 intact eyes). Animals of the main group were exposed for 30 minutes, through closed eyes, to high-intensity ultrasound (MI 0.9–1.0, TI 1.5–2.0, Ispta.3 50 mW/cm2) by colour Doppler imaging and pulsed Doppler. All animals of this group had corneal thickness measured by optical coherence tomography (OCT) before and immediately after exposure to ultrasound (20 rabbits) and also 2 weeks later (18 rabbits). During the same time span, the content of heat shock proteins HSP27 (HSPB1), HSP60 (HSPD1) and inflammatory mediators: monocytic chemotactic protein-1 (MCP-1), interleukin-6 (IL-6) and interleukin-8 (IL-8) in blood serum and vitreous was determined. Histopathological examinations of the enucleated eyes of rabbits with morphological and morphometric assessment of retinal tissues were performed on the 1st day and 2 weeks after exposure to ultrasound.Results. Immediately after ultrasound exposure and 2 weeks later OCT data reflected no structural changes in the cornea. Quantitative assessment of the levels of HSPD1, HSPB1, MCP-1, IL-6 and IL-8 in blood serum and vitreous did not reveal statistically significant changes after ultrasound exposure. A morphological study including an assessment of morphometric characteristics revealed the absence of apoptotic changes in the layers of the retina at different times after exposure to high-intensity ultrasound.Conclusions. We established no immediate or delayed bioeffects of high acoustic power diagnostic ultrasound exposure lasting up to 30 minutes on the biological media and ocular tissues of animals.
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Davis, R. E., and M. L. King. "The developmental expression of the heat-shock response in Xenopus laevis." Development 105, no. 2 (February 1, 1989): 213–22. http://dx.doi.org/10.1242/dev.105.2.213.

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We have investigated the Xenopus heat-shock response of somatic cells, oocytes and embryos. Xenopus defolliculated oocytes displayed a highly variable response to heat shock depending on the culture medium. Intact follicles, however, respond to heat stress by synthesizing an invariant pattern of hsps. Although a subset of the hsp70/68 complex is expressed constitutively in the absence of heat shock in oocytes and embryos (hsc70), actual induction of hsps in response to stress does not occur until the blastula stage when transcription of the zygotic genome is first activated. By gastrulation, the hsps of somatic cells, including members of the hsp30/26 complex, were expressed coordinately in response to heat shock. We further show that Xenopus hsps have different solubilities perhaps reflecting their different subcellular locations. The 26,000–30,000 Mr complex (hsp30/26) was present almost exclusively in a detergent-insoluble fraction, as was 25–50% of the hsp70/68 complex and greater than 50% of hsp56, suggesting that these hsps may be associated with the cytoskeleton during a heat shock. In contrast, the other Xenopus hsps (hsp86, hsp75 and hsp61) were totally solubilized in a low-salt buffer.
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Alabi, Mutiu A., Olugbenga O. Adebawo, Oluwole A. Daini, Stella B. Somiari, and Richard I. Somiari. "HSPD1, HSPB1 and VDAC1 are Over-expressed in Invasive Ductal Carcinoma of the Breast." International Journal of Cancer Research 12, no. 2 (March 15, 2016): 82–91. http://dx.doi.org/10.3923/ijcr.2016.82.91.

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40

Mujacic, Mirna, Martin W. Bader, and François Baneyx. "Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions." Molecular Microbiology 51, no. 3 (December 15, 2003): 849–59. http://dx.doi.org/10.1046/j.1365-2958.2003.03871.x.

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41

Rehman, Saif ur, Asif Nadeem, Maryam Javed, Faiz-ul Hassan, Xier Luo, Ruqayya Bint Khalid, and Qingyou Liu. "Genomic Identification, Evolution and Sequence Analysis of the Heat-Shock Protein Gene Family in Buffalo." Genes 11, no. 11 (November 23, 2020): 1388. http://dx.doi.org/10.3390/genes11111388.

