Journal articles: 'Hsp60 and Hsp70'

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Tiwari, Shraddha, Raman Thakur, and Jata Shankar. "Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi." Biotechnology Research International 2015 (December 31, 2015): 1–11. http://dx.doi.org/10.1155/2015/132635.

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Stress (biotic or abiotic) is an unfavourable condition for an organism including fungus. To overcome stress, organism expresses heat-shock proteins (Hsps) or chaperons to perform biological function. Hsps are involved in various routine biological processes such as transcription, translation and posttranslational modifications, protein folding, and aggregation and disaggregation of proteins. Thus, it is important to understand holistic role of Hsps in response to stress and other biological conditions in fungi. Hsp104, Hsp70, and Hsp40 are found predominant in replication and Hsp90 is found in transcriptional and posttranscriptional process. Hsp90 and Hsp70 in combination or alone play a major role in morphogenesis and dimorphism. Heat stress in fungi expresses Hsp60, Hsp90, Hsp104, Hsp30, and Hsp10 proteins, whereas expression of Hsp12 protein was observed in response to cold stress. Hsp30, Hsp70, and Hsp90 proteins showed expression in response to pH stress. Osmotic stress is controlled by small heat-shock proteins and Hsp60. Expression of Hsp104 is observed under high pressure conditions. Out of these heat-shock proteins, Hsp90 has been predicted as a potential antifungal target due to its role in morphogenesis. Thus, current review focuses on role of Hsps in fungi during morphogenesis and various stress conditions (temperature, pH, and osmotic pressure) and in antifungal drug tolerance.

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Gurer, Cagan, Andrea Cimarelli, and Jeremy Luban. "Specific Incorporation of Heat Shock Protein 70 Family Members into Primate Lentiviral Virions." Journal of Virology 76, no. 9 (May 1, 2002): 4666–70. http://dx.doi.org/10.1128/jvi.76.9.4666-4670.2002.

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ABSTRACT To determine if any heat shock proteins are incorporated into human immunodeficiency virus type 1 (HIV-1) virions in a manner similar to that of the peptidyl-prolyl isomerase cyclophilin A, we probed purified virions with antibodies against heat shock proteins Hsp27, Hsp40, Hsp60, Hsp70, Hsc70, and Hsp90. Of these proteins, Hsp60, Hsp70, and Hsc70 associated with virions purified based on either particle density or size and were shown to be incorporated within the virion membrane, where they were protected from digestion by exogenous protease. Virion incorporation of Hsp70 was also observed with HIV-2 and with simian immunodeficiency viruses SIVMAC and SIVAGM, but it appears to be specific for primate lentiviruses, since Hsp70 was not detected in association with Moloney murine leukemia virus virions. Of the HIV-1 genes, gag was found to be sufficient for Hsp70 incorporation, though Hsp70 was roughly equimolar with pol-encoded proteins in virions.

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Ziegert, M., S. S. Witkin, I. Sziller, H. Alexander, E. Brylla, and W. Härtig. "Heat Shock Proteins and Heat Shock Protein-Antibody Complexes in Placental Tissues." Infectious Diseases in Obstetrics and Gynecology 7, no. 4 (1999): 180–85. http://dx.doi.org/10.1155/s1064744999000307.

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Objective:The relationship between pregnancy outcome and expression of the heat shock proteins (hsps) or hsp-antibody complexes of 60kD (hsp60), 70kD (hsp70), and 90kD (hsp90) in placental tissue and circulating antibodies to hsps was evaluated.Method:Expression of hsp60, hsp70, and hsp90 in placentae from 12 women with preterm birth, eight with intrauterine growth restriction (IUGR), and 10 with term birth, as well as the presence of the corresponding antibodies, was investigated by a new carbocyanine double fluorescence technique. Results were compared with microbiological findings and circulating antibodies to hsps in sera.Results:In each placental specimen examined, hsp60, hsp70, and hsp90 were identified. However, hsp70-antibody complexes were detected in only four of the preterm labor cases. Similarly, hsp60-antibody complexes were detected in only five preterm labor patients and in one patient with IUGR. None of the placentae contained hsp90-antibody complexes. In the preterm birth group, all patients with hsp60-antibody complexes were also positive for circulating antibodies to hsp60. The presence of hsp70-antibody complexes also correlated with hsp70 antibody in sera.Conclusions:Formation of hsp60- and hsp70-antibody complexes in the placenta may contribute to the induction of preterm birth. Women sensitized to these antibodies may be at increased risk for adverse pregnancy outcome. Infect. Dis. Obstet. Gynecol. 7:180–185, 1999.

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Alexiou, George A., George Vartholomatos, Kalliopi Stefanaki, Amalia Patereli, Lefkothea Dova, Achilleas Karamoutsios, George Lallas, George Sfakianos, Maria Moschovi, and Neofytos Prodromou. "Expression of heat shock proteins in medulloblastoma." Journal of Neurosurgery: Pediatrics 12, no. 5 (November 2013): 452–57. http://dx.doi.org/10.3171/2013.7.peds1376.

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Object Medulloblastoma (MB) is the most common malignant brain tumor in children. Heat shock proteins (HSPs) comprise a superfamily of proteins that serve as molecular chaperones and are overexpressed in a wide range of human cancers. The purpose of the present study was to investigate the expression of HSP27 (pSer82), HSP27 (pSer15), HSP40, HSP60, HSP70, HSP90-α, Akt, and phospho-Akt by multiplex bead array assay of MBs. The results of HSP and Akt expression were correlated with MB subtype; immunohistochemical expression of Ki-67 index, bcl-2, and p53; and patients' prognosis. Methods The authors retrospectively evaluated 25 children with MB who underwent surgery. Immunohistochemical analysis of Ki-67, p53, and bcl-2 expression was performed in all cases. By using multiplex bead array assay, a simultaneous detection of HSP27 (pSer82), HSP27 (pSer15), HSP40, HSP60, HSP70, HSP90-α, Akt, and phospho-Akt was performed. Results Medulloblastoma with extensive nodularity had significantly lower HSP27 (pSer15) expression (p = 0.039) but significantly higher HSP60 expression (p = 0.021) than classic MB. Large-cell MB had significantly higher HSP70 expression (p = 0.028) than classic MB. No significant difference was found between HSP27 (pSer82), HSP40, HSP90-α, Akt, or phospho-Akt expression and MB subtype. Large-cell MBs had significantly higher Ki-67 index compared with classic MBs (p = 0.033). When analyzing all MBs, there was a significant negative correlation between HSP27 (pSer15) and Ki-67 index (r = −0.475, p = 0.016); a significant positive correlation between HSP70 expression and Ki-67 index (r = 0.407, p = 0.043); and a significant positive correlation between HSP70 expression and bcl-2 index (r = 0.491, p = 0.023). Patients with large-cell MB had a worse survival than those with classic MB, but the difference did not reach statistical significance (p = 0.076). Conclusions A substantial expression of several HSPs in MB was observed. Given that HSPs represent an attractive strategy for anticancer therapy, further studies, involving larger series of patients, are obviously necessary to clarify the relationship of HSPs with tumor aggressiveness and prognosis.

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Pitruzzella, Alessandro, Letizia Paladino, Alessandra Vitale, Stefania Martorana, Calogero Cipolla, Giuseppa Graceffa, Daniela Cabibi, et al. "Quantitative Immunomorphological Analysis of Heat Shock Proteins in Thyroid Follicular Adenoma and Carcinoma Tissues Reveals Their Potential for Differential Diagnosis and Points to a Role in Carcinogenesis." Applied Sciences 9, no. 20 (October 15, 2019): 4324. http://dx.doi.org/10.3390/app9204324.

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Hsp27, Hsp60, Hsp70, and Hsp90 are chaperones that play a crucial role in cellular homeostasis and differentiation, but they may be implicated in carcinogenesis. Follicular neoplasms of the thyroid include follicular adenoma and follicular carcinoma. The former is a very frequent benign encapsulated nodule, whereas the other is a nodule that infiltrates the capsule, blood vessels and the adjacent parenchyma, with a tendency to metastasize. The main objective was to assess the potential of the Hsps in differential diagnosis and carcinogenesis. We quantified by immunohistochemistry Hsp27, Hsp60, Hsp70, and Hsp90 on thin sections of human thyroid tissue with follicular adenoma or follicular carcinoma, comparing the tumor with the adjacent peritumoral tissue. Hsp60, Hsp70, and Hsp90 were increased in follicular carcinoma compared to follicular adenoma, while Hsp27 showed no difference. Histochemical quantification of Hsp60, Hsp70, and Hsp90 allows diagnostic distinction between follicular adenoma and carcinoma, and between tumor and adjacent non-tumoral tissue. The quantitative variations of these chaperones in follicular carcinoma suggest their involvement in tumorigenesis, for instance in processes such as invasion of thyroid parenchyma and metastasization.

