Journal articles: 'HSP18.5'

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Liu, Peng, Jundong Jia, Hanwen Wu, Zihan Song, and Xi He. "Hsp from Lactobacillus plantarum Expression in Lactococcus lactis MG1363." BIO Web of Conferences 61 (2023): 01010. http://dx.doi.org/10.1051/bioconf/20236101010.

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Small heat shock proteins are protective proteins produced by organisms under thermal stress. They are widely present in living organisms. Here, Hsp18, Hsp18.55 and Hsp19.5 genes were cloned from Lactobacillus plantarum and heterologous expressed in Lactococcus lactis, and their potential functions under ethanol stress were investigated. The results showed that the recombinant strain over expressing Hsp19.5 gene had stronger stress resistance, which provided a basis for further study of the survival ability of other microorganisms under ethanol stress.

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Kurre, Devanshu, and Kaza Suguna. "Network of Entamoeba histolytica HSP18.5 dimers formed by two overlapping [IV]‐X‐[IV] motifs." Proteins: Structure, Function, and Bioinformatics 89, no. 8 (April 8, 2021): 1039–54. http://dx.doi.org/10.1002/prot.26081.

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Kokke, Bas P. A., Michel R. Leroux, E. Peter M. Candido, Wilbert C. Boelens, and Wilfried W. de Jong. "Caenorhabditis eleganssmall heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity." FEBS Letters 433, no. 3 (August 21, 1998): 228–32. http://dx.doi.org/10.1016/s0014-5793(98)00917-x.

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Otani, Mieko, Toshiyuki Ueki, Satoshi Kozuka, Miki Segawa, Keiji Sano, and Sumiko Inouye. "Characterization of a Small Heat Shock Protein, Mx Hsp16.6, of Myxococcus xanthus." Journal of Bacteriology 187, no. 15 (August 1, 2005): 5236–41. http://dx.doi.org/10.1128/jb.187.15.5236-5241.2005.

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ABSTRACT A number of heat shock proteins in Myxococcus xanthus were previously identified by two-dimensional (2D) gel electrophoresis. One of these protein was termed Mx Hsp16.6, and the gene encoding Mx Hsp16.6 was isolated. Mx Hsp16.6 consists of 147 amino acid residues and has an estimated molecular weight of 16,642, in accordance with the apparent molecular mass in the 2D gel. An α-crystallin domain, typically conserved in small heat shock proteins, was found in Mx Hsp16.6. Mx Hsp16.6 was not detected during normal vegetative growth but was immediately induced after heat shock. Expression of the hsp16.6 gene was not induced by other stresses, such as starvation, oxidation, and high osmolarity. Mx Hsp16.6 was mostly localized in particles formed after heat shock and precipitated by low-speed centrifugation. Furthermore, Mx Hsp16.6 was detected in highly electron-dense particles in heat-shocked cells by immunoelectron microscopy, suggesting that it forms large complexes with heat-denatured proteins. An insertion mutation in the hsp16.6 gene resulted in lower viability during heat shock and lower acquired thermotolerance. Therefore, it is likely that Mx Hsp16.6 plays critical roles in the heat shock response in M. xanthus.

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Löw, Daniela, Kurt Brändle, Lutz Nover, and Christoph Forreiter. "Cytosolic heat-stress proteins Hsp17.7 class I and Hsp17.3 class II of tomato act as molecular chaperones in vivo." Planta 211, no. 4 (September 15, 2000): 575–82. http://dx.doi.org/10.1007/s004250000315.

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Zhang, Yanhao, Shanshan Li, Qianyi Liu, Ruiying Long, Jihong Feng, Huan Qin, Mao Li, Liping Liu, and Junmin Luo. "Mycobacterium tuberculosis Heat-Shock Protein 16.3 Induces Macrophage M2 Polarization Through CCRL2/CX3CR1." Inflammation 43, no. 2 (November 20, 2019): 487–506. http://dx.doi.org/10.1007/s10753-019-01132-9.

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Abstract Mycobacterium tuberculosis, the pathogen of tuberculosis (TB), can survive in host macrophages and induce macrophages to M2 phenotype might result in latent MTB infection. During the latent phase, the expression of MTB heat-shock protein 16.3 (Hsp16.3) is markedly increased among most of bacterial proteins, but the role of Hsp16.3 in macrophage M2 polarization is not clear. In this work, we found that macrophages incubated with 100 ng/ml MTB Hsp16.3 increased the production of Arg-1, IL-10, TGF-beta, and CD206. These results showed that MTB Hsp16.3 may induce macrophage M2 phenotype. And the interaction of Hsp16.3 with macrophages was found to depend on chemokine receptors CCRL2 and CX3CR1. Additionally, we used overexpression and silencing techniques to further verify the effect of CCRL2 and CX3CR1 on MTB Hsp16.3-induced M2 polarization macrophages. Furthermore, we explored the downstream signaling molecules of CCRL2 and CX3CR1 and we found MTB Hsp16.3 altered the signal transduction of the AKT/ERK/p38-MAPK. Taken together, this study provides evidence that MTB Hsp16.3 promotes macrophages to M2 phenotype and explores its underlying mechanism.

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Ma, Pengfei, Jie Li, Lei Qi, and Xiuzhu Dong. "The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation." International Journal of Molecular Sciences 22, no. 5 (March 4, 2021): 2591. http://dx.doi.org/10.3390/ijms22052591.

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Small heat shock proteins (sHsps) are widely distributed among various types of organisms and function in preventing the irreversible aggregation of thermal denaturing proteins. Here, we report that Hsp17.6 from Methanolobus psychrophilus exhibited protection of proteins from oxidation inactivation. The overexpression of Hsp17.6 in Escherichia coli markedly increased the stationary phase cell density and survivability in HClO and H2O2. Treatments with 0.2 mM HClO or 10 mM H2O2 reduced malate dehydrogenase (MDH) activity to 57% and 77%, whereas the addition of Hsp17.6 recovered the activity to 70–90% and 86–100%, respectively. A similar effect for superoxide dismutase oxidation was determined for Hsp17.6. Non-reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis assays determined that the Hsp17.6 addition decreased H2O2-caused disulfide-linking protein contents and HClO-induced degradation of MDH; meanwhile, Hsp17.6 protein appeared to be oxidized with increased molecular weights. Mass spectrometry identified oxygen atoms introduced into the larger Hsp17.6 molecules, mainly at the aspartate and methionine residues. Substitution of some aspartate residues reduced Hsp17.6 in alleviating H2O2- and HClO-caused MDH inactivation and in enhancing the E. coli survivability in H2O2 and HClO, suggesting that the archaeal Hsp17.6 oxidation protection might depend on an “oxidant sink” effect, i.e., to consume the oxidants in environments via aspartate oxidation.

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Wagner, Daniela, Jens Schneider-Mergener, and Christoph Forreiter. "Analysis of Chaperone Function and Formation of Hetero-oligomeric Complexes of Hsp18.1 and Hsp17.7, Representing Two Different Cytoplasmic sHSP Classes in Pisum sativum." Journal of Plant Growth Regulation 24, no. 3 (September 2005): 226–37. http://dx.doi.org/10.1007/s00344-005-0020-3.