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Heat-shock proteins (HSP) are conserved chaperones crucial for protein degradation, maturation, and refolding. These adenosine triphosphate dependent chaperones were classified based on their molecular mass that ranges between 10–100 kDA, including; HSP10, HSP40, HSP70, HSP90, HSPB1, HSPD, and HSPH1 family. HSPs are essential for cellular responses and imperative for protein homeostasis and survival under stress conditions. This study performed a computational analysis of the HSP protein family to better understand these proteins at the molecular level. Physiochemical properties, multiple sequence alignment, and phylogenetic analysis were performed for 64 HSP genes in the Bubalus bubalis genome. Four genes were identified as belonging to the HSP90 family, 10 to HSP70, 39 to HSP40, 8 to HSPB, one for each HSPD, HSPH1, and HSP10, respectively. The aliphatic index was higher for HSP90 and HSP70 as compared to the HSP40 family, indicating their greater thermostability. Grand Average of hydropathicity Index values indicated the hydrophilic nature of HSP90, HSP70, and HSP40. Multiple sequence alignment indicated the presence of highly conserved consensus sequences that are plausibly significant for the preservation of structural integrity of proteins. In addition, this study has expanded our current knowledge concerning the genetic diversity and phylogenetic relatedness of HSPs of buffalo with other mammalian species. The phylogenetic tree revealed that buffalo is more closely related to Capra hircus and distantly associated with Danio rerio. Our findings provide an understanding of HSPs in buffalo at the molecular level for the first time. This study highlights functionally important HSPs and indicates the need for further investigations to better understand the role and mechanism of HSPs.
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Ren, Juanhui, Bo Ren, Qiuwen Zhang, and Xiuqing Zheng. "A Novel Hybrid Extreme Learning Machine Approach Improved by K Nearest Neighbor Method and Fireworks Algorithm for Flood Forecasting in Medium and Small Watershed of Loess Region." Water 11, no. 9 (September 5, 2019): 1848. http://dx.doi.org/10.3390/w11091848.

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Sudden floods in the medium and small watershed by a sudden rainstorm and locally heavy rainfall often lead to flash floods. Therefore, it is of practical and theoretical significance to explore appropriate flood forecasting model for medium and small watersheds for flood control and disaster reduction in the loess region under the condition of underlying surface changes. This paper took the Gedong basin in the loess region of western Shanxi as the research area, analyzing the underlying surface and floods characteristics. The underlying surface change was divided into three periods (HSP1, HSP2, HSP3), and the floods were divided into three grades (great, moderate, small). The paper applied K Nearest Neighbor method and Fireworks Algorithm to improve the Extreme Learning Machine model (KNN-FWA-ELM) and proposed KNN-FWA-ELM hybrid flood forecasting model, which was further applied to flood forecasting of different underlying surface conditions and flood grades. Results demonstrated that KNN-FWA-ELM model had better simulation performance and higher simulation accuracy than the ELM model for flood forecasting, and the qualified rate was 17.39% higher than the ELM model. KNN-FWA-ELM model was superior to the ELM model in three periods and the simulation performance of three flood grades, and the simulation performance of KNN-FWA-ELM model was better in HSP1 stage floods and great floods.
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43

Li, Junwei, Jiufu Wen, Ruiping Hu, Surui Pei, Ting Li, Binbin Shan, Honghui Huang, and Changbo Zhu. "Transcriptome Responses to Different Environments in Intertidal Zones in the Peanut Worm Sipunculus nudus." Biology 12, no. 9 (August 29, 2023): 1182. http://dx.doi.org/10.3390/biology12091182.

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The peanut worm (Sipunculus nudus) is an important intertidal species worldwide. Species living in the same aquaculture area might suffer different environmental impacts. To increase knowledge of the molecular mechanisms underlying the response to environmental fluctuations, we performed a transcriptome analysis of S. nudus from different intertidal zones using a combination of the SMRT platform and the Illumina sequencing platform. (1) A total of 105,259 unigenes were assembled, and 23,063 unigenes were perfectly annotated. The results of the PacBio Iso-Seq and IIIumina RNA-Seq enriched the genetic database of S. nudus. (2) A total of 830 DEGs were detected in S. nudus from the different groups. In particular, 33 DEGs had differential expression in the top nine KEGG pathways related to pathogens, protein synthesis, and cellular immune response and signaling. The results indicate that S. nudus from different zones experience different environmental stresses. (3) Several DEGs (HSPA1, NFKBIA, eEF1A, etc.) in pathways related to pathogens (influenza A, legionellosis, measles, and toxoplasmosis) had higher expression in groups M and L. HSPA1 was clearly enriched in most of the pathways, followed by NFKBIA. The results show that the peanut worms from the M and L tidal flats might have suffered more severe environmental conditions. (4) Some DEGs (MKP, MRAS, and HSPB1) were upregulated in peanut worms from the H tidal flat, and these DEGs were mainly involved in the MAPK signaling pathway. These results indicate that the MAPK pathway may play a vital role in the immune response of the peanut worm to the effects of different intertidal flats. This study provides a valuable starting point for further studies to elucidate the molecular basis of the response to different environmental stresses in S. nudus.
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Chen, Keqin, Changmiao Hou, Lei Xu, Hanwu Peng, Chaogui He, Jing Liu, Guoqing Wang, Shaoshuai Huang, and Xiehong Liu. "HSPB1 Regulates Autophagy and Apoptosis in Vascular Smooth Muscle Cells in Arteriosclerosis Obliterans." Cardiovascular Therapeutics 2022 (November 14, 2022): 1–11. http://dx.doi.org/10.1155/2022/3889419.

