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Journal articles on the topic 'HSP32'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Kondo, Rudin, Karoline V. Gleixner, Matthias Mayerhofer, et al. "Identification of heat shock protein 32 (Hsp32) as a novel survival factor and therapeutic target in neoplastic mast cells." Blood 110, no. 2 (2007): 661–69. http://dx.doi.org/10.1182/blood-2006-10-054411.

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AbstractSystemic mastocytosis (SM) is a myeloid neoplasm characterized by increased survival and accumulation of neoplastic mast cells (MCs). In most patients, the D816V-mutated variant of KIT is detectable. We report here that heat shock protein 32 (Hsp32), also known as heme oxygenase-1 (HO-1), is a novel KIT-inducible survival factor in neoplastic MCs. As assessed by reverse transcription-polymerase chain reaction (RT-PCR), immunocytochemistry, and Western blotting, the KIT D816V+ MC line HMC-1.2 as well as highly enriched primary neoplastic MCs were found to express Hsp32 mRNA and the Hsp32 protein. Moreover, KIT D816V and stem cell factor (SCF)–activated wild-type KIT were found to induce Hsp32 promoter activity, expression of Hsp32 mRNA, and expression of the Hsp32 protein in Ba/F3 cells. Correspondingly, the KIT D816V-targeting drug PKC412 decreased the expression of Hsp32 as well as proliferation/survival in neoplastic MCs. The inhibitory effects of PKC412 on the survival of HMC-1.2 cells were counteracted by the HO-1 inductor hemin or lentiviral-transduced HO-1. Moreover, 2 Hsp32-targeting drugs, pegylated zinc protoporphyrin (PEG-ZnPP) and styrene maleic acid copolymer micelle-encapsulated ZnPP (SMA-ZnPP), were found to inhibit proliferation and to induce apoptosis in neoplastic MCs. Furthermore, both drugs were found to cooperate with PKC412 in producing growth inhibition. Together, these data show that Hsp32 is an important survival factor and interesting new therapeutic target in neoplastic MCs.

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2

Gleixner, K. V., M. Mayerhofer, A. Vales, et al. "The Hsp32/HO-1-targeted drug SMA-ZnPP counteracts the proliferation and viability of neoplastic cells in solid tumors and hematologic neoplasms." Journal of Clinical Oncology 25, no. 18_suppl (2007): 14122. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.14122.

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14122 Background: Heat shock protein 32 (Hsp32) is a stress-related survival factor that is overexpressed in various neoplastic cells. Recently, specific Hsp32- targeting drugs such as styrene maleic acid encapsulated zinc protoporphyrin (SMA-ZnPP) have been developed. Methods: We examined the effects of SMA-ZnPP on proliferation and survival of various tumor cell-lines, including U97MG (glioblastoma), A549 (lung cancer), MDA-MB-231 (breast cancer), BxPC-3 (pancreatic), HepG2 (hepatocellular), Colo201, Colo320DM, DLD-1 (colon), OvCar3 (ovarian carcinoma), KG1, U937, HL60, K562 (myeloid leukemias), RAJI, NALM-6 (lymphatic leukemias), RPMI 8226, U266 (multiple myeloma) as well as on primary neoplastic cells. Moreover, Ba/F3 cells with doxycycline-inducible expression of oncoproteins (RAS-G12V, BCR/ABL, KIT-D816V) were analyzed. Expression of Hsp32 mRNA was examined by RT-PCR and Northern blotting, and expression of the Hsp32 protein by Western blotting. To silence Hsp32 in neoplastic cells, we used specific siRNA as well as SMA-ZnPP. Proliferation was analyzed by 3H-thymidine uptake and apoptosis by light microscopy. Results: All neoplastic cells tested were found to express Hsp32 mRNA and the Hsp32 protein in a constitutive manner. In Ba/F3 cells, induction of RAS-G12V, BCR/ABL, or KIT D816V enhanced the expression of Hsp32. The Hsp32 siRNA was found to lead to a reduced viability and induction of apoptosis. Treatment of malignant cells with SMA-ZnPP resulted in a significant decrease in proliferation and induction of apoptosis. The effects of SMA- ZnPP on primary neoplastic cells and cell lines were dose-dependent and occurred at pharmacologic concentrations (IC50 1–30 μM). Moreover, SMA-ZnPP was found to synergize with various anti-neoplastic drugs (cisplatin, cytarabine, tyrosine kinase inhibitors, bortezomib) in producing growth-inhibition in neoplastic cells. Conclusions: The Hsp32-targeting drug SMA-ZnPP counteracts malignant cell growth and sensitizes neoplastic cells against various other targeted or conventional antineoplastic drugs. Hsp32-targeting drugs may represent an interesting new aproach to inhibit malignant cell growth in solid tumors and leukemias. No significant financial relationships to disclose.

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3

Meyer, Renata A., Harald Herrmann, Karoline V. Gleixner, et al. "Identification of Heat Shock Protein 32 (Hsp32) as a Novel Target in Acute Lymphoblastic Leukemia (ALL)." Blood 112, no. 11 (2008): 1616. http://dx.doi.org/10.1182/blood.v112.11.1616.1616.