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Zhang, L., C. Lohmann, R. Prändl, and F. Schöffl. "Heat Stress-Dependent DNA Binding of Arabidopsis Heat Shock Transcription Factor HSF1 to Heat Shock Gene Promoters in Arabidopsis Suspension Culture Cells in vivo." Biological Chemistry 384, no. 6 (June 16, 2003): 959–63. http://dx.doi.org/10.1515/bc.2003.108.

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AbstractUsing UV laser cross-linking and immunoprecipitation we measured the in vivo binding of Arabidopsis heat shock transcription factor HSF1 to the promoters of target genes, Hsp18.2 and Hsp70. The amplification of promoter sequences, co-precipitated with HSF1-specific antibodies, indicated that HSF1 is not bound in the absence of heat stress. Binding to promoter sequences of target genes is rapidly induced by heat stress, continues throughout the heat treatment, and declines during subsequent recovery at room temperature. The molecular mechanisms underlying the differences between Hsp18.2 and Hsp70 in the kinetics of HSF1/promoter binding and corresponding mRNA expression profiles are discussed.

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WANG, Z., B. LAI, J. CAO, Z. LI, L. QU, A. CAO, and L. LAI. "Hierarchical Unfolding of Mj HSP16.5." Acta Physico-Chimica Sinica 24, no. 10 (October 2008): 1745–50. http://dx.doi.org/10.1016/s1872-1508(08)60070-4.

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Saha, Abhik, Archna Sharma, Amlanjyoti Dhar, Bhabatarak Bhattacharyya, Siddhartha Roy, and Sujoy K. Das Gupta. "Antagonists of Hsp16.3, a Low-Molecular-Weight Mycobacterial Chaperone and Virulence Factor, Derived from Phage-Displayed Peptide Libraries." Applied and Environmental Microbiology 71, no. 11 (November 2005): 7334–44. http://dx.doi.org/10.1128/aem.71.11.7334-7344.2005.

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ABSTRACT The persistence of Mycobacterium tuberculosis is a major cause of concern in tuberculosis (TB) therapy. In the persistent mode the pathogen can resist drug therapy, allowing the possibility of reactivation of the disease. Several protein factors have been identified that contribute to persistence, one of them being the 16-kDa low-molecular-weight mycobacterial heat shock protein Hsp16.3, a homologue of the mammalian eye lens protein alpha-crystallin. It is believed that Hsp16.3 plays a key role in the persistence phase by protecting essential proteins from being irreversibly denatured. Because of the close association of Hsp16.3 with persistence, an attempt has been made to develop inhibitors against it. Random peptide libraries displayed on bacteriophage M13 were screened for Hsp16.3 binding. Two phage clones were identified that bind to the Hsp16.3 protein. The corresponding synthetic peptides, an 11-mer and a 16-mer, were able to bind Hsp16.3 and inhibit its chaperone activity in vitro in a dose-dependent manner. Little or no effect of these peptides was observed on alphaB-crystallin, a homologous protein that is a key component of human eye lens, indicating that there is an element of specificity in the observed inhibition. Two histidine residues appear to be common to the selected peptides. Nuclear magnetic resonance studies performed with the 11-mer peptide indicate that in this case these two histidines may be the crucial binding determinants. The peptide inhibitors of Hsp16.3 thus obtained could serve as the basis for developing potent drugs against persistent TB.

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Merewitz, Emily B., Thomas Gianfagna, and Bingru Huang. "Effects of SAG12-ipt and HSP18.2-ipt Expression on Cytokinin Production, Root Growth, and Leaf Senescence in Creeping Bentgrass Exposed to Drought Stress." Journal of the American Society for Horticultural Science 135, no. 3 (May 2010): 230–39. http://dx.doi.org/10.21273/jashs.135.3.230.

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Drought stress is a widespread abiotic stress that causes a decline in plant growth. Drought injury symptoms have been associated with an inhibition in cytokinin (CK) synthesis. The objectives of this study were to investigate whether expression of a gene (ipt) encoding the enzyme adenine isopentenyl phosphotransferase for CK synthesis ligated to a senescence-activated promoter (SAG12) or a heat shock promoter (HSP18.2) would improve drought tolerance in creeping bentgrass (Agrostis stolonifera) and to examine shoot and root growth responses to drought stress associated with changes in endogenous production of CK, and the proportional change in CK and abscisic acid (ABA) due to ipt transformation. Most SAG12-ipt and HSP18.2-ipt transgenic lines exhibited significantly higher turf quality, photochemical efficiency, chlorophyll content, leaf relative water content, and root:shoot ratio under drought stress than the null transformant or the wild-type ‘Penncross’ plants. Transgenic lines that had better growth and turf performance generally had higher CK content and a higher CK-to-ABA ratio, although the direct correlation of CK and ABA content with individual physiological parameters in individual lines was not clear. Our results demonstrated that expressing ipt resulted in the improvement of turf performance under drought stress in creeping bentgrass in some of the transgenic plants with SAG12-ipt or HSP18.2-ipt, which could be associated with the suppression of leaf senescence and promoting root growth relative to shoot growth due to the maintenance of higher CK level and a higher ratio of CK to ABA.

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Kim, Dong Ryoung, Ick Lee, Sung Chul Ha, and Kyeong Kyu Kim. "Activation mechanism of HSP16.5 from Methanococcus jannaschii." Biochemical and Biophysical Research Communications 307, no. 4 (August 2003): 991–98. http://dx.doi.org/10.1016/s0006-291x(03)01302-0.

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Chen, Ke-Jun, Feng-Zeng Li, Qian Ye, Meng Jia, and Sheng Fang. "HSP105 expression in cutaneous malignant melanoma: Correlation with clinicopathological characteristics." PLOS ONE 16, no. 10 (October 7, 2021): e0258053. http://dx.doi.org/10.1371/journal.pone.0258053.

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Background Heat shock proteins can protect against stress-associated cellular challenges, but they can also protect some tumors from human immune system monitoring. Heat shock protein 105 (HSP105/110) is a high molecular weight protein whose expression has been reported in many cancers, but few studies on its role in cutaneous malignant melanoma have been published. In this study, we analyzed the relationship between HSP105 expression and the clinicopathological characteristics of CMM. Methods This retrospective study included 91 patients with CMM. The clinicopathological characteristics of CMM patients, including age, lesion duration, location, pathological classification, Clark’s level, Breslow thickness, metastasis and recurrence, were collected. Immunohistochemical staining and Western blot analysis for HSP105 were performed. Pigmented nevi (n = 20) served as a control. The staining intensity and percentage of stained cells were expressed as a histochemical score (HSCORE). Results HSP105 was overexpressed in melanoma compared with nevi. Differences in the HSCORE between nevi (HSCORE = 1.05(0.15,1.50)) and CMM (HSCORE = 2.68(1.80,3.60)) were remarkable (P<0.001). Exposed site lesions, recurrent and metastatic lesions, nodular melanoma and lentigo maligna melanoma were closely associated with higher HSP105 expression (P = 0.011, P = 0.001 and P = 0.001, respectively). Moreover, no significant difference was observed in Clark’s level, Breslow thickness, or lesion duration (P>0.05). Conclusion HSP105 is overexpressed in CMM. Higher HSP105 expression in lesions is associated with different clinicopathological variables. HSP105 may be a potential target for the diagnosis, treatment and prognostic prediction of CMM.