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Objective. Small heat shock protein-1 (HSPB1) is a small heat shock protein that participates in many cellular processes and alleviates stress-induced cell injury. Autophagy protects cells from many types of stress and plays a key role in preventing stress in arteriosclerosis obliterans (ASO). However, the roles of HSPB1 in autophagy and apoptosis in the context of ASO pathogenesis remain unclear. Methods. In vivo and in vitro studies were used to determine whether HSPB1 is associated with ASO progression. The expression of HSPB1 was measured in normal and sclerotic blood vessels. The role of HSPB1 and its potential downstream signaling pathway were determined in VSMCs by overexpressing and silencing HSPB1. Results. A total of 91 ASO patients admitted to and treated at our hospital from Sep. 2020 to Sep. 2021 were selected, and plasma HSPB1 expression was assessed. We divided the patients with ASO into the grade I ( n = 39 ), II ( n = 29 ), III ( n = 10 ), and IV ( n = 13 ) groups according to Fontaine’s classification. Plasma HSPB1 levels were markedly decreased in patients with grade III ( n = 10 ) and IV ( n = 13 ) ASO compared with patients with grade I ASO. Furthermore, HSPB1 expression was significantly decreased, and p62 and cleaved caspase-3 were increased in the sclerotic vasculature compared to the normal vasculature ( p < 0.05 ). Overexpression of HSPB1 promoted apoptosis of VSMCs following ox-LDL treatment. Knockdown of HSPB1 led to a marked increase in the expression of LC3II and Beclin-1 in ox-LDL-stimulated VSMCs, whereas knockdown of HSPB1 attenuated these changes ( p < 0.05 ). Importantly, overexpression of HSPB1 promoted the dephosphorylation of JNK in ox-LDL-stimulated VSMCs. Conversely, downregulation of HSPB1 induced the opposite change. Conclusion. Loss of HSPB1 promotes VSMC autophagy and inhibits VSMC apoptosis, which are associated with ASO. HSPB1 and its downstream signaling pathways could be potential therapeutic targets for ASO treatment.
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Zhao, Sida, Bin Li, Yiyuan Chen, Chuzhong Li, and Yazhuo Zhang. "Analysis of the Prognostic and Immunological Role of HSPB1 in Pituitary Adenoma: A Potential Target for Therapy." Medicina 59, no. 5 (May 5, 2023): 885. http://dx.doi.org/10.3390/medicina59050885.

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Background and Objectives: The diagnosis and treatment of pituitary adenomas with cavernous sinus invasion pose significant challenges for clinicians. The objective of this study is to investigate the expression profile and prognostic value of HSPB1 (heat shock protein beta-1) in pituitary adenomas with invasive and non-invasive features. Additionally, we aim to explore the potential relationship between HSPB1 expression and immunological functions in pituitary adenoma. Materials and Methods: A total of 159 pituitary adenoma specimens (73 invasive tumours and 86 non-invasive tumours) underwent whole-transcriptome sequencing. Differentially expressed genes and pathways in invasive and non-invasive tumours were analysed. HSPB1 was subjected to adequate bioinformatics analysis using various databases such as TIMER, Xiantao and TISIDB. We investigated the correlation between HSPB1 expression and immune infiltration in cancers and predicted the target drug of HSPB1 using the TISIDB database. Results: HSPB1 expression was upregulated in invasive pituitary adenomas and affected immune cell infiltration. HSPB1 was significantly highly expressed in most tumours compared to normal tissues. High expression of HSPB1 was significantly associated with poorer overall survival. HSPB1 was involved in the regulation of the immune system in most cancers. The drugs DB11638, DB06094 and DB12695 could act as inhibitors of HSPB1. Conclusions: HSPB1 may serve as an important marker for invasive pituitary adenomas and promote tumour progression by modulating the immune system. Inhibitors of HSPB1 expression are currently available, making it a potential target for therapy in invasive pituitary adenoma.
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Cai, Qiaoyan, Jing Lin, Ling Zhang, Jiumao Lin, Lili Wang, Daxin Chen, and Jun Peng. "Comparative proteomics—network analysis of proteins responsible for ursolic acid–induced cytotoxicity in colorectal cancer cells." Tumor Biology 39, no. 3 (March 2017): 101042831769501. http://dx.doi.org/10.1177/1010428317695015.