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Cheng, Yunfeng, Yong Tang, and Neal S. Young. "T Cells Response and Autoantibodies to Human Heat Shock Proteins in Aplastic Anemia Patients." Blood 106, no. 11 (November 16, 2005): 2403. http://dx.doi.org/10.1182/blood.v106.11.2403.2403.

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Abstract Heat shock proteins (HSP) have been implicated in autoimmune diseases such as type I diabetes mellitus, systemic lupus erythematosus, and multiple sclerosis, in which T cell proliferative responses or autoantibodies towards endogenous HSP have been detected (Journal of Autoimmunity2003;20:313). HSP70 can function as an endogenous ‘danger’ signal, acting on antigen-presenting cells and critically influencing the decision between induction of tolerance and immunity upon antigen encounter (Millar et al. Nature Medicine2003; 9:1469). We studied T-cell proliferative responses and auto-antibodies to human HSP60, HSP70 and HSP90 proteins in 20 newly diagnosed aplastic anemia patients, peripheral blood was obtained (11 females, 9 males; age average 36.1±19 years). A non-isotopic immunoassay was used for BrdU incorporation into proliferative T cells and ELISA to measure HSP antibody titer. T cell proliferation was measured as the Eu-fluorescence in a time-resolved fluorometer. A positive result was defined as > 2 standard deviations (SD) from the mean of the controls. T-cell responses to HSP70 in the patient group (N=20; mean±SD Eu-fluorescence= 47,129±36,248) were significantly greater than those of the control group (N=18 healthy adult; mean Eu-fluorescence= 23,941±12,996; p=0.01). Fifty percent of the patients showed increased T cell proliferation after HSP70 stimulation compared to 5% in the control group (p=0.03). T-cell responses of the patient group to HSP90 and HSP60 were similar to those of the control group. Twenty percent of patients showed increased T cell proliferation to HSP 60 and HSP 90 stimulation compared to 5% in the control group (p=0.363). HSP antibody (IgG/A/M) seropositivity was 25% to HSP60, 50% to HSP70, and 5% to HSP90 in patients and 8% to HSP60, 0% to HSP70, and 0% to HSP90 in controls. Heightened autoimmunity to HSP70, but not to HSP60 and HSP90, is a feature of acquired aplastic anemia at presentation.

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Barutta, Federica, Silvia Pinach, Sara Giunti, Ferdinando Vittone, Josephine M. Forbes, Roberto Chiarle, Maryann Arnstein, et al. "Heat shock protein expression in diabetic nephropathy." American Journal of Physiology-Renal Physiology 295, no. 6 (December 2008): F1817—F1824. http://dx.doi.org/10.1152/ajprenal.90234.2008.

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Heat shock protein (HSP) HSP27, HSP60, HSP70, and HSP90 are induced by cellular stresses and play a key role in cytoprotection. Both hyperglycemia and glomerular hypertension are crucial determinants in the pathogenesis of diabetic nephropathy and impose cellular stresses on renal target cells. We studied both the expression and the phosphorylation state of HSP27, HSP60, HSP70, and HSP90 in vivo in rats made diabetic with streptozotocin and in vitro in mesangial cells and podocytes exposed to either high glucose or mechanical stretch. Diabetic and control animals were studied 4, 12, and 24 wk after the onset of diabetes. Immunohistochemical analysis revealed an overexpression of HSP25, HSP60, and HSP72 in the diabetic outer medulla, whereas no differences were seen in the glomeruli. Similarly, exposure neither to high glucose nor to stretch altered HSP expression in mesangial cells and podocytes. By contrast, the phosphorylated form of HSP27 was enhanced in the glomerular podocytes of diabetic animals, and in vitro exposure of podocytes to stretch induced HSP27 phosphorylation via a P38-dependent mechanism. In conclusion, diabetes and diabetes-related insults differentially modulate HSP27, HSP60, and HSP70 expression/phosphorylation in the glomeruli and in the medulla, and this may affect the ability of renal cells to mount an effective cytoprotective response.

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Caruso Bavisotto, Celeste, Calogero Cipolla, Giuseppa Graceffa, Rosario Barone, Fabio Bucchieri, Donatella Bulone, Daniela Cabibi, et al. "Immunomorphological Pattern of Molecular Chaperones in Normal and Pathological Thyroid Tissues and Circulating Exosomes: Potential Use in Clinics." International Journal of Molecular Sciences 20, no. 18 (September 11, 2019): 4496. http://dx.doi.org/10.3390/ijms20184496.

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The thyroid is a major component of the endocrine system and its pathology can cause serious diseases, e.g., papillary carcinoma (PC). However, the carcinogenic mechanisms are poorly understood and clinical useful biomarkers are scarce. Therefore, we determined if there are quantitative patterns of molecular chaperones in the tumor tissue and circulating exosomes that may be useful in diagnosis and provide clues on their participation in carcinogenesis. Hsp27, Hsp60, Hsp70, and Hsp90 were quantified by immunohistochemistry in PC, benign goiter (BG), and normal peritumoral tissue (PT). The same chaperones were assessed in plasma exosomes from PC and BG patients before and after ablative surgery, using Western blotting. Hsp27, Hsp60, and Hsp90 were increased in PC in comparison with PT and BG but no differences were found for Hsp70. Similarly, exosomal levels of Hsp27, Hsp60, and Hsp90 were higher in PC than in BG, and those in PC were higher before ablative surgery than after it. Hsp27, Hsp60, and Hsp90 show distinctive quantitative patterns in thyroid tissue and circulating exosomes in PC as compared with BG, suggesting some implication in the carcinogenesis of these chaperones and indicating their potential as biomarkers for clinical applications.

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Lebret, Thierry, R. William G. Watson, Vincent Molinié, Amanda O'Neill, Christophe Gabriel, John M. Fitzpatrick, and Henry Botto. "Heat shock proteins HSP27, HSP60, HSP70, and HSP90." Cancer 98, no. 5 (July 16, 2003): 970–77. http://dx.doi.org/10.1002/cncr.11594.

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Wu, Reen, Yu Hua Zhao, Charles G. Plopper, Mary Mann-Jong Chang, Ken Chmiel, John J. Cross, Alison Weir, Jerold A. Last, and Brian Tarkington. "Differential expression of stress proteins in nonhuman primate lung and conducting airway after ozone exposure." American Journal of Physiology-Lung Cellular and Molecular Physiology 277, no. 3 (September 1, 1999): L511—L522. http://dx.doi.org/10.1152/ajplung.1999.277.3.l511.

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The presence of seven stress proteins including various heat shock proteins [27-kDa (HSP27), 60-kDa (HSP60), 70-kDa (HSP70) and its constitutive form HSC70, and 90-kDa (HSP90) HSPs] and two glucose-regulated proteins [75-kDa (GRP75) and 78-kDa (GRP78) GRPs] in ozone-exposed lungs of nonhuman primates and in cultured tracheobronchial epithelial cells was examined immunohistochemically by various monoclonal antibodies. Heat treatment (42°C) resulted in increased HSP70, HSP60, and HSP27 and slightly increased HSC70 and GRP75 but no increase in GRP78 in primary cultures of monkey tracheobronchial epithelial cells. Ozone exposure did not elevate the expression of these HSPs and GRPs. All of these HSPs including HSP90, which was undetectable in vitro, were suppressed in vivo in monkey respiratory epithelial cells after ozone exposure. Both GRP75 and GRP78 were very low in control cells, and ozone exposure in vivo significantly elevated these proteins. These results suggest that the stress mechanism exerted on pulmonary epithelial cells by ozone is quite different from that induced by heat. Furthermore, differences between in vitro and in vivo with regard to activation of HSPs and GRPs suggest a secondary mechanism in vivo, perhaps related to inflammatory response after ozone exposure.

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MARTINEZ, J., J. PEREZ SERRANO, W. E. BERNADINA, and F. RODRIGUEZ-CAABEIRO. "Influence of parasitization by Trichinella spiralis on the levels of heat shock proteins in rat liver and muscle." Parasitology 118, no. 2 (February 1999): 201–9. http://dx.doi.org/10.1017/s0031182098003692.