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FENG, Xiuguang, Sufang HUANG, Xinmiao FU, Abuduaini ABULIMITI, and Zengyi CHANG. "The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein Hsp16.3 occurs via a stepwise mechanism." Biochemical Journal 363, no. 2 (April 8, 2002): 329–34. http://dx.doi.org/10.1042/bj3630329.

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Conditions are reported under which the reassembled intermediates of the heat-shock protein Hsp16.3 after being denatured in 8M urea were detected by mainly using urea-gradient PAGE (with modifications) and urea-denaturing pore-gradient PAGE. Hsp16.3 is the small heat-shock protein from Mycobacterium tuberculosis, which exists as a specific nonamer and was proposed to form a trimer-of-trimers structure. The refolding and reassembling of this protein was achieved rapidly by dilution or dialysis, suggesting an effectively spontaneous recovery of quaternary structure. Data presented in this report demonstrate that the in vitro reassembling process of Hsp16.3 protein occurs through a spontaneous and effective stepwise mechanism. Modified urea-gradient PAGE may provide a general method for studying the reassembling processes of other oligomeric proteins.

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Kozhabek, Zh, J. L. Үu, and X. L. Wang. "Analysis of the HSP17.6 protein mechanism in BBSV infection." BULLETIN of the L.N. Gumilyov Eurasian National University. BIOSCIENCE Series 135, no. 2 (2021): 38–47. http://dx.doi.org/10.32523/2616-7034-2021-135-2-38-47.

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Beet black scorch virus (BBSV) has been reported as a natural pathogen of sugar beet and distributed all over the world, causing great economic losses to the sugar industry. Research on interactions between BBSV and its host by using model plant Nicotiana benthamiana is significantly important and nessesary for understanding virus infection process and exploring plant resistance mechanism. The results of sequencing the transcriptome of N. benthamiana infected with BBSV as well as gene screening in response to viral infection revealed upregulation of the small heat shock protein 17.6 gene (NbHSP17.6) and the effect of the protein on resistance to the virus. To further examine the involvement of HSP17.6 in defense responses in N. benthamiana, we tested interaction between HSP17.6 and other heat shock proteins such as HSP70 and HSP90 as well as BBSV encoded proteins. The results showed that HSP17.6 interacted with HSP70 and HSP90 but not with BBSV encoded proteins. When combined with other available results, it is possible that HSP17.6 acted as a small molecular chaperone to facilitate proper refolding of the specific proteins HSP70 and HSP90 required for BBSV infection and/or replication.

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Yu, Nancy, Michael Kakunda, Victoria Pham, Jennie R. Lill, Pan Du, Matthew Wongchenko, Yibing Yan, Ron Firestein, and XiaoDong Huang. "HSP105 Recruits Protein Phosphatase 2A To Dephosphorylate β-Catenin." Molecular and Cellular Biology 35, no. 8 (February 2, 2015): 1390–400. http://dx.doi.org/10.1128/mcb.01307-14.

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The Wnt/β-catenin pathway causes accumulation of β-catenin in the cytoplasm and its subsequent translocation into the nucleus to initiate the transcription of the target genes. Without Wnt stimulation, β-catenin forms a complex with axin (axis inhibitor), adenomatous polyposis coli (APC), casein kinase 1α (CK1α), and glycogen synthase kinase 3β (GSK3β) and undergoes phosphorylation-dependent ubiquitination. Phosphatases, such as protein phosphatase 2A (PP2A), interestingly, also are components of this degradation complex; therefore, a balance must be reached between phosphorylation and dephosphorylation. How this balance is regulated is largely unknown. Here we show that a heat shock protein, HSP105, is a previously unidentified component of the β-catenin degradation complex. HSP105 is required for Wnt signaling, since depletion of HSP105 compromises β-catenin accumulation and target gene transcription upon Wnt stimulation. Mechanistically, HSP105 depletion disrupts the integration of PP2A into the β-catenin degradation complex, favoring the hyperphosphorylation and degradation of β-catenin. HSP105 is overexpressed in many types of tumors, correlating with increased nuclear β-catenin protein levels and Wnt target gene upregulation. Furthermore, overexpression of HSP105 is a prognostic biomarker that correlates with poor overall survival in breast cancer patients as well as melanoma patients participating in the BRIM2 clinical study.

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Zappasodi, Roberta, Italia Bongarzone, Gaia C. Ghedini, Lorenzo Castagnoli, Antonello D. Cabras, Antonella Messina, Monica Tortoreto, et al. "Serological identification of HSP105 as a novel non-Hodgkin lymphoma therapeutic target." Blood 118, no. 16 (October 20, 2011): 4421–30. http://dx.doi.org/10.1182/blood-2011-06-364570.

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Abstract We reported that the clinical efficacy of dendritic cell–based vaccination is strongly associated with immunologic responses in relapsed B-cell non-Hodgkin lymphoma (B-NHL) patients. We have now investigated whether postvaccination antibodies from responders recognize novel shared NHL-restricted antigens. Immunohistochemistry and flow cytometry showed that they cross-react with allogeneic B-NHLs at significantly higher levels than their matched prevaccination samples or nonresponders' antibodies. Western blot analysis of DOHH-2 lymphoma proteome revealed a sharp band migrating at approximately 100 to 110 kDa only with postvaccine repertoires from responders. Mass spectrometry identified heat shock protein-105 (HSP105) in that molecular weight interval. Flow cytometry and immunohistochemistry disclosed HSP105 on the cell membrane and in the cytoplasm of B-NHL cell lines and 97 diagnostic specimens. A direct correlation between HSP105 expression and lymphoma aggressiveness was also apparent. Treatment of aggressive human B-NHL cell lines with an anti-HSP105 antibody had no direct effects on cell cycle or apoptosis but significantly reduced the tumor burden in xenotransplanted immunodeficient mice. In vivo antilymphoma activity of HSP105 engagement was associated with a significant local increase of Granzyme B+ killer cells that very likely contributed to the tumor-restricted necrosis. Our study adds HSP105 to the list of nononcogenes that can be exploited as antilymphoma targets.

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Wang, Zheng, AoNeng Cao, and LuHua Lai. "High activity of Mj HSP16.5 under acidic condition." Science in China Series B: Chemistry 52, no. 3 (December 16, 2008): 325–31. http://dx.doi.org/10.1007/s11426-008-0158-5.

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Zappasodi, Roberta, Alessandra Cavanè, Monica Tortoreto, Cristina Tringali, Giusi Ruggiero, Lorenzo Castagnoli, Bruno Venerando, et al. "HSP105 Inhibition Counteracts Key Oncogenic Pathways and Hampers the Growth of Human Aggressive B-Cell Non-Hodgkin Lymphoma." Blood 120, no. 21 (November 16, 2012): 1562. http://dx.doi.org/10.1182/blood.v120.21.1562.1562.