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Ursolic acid is a key active compound present in many medicinal herbs that have been widely used in traditional Chinese medicine for the clinical treatment of various cancers. However, the precise mechanisms of its antitumor activity have been poorly understood. To identify the cellular targets of ursolic acid, two-dimensional gel electrophoresis combined with mass spectrometry was performed in this study, which identified 15 proteins with significantly altered levels in protein expression. This demonstrated that ursolic acid–induced cytotoxicity in colorectal cancer cells involves dysregulation in protein folding, signal transduction, cell proliferation, cell cycle, and apoptosis. Corresponding protein regulation was also confirmed by Western blotting. Furthermore, the study of functional association between these 15 proteins revealed that 10 were closely related in a protein–protein interaction network, whereby the proteins either had a direct interaction with each other or were associated via only one intermediary protein. In this instance, the ATP5B/CALR/HSP90B1/HSPB1/HSPD1-signaling network was revealed as the predominant target which was associated with the majority of the observed protein–protein interactions. As a result, the identified targets may be useful in explaining the anticancer mechanisms of ursolic acid and as potential targets for colorectal cancer therapy.
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47

Wang, Yana, Jiali Liu, Qiuyue Kong, Hao Cheng, Fei Tu, Peng Yu, Ying Liu, et al. "Cardiomyocyte-specific deficiency of HSPB1 worsens cardiac dysfunction by activating NFκB-mediated leucocyte recruitment after myocardial infarction." Cardiovascular Research 115, no. 1 (July 2, 2018): 154–67. http://dx.doi.org/10.1093/cvr/cvy163.

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Abstract Aims Inadequate healing after myocardial infarction (MI) leads to heart failure and fatal ventricular rupture, while optimal healing requires timely induction and resolution of inflammation. This study tested the hypothesis that heat shock protein B1 (HSPB1), which limits myocardial inflammation during endotoxemia, modulates wound healing after MI. Methods and results To test this hypothesis, cardiomyocyte-specific HSPB1 knockout (Hspb1−/−) mice were generated using the Cre-LoxP recombination system. MI was induced by ligation of the left anterior descending coronary artery in Hspb1−/− and wild-type (WT) littermates. HSPB1 was up-regulated in cardiomyocytes of WT animals in response to MI, and deficiency of cardiomyocyte HSPB1 increased MI-induced cardiac rupture and mortality within 21 days after MI. Serial echocardiography showed more aggravated remodelling and cardiac dysfunction in Hspb1−/− mice than in WT mice at 1, 3, and 7 days after MI. Decreased collagen deposition and angiogenesis, as well as increased MMP2 and MMP9 activity, were also observed in Hspb1−/− mice compared with WT controls after MI, using immunofluorescence, polarized light microscopy, and zymographic analyses. Notably, Hspb1−/− hearts exhibited enhanced and prolonged leucocyte infiltration, enhanced expression of inflammatory cytokines, and enhanced TLR4/MyD88/NFκB activation compared with WT controls after MI. In-depth molecular analyses in both mice and primary cardiomyocytes demonstrated that cardiomyocyte-specific knockout of HSPB1 increased nuclear factor-κB (NFκB) activation, which promoted the expression of proinflammatory mediators. This led to increased leucocyte recruitment, thereby to excessive inflammation, ultimately resulting in adverse remodelling, cardiac dysfunction, and cardiac rupture following MI. Conclusion These data suggest that HSPB1 acts as a negative regulator of NFκB-mediated leucocyte recruitment and the subsequent inflammation in cardiomyocytes. Cardiomyocyte HSPB1 is required for wound healing after MI and could be a target for myocardial repair in MI patients.
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Jundra, Nuntawat, Aksarakorn Kummasook, and Monsicha Pongpom. "Expression of Heat Shock Protein 30 in Talaromyces marneffei during Phase Transition and in Response to Heat and Oxidative Stresses." Biomedical Sciences and Clinical Medicine 62, no. 2 (June 29, 2023): 63–72. http://dx.doi.org/10.12982/bscm.2023.07.