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Abstract Heat shock proteins (Hsp) are increasingly employed as therapeutic targets in various solid tumors and leukemias. We have recently shown that Hsp32 is expressed in leukemic cells and serves as a survival-factor and molecular target in Ph+ chronic myeloid leukemia. In the present study, we examined the expression and functional role of Hsp32 in acute lymphoblastic leukemia (ALL). Leukemic cells were obtained from patients with Ph+ ALL (n=5) and Ph− ALL (n=5). In addition, Ph+ ALL cell lines (Z-119, BV-173, TOM-1, NALM-1) and Ph− ALL cell lines (RAJI, RAMOS, REH, BL-41) were used. As assessed by immunocytochemistry and qRT-PCR, leukemic cells were found to express the Hsp32 protein as well as Hsp32 mRNA in all patients and in all cell lines examined. The Hsp32-inductor hemin was found to promote the expression of Hsp32 in leukemic cells. To determine the functional role of Hsp32 in lymphoblasts, an siRNA against Hsp32 was applied. The siRNA-induced knock down of Hsp32 in RAJI cells was found to be associated with reduced growth and with an increase in apoptotic cells compared to a control siRNA against luciferase (p&lt;0.05). In a next step, two pharmacologic inhibitors of Hsp32, pegylated zinc protoporphyrine (PEG-ZnPP) and styrene maleic acid-micelle-encapsulated ZnPP (SMA-ZnPP), were applied. As assessed by 3H-thymidine uptake experiments, both drugs were found to inhibit proliferation in the BCR/ABL+ cell lines Z-119, BV-173, and TOM-1, and in the BCR/ABL-negative ALL cell lines RAJI, RAMOS, REH, and BL-41. The effects of PEG-ZnPP and SMA-ZnPP were dose-dependent with IC50 values ranging between 1 and 10 μM, and were found to be associated with apoptosis as determined by microscopy as well as by flow cytometry and AnnexinV-staining. In NALM-1 cells, PEG-ZnPP and SMA-ZnPP also produced apoptosis and growth arrest, but the IC50 for SMA-ZnPP was slightly higher compared to other cell lines (20 μM). Effects of Hsp32-targeting drugs were also observed in primary leukemic cells obtained from patients with Ph+ ALL and Ph− ALL, with IC50 values ranging between 1 and 10 μM. No major differences were found when comparing results in imatinib-sensitive and imatinib-resistant patients. In drug combination experiments, Hsp32-targeting drugs were found to cooperate with imatinib and with AMN107 (nilotinib) in producing growth-inhibition and apoptosis in all Ph+ ALL cell lines tested. Furthermore, we were able to demonstrate strong cooperative antileukemic effects when applying Hsp32-targeting drugs in combination with bendamustine. Overall, these results suggest that Hsp32 may be a novel molecular target in ALL.

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4

Gleixner, Karoline V., Mayerhofer Matthias, Anja Vales, et al. "Targeting of Heat Shock Protein 32 (Hsp32) in Neoplastic Cells by Styrene Maleic Acid Zinc Protoporphyrin (SMA-ZnPP) Is Associated with Reduced Growth and Induction of Apoptosis." Blood 108, no. 11 (2006): 4323. http://dx.doi.org/10.1182/blood.v108.11.4323.4323.

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Abstract Heat shock protein 32 (Hsp32), also known as heme oxygenase-1 (HO-1), is a stress-related survival factor that has recently been implicated in enhanced survival of neoplastic cells. We here show that Hsp32/HO-1 is expressed abundantly in primary neoplastic cells in various solid tumors and hematopoietic neoplasms such as acute myeloid leukemia (AML) or chronic myeloid leukemia (CML), and in respective cell lines including the AML cell lines HL60, KG1, KG1a, and U937, CML cell lines K562 and KU812, eosinophilic leukemia cell line EOL-1, mast cell leukemia cell line HMC-1, myeloma cell lines RPMI8226 and U266, breast cancer cell line MDA MB 231, lung cancer cell line A549, pancreatic carcinoma cell line BxPC-3, colon carcinoma cell lines COLO201, COLO205, COLO320DM, and DLD-1, and the ovarian carcinoma cell line OVCAR-3. Expression of Hsp32 mRNA was demonstrable by RT-PCR and Northern blotting, and expression of the Hsp32 protein by Western blotting and immunocytochemistry. The CML-specific oncoprotein BCR/ABL and the transforming oncoprotein KIT D816V that is expressed in neoplastic mast cells, were found to promote expression of Hsp32 in Ba/F3 cells. In order to examine the functional role of Hsp32 in neoplastic cells, a specific siRNA was employed. Expression of Hsp32 siRNA resulted in reduced viability and induction of apoptosis in all cell lines tested. To further explore the value of Hsp32 as a target in neoplastic cells, a novel specific Hsp32-targeting compound, styrene maleic acid copolymer zinc protoporphyrin micelles (SMA-ZnPP) was applied. Exposure to SMA-ZnPP resulted in a significant decrease in proliferation determined by 3H-thymidine uptake, in all cell lines as well as in all primary neoplastic cells tested (AML, n=5; CML, n=5; mastocytosis, n=3; breast cancer, n=2; lung cancer, n=1). As assessed by AnnexinV-staining, Tunel assay and electron microscopy, the growth-inhibitory effects of SMA-ZnPP were found to be associated with induction of apoptosis. In each cell type, the effect of SMA-ZnPP on growth was dose-dependent and found to occur at pharmacologic concentrations (IC50 1–30 μM). Moreover, SMA-ZnPP was found to synergize with various anti-neoplastic drugs (tumor cell lines: cisplatin, leukemias: cytarabine, myeloma: bortezomib) in producing growth inhibition. In summary, these data show that Hsp32/HO-1 is an important survival factor and novel interesting target in various hematopoietic and non-hematopoietic neoplasms. Based on these data, it seems desirable to explore the value of the Hsp32-targeting drug SMA-ZnPP in clinical trials in patients with leukemias and solid tumors.