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To examine levels of heat shock proteins (HSPs) in host responses to helminth infection, rats were infected with Trichinella spiralis. The kinetics of HSP25, HSP60, HSP70 and HSP90 production in the liver and muscle of infected rats was compared with that of non-infected controls. HSPs were detected using electrophoretic analysis of fixed amounts of proteins (0·02 mg) and then blotting and incubation of membranes with polyclonal anti-HSP25 antibody, or monoclonal antibody against HSP60, or HSP70 or HSP90. Quantitation of blotted separated polypeptides reactive with the specific anti-HSP antibodies was achieved using an image analyser. Enhancement of HSP25 production was observed in the liver of infected rats, whereas muscle from the same rats exhibited enhanced production of HSP25 and HSP60 one day after infection only. These data indicate that HSPs levels can be used successfully to measure stress injury brought about by helminth infection in organs and tissues of the host.

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Shevtsov, Maxim, Zsolt Balogi, William Khachatryan, Huile Gao, László Vígh, and Gabriele Multhoff. "Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets." Cells 9, no. 5 (May 20, 2020): 1263. http://dx.doi.org/10.3390/cells9051263.

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Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as molecular chaperones that play a key role in intracellular protein homeostasis, regulation of apoptosis, and protection from various stress factors (including hypoxia, thermal stress, oxidative stress). Apart from their intracellular localization, members of different HSP families such as small HSPs, HSP40, HSP60, HSP70 and HSP90 have been found to be localized on the plasma membrane of malignantly transformed cells. In the current article, the role of membrane-associated molecular chaperones in normal and tumor cells is comprehensively reviewed with implications of these proteins as plausible targets for cancer therapy and diagnostics.

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Fink, Anthony L. "Chaperone-Mediated Protein Folding." Physiological Reviews 79, no. 2 (April 1, 1999): 425–49. http://dx.doi.org/10.1152/physrev.1999.79.2.425.

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The folding of most newly synthesized proteins in the cell requires the interaction of a variety of protein cofactors known as molecular chaperones. These molecules recognize and bind to nascent polypeptide chains and partially folded intermediates of proteins, preventing their aggregation and misfolding. There are several families of chaperones; those most involved in protein folding are the 40-kDa heat shock protein (HSP40; DnaJ), 60-kDa heat shock protein (HSP60; GroEL), and 70-kDa heat shock protein (HSP70; DnaK) families. The availability of high-resolution structures has facilitated a more detailed understanding of the complex chaperone machinery and mechanisms, including the ATP-dependent reaction cycles of the GroEL and HSP70 chaperones. For both of these chaperones, the binding of ATP triggers a critical conformational change leading to release of the bound substrate protein. Whereas the main role of the HSP70/HSP40 chaperone system is to minimize aggregation of newly synthesized proteins, the HSP60 chaperones also facilitate the actual folding process by providing a secluded environment for individual folding molecules and may also promote the unfolding and refolding of misfolded intermediates.

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MARTINEZ, J., J. PEREZ-SERRANO, W. E. BERNADINA, and F. RODRIGUEZ-CAABEIRO. "Shock response induced in rat brain and spleen during primary infection with Trichinella spiralis larvae." Parasitology 118, no. 6 (June 1999): 605–13. http://dx.doi.org/10.1017/s0031182099004291.

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An infection approach was adopted for examining consequential heat shock (HS) or stress response in brain and spleen tissues from Wistar rats. Stress in this system was due to interactions with the infecting helminth, Trichinella spiralis, or its body-dwelling larval stages, or products thereof. It was argued that in the infection model used, elements effecting stress in the brain would differ from those in the spleen. HS responses were measured by quantitation of 4 levels of HS proteins (HSP25, HSP60, HSP70 and HSP90) with time, in infected and uninfected rat tissues using an assay depending on immunoblotting specifically to detect the separate HSPs and image analysis to measure HSP content. In brain and spleen tissue from uninfected rats, a continuous expression of the above HSPs was observed at levels which hardly varied throughout the experiment. In contrast, HSP25, HSP60 and HSP70 levels in infected rat tissues varied and apparently depended on ‘infection cycle’-related events. Thus, an enhanced expression of HSP25 and HSP60 and of these plus HSP70 was observed at certain, yet different, time-points during infection in rat spleen and rat brain, respectively. Interestingly, HSP90 expression in spleen tissue from infected rats versus controls, was significantly reduced throughout the experiment suggesting some important (as yet undefined) role for HSP90 in the infection cycle. These studies seem to have provided evidence for the occurrence of soluble factors causing altered HSP expression at both sides of the blood-brain barrier in rats with a primary T. spiralis infection.

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Zhang, Yilan, Norio Ohashi, and Yasuko Rikihisa. "Cloning of the Heat Shock Protein 70 (HSP70) Gene of Ehrlichia sennetsu and Differential Expression of HSP70 and HSP60 mRNA after Temperature Upshift." Infection and Immunity 66, no. 7 (July 1, 1998): 3106–12. http://dx.doi.org/10.1128/iai.66.7.3106-3112.1998.

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ABSTRACT Ehrlichia sennetsu is the causative agent of human Sennetsu ehrlichiosis. Heat shock protein 60 (HSP60) and HSP70 (DnaK) are two major bacterial HSPs, and their interaction modulates the stress response. Previously, we cloned and sequenced groEand expressed groEL of E. sennetsu. HSP60 (GroEL) was immunogenic and cross-reactive in Ehrlichiaspp. The present study was designed to (i) characterize the HSP70 gene of this organism and (ii) determine whether the expression of these two HSPs is inducible upon exposure to heat stress. A gene encoding an HSP70 homolog was isolated and sequenced from a gene library. The ehrlichial HSP70 gene encoded a 637-amino-acid protein, which had an approximate molecular mass of 68,354 Da and which was homologous to DnaK of Escherichia coli. A DNA sequence resembling −35 and −10 promoter sequences of E. coli dnaK was observed upstream of the ehrlichial HSP70 gene. Alignment of the predicted amino acid sequence with that of E. coli DnaK andBrucella, Salmonella, Borrelia,Chlamydia, and Mycobacterium HSP70s showed 63, 67, 63, 62, 58, and 53% identity, respectively. By reverse transcription-PCR analysis, the mRNA levels of ehrlichial HSP70 and HSP60 were examined after temperature shifts from 28 to 37°C and from 37 to 40°C. HSP70 mRNA induction levels were greater than those of HSP60 mRNA after a 37-to-40°C temperature shift, whereas the reverse was true after a 28-to-37°C temperature shift. Our data suggest that HSP60 and HSP70 may play different roles during transfer from vector temperature to human body temperature and during a febrile condition characteristic of ehrlichial disease. This study also provides a useful model system for examining mRNA expression in obligatory intracellular bacteria.

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Jing, Xiao-Yang, and Feng-Min Li. "Identifying Heat Shock Protein Families from Imbalanced Data by Using Combined Features." Computational and Mathematical Methods in Medicine 2020 (September 23, 2020): 1–11. http://dx.doi.org/10.1155/2020/8894478.

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Heat shock proteins (HSPs) are ubiquitous in living organisms. HSPs are an essential component for cell growth and survival; the main function of HSPs is controlling the folding and unfolding process of proteins. According to molecular function and mass, HSPs are categorized into six different families: HSP20 (small HSPS), HSP40 (J-proteins), HSP60, HSP70, HSP90, and HSP100. In this paper, improved methods for HSP prediction are proposed—the split amino acid composition (SAAC), the dipeptide composition (DC), the conjoint triad feature (CTF), and the pseudoaverage chemical shift (PseACS) were selected to predict the HSPs with a support vector machine (SVM). In order to overcome the imbalance data classification problems, the syntactic minority oversampling technique (SMOTE) was used to balance the dataset. The overall accuracy was 99.72% with a balanced dataset in the jackknife test by using the optimized combination feature SAAC+DC+CTF+PseACS, which was 4.81% higher than the imbalanced dataset with the same combination feature. The Sn, Sp, Acc, and MCC of HSP families in our predictive model were higher than those in existing methods. This improved method may be helpful for protein function prediction.

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Wasilah, Ummi, Dian A. G. Perwitasari, and Mukhamad Su'udi. "Peran Chaperone Pada Tumbuhan: Mini Review." JURNAL BIOLOGI PAPUA 11, no. 2 (October 31, 2019): 110–15. http://dx.doi.org/10.31957/jbp.880.

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Plants respond to various conditions in the surrounding environment, whether favorable conditions or vice versa. Abiotic and biotic factors affect plant responses such as temperature, humidity, salinity, insects and pathogens such as viruses and bacteria. Plants have a defense system in tolerancing stress from the surrounding environment, for example heat shock protein (HSP) is a chaperone protein that plays a role in plant defenses when experiencing stress to the temperature. HSP is classified into six families based on their molecular weight, namely HSP100, HSP90, HSP70, HSP60, HSP40, and small HSP. Each has a role in maintaining the stability of plant metabolism. HSP is especially important for correct protein refolding, preventing degradation and denaturation of protein. Key words: plants; chaperone; heat shock protein; refolding; protein denaturation.