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OBJECTIVE Heat shock protein 30 (Hsp30) has been identified as an immunogenic, yeast phase-specific protein in Talaromyces marneffei. The purpose of this study was to investigate how the hsp30 gene and Hsp30 protein are expressed during phase transition and in response to heat and oxidative stress exposure. METHODS Several sequence analysis tools were employed to predict hsp30 control elements and to determine the subcellular localization of Hsp30. In the phase transition experiment, Talaromyces marneffei conidia were cultivated at two different temperatures, 25 °C and 37 °C. Subsequently, stress response tests were conducted by subjecting the yeast cells to heat at 42 °C and by treating them with hydrogen peroxide. The levels of the hsp30 transcript and its protein were measured using real-time RT-PCR and western immunoblot analysis, respectively. RESULTS The sequence analysis revealed the presence of heat response element (HRE), stress responsive element (STRE), and xenobiotic responsive element (XRE), which are typically involved in regulating hsp genes. A web-based tool predicted that Hsp30 protein is localized in cytoplasm, nucleus, and cell membrane. The hsp30 transcript and Hsp30 protein were highly clearly detected in both yeast cells and conidia. Furthermore, the hsp30 transcript in yeast cells was upregulated following heat shock at 42° C and exposure to hydrogen peroxide. These findings indicate that Hsp30 plays a crucial role in assisting the yeast phase of T. marneffei to cope with heat and oxidative stresses. CONCLUSIONS Hsp30 is a protein specific to the conidial and yeast phases of T. marneffei. It likely performs a conserved chaperone function during yeast growth and plays a significant role in stress response by mitigating protein aggregation issues. KEYWORDS Talaromyces marneffei, heat shock protein 30, expression
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Gibert, Benjamin, Stéphanie Simon, Valeriya Dimitrova, Chantal Diaz-Latoud, and André-Patrick Arrigo. "Peptide aptamers: tools to negatively or positively modulate HSPB1(27) function." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1617 (May 5, 2013): 20120075. http://dx.doi.org/10.1098/rstb.2012.0075.

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Human HSP27 (HSPB1) is a molecular chaperone sensor which, through dynamic changes in its phosphorylation and oligomerization, allows cells to adapt to changes in their physiology and/or mount a protective response to injuries. In pathological conditions, the high level of HSPB1 expression can either be beneficial, such as in diseases characterized by cellular degenerations, or be malignant in cancer cells where it promotes tumourigenesis, metastasis and anti-cancer drug resistance. Structural changes allow HSPB1 to interact with specific client protein partners in order to modulate their folding/activity and/or half-life. Therefore, the search is open for therapeutic compounds aimed at either down- or upregulating HSPB1 activity. In this respect, we have previously described two peptide aptamers (PA11 and PA50) that specifically interact with HSPB1 small oligomers and decrease its anti-apoptotic and tumourigenic activities. A novel analysis of the different HSPB1-interacting aptamers that were isolated earlier revealed that one aptamer (PA23) has the intriguing ability to stimulate the protective activity of HSPB1. We show here that this aptamer abolishes the dominant negative effect induced by the R120G mutant of αB-crystallin (HSPB5) by disrupting its interaction with HSPB1. Hence, developing structure-based interfering strategies could lead to the discovery of HSPB1-based therapeutic drugs.
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Kovács, Árpád Ferenc, Nóra Fekete, Lilla Turiák, András Ács, László Kőhidai, Edit I. Buzás, and Éva Pállinger. "Unravelling the Role of Trophoblastic-Derived Extracellular Vesicles in Regulatory T Cell Differentiation." International Journal of Molecular Sciences 20, no. 14 (July 14, 2019): 3457. http://dx.doi.org/10.3390/ijms20143457.

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Regulatory T cells (Treg) are mandatory elements in the maintenance of human pregnancy, but their de novo differentiation has not been completely exposed. HSPE1 chaperone expressing trophoblast cells may have a role in it. Trophoblast-derived extracellular vesicles (EVs), either at the feto–maternal interface or in circulation, target CD4+ T cells. We hypothesized that HSPE1-associated trophoblastic cell line (BeWo)-derived EVs are active mediators of Treg cell differentiation. We proved at first that recombinant HSPE1 promote human Treg cell differentiation in vitro. Developing a CRISPR-Cas9 based HSPE1 knockout BeWo cell line we could also demonstrate, that EV-associated HSPE1 induces Treg development. Next-generation sequencing of miRNA cargo of BeWo-EVs characterized the regulatory processes of Treg polarization. By the use of single-cell transcriptomics analysis, seven Treg cell subtypes were distinguished and we demonstrated for the first time that the expression level of HSPE1 was Treg subtype dependent, and CAPG expression is characteristic to memory phenotype of T cells. Our data indicate that HSPE1 and CAPG may be used as markers for identification of Treg subtypes. Our results suggest, that trophoblastic-derived iEVs-associated HSPE1 and miRNA cargo have an important role in Treg cell expansion in vitro and HSPE1 is a useful marker of Treg subtype characterization.
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