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Abstract Abstract 1562 Our previous findings have made it clear that the significant clinical efficacy attained by dendritic cell-based vaccination in relapsed B-cell non-Hodgkin lymphoma (B-NHL) patients is firmly associated with multifaceted immunologic responses, including the development of anti-heat shock protein (HSP)105 humoral immunity (Di Nicola et al., Blood 2009 113:18–27; Zappasodi et al., Cancer Res. 2010 70:9062–9072; Zappasodi et al., Blood 2011 118:4421–4430). Human HSP105 is a high-molecular-weight chaperone constitutively expressed at low levels within the cytoplasm, and can also be induced in the nucleus by various forms of stress. It is overexpressed in several solid tumors, including melanoma, breast, thyroid and gastroenteric cancers. We have recently shown that this is also true for B-NHLs, in which HSP105 levels increase in function of their aggressiveness and proliferation index (Zappasodi et al., Blood 2011 118:4421–4430). Accordingly, in normal lymph nodes HSP105 expression is confined to the hyper-proliferating germinal center (GC) B cells, suggesting its involvement in the potentially oncogenic GC reactions. We have now set out to clarify the functional role of HSP105 in B-NHLs by stably silencing its expression in the Namalwa aggressive lymphoma cell line. Namalwa cells were infected by using a lentiviral vector carrying a HSP105-targeting pre-microRNA sequence and the Emerald Green Fluorescent Protein (EmGFP) gene, both under the human cytomegolovirus immediate early promoter, as well as the blasticidin resistance gene. Control cells were mock-infected with the empty vector. Infected cells were initially selected in the presence of blasticidin, and then single GFP+ cells were sorted on a flow cytometry device. In this way, we achieved 100% GFP+ subclones that displayed a specific constitutive down-regulation of HSP105, as there was no significant decrease in the expression of its cognate molecular homolog HSP70, or the other major cellular chaperone HSP90. Comparison of the in vitro proliferation rate of two silenced clones with that of the mock culture showed that the cell doubling time of both clones significantly increased and their in vitro growth was accordingly delayed (P= 0.01 and P= 0.04). Western blot analysis in 6 different silenced clones of the oncoproteins most frequently involved in B-NHLs revealed that BCL-6 and c-Myc were down-regulated in function of HSP105 knockdown levels, whereas in mock cells no modifications were detected with respect to their wild-type counterparts. Further strengthening the association between HSP105, BCL-6 and c-Myc expression, immunohistochemistry analysis of 50 primary human aggressive B-NHLs revealed that HSP105 expression, measured both as intensity and percentage of positive cells, was significantly higher in c-Myc- or BCL-6-dependent Burkitt (P= 0.0264) and diffuse large B-cell lymphomas (P= 0.0068) respectively than in other aggressive istotypes that do not overexpress these oncoproteins. These findings support the potential pro-tumorigenic cooperation of HSP105 with BCL-6 and c-Myc transcription factors. To find out whether counteracting HSP105 functions hampers in vivo lymphoma growth, we evaluated the tumor-forming capability of HSP105-silenced (siHSP105) or mock Namalwa cells subcutaneously injected into severe combined immunodeficient mice at serial 10-fold dilutions from 106 to 104 cells/injection (Figure 1). We found that HSP105 knockdown slightly delayed in vivo Namalwa tumor formation when 106 and 105 cells were injected. Noteworthy, no lesions appeared over 70-day observation in mice inoculated with 104 siHSP105 cells, whereas palpable tumors were present in 67% of the animals 24 days after injection of the mock cells (Figure 1). Overall, these results indicate that HSP105 may be a per se nononcogenic molecule that contributes to lymphomagenesis by facilitating the tumorigenic functions of key oncoproteins. They equally provide the rationale for developing HSP105 inhibitors as a novel strategy for improving the treatment of aggressive B-NHLs. Figure 1. In vivo tumor-forming capability of siHSP105 or mock Namalwa cells Figure 1. In vivo tumor-forming capability of siHSP105 or mock Namalwa cells Disclosures: Gianni: Hoffmann-La Roche: Consultancy, Honoraria.

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Park, Hanseul, and Yeh-Jin Ahn. "Development of Transgenic Escherichia coli with Improved Viability by Heterologous Expression of a Heat Shock Protein Gene from Carrot (Daucus carota L.)." HortScience 51, no. 3 (March 2016): 305–10. http://dx.doi.org/10.21273/hortsci.51.3.305.

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A small heat shock protein gene from carrot (Daucus carota L.), Hsp17.7, was inserted into the Escherichia coli chromosome by RecE/RecT-based homologous recombination to increase cell viability during industrial fermentation, which frequently encounters adverse growth conditions. DNA construct “lipoprotein (Lpp) gene promoter—Hsp17.7 gene—flippase recombination target (Frt) cassette” flanked by the sequences of the insertion site of the E. coli chromosome (yddE pseudogene) was generated by polymerase chain reaction (PCR). The transformed E. coli cell lines that heterologously expressed Hsp17.7 exhibited shorter lag phase, compared with control cell line under normal (37 °C), heat (45 °C), and antifoam conditions. Cell viability was higher in the transformed cell lines in the heat (50 °C, up to 2-fold) and cold (2 °C, up to 1.7-fold) conditions. The soluble protein levels were also higher in the transformed E. coli cell lines by up to 20%, compared with control cell line in both stress conditions. The stress-tolerant transgenic cell lines developed in this study can contribute to more efficient and cost saving industrial cultivation of E. coli, which is most frequently used for recombinant protein production.

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Zappasodi, Roberta, Gaia C. Ghedini, Italia Bongarzone, Lorenzo Castagnoli, Maida de Bortoli, Piera Aiello, Alessandra Cavanè, et al. "Serological Identification of HSP105 as a Novel Non-Hodgkin Lymphoma Therapeutic Target." Blood 116, no. 21 (November 19, 2010): 463. http://dx.doi.org/10.1182/blood.v116.21.463.463.