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Chan, Julie Y. H., Hsiao-Lei Cheng, Jimmy L. J. Chou, Faith C. H. Li, Kuang-Yu Dai, Samuel H. H. Chan, and Alice Y. W. Chang. "Heat Shock Protein 60 or 70 Activates Nitric-oxide Synthase (NOS) I- and Inhibits NOS II-associated Signaling and Depresses the Mitochondrial Apoptotic Cascade during Brain Stem Death." Journal of Biological Chemistry 282, no. 7 (December 5, 2006): 4585–600. http://dx.doi.org/10.1074/jbc.m603394200.

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The cellular and molecular basis of brain stem death remains an enigma. As the origin of a “life-and-death” signal that reflects the progression toward brain stem death, the rostral ventrolateral medulla (RVLM) is a suitable neural substrate for mechanistic delineation of this phenomenon. Here, we evaluated the hypothesis that heat shock proteins (HSPs) play a neuroprotective role in the RVLM during brain stem death and delineated the underlying mechanisms, using a clinically relevant animal model that employed the organophosphate pesticide mevinphos (Mev) as the experimental insult. In Sprague-Dawley rats, proteomic, Western blot, and real-time PCR analyses demonstrated that Mev induced de novo synthesis of HSP60 or HSP70 in the RVLM without affecting HSP90 level. Loss-of-function manipulations of HSP60 or HSP70 in the RVLM using anti-serum or antisense oligonucleotide potentiated Mev-elicited cardiovascular depression alongside reduced nitric-oxide synthase (NOS) I/protein kinase G signaling, enhanced NOS II/peroxynitrite cascade, intensified nucleosomal DNA fragmentation, elevated cytoplasmic histone-associated DNA fragments or activated caspase-3, and augmented the cytochrome c/caspase-3 cascade of apoptotic signaling in the RVLM. Co-immunoprecipitation experiments further revealed a progressive increase in the complex formed between HSP60 and mitochondrial or cytosolic Bax or mitochondrial Bcl-2 during Mev intoxication, alongside a dissociation of the cytosolic HSP60-Bcl-2 complex. We conclude that HSP60 and HSP70 confer neuroprotection against Mev intoxication by ameliorating cardiovascular depression via an anti-apoptotic action in the RVLM. The possible underlying intracellular processes include enhancing NOS I/protein kinase G signaling and inhibiting the NOS II/peroxynitrite cascade. In addition, HSP60 exerts its effects against apoptosis by blunting Mev-induced activation of the Bax/cytochrome c/caspase-3 cascade.

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Kotsiopriftis, Maria, Jerome E. Tanner, and Caroline Alfieri. "Heat Shock Protein 90 Expression in Epstein-Barr Virus-Infected B Cells Promotes γδ T-Cell Proliferation In Vitro." Journal of Virology 79, no. 11 (June 1, 2005): 7255–61. http://dx.doi.org/10.1128/jvi.79.11.7255-7261.2005.

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ABSTRACT The aim of this study was to elucidate the in vitro response of γδ T cells to Epstein-Barr virus (EBV)-infected B cells and to determine whether EBV-induced heat shock proteins (HSPs) might serve as γδ T-cell stimulants. Cytofluorometric analysis revealed HSP90 cell surface expression in 12% of the EBV-immortalized B-cell population in all four of the B-cell lines tested. HSP27, HSP60, and HSP70 were not detected on the cell surface by cytofluorometry in these same B-cell lines. HSP90 and HSP60, but not HSP70 or HSP27, were detected on the cell surface after 125I cell surface labeling and immunoprecipitation with anti-human HSP monoclonal antibodies. In vitro kinetic studies indicated that γδ T cells increased at least twofold by day 11 postinfection in cultures of EBV-seronegative peripheral blood lymphocytes infected with EBV, whereas percentages of αβ T cells in these same cultures either decreased slightly or remained relatively unchanged in response to EBV infection. Addition of anti-human HSP90 monoclonal antibody to the EBV-infected lymphocyte cultures inhibited γδ T-cell expansion by 92%. The inhibition of γδ T-cell expansion by anti-HSP90 antibody was reversed upon treatment with exogenous HSP90. Taken together, these results indicate that HSP90 played an important role in the stimulation of γδ T cells during EBV infection of B cells in vitro and may serve as an important immunomodulator of γδ T cells during acute EBV infection.

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Finger, John W., Meghan D. Kelley, Yufeng Zhang, Matthew T. Hamilton, Ruth M. Elsey, Mary T. Mendonca, and Andreas Kavazis. "Short-term capture stress and its effects on corticosterone levels and heat shock proteins in captive American Alligators (Alligator mississippiensis)." Canadian Journal of Zoology 99, no. 8 (August 2021): 665–71. http://dx.doi.org/10.1139/cjz-2021-0014.

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Heat shock proteins (HSPs) are important mediators of the normal cellular function and the cellular stress response. As such, HSPs are often utilized to measure the effects of stressors on organisms in vivo. However, multiple variables can influence their expression, including time or season, confounding results. To investigate the utility of HSPs in measuring effects of stressors in a top-trophic carnivore, we captured 20 American Alligators (Alligator mississippiensis (Daudin, 1802)), placed them in burlap sacks for 2 h and collected blood samples over four time points (baseline, 1 and 2 h after placement into burlap sacks, and 24 h after initial capture) to measure plasma corticosterone (the main crocodilian glucocorticoid) and levels of HSP60, HSP70, and HSP90. Time point significantly affected plasma corticosterone levels in Alligators (p < 0.0001), with levels significantly elevated at 1, 2, and 24 h, relative to baseline (all p < 0.05). However, capture stress did not affect HSP60, HSP70, or HSP90 in red blood cells (all p > 0.05). Our results suggest HSPs may be important biomarkers for investigating the impacts of stressors on captive and wild crocodilians, as they are not acutely elevated by capture or handling stress.

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Lebret, T., R. Watson, V. Molinie, A. O'Neill, H. Botto, and J. M. Fitzpatrick. "Heat shock proteins -HSP27, HSP60, HSP70, HSP90 - expression in bladder cancer." European Urology Supplements 2, no. 1 (February 2003): 88. http://dx.doi.org/10.1016/s1569-9056(03)80347-0.

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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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Das, Jugal Kishore, Xiaofang Xiong, Xingcong Ren, Jin-Ming Yang, and Jianxun Song. "Heat Shock Proteins in Cancer Immunotherapy." Journal of Oncology 2019 (December 11, 2019): 1–9. http://dx.doi.org/10.1155/2019/3267207.

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Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90. The HSPs prevent nonspecific cellular aggregation of proteins by maintaining their native folding energetics. The disruption of this vital cellular process, driven by the aberrant expression of HSPs, is implicated in the progression of several different carcinomas. Many HSPs are also actively involved in promoting the proliferation and differentiation of tumor cells, contributing to their metastatic phenotype. Upregulation of these HSPs is associated with the poor outcome of anticancer therapy in clinical settings. On the other hand, these highly expressed HSPs may be exploited as viable immunotherapeutic targets for different types of cancers. This review discusses recent advances and perspectives on the research of HSP-based cancer immunotherapy.

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Jankovičová, Karolína, Manuela Kudlová, Martina Koláčková, Pavel Kuneš, Ctirad Andrýs, Jiří Manďák, Vladimír Lonský, and Jan Krejsek. "Heat shock proteins Hsp60 and Hsp70 in cardiac surgical patients." Cor et Vasa 49, no. 10 (October 1, 2007): 356–61. http://dx.doi.org/10.33678/cor.2007.128.

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Martinez, J., J. Perez-Serrano, W. E. Bernadina, I. Rincon, and F. Rodriguez-Caabeiro. "Heat shock protein synthesis over time in infective Trichinella spiralis larvae raised in suboptimal culture conditions." Journal of Helminthology 78, no. 3 (September 2004): 243–47. http://dx.doi.org/10.1079/joh2003225.

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AbstractChanges in the viability, infectivity and heat shock protein (Hsp) levels are reported in Trichinella spiralis first stage larvae (L1) stored in 199 medium for up to seven days at 37°C. These conditions induce stress that the larvae, eventually, cannot overcome. After three days of storage, the infectivity and viability were unchanged, although higher Hsp70 levels were observed. After this time, larvae gradually lost viability and infectivity, coinciding with a decrease in Hsp70 and Hsp90 and an increase in actin (a housekeeping protein). In addition, a possibly inducible heat shock protein, Hsp90i, appeared as constitutive Hsp90 disappeared. No significant changes in Hsp60 levels were detected at any time. These results suggest that heat shock proteins initially try to maintain homeostasis, but on failing, may be involved in cell death.