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5

Essig, D. A., D. R. Borger, and D. A. Jackson. "Induction of heme oxygenase-1 (HSP32) mRNA in skeletal muscle following contractions." American Journal of Physiology-Cell Physiology 272, no. 1 (1997): C59—C67. http://dx.doi.org/10.1152/ajpcell.1997.272.1.c59.

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The capacity of preexisting antioxidant pathways to handle oxidative stress during exercise may be complemented by the synthesis of inducible heat stress proteins (HSP). Our purpose was to determine if the amount of mRNA for HSP32, a major oxidative stress protein, was increased in muscle after repetitive contractions. Reverse transcriptase-polymerase chain reaction analysis showed that HSP32 mRNA (normalized to alpha-actin mRNA) was increased about seven- and about fourfold (P < 0.35) immediately after 1 h of exhaustive running and after 3 h of muscle contractions (10 Hz nerve stimulation), respectively. Northern blot analysis revealed that HSP70 mRNAs were 3.5- to 15.5-fold above control value (P < 0.05), whereas the content of another oxidative stress protein mRNA (macrophage stress protein 23) was unchanged 0 h after contractions. The relative increase in HSP32 mRNA was found to be dependent on active tension generation; passive tension did not increase the HSP32-to-actin mRNA ratio. Increases in HSP32 mRNA may underlie an inducible antioxidant pathway in muscle responsive to metabolic stresses associated with repeated muscle contractions.

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6

Arock, Michel A. "Hsp32: MASTer of KIT?" Blood 110, no. 2 (2007): 471. http://dx.doi.org/10.1182/blood-2007-04-086629.

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7

Romanucci, M., M. Massimini, A. Ciccarelli, et al. "HSP32 and HSP90 Immunoexpression, in Relation to Kit Pattern, Grading, and Mitotic Count in Canine Cutaneous Mast Cell Tumors." Veterinary Pathology 54, no. 2 (2016): 222–25. http://dx.doi.org/10.1177/0300985816669405.

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Literature data indicate heat shock protein (Hsp) 32 and 90 as potential molecular targets in canine neoplastic mast cells (MCs). However, their immunoexpression patterns in canine mast cell tumors (MCTs) have not been investigated. Thus, the aim of this study was to evaluate the immunohistochemical expression of Hsp32 and Hsp90 in 22 canine cutaneous MCTs, in relation to KIT immunolabeling pattern, histological grade, and mitotic count. All cases showed cytoplasmic labeling of Hsp90, variably associated with nuclear and/or membranous labeling. Relationships of Hsp90 or Hsp32 immunolabeling with KIT pattern, mitotic count, and tumor grade were not observed. However, the reduced Hsp32 immunoexpression observed in most grade III/high-grade MCTs suggests a tendency toward a loss of immunosignal in poorly differentiated MCs. The great heterogeneity in extent and distribution of Hsp90 immunoexpression among the different MCT cases may also partially explain the difficulties in predicting the in vivo biologic activity of Hsp90 inhibitors on canine MCTs.

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8

Lee, Ben J., Tessa R. Flood, Ania M. Hiles та ін. "New Zealand Blackcurrant Extract Increases Circulating Hsp32 And Hsp90α But DoesnʼT Affect Circulating Hsp72". Medicine & Science in Sports & Exercise 51, Supplement (2019): 91. http://dx.doi.org/10.1249/01.mss.0000560767.94376.c0.

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9

Taylor, Lee, Adrian Midgley, Bryna Chrismas, Daniel Peart, Angela Hillman, and Lars McNaughton. "Hypoxia Mediated Prior Induction Of Hsp72 And Hsp32 Provides Protection To Sub-maximal Exercise." Medicine & Science in Sports & Exercise 43, Suppl 1 (2011): 153. http://dx.doi.org/10.1249/01.mss.0000400399.34716.bf.

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10

Mayerhofer, Matthias, Karoline V. Gleixner, Julia Mayerhofer, et al. "Targeting of heat shock protein 32 (Hsp32)/heme oxygenase-1 (HO-1) in leukemic cells in chronic myeloid leukemia: a novel approach to overcome resistance against imatinib." Blood 111, no. 4 (2008): 2200–2210. http://dx.doi.org/10.1182/blood-2006-11-055723.