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Abstract Abstract 463 We recently reported that vaccination with autologous monocyte-derived dendritic cells pulsed with dying autologous tumor cells elicited a clinical response strongly associated with multifaceted antitumor immune-activation in relapsed indolent non-Hodgkin lymphoma (NHL) patients. We have now set out to determine whether vaccine-induced humoral response is directed against common indolent NHL-restricted antigens (ags), which could thus be exploited as novel targets for therapy. Antibodies (Abs) were purified from pre- and post-vaccine patients' serum samples, biotin-conjugated, and initially tested by immunohistochemistry (IHC) and flow cytometry (FC) on allogeneic tumors biopsies or live tumor cells, both primary tumors and cell lines. We found that post-vaccine Abs from responders (R) reacted with allogeneic NHL at significantly higher levels than their matched pre-vaccine samples or non-R Abs. Furthermore, Rs' post-vaccine sera significantly impaired the growth of DOHH-2 and RL-19 follicular lymphoma (FL) cell lines, as revealed by standard 3-(4,5- dimethylthiazol- 2-yl)-2,5-diphenyltetrazolium bromide (MTT) assays. To identify the therapeutically targeted NHL ags, we then used biotin-conjugated patient Abs to immunoblot one-dimensional SDS-PAGE of DOHH-2 cell protein fractions obtained by isoelectrofocusing. Protein bands differentially revealed by post-vaccine Abs from R were analyzed by Mass Spectrometry (MS). One differential band migrating at about 100 kDa was revealed among the most acidic protein fractions only when post-vaccine samples from R were used. MS analysis identified heat shock protein (HSP) 105 in the differentially reacting bands. Immunoprecipitation with a commercial anti-HSP105 Ab followed by Western blot analysis with biotin-conjugated pre- and post-vaccine Abs from R confirmed the increased ability of the post-vaccine sample to recognize HSP105. FC disclosed HSP105 both on the cell membrane and in the cytoplasm of a panel of B-cell NHL cell lines and normal B cells. The extent of HSP105 surface expression increased in function of lymphoma istotype aggressiveness. The antitumor activity of anti-HSP105 Ab, measured by MTT assays, was thus higher against Burkitt's lymphoma (BL) cell lines than germinal centre-derived diffuse large B cell lymphoma and FL cell lines, which displayed an IC50 of 4.5, 7.5, 11.7 μg/ml, respectively. To confirm these finding in primary human tumors, we performed IHC analyses of HSP105 on 68 diagnostic NHL specimens (35 low-grade and 33 high-grade NHL) and 23 non-malignant lymph nodes obtained from our Institutional Tissue Bank. Low-grade NHL's cytoplasmic immunoreactivity was mainly restricted to actively proliferating cells (i.e. Ki67 positive germinal centre cells), whereas high-grade NHL displayed a significantly higher expression of HSP105, measured both as intensity and percentage of positive cells (p=0.0002). In addition, malignant cells in high-grade NHL more often displayed a specific cell-surface staining. Interestingly, the expression pattern and intensity of HSP105 was widely superimposable on that of the proliferation marker Ki67, as detected by the specific monoclonal Ab Mib-1. Lastly, the therapeutic effects of HSP105 functional inhibition was studied in Namalwa BL xenotransplanted SCID mice using a specific commercial Ab. Treated mice showed a significant delay in tumor growth compared to untreated control animals (p=0.0014). Taken as a whole, our results indicate that HSP105 could be a new potential biotarget for the treatment of NHL and a novel candidate biomarker for an improved management of B-cell lymphoma. Its location on the normal B cell surface, and its increasing expression with NHL aggressiveness open a new area in which to assess its role in B-cell biology and lymphoma physiopathology. Disclosures: No relevant conflicts of interest to declare.

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Liman, Narin, and Murat Kuzkale. "Heat shock proteins exhibit distinct spatiotemporal expression patterns in the domestic cat (." Reproduction, Fertility and Development 34, no. 6 (February 4, 2022): 498–515. http://dx.doi.org/10.1071/rd21155.

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Heat shock proteins (HSP) are significant regulators of cell proliferation, differentiation and apoptosis. HSP participate in ovarian physiology through proliferative and apoptotic mechanisms and the modulation of sex steroid receptor functions. We investigated whether the expression and localisation patterns of HSP in the domestic cat ovary vary with the oestrous cycle stage. Immunohistochemical analysis revealed cell type-specific localisation patterns of HSPD1/HSP60, HSPA/HSP70, HSPC/HSP90 and HSPH/HSP105 in several ovarian cells of the domestic cat, including oocytes, follicular (granulosa and theca cells) and luteal cells, stromal and thecal interstitial cells, stromal cells, and vascular endothelial and smooth muscle cells during the anoestrous, follicular and luteal phases of the oestrous cycle. Western blot results showed that the expression of three HSP (HSPD1/HSP60, HSPA/HSP70 and HSPH/HSP105) varied with the oestrous cycle stage. While the maximal expression of HSPD1/HSP60 and HSPH/HSP105 occurred during the luteal phase, the expression of HSPA/HSP70 was minimal. The expressions of HSPA/HSP70 and HSPH/HSP105 were low during the follicular phase compared to the anoestrous phase. In conclusion, the alterations that occur in the expression of HSP in the domestic cat ovary during the different stages of the oestrous cycle imply that these proteins participate in the regulation of ovarian function under different physiological conditions.

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Zhang, Yang, Xing-Hui Cai, Rong-Jun Zhang, Xiao-Rong Hou, Xiao-Ge Song, Sheng-Bing Wu, Shuang Yu, and Jiang-Peng Cao. "Acupuncture Regulates the Unfolded Protein Response and Inhibits Apoptosis in a Rat Model of Heroin Relapse." Acupuncture in Medicine 34, no. 6 (December 2016): 441–48. http://dx.doi.org/10.1136/acupmed-2015-010954.

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Object To explore the unfolded protein response (UPR) in the hippocampus of rats undergoing heroin relapse and the mechanisms underlying the acupuncture-mediated inhibition of brain damage caused by heroin relapse. Methods 60 Sprague-Dawley rats (30 females and 30 males) were randomly divided into four groups: Control group, Heroin group, Heroin+acupuncture group, and Heroin+methadone group (n=15 each). In the latter three groups, a model of heroin addiction was established by successive increments of intramuscular heroin injections for 8 days, according to the exposure (addiction)→detoxification method. A UPR RT2 Profiler PCR array was used to screen for differentially expressed genes in the hippocampus. Apoptosis was detected by terminal deoxynucleotidyl transferase dUTP nick end labelling (TUNEL) staining. The protein expression levels of the following three differentially expressed genes were detected by Western blot to validate the results of the PCR array: heat shock protein (HSP)70, HSP105, and valosin-containing protein (Vcp). Results The UPR RT2 Profiler PCR Array detection results indicated that acupuncture increased the expression levels of the molecular chaperones HSP70, HSP105, and Vcp. The degree of neuronal apoptosis in the hippocampus of rats in the Heroin+acupuncture and Heroin+methadone groups was significantly reduced compared with the untreated Heroin group (p<0.01). Protein expression of HSP70, HSP105, and Vcp in the Heroin+acupuncture and Heroin+methadone groups was significantly higher than the Heroin group (p<0.01). Conclusions The positive effects of acupuncture on brain damage caused by heroin may be closely related to up-regulation of HSP70, HSP105, and Vcp, and reduced apoptosis.

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Mchaourab, Hassane S., Yi-Lun Lin, and Benjamin W. Spiller. "Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5." Biochemistry 51, no. 25 (June 15, 2012): 5105–12. http://dx.doi.org/10.1021/bi300525x.

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Vlachonasios, Konstantinos E., Dina K. Kadyrzhanova, and David R. Dilley. "Application of Gene-specific mRNA Differential Display for Identification of cDNAs that Encode Small HSPs Correlated with the Heat-induced Chilling Tolerance of Tomato Fruit." HortScience 32, no. 3 (June 1997): 498D—498. http://dx.doi.org/10.21273/hortsci.32.3.498d.

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Heat-treatment of mature-green tomato fruit (Lycopersicon esculentum) for 48 h at 42°C has been shown to prevent chilling injury from developing after 2 or 3 weeks at 2°C. Using mRNA differential display, we recently cloned and characterized a cDNA that encodes a cytosolic class II small heat-shock protein (Le HSP17.6). The mRNA of Le HSP17.6 is up-regulated during heat shock and the level of transcription remains high during subsequent storage at chilling temperatures. We used mRNA differential display with gene-specific primers from the other small HSPs families and find that the transcription of the other small heat-shock proteins is up-regulated during heat shock and persists at elevated levels at 2°C for at least 2 weeks. When the fruits are returned to a permissive ripening temperature after the chilling period, the mRNA of the small HSPs declines slowly for 3 days. These results suggest that the persistence of the small heat-shock proteins at low temperatures may provide protection against chilling injury.