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Scalia, Federica, Alessandra Maria Vitale, Radha Santonocito, Everly Conway de Macario, Alberto J. L. Macario, and Francesco Cappello. "The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders." Applied Sciences 11, no. 3 (January 20, 2021): 898. http://dx.doi.org/10.3390/app11030898.

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The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control. A malfunction of the CS may cause diseases, known as the chaperonopathies. These are caused by qualitatively and/or quantitatively abnormal molecular chaperones. Since the CS is ubiquitous, chaperonopathies are systemic, affecting various tissues and organs, playing an etiologic-pathogenic role in diverse conditions. In this review, we focus on chaperonopathies involved in the pathogenic mechanisms of diseases of the central and peripheral nervous systems: the neurochaperonopathies (NCPs). Genetic NCPs are linked to pathogenic variants of chaperone genes encoding, for example, the small Hsp, Hsp10, Hsp40, Hsp60, and CCT-BBS (chaperonin-containing TCP-1- Bardet–Biedl syndrome) chaperones. Instead, the acquired NCPs are associated with malfunctional chaperones, such as Hsp70, Hsp90, and VCP/p97 with aberrant post-translational modifications. Awareness of the chaperonopathies as the underlying primary or secondary causes of disease will improve diagnosis and patient management and open the possibility of investigating and developing chaperonotherapy, namely treatment with the abnormal chaperone as the main target. Positive chaperonotherapy would apply in chaperonopathies by defect, i.e., chaperone insufficiency, and consist of chaperone replacement or boosting, whereas negative chaperonotherapy would be pertinent when a chaperone actively participates in the initiation and progression of the disease and must be blocked and eliminated.

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Bukau, Bernd, and Arthur L. Horwich. "The Hsp70 and Hsp60 Chaperone Machines." Cell 92, no. 3 (February 1998): 351–66. http://dx.doi.org/10.1016/s0092-8674(00)80928-9.

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Yun, Chul Won, Hyung Joo Kim, Ji Ho Lim, and Sang Hun Lee. "Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy." Cells 9, no. 1 (December 24, 2019): 60. http://dx.doi.org/10.3390/cells9010060.

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Heat shock proteins (HSPs) constitute a large family of molecular chaperones classified by their molecular weights, and they include HSP27, HSP40, HSP60, HSP70, and HSP90. HSPs function in diverse physiological and protective processes to assist in maintaining cellular homeostasis. In particular, HSPs participate in protein folding and maturation processes under diverse stressors such as heat shock, hypoxia, and degradation. Notably, HSPs also play essential roles across cancers as they are implicated in a variety of cancer-related activities such as cell proliferation, metastasis, and anti-cancer drug resistance. In this review, we comprehensively discuss the functions of HSPs in association with cancer initiation, progression, and metastasis and anti-cancer therapy resistance. Moreover, the potential utilization of HSPs to enhance the effects of chemo-, radio-, and immunotherapy is explored. Taken together, HSPs have multiple clinical usages as biomarkers for cancer diagnosis and prognosis as well as the potential therapeutic targets for anti-cancer treatment.

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Martinez, J., J. Perez-Serrano, W. E. Bernadina, and F. Rodriguez-Caabeiro. "Expression of Hsp90, Hsp70 and Hsp60 in Trichinella species exposed to oxidative shock." Journal of Helminthology 76, no. 3 (September 2002): 217–23. http://dx.doi.org/10.1079/joh2002127.

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AbstractStress response and phosphorylation of heat shock proteins (HSPs) 60, 70 and 90 were studied in Trichinella nativa, T. nelsoni, T. pseudospiralis and T. spiralis larvae at 30-min intervals following exposure to 20, 100 and 200 mM H2O2. There was a time- and dose-dependent differential survival for the infective stage larvae (L1) of these four Trichinella species. Immunoblotting analysis revealed that constitutive Hsp60 and Hsp70, but not Hsp90, from test Trichinella species are constitutively phosphorylated on serine/threonine residues as they converted to forms with increased sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) mobility by treatment with alkaline phosphatase. After exposure to H2O2, while there was a time-related occurrence of the three HSPs with decreased SDS–PAGE mobility, these HSPs were insensitive to alkaline phosphatase except in the case of exposure to 20 mM H2O2 for Hsp60 from all Trichinella species and Hsp70 from T. spiralis and T. nelsoni. The synthesis of HSPs forms with decreased SDS–PAGE mobility is a susceptibility signal because the lower concentration of peroxide (20 mM) did not cause a decrease on HSPs SDS–PAGE mobility in T. spiralis and T. nelsoni, the two more resistant selected Trichinella species.

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Alberti, Giusi, Letizia Paladino, Alessandra Maria Vitale, Celeste Caruso Bavisotto, Everly Conway de Macario, Claudia Campanella, Alberto J. L. Macario, and Antonella Marino Gammazza. "Functions and Therapeutic Potential of Extracellular Hsp60, Hsp70, and Hsp90 in Neuroinflammatory Disorders." Applied Sciences 11, no. 2 (January 14, 2021): 736. http://dx.doi.org/10.3390/app11020736.

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Neuroinflammation is implicated in central nervous system (CNS) diseases, but the molecular mechanisms involved are poorly understood. Progress may be accelerated by developing a comprehensive view of the pathogenesis of CNS disorders, including the immune and the chaperone systems (IS and CS). The latter consists of the molecular chaperones; cochaperones; and chaperone cofactors, interactors, and receptors of an organism and its main collaborators in maintaining protein homeostasis (canonical function) are the ubiquitin–proteasome system and chaperone-mediated autophagy. The CS has also noncanonical functions, for instance, modulation of the IS with induction of proinflammatory cytokines. This deserves investigation because it may be at the core of neuroinflammation, and elucidation of its mechanism will open roads toward developing efficacious treatments centered on molecular chaperones (i.e., chaperonotherapy). Here, we discuss information available on the role of three members of the CS—heat shock protein (Hsp)60, Hsp70, and Hsp90—in IS modulation and neuroinflammation. These three chaperones occur intra- and extracellularly, with the latter being the most likely involved in neuroinflammation because they can interact with the IS. We discuss some of the interactions, their consequences, and the molecules involved but many aspects are still incompletely elucidated, and we hope that this review will encourage research based on the data presented to pave the way for the development of chaperonotherapy. This may consist of blocking a chaperone that promotes destructive neuroinflammation or replacing or boosting a defective chaperone with cytoprotective activity against neurodegeneration.

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Chen, Harn-Shen, Jia Jia, Hou-Fen Su, Hong-Da Lin, Jaw-Wen Chen, Shing-Jong Lin, Jia-Ying Yang, Hui-Chin Lai, Ruben Mestril, and Ping H. Wang. "Downregulation of the constitutively expressed Hsc70 in diabetic myocardium is mediated by insulin deficiency." Journal of Endocrinology 190, no. 2 (August 2006): 433–40. http://dx.doi.org/10.1677/joe.1.06692.

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The 70 kDa heat shock protein family plays important cardiac protective roles against myocardial injuries. Reduced myocardial protection is a common feature of diabetic myocardium. This study was carried out to define the changes in the 70 kDa heat shock protein family in the myocardium in the of streptozotocin-diabetes rats, and to explore the mechanisms through which diabetes alters the abundance of Hsp70/Hsc70 in cardiac muscle. In the diabetic myocardium, the abundance of Hsc70 was significantly reduced. The abundance of Hsp70 was low in cardiac muscle and was not induced in the diabetic myocardium. Unlike Hsp60, Hsp70 and Hsc70 did not augment insulin-like growth factor-I receptor signaling in cardiac muscle cells. In cultured cardiomyocytes, insulin directly increased the abundance of Hsc70, whereas insulin could not modulate Hsp70. Treating diabetic rats with insulin restored myocardial Hsc70 level, but phlorizin treatment failed to restore myocardial Hsc70. These in vivo and in vitro studies showed that downregulation of Hsc70 in diabetic myocardium was secondary to insulin deficiency. Thus, insulin played a major role in maintaining adequate expression of Hsc70 in cardiac muscle.

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Schäfer-Somi, Sabine, Okan Ali Aksoy, Osman Ergene, Isfendiyar Darbaz, Kurt R. Herkner, and Selim Aslan. "First detection of heat shock protein 60 and 70 in the serum of early pregnant bitches." Acta Veterinaria Hungarica 67, no. 3 (September 2019): 445–55. http://dx.doi.org/10.1556/004.2019.044.