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Resistance toward imatinib and other BCR/ABL tyrosine kinase inhibitors remains an increasing clinical problem in the treatment of advanced stages of chronic myeloid leukemia (CML). We recently have identified the heat shock protein 32 (Hsp32)/heme oxygenase-1 (HO-1) as a BCR/ABL-dependent survival molecule in CML cells. We here show that silencing Hsp32/HO-1 in CML cells by an siRNA approach results in induction of apoptosis. Moreover, targeting Hsp32/HO-1 by either pegylated zinc protoporphyrine (PEG-ZnPP) or styrene maleic acid-micelle–encapsulated ZnPP (SMA-ZnPP) resulted in growth inhibition of BCR/ABL-transformed cells. The effects of PEG-ZnPP and SMA-ZnPP were demonstrable in Ba/F3 cells carrying various imatinib-resistant mutants of BCR/ABL, including the T315I mutant, which exhibits resistance against all clinically available BCR/ABL tyrosine kinase inhibitors. Growth-inhibitory effects of PEG-ZnPP and SMA-ZnPP also were observed in the CML-derived human cell lines K562 and KU812 as well as in primary leukemic cells obtained from patients with freshly diagnosed CML or imatinib-resistant CML. Finally, Hsp32/HO-1–targeting compounds were found to synergize with either imatinib or nilotinib in producing growth inhibition in imatinib-resistant K562 cells and in Ba/F3 cells harboring the T315I mutant of BCR/ABL. In summary, these data show that HO-1 is a promising novel target in imatinib-resistant CML.

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11

Zhukova, Anna G., L. G. Gorokhova, A. V. Kiseleva, T. G. Sazontova, and N. N. Mikhailova. "EXPERIMENTAL STUDY OF THE IMPACT OF LOW FLUORINE CONCENTRATIONS ON THE TISSUE LEVEL OF HSP FAMILY PROTEINS." Hygiene and sanitation 97, no. 7 (2018): 604–8. http://dx.doi.org/10.18821/0016-9900-2018-97-7-604-608.

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Introduction. Fluoride in high concentrations has a toxic effect not only on bone tissue but also on the heart, liver, kidneys, and brain. In the implementation of the response to toxic doses of fluorine the proteins of the HSP family are involved regulating intracellular and tissue homeostasis under various stress effects. The toxic effect of high fluorine concentrations the mechanisms of which are disclosed in fluorosis can be realized and at a level significantly lower than a toxic one. In the literature, there is little data on the peculiarities of the effects of low fluorine concentrations at the tissue and cellular levels. The aim of the study. To investigate the impact of low fluorine concentrations on the tissue level of HSP family proteins in the brain and liver of laboratory animals. Material and methods. The experiments were carried out on 60 white male rats of the same age weighing 200-250 g. The rats were divided into 2 groups: the control and the group of the animals exposed to sodium fluoride (NaF) within 6 weeks (at a concentration of 10 mg/l corresponding to the daily fluorine dose of 1.2 mg/kg per body weight). We determined the level of inducible HSP72 and HSP32 (heme-oxygenase-1) referred to proteins of HSP family (Heat shock proteins), the activity of free radical processes and antioxidant enzymes (superoxide dismutase (SOD) and catalase) in the brain and liver tissues. Results. The important role of stress-inducible HSP72 protein in protecting the brain from the damage caused by the prolonged exposure to low fluorine concentrations was shown. In the liver, a protective role against fluoride exposure is played by the protein HSP32 with antioxidant properties. At the tissue level, the prolongation of the terms of the development of chronic fluoride intoxication with low fluorine concentrations was revealed. In the liver appeared to be the highly sensitive organ to the fluorine accumulation, the significant lesion was detected.

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12

Stuhlmeier, Karl M. "Activation and regulation of Hsp32 and Hsp70." European Journal of Biochemistry 267, no. 4 (2000): 1161–67. http://dx.doi.org/10.1046/j.1432-1327.2000.01112.x.

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13

Kneidinger, Michael, Karoline V. Gleixner, Rudin Kondo, et al. "Heme Oxygenase-1 (HO-1)/Heat Shock Protein 32 (Hsp32) as a Novel Survival Factor and Target in AML." Blood 108, no. 11 (2006): 1901. http://dx.doi.org/10.1182/blood.v108.11.1901.1901.

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Abstract Heme oxygenase 1 (HO-1), also known as heat shock protein 32 (Hsp32), has recently been identified as a stress-related survival molecule that acts anti-apoptotic and cytoprotective in inflammatory reactions. Recent data suggest that HO-1/Hsp32 is also expressed in neoplastic cells in various malignancies. In the present study, we provide evidence that HO-1 is constitutively expressed in primary leukemic cells in patients with acute myeloid leukemia (AML, n=17) and in various AML cell lines such as HL60, KG1, KG1a, and U937. Expression of HO-1 mRNA was demonstrable by RT-PCR, and the HO-1 protein by immunocytochemistry and Western blotting. In addition, we were able to demonstrate expression of HO-1 mRNA and of HO-1 protein in the CD34+/CD38− progenitor/stem cell fraction in the leukemic clone in patients with AML. The HO-1 inductor hemin (10 μM) was found to promote expression of HO-1 in AML cells. Incubation with the HO-1-targeting drugs pegylated zink protoporphyrin (PEG-ZnPP) or styrene maleic acid-conjugated ZnPP (SMA-ZnPP), resulted in a dose-dependent inhibition of growth of leukemic cells at pharmacologic concentrations (IC50: 5–20 μM for cell lines and primary AML cells). The SMA-ZnPP-induced growth-inhibition of AML cells were found to be associated with induction of apoptosis as evidenced by light microscopy, electron microscopy, and by a Tunel assay. In consecutive experiments, combination experiments were performed using SMA-ZnPP and AML cell lines. In these experiments, SMA-ZnPP was found to synergize with cytarabine in producing growth inhibition in all AML cell lines tested. In summary, these data show that HO-1/Hsp32 is a novel survival factor and interesting target in AML. The clinical significance of this observation remains to be determined in forthcoming trials.