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Ao-Neng, CAO, WANG Wei-Xue, YUWEN Tai-Ran, DENG Wei, and LAI Lu-Hua. "Inhibition of Amyloid Fibrillization and Dissociation of Matured Amyloid Fibrils by Mj HSP16.5." Acta Physico-Chimica Sinica 26, no. 07 (2010): 2015–20. http://dx.doi.org/10.3866/pku.whxb20100708.

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Bettey, Mary, and W. E. Finch-Savage. "Stress protein content of mature Brassica seeds and their germination performance." Seed Science Research 8, no. 3 (September 1998): 347–55. http://dx.doi.org/10.1017/s096025850000427x.

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AbstractPlants respond to sub-optimal conditions by the synthesis of specific ‘stress’ proteins, and these are thought to play a role in stress tolerance. Some of these proteins accumulate during late seed development, arguably to protect against damage during post-maturation drying and subsequent imbibition, prior to germination. Seed vigour is also determined during this late stage of seed development. High vigour seeds are those that can withstand the desiccation required for storage and successfully germinate under sub-optimal conditions to establish healthy seedlings. If stress proteins are involved in tolerating stress conditions, then they are likely to be important determinants of seed vigour. In this work the relationship between seed vigour (measured by seed germination performance following rapid aging, or under water stress) in Brassica oleracea var. capitata and the content of two classes of stress protein (dehydrins and a low molecular weight heat shock protein HSP17.6) at maturity was examined. Dehydrins did not show a positive relationship with seed performance. However, the protein HSP17.6 showed a positive correlation with seed performance, and a treatment that reduced the amount of this protein in the seed also caused a reduction in subsequent seed performance.

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Han, Dong, and Huang Xu. "Cloning, expression, purification and characterization of HSP105." Cell Biology International 34, no. 8 (August 1, 2010): S46. http://dx.doi.org/10.1042/cbi034s046a.

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Xie, Jia, Xing‐Xing Hu, Meng‐Fan Zhai, Xiao‐Juan Yu, Xiao‐Wen Song, Shan‐Shan Gao, Wei Wu, and Bin Li. "Characterization and functional analysis of hsp18.3 gene in the red flour beetle, Tribolium castaneum." Insect Science 26, no. 2 (December 7, 2017): 263–73. http://dx.doi.org/10.1111/1744-7917.12543.

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Nandi, Sandip Kumar, Ayon Chakraborty, Alok Kumar Panda, and Ashis Biswas. "Conformational perturbation, hydrophobic interactions and oligomeric association are responsible for the enhanced chaperone function of Mycobacterium leprae HSP18 under pre-thermal condition." RSC Advances 6, no. 67 (2016): 62146–56. http://dx.doi.org/10.1039/c6ra00167j.

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Hayakawa, Toshihiko, Toru Kudo, Takashi Ito, Nobuyuki Takahashi, and Tomoyuki Yamaya. "ACT Domain Repeat Protein 7, ACR7, Interacts with a Chaperone HSP18.0-CII in Rice Nuclei." Plant and Cell Physiology 47, no. 7 (July 2006): 891–904. http://dx.doi.org/10.1093/pcp/pcj062.

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Koteiche, Hanane A., and Hassane S. Mchaourab. "The determinants of the oligomeric structure in Hsp16.5 are encoded in the α-crystallin domain." FEBS Letters 519, no. 1-3 (April 19, 2002): 16–22. http://dx.doi.org/10.1016/s0014-5793(02)02688-1.

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Xi, Dong, Ping Wei, Changsheng Zhang, and Luhua Lai. "The minimal α-crystallin domain of Mj Hsp16.5 is functional at non-heat-shock conditions." Proteins: Structure, Function, and Bioinformatics 82, no. 7 (December 6, 2013): 1156–67. http://dx.doi.org/10.1002/prot.24480.

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Savic, Jelena, Ivana Dragicevic, D. Pantelic, Jasmina Oljaca, and Ivana Momcilovic. "Expression of small heat shock proteins and heat tolerance in potato (Solanum tuberosum L.)." Archives of Biological Sciences 64, no. 1 (2012): 135–44. http://dx.doi.org/10.2298/abs1201135s.

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We have examined the correlation between heat tolerance and small heat shock protein (sHSP) expression under heat stress conditions in potato (Solanum tuberosum L.). The relative heat tolerance of nine potato cultivars grown under greenhouse conditions was determined using the electrolyte leakage assay (ELA), a standard quantitative assay for heat tolerance. Three cultivars differing in heat tolerance were selected and designated as heat-tolerant (?Laura?), moderately sensitive (?Liseta?) and heat-sensitive (?Agria?) genotypes. The expression of cytosolic HSP18 and chloroplast HSP21 was analyzed at the protein level in the leaves of selected cultivars, both ex vitro- and in vitro-grown, after heat stress or control treatment. Immunoblot analysis revealed heat-induced HSP18 and HSP21 expression in all examined genotypes. A similar pattern of examined sHSP expression was observed ex vitro and in vitro: heat-tolerant ?Laura? accumulated higher levels of both HSP18 and HSP21 compared to heat-sensitive ?Liseta? and ?Agria?. Our results indicate that ELA combined with immunoblot analysis of sHSP accumulation under HS conditions, might be considered as a reliable procedure in screening potato genotypes for heat tolerance. To our knowledge, this is the first study where sHSP expression between ex vitro- and in vitro-grown potato plants was compared.

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Mangas, Kirstie M., Nicholas J. Tobias, Estelle Marion, Jérémie Babonneau, Laurent Marsollier, Jessica L. Porter, Sacha J. Pidot, et al. "High antibody titres induced by protein subunit vaccines using Mycobacterium ulcerans antigens Hsp18 and MUL_3720 with a TLR-2 agonist fail to protect against Buruli ulcer in mice." PeerJ 8 (August 7, 2020): e9659. http://dx.doi.org/10.7717/peerj.9659.

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Background Mycobacterium ulcerans is the causative agent of a debilitating skin and soft tissue infection known as Buruli ulcer (BU). There is no vaccine against BU. The purpose of this study was to investigate the vaccine potential of two previously described immunogenic M. ulcerans proteins, MUL_3720 and Hsp18, using a mouse tail infection model of BU. Methods Recombinant versions of the two proteins were each electrostatically coupled with a previously described lipopeptide adjuvant. Seven C57BL/6 and seven BALB/c mice were vaccinated and boosted with each of the formulations. Vaccinated mice were then challenged with M. ulcerans via subcutaneous tail inoculation. Vaccine performance was assessed by time-to-ulceration compared to unvaccinated mice. Results The MUL_3720 and Hsp18 vaccines induced high titres of antigen-specific antibodies that were predominately subtype IgG1. However, all mice developed ulcers by day-40 post-M. ulcerans challenge. No significant difference was observed in the time-to-onset of ulceration between the experimental vaccine groups and unvaccinated animals. Conclusions These data align with previous vaccine experiments using Hsp18 and MUL_3720 that indicated these proteins may not be appropriate vaccine antigens. This work highlights the need to explore alternative vaccine targets and different approaches to understand the role antibodies might play in controlling BU.

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Lini, Nirmala, Nallakandy Panangadan Shankernarayan, and Kuppamuthu Dharmalingam. "Quantitative real-time PCR analysis of Mycobacterium leprae DNA and mRNA in human biopsy material from leprosy and reactional cases." Journal of Medical Microbiology 58, no. 6 (June 1, 2009): 753–59. http://dx.doi.org/10.1099/jmm.0.007252-0.