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Heat shock proteins (HSPs) belong to a group of cellular stress proteins. Heat shock protein 10 immunoregulates and promotes growth during early gestation in humans, while HSP70 is considered to regulate autophagy and apoptosis during pregnancy and parturition. Both HSPs are detectable in the serum and placentas of early pregnant women and considered to contribute to the establishment of pregnancy. Within this pilot study we aimed (1) to assess whether HSPs 10, 60 and 70 are measurable in the serum of healthy early pregnant and non-pregnant bitches, and (2) to explore whether measurable differences between groups indicate pregnancy. Blood was collected from 31 bitches on days 7, 14 and 21 after mating. At 21 days post mating, all bitches were examined for pregnancy by ultrasonography; 23 were pregnant, and the eight non-pregnant bitches served as controls. Pregnant bitches had normal parturitions and gave birth to healthy puppies. The serum concentrations of HSPs 10, 60 and 70 were measured by electrophoresis and western blot. Serum HSP10 was not detectable. Average serum HSP70 concentration was significantly (d7, P = 0.030; d14, P = 0.023; d21, P = 0.030) lower in pregnant animals at all days investigated, while serum HSP60 was significantly lower at day 21 of gestation (P = 0.024) when compared to the controls. HSP 60 and HSP70 concentrations correlated positively (d7, r = +0.386, P = 0.021; d14, r = 0.450, P = 0.008; d21, r = +0.472, P = 0.006). We conclude that in pregnant bitches, serum concentrations of HSP60 and HSP70 are significantly decreased between days 7 and 21 of gestation, in comparison to non-pregnant bitches in early dioestrus, raising the question about intrauterine functions during the peri-implantation period.

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Mantej, Jagoda, Marta Bednarek, Krzysztof Sitko, Marta Świętoń, and Stefan Tukaj. "Autoantibodies to heat shock protein 60, 70, and 90 are not altered in the anti-SARS-CoV-2 IgG-seropositive humans without or with mild symptoms." Cell Stress and Chaperones 26, no. 4 (June 2, 2021): 735–40. http://dx.doi.org/10.1007/s12192-021-01215-3.

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AbstractHighly conserved heat shock proteins (Hsps) are localized in the cytoplasm and cellular organelles, and act as molecular chaperones or proteases. Members of Hsp families are released into the extracellular milieu under both normal and stress conditions. It is hypothesized that the severe acute respiratory syndrome corona virus 2 (SARS-CoV-2) has the potential to elicit autoimmunity due to molecular mimicry between human extracellular Hsps and immunogenic proteins of the virus. To confirm the above hypothesis, levels of circulating autoantibodies directed to the key human chaperones i.e., Hsp60, Hsp70, and Hsp90 in the anti-SARS-CoV-2 IgG-seropositive participants have been evaluated. Twenty-six healthy volunteers who got two doses of the mRNA vaccine encoding the viral spike protein, anti-SARS-CoV-2 IgG-positive participants (n = 15), and healthy naïve (anti-SARS-CoV-2 IgG-negative) volunteers (n = 51) have been included in this study. We found that the serum levels of anti-Hsp60, anti-Hsp70, and anti-Hsp90 autoantibodies of the IgG, IgM, or IgA isotype remained unchanged in either the anti-COVID-19-immunized humans or the anti-SARS-CoV-2 IgG-positive participants when compared to healthy naïve volunteers, as measured by enzyme-linked immunosorbent assay. Our results showing that the humoral immune response to SARS-CoV-2 did not include the production of anti-SARS-CoV-2 antibodies that also recognized extracellular heat shock protein 60, 70, and 90 represent a partial evaluation of the autoimmunity hypothesis stated above. Further testing for cell-based immunity will be necessary to fully evaluate this hypothesis.

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Giraldo, P. C., A. D. Ribeiro-Filho, J. A. Simões, A. Neuer, S. B. N. Feitosa, and S. S. Witkin. "Circulating Heat Shock Proteins in Women With a History of Recurrent Vulvovaginitis." Infectious Diseases in Obstetrics and Gynecology 7, no. 3 (1999): 128–32. http://dx.doi.org/10.1155/s1064744999000204.

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Objective:Predisposing factors influencing recurrences of bacterial vaginosis (BV) or vaginitis fromCandidaremain unidentified for most women. As a component of studies to determine host susceptibility factors to genital tractiiafeetions in women, we measured expression of the 60-kDa and 70-kDa heat shock proteins (hsp60 and hsp70, respectively) in the circulation of women with or without a history of recurrent BV or candidal vaginitis and with or without a current lower genital tract infection. Heat shock protein expression is associated with a down-regulation of proinflammatory immune responses that would inhibit microbial infection.Method:The investigators measured hsp60 and hsp70, antibodies to these proteins, the proinflammatory cytokine tumor necrosis factor-α (TNF-α), and the anti-inflammatory cytokine interleukin- 10 (IL-10) in sera by ELISA. The study population consisted of 100 women who attended a gynecology clinic in Campinas, Brazil. Of those, 55 had a history of recurrent vulvovaginitis (RV), while 45 were controls with no such history. Only women who were asymptomatic for at least 1 month were studied.Results:Although all were asymptomatic, clinical and microbiological examination revealed that five of the women with a history of RV and two controls had a current candidal vaginal infection; 16 RV patients and 12 controls had BV; and six RV patients had both BV and candidiasis. Twenty-eight RV patients and 31 controls had no clinical or microbiological detectable vaginal infection. Among the RV patients, hsp60 and hsp70 were more prevalent in those with current BV (40.9% and 50.0%, respectively) or a candidal infection (45.5% and 54.5%) than in women with no current infection (21.4% and 17.9%). In the women with no history of RV, BV was not associated with a high prevalence of hsp60 (8.3%) or hsp70 (8.3%). Interleukin-10 and TNF were not more prevalent in vaginitis patients or controls with a current candidal infection or BV than in uninfected subjects.Conclusion:The high prevalence of circulating hsp60 and hsp70 in women with a history of RV and current BV or vaginal candidiasis, but not in women with no history of RV, suggests that differences in heat shock protein induction may be related to susceptibility to recurrent vaginal infections. Infect. Dis. Obstet. Gynecol. 7:128–132, 1999.

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Burt, Sara A., Ruurd van der Zee, Ad P. Koets, Anko M. de Graaff, Frans van Knapen, Wim Gaastra, Henk P. Haagsman, and Edwin J. A. Veldhuizen. "Carvacrol Induces Heat Shock Protein 60 and Inhibits Synthesis of Flagellin in Escherichia coli O157:H7." Applied and Environmental Microbiology 73, no. 14 (May 25, 2007): 4484–90. http://dx.doi.org/10.1128/aem.00340-07.

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ABSTRACT The essential oils of oregano and thyme are active against a number of food-borne pathogens, such as Escherichia coli O157:H7. Carvacrol is one of the major antibacterial components of these oils, and p-cymene is thought to be its precursor in the plant. The effects of carvacrol and p-cymene on protein synthesis in E. coli O157:H7 ATCC 43895 cells were investigated. Bacteria were grown overnight in Mueller-Hinton broth with a sublethal concentration of carvacrol or p-cymene, and their protein compositions were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and confirmed by Western blotting. The presence of 1 mM carvacrol during overnight incubation caused E. coli O157:H7 to produce significant amounts of heat shock protein 60 (HSP60) (GroEL) (P < 0.05) and inhibited the synthesis of flagellin highly significantly (P < 0.001), causing cells to be aflagellate and therefore nonmotile. The amounts of HSP70 (DnaK) were not significantly affected. p-Cymene at 1 mM or 10 mM did not induce HSP60 or HSP70 in significant amounts and did not have a significant effect on flagellar synthesis. Neither carvacrol (0.3, 0.5, 0.8, or 1 mM) nor p-cymene (0.3, 0.5, or 0.8 mM) treatment of cells in the mid-exponential growth phase induced significant amounts of HSP60 or HSP70 within 3 h, although numerical increases of HSP60 were observed. Motility decreased with increasing concentrations of both compounds, but existing flagella were not shed. This study is the first to demonstrate that essential oil components induce HSP60 in bacteria and that overnight incubation with carvacrol prevents the development of flagella in E. coli O157:H7.

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Merino, S., M. C. Blázquez, J. Martínez, and R. Rodríguez-Estrella. "Stress protein expression is related to tail loss in two species of iguanid lizards." Canadian Journal of Zoology 82, no. 3 (March 1, 2004): 436–41. http://dx.doi.org/10.1139/z04-008.