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14

Zhukova, A. G., L. G. Gorokhova, A. S. Kazitskaya, T. K. Yadykina, N. N. Mikhailova, and Yu V. Arkhipenko. "Adaptogenic correction of free radical brain damage in subchronic exposure to sodium fl uoride." Russian Journal of Occupational Health and Industrial Ecology, no. 6 (July 10, 2020): 381–86. http://dx.doi.org/10.31089/1026-9428-2020-60-6-381-386.

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Introduction. Fluorine compounds in small doses, but with prolonged exposure, cause various disorders in organs at the cellular and molecular levels. Activation of free-radical processes plays an important role in the damaging eff ect of fl uorides. Th erefore, one of the most eff ective ways to limit fl uorine-induced damage is to directly aff ect free-radical processes using herbal preparations with antioxidant properties.The aim of the study is to study the eff ect of a dihydroquercetin-based drug on the activity of free radical processes in brain tissue under subchronic exposure to sodium fl uoride (NaF).Materials and methods. Th e work was performed on white male laboratory rats weighing 200-250 g. Th e rats were divided into 3 groups: 1 — control; 2 — rats with chronic exposure to sodium fl uoride (NaF) for 9 weeks; 3 — rats receiving a NAF solution with simultaneous administration of a complex drug based on dihydroquercetin at a dose of 3 mg/kg in 1% starch gel for 3, 6 and 9 weeks. The activity of free radical oxidation and antioxidant defense enzymes — superoxide dismutase (SOD) and catalase-was determined in the cerebral cortex. Th e level of expression of hypoxia-induced transcription factor HIF — 1A and inducible forms of proteins HSP72 and HSP32 were determined in the cytosolic fraction of brain tissue.Results. In the early stages of subchronic fl uoride exposure (1-3 weeks), the expression of protective proteins HIF-1α, HSP72, HSP32 and catalase was shown in the rat cortex, as a result of which the activity of free-radical processes was maintained at the control level. An increase in the timing of fl uoride intake to 9 weeks led to a decrease in antioxidant protection and signifi cant activation of free radical oxidation in brain tissue. Daily administration of a complex drug with dihydroquercetin for 3, 6 and 9 weeks to rats with subchronic fl uoride exposure led to a decrease in the severity of pro- and antioxidant balance disorders in the cerebral cortex. At the same time, the greatest protective eff ect of dihydroquercetin with fl uoride exposure was manifested by the 9th week of its administration.Conclusions. When subchronic intake of fl uorides in the body, the drug based on dihydroquercetin has a neuroprotective eff ect, which is manifested by an increase in the activity of antioxidant enzymes of fr ee radical oxidation and catalase and the resistance of the cortex to induced fr ee radical oxidation.

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15

Novo, Giuseppina, Francesco Cappello, Manfredi Rizzo, et al. "Hsp60 and heme oxygenase-1 (Hsp32) in acute myocardial infarction." Translational Research 157, no. 5 (2011): 285–92. http://dx.doi.org/10.1016/j.trsl.2011.01.003.

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16

Moerman, Andrea M., and Claudette Klein. "Dictyostelium discoideum Hsp32 is a resident nucleolar heat-shock protein." Chromosoma 107, no. 3 (1998): 145–54. http://dx.doi.org/10.1007/s004120050291.

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17

Bilszta, Justin L. C., Gregory J. Dusting, and Fan Jiang. "Arsenite Increases Vasoconstrictor Reactivity in Rat Blood Vessels: Role of Endothelial Nitric Oxide Function." International Journal of Toxicology 25, no. 4 (2006): 303–10. http://dx.doi.org/10.1080/10915810600746130.

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Arsenite has been shown to inhibit endothelium-dependent, nitric oxide-mediated vasodilation in vitro. This study investigated the effects of arsenite on vascular reactivity in vivo. Saline or sodium arsenite (6 mg kg−1) was administered intravenously in Wistar-Kyoto rats for 4 h. As compared to saline, arsenite significantly increased vasoconstrictor responses to phenylephrine in both rat isolated aorta and renal arteries examined in tissue bath. This change was diminished after preincubation of the tissues with the nitric oxide synthase inhibitor NG-nitro-l-arginine methyl ester, which increased phenylephrine-induced vasoconstriction to a similar extent as arsenite. In contrast, acetylcholine-induced vasodilation, mediated by nitric oxide in the aorta and by an endothelium-derived hyperpolarizing factor in renal arteries, was not affected by arsenite. Arsenite induced expression of heat shock proteins Hsp72, Hsp32, and Hsp90, but endothelial nitric oxide synthase expression was not changed. The effects of arsenite on vasoreactivity were unlikely to be mediated by heat shock protein induction, because blockade of heat shock protein induction had little effect on the increased vasoconstriction in vessels from arsenite-treated animals. Our study suggests that in vivo arsenic treatment increases vasoconstrictor reactivity by compromising basal endothelial nitric oxide function, which is not caused by altered endothelial nitric oxide synthase expression.