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Mycobacterium leprae, the causative agent of leprosy, is uncultivable in defined media. Development of new diagnostic tools which do not depend on growth of bacteria is needed for the early detection of M. leprae and for monitoring the effectiveness of chemotherapy. We used a real-time PCR-based assay to quantify the copy number of bacterial DNA and hsp18 mRNA from 47 leprosy patients using paraffin-embedded biopsy samples. The assay used was specific, sensitive and reproducible. The applicability of this approach in monitoring the chemotherapy of leprosy was examined. A reduction in DNA and mRNA during chemotherapy was observed and hsp18 mRNA could not be detected in patients who underwent 2 years of multidrug therapy (MDT). However, a considerable amount of M. leprae DNA could be detected even after 2 years of MDT. A significant amount of hsp18 mRNA was found in reactional cases as well. This raises important questions regarding the role of bacterial antigens in leprosy reactions and the rationale of omitting antibiotics in the treatment of reactional cases. Results in this study show that real-time PCR could be a better tool for the careful monitoring of bacillary DNA and mRNA in lesions, which will help to improve diagnosis, disease progression and the treatment regimen.

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Zhao, Shanmin, Jieran Shi, Caiqin Zhang, Yong Zhao, Fengfeng Mao, Wei Yang, Bing Bai, Hai Zhang, Changhong Shi, and Zhikai Xu. "Monoclonal Antibodies Against a Mycobacterium tuberculosis Ag85B-Hsp16.3 Fusion Protein." Hybridoma 30, no. 5 (October 2011): 427–32. http://dx.doi.org/10.1089/hyb.2011.0047.

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Rauch, Jennifer N., and Jason E. Gestwicki. "Binding of Human Nucleotide Exchange Factors to Heat Shock Protein 70 (Hsp70) Generates Functionally Distinct Complexes in Vitro." Journal of Biological Chemistry 289, no. 3 (December 5, 2013): 1402–14. http://dx.doi.org/10.1074/jbc.m113.521997.

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Proteins with Bcl2-associated anthanogene (BAG) domains act as nucleotide exchange factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70). There are six BAG family NEFs in humans, and each is thought to link Hsp70 to a distinct cellular pathway. However, little is known about how the NEFs compete for binding to Hsp70 or how they might differentially shape its biochemical activities. Toward these questions, we measured the binding of human Hsp72 (HSPA1A) to BAG1, BAG2, BAG3, and the unrelated NEF Hsp105. These studies revealed a clear hierarchy of affinities: BAG3 > BAG1 > Hsp105 ≫ BAG2. All of the NEFs competed for binding to Hsp70, and their relative affinity values predicted their potency in nucleotide and peptide release assays. Finally, we combined the Hsp70-NEF pairs with cochaperones of the J protein family (DnaJA1, DnaJA2, DnaJB1, and DnaJB4) to generate 16 permutations. The activity of the combinations in ATPase and luciferase refolding assays were dependent on the identity and stoichiometry of both the J protein and NEF so that some combinations were potent chaperones, whereas others were inactive. Given the number and diversity of cochaperones in mammals, it is likely that combinatorial assembly could generate a large number of distinct permutations.

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Saito, Youhei, Nobuyuki Yamagishi, and Takumi Hatayama. "Different localization of Hsp105 family proteins in mammalian cells." Experimental Cell Research 313, no. 17 (October 2007): 3707–17. http://dx.doi.org/10.1016/j.yexcr.2007.06.009.

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Xing, Jinpeng, Yan Xu, Jiang Tian, Thomas Gianfagna, and Bingru Huang. "Suppression of Shade- or Heat-induced Leaf Senescence in Creeping Bentgrass through Transformation with the ipt Gene for Cytokinin Synthesis." Journal of the American Society for Horticultural Science 134, no. 6 (November 2009): 602–9. http://dx.doi.org/10.21273/jashs.134.6.602.

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Cytokinins have been associated with delaying or suppressing leaf senescence in plants. The objectives of this study were to determine whether the expression of the ipt gene that encodes adenine isopentenyltransferase would delay leaf senescence induced by shade or heat stress in a perennial grass species. Creeping bentgrass (Agrostis stolonifera cv. Penncross) was transformed with ipt isolated from agrobacterium (Agrobacterium tumefaciens) using two gene constructs (SAG12-ipt and HSP18-ipt) designed to activate cytokinin synthesis during shade or heat stress. Whole plants of nine SAG12-ipt transgenic lines and the nontransgenic control plants were incubated in darkness at 20 °C for 20 days. Chlorophyll content of all transgenic lines and the control line decreased after dark treatment, but the decline was less pronounced in transgenic lines. All transgenic lines had higher isopentenyladenine (iP/iPA) content than the control line after 20 days of treatment. In six of the transgenic lines, iP/iPA content remained the same or higher after dark treatment. Whole plants of nine HSP18-ipt transgenic lines and the control plants were incubated at 35 °C for 7 days. Chlorophyll and iP/iPA content declined in the control plants, but the nine transgenic lines had a significantly higher concentration of iP/iPA and were able to maintain chlorophyll content at the prestress level. Our results suggest that expression of SAG12-ipt or HSP18-ipt in creeping bentgrass resulted in increases in cytokinin production, which may have led to the delay and suppression of leaf senescence induced by shade or heat stress.

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Atkinson, Burr G., Ling Liu, Ing Swie Goping, and David B. Walden. "Expression of the genes encoding hsp73, hsp18, and ubiquitin in radicles of heat-shocked maize seedlings." Genome 31, no. 2 (January 15, 1989): 698–704. http://dx.doi.org/10.1139/g89-127.

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Radicles of intact 5-day-old maize (cv. OH43) seedlings exposed to a rapid, short-term elevation (2 h) in environmental (25 to 42.5 °C) temperature exhibit new and (or) enhanced synthesis of a specific set of proteins, the so-called heat shock proteins (hsps), with molecular masses of 108 000, 89 000, 84 000, 76 000, 73 000, 30 000, 23 000, and 18 000. Continuous exposure of intact seedlings to this elevated temperature results in a depression in the synthesis of these hsps after 8 – 12 h and a shift in the pattern of the proteins synthesized to one that resembles those proteins synthesized by radicles from seedlings grown at 25 °C. The transient synthesis of hsp73 and the hsp18 family in radicles from seedlings exposed to, and maintained at, an elevated temperature correlates with the levels of hsp73 and hsp18 mRNAs associated with their polyribosomes. The heat shock induced accumulation of these hsp mRNAs occurs concomitantly with a fourfold increase in polyribosome-associated ubiquitin mRNAs. However, unlike the transient association of hsp73 and hsp18 mRNAs with polyribosomes in radicles from seedlings maintained at 42.5 °C (8 – 12 h), the level of uniquitin mRNAs associated with polyribosomes does not return to a steady-state control (25 °C) level for at least 24 h. The marked, rapid increase in the level of ubiquitin mRNAs associated with polyribosomes in radicles from heat-shocked seedlings provides the first evidence implicating ubiquitin as a heat shock protein of plants.Key words: heat Shock, heat shock proteins, ubiquitin, maize.