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During the spring of 1999, two species of iguanid lizards were captured in southern Baja California peninsula, Mexico. Blood was obtained from the tail to check for the presence of blood parasites in smears and stress proteins in cells. Levels of HSP70- and HSP60-like proteins from Sceloporus licki Van Denburgh, 1895 and Petrosaurus thalassinus (Cope, 1863) were analyzed with Western blot using antisera to human HSP60 and bovine HSP70. The potential effects of sex, tail regeneration, and haemoparasites on the expression of these proteins were also investigated. Both species differ significantly in stress protein levels and infection by haemoparasites. Petrosaurus thalassinus show the lower stress protein levels and the higher proportion of infection. Although blood parasites apparently affect the condition of P. thalassinus, stress protein levels are not significantly related with haemoparasites or condition. However, S. licki lizards showing tail regeneration have lower levels of HSP60-like protein. A negative relationship exists between the length of the regenerated part of the tail and the level of HSP60-like protein for S. licki. Based on what is known of the function of HSP60, down-regulation of the protein in blood cells may be linked to reallocation of energies to other tissues more active metabolically.

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Muller, M., J. Gauley, and John J. Heikkila. "Hydrogen peroxide induces heat shock protein and proto-oncogene mRNA accumulation in Xenopus laevis A6 kidney epithelial cells." Canadian Journal of Physiology and Pharmacology 82, no. 7 (July 1, 2004): 523–29. http://dx.doi.org/10.1139/y04-059.

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In this study, we examined the effect of hydrogen peroxide on the accumulation of various mRNAs encoding heat shock proteins (hsps) and proto-oncogenes in Xenopus A6 kidney epithelial cells. Hydrogen peroxide treatment enhanced the accumulation of hsp90, hsp70, hsp30, c-jun, c-fos, and actin mRNAs with distinct temporal patterns. Although hsp70, c-fos, and c-jun mRNA levels peaked at 1–2 h before declining, hsp30 and hsp90 mRNA levels were maximal at 4–6 h. Other mRNAs, including heat shock cognate hsc70, immunoglobulin binding protein, and ribosomal L8, were unaffected. Treatment of kidney cells with a combination of mild heat shock plus hydrogen peroxide resulted in a synergistic increase in the relative levels of both hsp70 and hsp30 mRNA, but not hsp90, c-fos, c-jun, or actin. This study suggests that analysis of hsp and proto-oncogene mRNA levels may be of value as molecular biomarkers of oxidative stress associated with various disease states and nephrotoxicity in kidney.Key words: Xenopus, kidney, mRNA, heat shock protein, hydrogen peroxide.

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Ali, Adnan, and John J. Heikkila. "Enhanced accumulation of constitutive heat shock protein mRNA is an initial response of eye tissue to mild hyperthermia in vivo in adult Xenopus laevis." Canadian Journal of Physiology and Pharmacology 80, no. 11 (November 1, 2002): 1119–23. http://dx.doi.org/10.1139/y02-133.

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We have examined the effect of mild hyperthermia in vivo on heat shock transcription factor (HSF) binding activity and heat shock protein (hsp) gene expression in eye tissue of adult Xenopus laevis. A specific interaction between HSF and a synthetic oligonucleotide corresponding to the proximal heat shock element of the Xenopus hsp70B gene was greatly enhanced in eyes from hyperthermic animals compared with controls. Given these results, we examined the effect of hyperthermia in vivo on the expression of five hsp genes (hsp70, hsc70, BiP, hsp90, and hsp30) in eye tissue. Interestingly, at 28°C constitutively expressed hsp genes hsc70, BiP, and hsp90 were strongly enhanced, with further accumulation at 30°C. However, hsp70 and hsp30 mRNA accumulation were not detectable at 28°C but were strongly induced at 30°C. No enhancement of the relative levels of cytoskeletal actin mRNA was observed in the eye tissue of hyperthermic animals. These results suggest that one of the primary responses of eye tissue to hyperthermia in vivo is in the elevation of mRNAs encoding a set of constitutively expressed molecular chaperones.Key words: Xenopus, mRNA, eye, heat shock, heat shock factor.

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Hasan Siddiqui, Sharif, Darae Kang, Jinryong Park, Hyun Woo Choi, and Kwanseob Shim. "Acute Heat Stress Induces the Differential Expression of Heat Shock Proteins in Different Sections of the Small Intestine of Chickens Based on Exposure Duration." Animals 10, no. 7 (July 21, 2020): 1234. http://dx.doi.org/10.3390/ani10071234.

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In this study, we examined the protein and gene expression of heat shock proteins (HSPs) in different sections of the small intestine of chickens. In total, 300 one-day-old Ross 308 broiler chicks were randomly allocated to the control and treatment groups. The treatment group was divided into four subgroups, according to the duration of acute heat exposure (3, 6, 12, and 24 h). The influence of heat stress on the protein and gene expression of HSP70, HSP60, and HSP47 in different sections of the small intestine of chickens was determined. The protein expression of HSP70 and HSP60 was significantly higher at 6 h in the duodenum and jejunum and 12 h in the ileum. The HSP47 protein expression was significantly higher at 3 h in the duodenum and ileum and at 6 h in the jejunum. The gene expression levels of HSP70, HSP60, and HSP47 were significantly higher at the 3 h treatment group than the control group in the duodenum, jejunum, and ileum. The glutamate pyruvate transaminase and glutamate oxaloacetate transaminase levels were significantly higher at 12 and 24 h in the serum of the blood. Acute heat stress affected the expression of intestinal proteins and genes in chickens, until the induction of heat tolerance.

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Emelyanov, Victor V. "Phylogenetic relationships of organellar Hsp90 homologs reveal fundamental differences to organellar Hsp70 and Hsp60 evolution." Gene 299, no. 1-2 (October 2002): 125–33. http://dx.doi.org/10.1016/s0378-1119(02)01021-1.

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Yasa, N. S., L. Anshory, S. J. Purnomo, and G. M. Samadan. "Induction of Hsp60, Hsp70, and Hsp90 in formalin exposed white shrimp (Litopenaeus vannamei) stress test." IOP Conference Series: Earth and Environmental Science 584 (October 16, 2020): 012054. http://dx.doi.org/10.1088/1755-1315/584/1/012054.

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J., Martinez, Pérez-Serrano J., Bernadina W., and Rodríguez-Caabeiro F. "HSP60, HSP70 and HSP90 from Trichinella spiralis as targets of humoral immune response in rats." Parasitology Research 87, no. 6 (May 18, 2001): 453–58. http://dx.doi.org/10.1007/s004360000315.

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Zhu, Yihao, Xinxing Lu, Di Wu, Shaohe Cai, Shu Li, and Xiaohua Teng. "The Effect of Manganese-induced Cytotoxicity on mRNA Expressions of HSP27, HSP40, HSP60, HSP70 and HSP90 in Chicken Spleen Lymphocytes in Vitro." Biological Trace Element Research 156, no. 1-3 (October 2, 2013): 144–52. http://dx.doi.org/10.1007/s12011-013-9817-2.

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Hoter, Abdullah, and Hassan Y. Naim. "The Functions and Therapeutic Potential of Heat Shock Proteins in Inflammatory Bowel Disease—An Update." International Journal of Molecular Sciences 20, no. 21 (October 26, 2019): 5331. http://dx.doi.org/10.3390/ijms20215331.

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Inflammatory bowel disease (IBD) is a multifactorial human intestinal disease that arises from numerous, yet incompletely defined, factors. Two main forms, Crohn’s disease (CD) and ulcerative colitis (UC), lead to a chronic pathological form. Heat shock proteins (HSPs) are stress-responsive molecules involved in various pathophysiological processes. Several lines of evidence link the expression of HSPs to the development and prognosis of IBD. HSP90, HSP70 and HSP60 have been reported to contribute to IBD in different aspects. Moreover, induction and/or targeted inhibition of specific HSPs have been suggested to ameliorate the disease consequences. In the present review, we shed the light on the role of HSPs in IBD and their targeting to prevent further disease progression.

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Neufer, P. D., G. A. Ordway, G. A. Hand, J. M. Shelton, J. A. Richardson, I. J. Benjamin, and R. S. Williams. "Continuous contractile activity induces fiber type specific expression of HSP70 in skeletal muscle." American Journal of Physiology-Cell Physiology 271, no. 6 (December 1, 1996): C1828—C1837. http://dx.doi.org/10.1152/ajpcell.1996.271.6.c1828.