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MOERMAN, A., and C. KLEIN. "Developmental Regulation of Hsp32, a Small Heat Shock Protein inDictyostelium discoideum☆." Experimental Cell Research 237, no. 1 (1997): 149–57. http://dx.doi.org/10.1006/excr.1997.3774.

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19

Rössner, Pavel, Blanka Binková, and Radim J. Šrám. "Heat shock proteins hsp32 and hsp70 as biomarkers of an early response?" Mutation Research/Genetic Toxicology and Environmental Mutagenesis 542, no. 1-2 (2003): 105–16. http://dx.doi.org/10.1016/j.mrgentox.2003.09.005.

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20

Hirata, K. "Induction of HSP27 and HSP32 in Schwann cells of injured sciatic nerves." Neuroscience Research 38 (2000): S107. http://dx.doi.org/10.1016/s0168-0102(00)81488-1.

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21

Wang, Jishi, Baisheng Chai, Cheng Chen, and Qin Fang. "The Effect of HO-1 on AMN107 In Promoting K562/A02 Apoptosis." Blood 116, no. 21 (2010): 1231. http://dx.doi.org/10.1182/blood.v116.21.1231.1231.

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Abstract Abstract 1231 Aim: Heme oxygenase-1(HO-1), also known as heat shock protein 32(Hsp32), has recently been identified as a stress-related survival molecule that acts anti-apoptotic and cytoprotective in inflammatory reactions. In the present study, we provide evidence that HO-1 is effective on AMN107(Nilotinib) in promoting K562/A02 apoptosis which is induced by STI571(Imatinib),and investigate AMN107 on the mechanism of resistance to STI571. Method: HO-1 gene was cloned from rat liver by RT-PCR. And the retrovirus vector pQCXIP-EGFP-C1 was constructed. K562/A02 cell which was expressed HO-1 highly was seemed as gene-transfected group. At the same time, we set the empty vector transfected group and untransfected group. K562/A02 cell was cultivated with AMN107 in gene-transfected, empty vector transfected and untransfected groups. Expression of HO-1 mRNA was demonstrable by RT-PCR, Real-time PCR, and the HO-1 protein by Western blotting. Constant MTT assay and cell number count were used to detect the proliferation of leukemia cells after treatment with AMN107. Apoptosis was determined by morphological observation and flow cytomertry analysis after AnnexinV/PI double labeling. Also we detected the intracellular drug concentration by HPLC after treatment with the same concentration of AMN107. Result: HO-1 gene was cloned from rat liver successfully. The sequences were confirmed by restriction enzyme digestion analysis and sequencing. The virus was packaged in 293T cells and titer of virus was tested by Real-Time PCR, 8.09×1010v.p./mL. Following transfer the retrovirus vector into K562/A02, 72 hours after transfection, it showed that HO-1 was expressed highest by fluorescence micrope. High expression of HO-1 was detected by RT-PCR, Real-Time PCR and Western blotting. After 10umol/L AMN107 treated, the expression of HO-1 was clearly lower in empty vector transfected group and untransfected group (p <0.05), but in transfected group there was no obvious change. MTT assay showed that after AMN107 treated, IC50 value in transfected group was 5.62174 mmol/L, significantly higher than empty vector transfected and untransfected group(P<0.05). Cell number count showed that after AMN107 treated the activity of cells were decreased sharply in empty vector transfected and untransfected group, but no significant change in transfected group. At 48 hours after treatment with 10umol/L AMN107 by flow cytometry, the survival rate in transfected group was lowest which is 8.3±1.2%(P>0.05). And in empty vector transfected and untransfected group the survival rate was 35.3±1.6% and 37.5±1.3%(P<0.01). HPLC analysis showed that intracellular drug concentration was lowest in transfected group which treatment with the same concentration of AMN107. Conclusion: STI571 resistance is a major cause of STI571 treatment failure in chronic myeloid leukemia(CML) patients. Our data showed that HO-1/Hsp32 is a novel survival factor and interesting target in K562/A02. In addition, it could predict the risk of resistance to STI571 therapy. Down-regulating of HO-1/Hsp32 in chronic myeloid leukemia cell is associated with reduced tumor cell growth and induction of apoptosis. Based on these data, it seems desirable to explore the value of the Hsp32-targeting drug in clinical trials in patients with leukemia and solid tumors. Disclosures: No relevant conflicts of interest to declare.