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Marmiroli, Nelson, Angelo Pavesi, Gabriella Di Cola, Hans Hartings, Giovanna Raho, Maria Rosaria Conte, and Carla Perrotta. "Identification, characterization, and analysis of cDNA and genomic sequences encoding two different small heat shock proteins in Hordeum vulgare." Genome 36, no. 6 (December 1, 1993): 1111–18. http://dx.doi.org/10.1139/g93-148.

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In vitro translation of mRNAs prepared from barley (Hordeum vulgare) seedlings (cv. Onice) exposed at 40 °C directed the synthesis of major heat shock proteins (HSPs) with molecular masses of 80–90, 70, 42 and 16–22 kDa. A cDNA library prepared from the 40 °C mRNAs and screened by differential hybridization led to the isolation of heat shock specific sequences. One of these (Hv hsp18) was confirmed by hybrid-arrested and hybrid-released translation as encoding for an 18-kDa HSP. The barley hsp18 sequence has an open reading frame encoding a 160 amino acid residue 18-kDa protein that is 63% identical to wheat 16.9-kDa HSP (clone C5-8), 54% identical to soybean (Glycine max) 17.5-kDa HSP, and 49% identical to Arabidopsis thaliana 17.6-kDa HSP. Lower similarities were found with class II plant small HSPs such as soybean 17.9-kDa HSP (27%), Pisum sativum 17.7-kDa HSP (30%), wheat (Triticum aestivum) 17.3-kDa HSP (clone Ta hsp 17.3) (30%), and with animal small HSPs and α-crystallins. The Hv hsp18 sequence was used to pick up Hv hsp17 genomic sequence encoding for another class I 17-kDa HSP. By computer analysis of the nucleotide sequence the TATA box, two heat shock promoter elements, a metal-ion response element, and the polyadenylation signals were identified. Barley HSP 18 has an additional cysteine-rich region when compared with HSP17 mapping at the carboxy terminal end.Key words: barley, cDNA, genomic clone, heat shock, nucleotide sequence, small heat shock proteins.

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Korber, Philipp, Jennifer M. Stahl, Knud H. Nierhaus, and James C. A. Bardwell. "Hsp15: a ribosome-associated heat shock protein." EMBO Journal 19, no. 4 (February 15, 2000): 741–48. http://dx.doi.org/10.1093/emboj/19.4.741.

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Maitre, Magali, Stéphanie Weidmann, Aurélie Rieu, Daphna Fenel, Guy Schoehn, Christine Ebel, Jacques Coves, and Jean Guzzo. "The oligomer plasticity of the small heat-shock protein Lo18 from Oenococcus oeni influences its role in both membrane stabilization and protein protection." Biochemical Journal 444, no. 1 (April 26, 2012): 97–104. http://dx.doi.org/10.1042/bj20120066.

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The ability of the small Hsp (heat-shock protein) Lo18 from Oenococcus oeni to modulate the membrane fluidity of liposomes or to reduce the thermal aggregation of proteins was studied as a function of the pH in the range 5–9. We have determined by size-exclusion chromatography and analytical ultracentrifugation that Lo18 assembles essentially as a 16-mer at acidic pH. Its quaternary structure evolves to a mixture of lower molecular mass oligomers probably in dynamic equilibrium when the pH increases. The best Lo18 activities are observed at pH 7 when the particle distribution contains a major proportion of dodecamers. At basic pH, particles corresponding to a dimer prevail and are thought to be the building blocks leading to oligomerization of Lo18. At acidic pH, the dimers are organized in a double-ring of stacked octamers to form the 16-mer as shown by the low-resolution structure determined by electron microscopy. Experiments performed with a modified protein (A123S) shown to preferentially form dimers confirm these results. The α-crystallin domain of Methanococcus jannaschii Hsp16.5, taken as a model of the Lo18 counterpart, fits with the electron microscopy envelope of Lo18.

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Fodor, Dávid, Éva Pozsgai, Andrew V. Schally, Zoltán László, Éva Gömöri, Éva Szabó, László Rumi, Dorottya Lőcsei, Árpád Boronkai, and Szabolcs Bellyei. "Expression Levels of GHRH-Receptor, pAkt and Hsp90 Predict 10-Year Overall Survival in Patients with Locally Advanced Rectal Cancer." Biomedicines 11, no. 3 (February 27, 2023): 719. http://dx.doi.org/10.3390/biomedicines11030719.

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Background: Rectal cancer constitutes nearly one-third of all colorectal cancer diagnoses, and certain clinical and molecular markers have been studied as potential prognosticators of patient survival. The main objective of our study was to investigate the relationship between the expression intensities of certain proteins, including growth-hormone-releasing hormone receptor (GHRH-R), Hsp90, Hsp16.2, p-Akt and SOUL, in specimens of locally advanced rectal cancer patients, as well as the time to metastasis and 10-year overall survival (OS) rates. We also investigated whether these outcome measures were associated with the presence of other clinical parameters. Methods: In total, 109 patients were investigated retrospectively. Samples of pretreatment tumors were stained for the proteins GHRH-R, Hsp90, Hsp16.2, p-Akt and SOUL using immunhistochemistry methods. Kaplan–Meier curves were used to show the relationships between the intensity of expression of biomarkers, clinical parameters, the time to metastasis and the 10-year OS rate. Results: High levels of p-Akt, GHRH-R and Hsp90 were associated with a significantly decreased 10-year OS rate (p = 0.001, p = 0.000, p = 0.004, respectively) and high expression levels of p-Akt and GHRH-R were correlated with a significantly shorter time to metastasis. Tumors localized in the lower third of the rectum were linked to both a significantly longer time to metastasis and an improved 10-year OS rate. Conclusions: Hsp 90, pAkt and GHRH-R as well as the lower-third localization of the tumor were predictive of the 10-year OS rate in locally advanced rectal cancer patients. The GHRH-R and Hsp90 expression levels were independent prognosticators of OS. Our results imply that GHRH-R could play a particularly important role both as a molecular biomarker and as a target for the anticancer treatment of advanced rectal cancer.

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Hatayama, T., K. Ishihara, and K. Yasuda. "Mammalian stress protein HSP105 is phosphorylated by casein kinase II." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A411. http://dx.doi.org/10.1042/bst028a411.

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Chen, Y., J. An, Y. Ding, H. Dai, Q. Mao, L. Feng, B. Liu, et al. "Preliminary X-Ray Crystallographic Studies Of The Mycobacterium Tuberculosis Hsp16.3 Molecular Chaperone." Protein & Peptide Letters 8, no. 6 (December 1, 2001): 499–502. http://dx.doi.org/10.2174/0929866013409111.

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Chang, Yong, Xuemei Li, and Zihe Rao. "A preliminary study on functional domains of small heat shock protein Hsp16.3 *." Progress in Natural Science 14, no. 1 (January 1, 2004): 21–25. http://dx.doi.org/10.1080/10020070412331343081.

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Park, Hanseul, Joohee Lee, and Yeh-Jin Ahn. "Heterologously expressed carrot Hsp17.7 was denatured by ATP treatment under abiotic stress." Biocatalysis and Agricultural Biotechnology 15 (July 2018): 240–44. http://dx.doi.org/10.1016/j.bcab.2018.06.020.

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Journal articles on the topic 'HSP18.5'

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