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Continuous contractile activity of skeletal muscle elicits an early and dramatic increase in ribosomal RNA, suggesting that translational efficiency and/or capacity is enhanced during the adaptive response to increased metabolic demand. In view of the important role heat shock or stress proteins (HSPs) play as molecular chaperones during protein synthesis, we examined whether expression of the inducible 70-kDa HSP (HSP70) and/or mitochondrial 60-kDa HSP (HSP60) is altered in rabbit tibialis anterior muscle during continuous low-frequency motor nerve stimulation. Induction of the HSP70 gene was evident within 24 h after the onset of stimulation as reflected by increases in HSP70 transcription (> 20-fold) and mRNA (> 50-fold). HSP70 protein levels were significantly elevated (10- to 12-fold) after 14 and 21 days of stimulation. Mitochondrial HSP60 mRNA and protein also increased during stimulation (> 18- and > 5-fold after 21 days, respectively). In situ hybridization and immunohistochemistry coupled with myosin ATPase staining revealed that expression of HSP70 was restricted to oxidative type I and IIa fibers during the first 3 days of stimulation but shifted to primarily type II fibers after 21 days of stimulation. These findings demonstrate that induction of HSP70 during the adaptive response to chronic motor nerve stimulation proceeds from type I/IIa to type IId(x)/b fibers, suggesting that the expression of HSPs may be required to support the folding and compartmentalization of nascent proteins during the transformation process.

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Agarraberes, Fernando A., and J. Fred Dice. "A molecular chaperone complex at the lysosomal membrane is required for protein translocation." Journal of Cell Science 114, no. 13 (July 1, 2001): 2491–99. http://dx.doi.org/10.1242/jcs.114.13.2491.

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A group of cytosolic proteins are targeted to lysosomes for degradation in response to serum withdrawal or prolonged starvation by a process termed chaperone-mediated autophagy. In this proteolytic pathway little is known about how proteins are translocated across lysosomal membranes. We now show that an isoform of the constitutively expressed protein of the heat shock family of 70 kDa (Hsc70) is associated with the cytosolic side of the lysosomal membrane where it binds to substrates of this proteolytic pathway. Results from coimmunoprecipitation and colocalization studies indicate that this molecular chaperone forms complexes with other molecular chaperones and cochaperones, including Hsp90, Hsp40, the Hsp70-Hsp90 organizing protein (Hop), the Hsp70-interacting protein (Hip), and the Bcl2-associated athanogene 1 protein (BAG-1). Antibodies against Hip, Hop, Hsp40 and Hsc70 block transport of protein substrates into purified lysosomes.

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Spinaci, M., S. Volpe, C. Bernardini, M. de Ambrogi, C. Tamanini, E. Seren, and G. Galeati. "Sperm Sorting Procedure Induces a Redistribution of Hsp70 but Not Hsp60 and Hsp90 in Boar Spermatozoa." Journal of Andrology 27, no. 6 (July 12, 2006): 899–907. http://dx.doi.org/10.2164/jandrol.106.001008.

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Macario, Alberto J. L., Marianne Lange, Birgitte K. Ahring, and Everly Conway De Macario. "Stress Genes and Proteins in the Archaea." Microbiology and Molecular Biology Reviews 63, no. 4 (December 1, 1999): 923–67. http://dx.doi.org/10.1128/mmbr.63.4.923-967.1999.

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SUMMARY The field covered in this review is new; the first sequence of a gene encoding the molecular chaperone Hsp70 and the first description of a chaperonin in the archaea were reported in 1991. These findings boosted research in other areas beyond the archaea that were directly relevant to bacteria and eukaryotes, for example, stress gene regulation, the structure-function relationship of the chaperonin complex, protein-based molecular phylogeny of organisms and eukaryotic-cell organelles, molecular biology and biochemistry of life in extreme environments, and stress tolerance at the cellular and molecular levels. In the last 8 years, archaeal stress genes and proteins belonging to the families Hsp70, Hsp60 (chaperonins), Hsp40(DnaJ), and small heat-shock proteins (sHsp) have been studied. The hsp70(dnaK), hsp40(dnaJ), and grpE genes (the chaperone machine) have been sequenced in seven, four, and two species, respectively, but their expression has been examined in detail only in the mesophilic methanogen Methanosarcina mazei S-6. The proteins possess markers typical of bacterial homologs but none of the signatures distinctive of eukaryotes. In contrast, gene expression and transcription initiation signals and factors are of the eucaryal type, which suggests a hybrid archaeal-bacterial complexion for the Hsp70 system. Another remarkable feature is that several archaeal species in different phylogenetic branches do not have the gene hsp70(dnaK), an evolutionary puzzle that raises the important question of what replaces the product of this gene, Hsp70(DnaK), in protein biogenesis and refolding and for stress resistance. Although archaea are prokaryotes like bacteria, their Hsp60 (chaperonin) family is of type (group) II, similar to that of the eukaryotic cytosol; however, unlike the latter, which has several different members, the archaeal chaperonin system usually includes only two (in some species one and in others possibly three) related subunits of ∼60 kDa. These form, in various combinations depending on the species, a large structure or chaperonin complex sometimes called the thermosome. This multimolecular assembly is similar to the bacterial chaperonin complex GroEL/S, but it is made of only the large, double-ring oligomers each with eight (or nine) subunits instead of seven as in the bacterial complex. Like Hsp70(DnaK), the archaeal chaperonin subunits are remarkable for their evolution, but for a different reason. Ubiquitous among archaea, the chaperonins show a pattern of recurrent gene duplication—hetero-oligomeric chaperonin complexes appear to have evolved several times independently. The stress response and stress tolerance in the archaea involve chaperones, chaperonins, other heat shock (stress) proteins including sHsp, thermoprotectants, the proteasome, as yet incompletely understood thermoresistant features of many molecules, and formation of multicellular structures. The latter structures include single- and mixed-species (bacterial-archaeal) types. Many questions remain unanswered, and the field offers extraordinary opportunities owing to the diversity, genetic makeup, and phylogenetic position of archaea and the variety of ecosystems they inhabit. Specific aspects that deserve investigation are elucidation of the mechanism of action of the chaperonin complex at different temperatures, identification of the partners and substitutes for the Hsp70 chaperone machine, analysis of protein folding and refolding in hyperthermophiles, and determination of the molecular mechanisms involved in stress gene regulation in archaeal species that thrive under widely different conditions (temperature, pH, osmolarity, and barometric pressure). These studies are now possible with uni- and multicellular archaeal models and are relevant to various areas of basic and applied research, including exploration and conquest of ecosystems inhospitable to humans and many mammals and plants.

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Ballinger, Carol A., Patrice Connell, Yaxu Wu, Zhaoyong Hu, Larry J. Thompson, Li-Yan Yin, and Cam Patterson. "Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions." Molecular and Cellular Biology 19, no. 6 (June 1, 1999): 4535–45. http://dx.doi.org/10.1128/mcb.19.6.4535.

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ABSTRACT The chaperone function of the mammalian 70-kDa heat shock proteins Hsc70 and Hsp70 is modulated by physical interactions with four previously identified chaperone cofactors: Hsp40, BAG-1, the Hsc70-interacting protein Hip, and the Hsc70-Hsp90-organizing protein Hop. Hip and Hop interact with Hsc70 via a tetratricopeptide repeat domain. In a search for additional tetratricopeptide repeat-containing proteins, we have identified a novel 35-kDa cytoplasmic protein, carboxyl terminus of Hsc70-interacting protein (CHIP). CHIP is highly expressed in adult striated muscle in vivo and is expressed broadly in vitro in tissue culture. Hsc70 and Hsp70 were identified as potential interaction partners for this protein in a yeast two-hybrid screen. In vitro binding assays demonstrated direct interactions between CHIP and both Hsc70 and Hsp70, and complexes containing CHIP and Hsc70 were identified in immunoprecipitates of human skeletal muscle cells in vivo. Using glutathione S-transferase fusions, we found that CHIP interacted with the carboxy-terminal residues 540 to 650 of Hsc70, whereas Hsc70 interacted with the amino-terminal residues 1 to 197 (containing the tetratricopeptide domain and an adjacent charged domain) of CHIP. Recombinant CHIP inhibited Hsp40-stimulated ATPase activity of Hsc70 and Hsp70, suggesting that CHIP blocks the forward reaction of the Hsc70-Hsp70 substrate-binding cycle. Consistent with this observation, both luciferase refolding and substrate binding in the presence of Hsp40 and Hsp70 were inhibited by CHIP. Taken together, these results indicate that CHIP decreases net ATPase activity and reduces chaperone efficiency, and they implicate CHIP in the negative regulation of the forward reaction of the Hsc70-Hsp70 substrate-binding cycle.

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Boxma, B., JHP Hackstein, and GD Vogels. "Hsp60 and hsp70 encoding genes in anaerobic chytridiomycete fungi." Reproduction Nutrition Development 37, Suppl. 1 (1997): 39–40. http://dx.doi.org/10.1051/rnd:19970720.

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Journal articles on the topic 'Hsp60 and Hsp70'

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