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De Maria, Adriana Clerici, Andréa Moerman, Claudette Klein, and Suely Lopes Gomes. "Cloning, structural analysis and expression of the gene encoding Hsp32 from Dictyostelium discoideum." Gene 193, no. 2 (1997): 173–80. http://dx.doi.org/10.1016/s0378-1119(97)00110-8.

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Fairfield, Damon A., Ariane C. Kanicki, Margaret I. Lomax, and Richard A. Altschuler. "Induction of heat shock protein 32 (Hsp32) in the rat cochlea following hyperthermia." Hearing Research 188, no. 1-2 (2004): 1–11. http://dx.doi.org/10.1016/s0378-5955(03)00369-1.

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Huang, Guoyang, Jiale Diao, Hongjie Yi, Li Xu, Jiajun Xu, and Weigang Xu. "Signaling pathways involved in HSP32 induction by hyperbaric oxygen in rat spinal neurons." Redox Biology 10 (December 2016): 108–18. http://dx.doi.org/10.1016/j.redox.2016.09.011.

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25

Ewing, James F., and Mahin D. Maines. "Glutathione Depletion Induces Heme Oxygenase-1 (HSP32) mRNA and Protein in Rat Brain." Journal of Neurochemistry 60, no. 4 (1993): 1512–19. http://dx.doi.org/10.1111/j.1471-4159.1993.tb03315.x.

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26

Bergeron, Marcelle, Donna M. Ferriero, and Frank R. Sharp. "Developmental expression of heme oxygenase-1 (HSP32) in rat brain: an immunocytochemical study." Developmental Brain Research 105, no. 2 (1998): 181–94. http://dx.doi.org/10.1016/s0165-3806(97)00169-7.

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27

Szalay, László, Tomoharu Shimizu, Takao Suzuki, et al. "Estradiol improves cardiac and hepatic function after trauma-hemorrhage: role of enhanced heat shock protein expression." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 290, no. 3 (2006): R812—R818. http://dx.doi.org/10.1152/ajpregu.00658.2005.

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Although studies indicate that 17β-estradiol administration after trauma-hemorrhage (T-H) improves cardiac and hepatic functions, the underlying mechanisms remain unclear. Because the induction of heat shock proteins (HSPs) can protect cardiac and hepatic functions, we hypothesized that these proteins contribute to the salutary effects of estradiol after T-H. To test this hypothesis, male Sprague-Dawley rats (∼300 g) underwent laparotomy and hemorrhagic shock (35–40 mmHg for ∼90 min) followed by resuscitation with four times the shed blood volume in the form of Ringer lactate. 17β-estradiol (1 mg/kg body wt) was administered at the end of the resuscitation. Five hours after T-H and resuscitation there was a significant decrease in cardiac output, positive and negative maximal rate of left ventricular pressure. Liver function as determined by bile production and indocyanine green clearance was also compromised after T-H and resuscitation. This was accompanied by an increase in plasma alanine aminotransferase (ALT) levels and liver perfusate lactic dehydrogenase levels. Furthermore, circulating levels of TNF-α, IL-6, and IL-10 were also increased. In addition to decreased cardiac and hepatic function, there was an increase in cardiac HSP32 expression and a reduction in HSP60 expression after T-H. In the liver, HSP32 and HSP70 were increased after T-H. There was no change in heart HSP70 and liver HSP60 after T-H and resuscitation. Estradiol administration at the end of T-H and resuscitation increased heart/liver HSPs expression, ameliorated the impairment of heart/liver functions, and significantly prevented the increase in plasma levels of ALT, TNF-α, and IL-6. The ability of estradiol to induce HSPs expression in the heart and the liver suggests that HSPs, in part, mediate the salutary effects of 17β-estradiol on organ functions after T-H.

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Grasso, S., C. Scifo, V. Cardile, R. Gulino, and M. Renis. "Adaptive Responses to the Stress Induced by Hyperthermia or Hydrogen Peroxide in Human Fibroblasts." Experimental Biology and Medicine 228, no. 5 (2003): 491–98. http://dx.doi.org/10.1177/15353702-0322805-12.

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Perturbation of oxidant/antioxidant cellular balance, induced by cellular metabolism and by exogenous sources, causes deleterious effects to proteins, lipids, and nucleic acids, leading to a condition named “oxidative stress” that is involved in several diseases, such as cancer, ischemia-reperfusion injury, and neurodegenerative disorders. Among the exogenous agents, both H2O2 and hyperthermia have been implicated in oxidative stress promotion linked with the activation of apoptotic or necrotic mechanisms of cell death. The goal of this work was to better understand the involvement of some stress-related proteins in adaptive responses mounted by human fibroblasts versus the oxidative stress differently induced by 42°C hyperthermia or H2O2. The research was developed, switching off inducible nitric oxide synthase (iNOS) expression through antisense oligonucleotide transfection by studying the possible coregulation in the expression of HSP32 (also named HO-1), HSP70, and iNOS and their involvement in the induction of DNA damage. Several biochemical parameters, such as cell viability (MTT assay), cell membrane integrity (lactate dehydrogenase release), reactive oxygen species formation, glutathione levels, immunocytochemistry analysis of iNOS, HSP70, and HO-1 levels, genomic DNA fragmentation (HALO/COMET assay), and transmembrane mitochondrial potential (ΔΨ) were examined. Cells were collected immediately at the end of the stress-inducing treatment. The results, confirming the pleiotropic function of i-NOS, indicate that: (i) HO-1/HSP32, HSP70, and iNOS are finely tuned in their expression to contribute all together, in human fibroblasts, in ameliorating the resistance to oxidative stress damage; (ii) ROS exposure, at least in hyperthermia, in human fibroblasts contributes to growth arrest more than to apoptosis activation; and (iii) mitochondrial dysfunction, in presence of iNOS inhibition seems to be clearly involved in apoptotic cell death of human fibroblasts after H2O2 treatment, but not after hyperthermia.

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Taylor, Lee, Angela R. Hillman, Adrian W. Midgley, Daniel J. Peart, Bryna Chrismas, and Lars R. McNaughton. "Hypoxia-mediated prior induction of monocyte-expressed HSP72 and HSP32 provides protection to the disturbances to redox balance associated with human sub-maximal aerobic exercise." Amino Acids 43, no. 5 (2012): 1933–44. http://dx.doi.org/10.1007/s00726-012-1265-3.

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30

Cerny-Reiterer, Sabine, Renata A. Meyer, Harald Herrmann, et al. "Identification of heat shock protein 32 (Hsp32) as a novel target in acute lymphoblastic leukemia." Oncotarget 5, no. 5 (2014): 1198–211. http://dx.doi.org/10.18632/oncotarget.1805.

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31

Maines, Mahin D., and Per-Anders Abrahamsson. "Expression of heme oxygenase-1 (HSP32) in human prostate: normal, hyperplastic, and tumor tissue distribution." Urology 47, no. 5 (1996): 727–33. http://dx.doi.org/10.1016/s0090-4295(96)00010-6.

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32

Hillman, Angela R., Rebecca V. Vince, Lee Taylor, Lars McNaughton, Nigel Mitchell, and Jason Siegler. "Exercise-induced dehydration with and without environmental heat stress results in increased oxidative stress." Applied Physiology, Nutrition, and Metabolism 36, no. 5 (2011): 698–706. http://dx.doi.org/10.1139/h11-080.

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While in vitro work has revealed that dehydration and hyperthermia can elicit increased cellular and oxidative stress, in vivo research linking dehydration, hyperthermia, and oxidative stress is limited. The purpose of this study was to investigate the effects of exercise-induced dehydration with and without hyperthermia on oxidative stress. Seven healthy male, trained cyclists (power output (W) at lactate threshold (LT): 199 ± 19 W) completed 90 min of cycling exercise at 95% LT followed by a 5-km time trial (TT) in 4 trials: (i) euhydration in a warm environment (EU-W, control), (ii) dehydration in a warm environment (DE-W), (iii) euhydration in a thermoneutral environment (EU-T), and (iv) dehydration in a thermoneutral environment (DE-T) (W: 33.9 ± 0.9 °C; T: 23.0 ± 1.0 °C). Oxidized glutathione (GSSG) increased significantly postexercise in dehydration trials only (DE-W: p < 0.01, DE-T: p = 0.03), and while not significant, total glutathione (TGSH) and thiobarbituric acid reactive substances (TBARS) tended to increase postexercise in dehydration trials (p = 0.08 for both). Monocyte heat shock protein 72 (HSP72) concentration was increased (p = 0.01) while lymphocyte HSP32 concentration was decreased for all trials (p = 0.02). Exercise-induced dehydration led to an increase in GSSG concentration while maintenance of euhydration attenuated these increases regardless of environmental condition. Additionally, we found evidence of increased cellular stress (measured via HSP) during all trials independent of hydration status and environment. Finally, both 90-min and 5-km TT performances were reduced during only the DE-W trial, likely a result of combined cellular stress, hyperthermia, and dehydration. These findings highlight the importance of fluid consumption during exercise to attenuate thermal and oxidative stress during prolonged exercise in the heat.

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Bechtold, David A., and Ian R. Brown. "Heat shock proteins Hsp27 and Hsp32 localize to synaptic sites in the rat cerebellum following hyperthermia." Molecular Brain Research 75, no. 2 (2000): 309–20. http://dx.doi.org/10.1016/s0169-328x(99)00323-x.

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34

Barton, SGRG, S. Jordan, VR Winrow, P. Domizio, and DS Rampton. "Expression of heat shock proteins hsp60 and hsp32 is increased in H. pylori-infected gastric mucosa." Gastroenterology 114 (April 1998): A928. http://dx.doi.org/10.1016/s0016-5085(98)83778-5.

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35

Abe, Tetsuya, Osamu Yamamoto, Sadao Gotoh, Ying Yan, Nanae Todaka, and Ken Higashi. "Cadmium-Induced mRNA Expression of Hsp32 Is Augmented in Metallothionein-I and -II Knock-out Mice." Archives of Biochemistry and Biophysics 382, no. 1 (2000): 81–88. http://dx.doi.org/10.1006/abbi.2000.1997.

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36

Gleixner, K., M. Mayerhofer, A. Vales, et al. "Targeting of Hsp32 in Solid Tumors and Leukemias: A Novel Approach to Optimize Anticancer Therapy (Supplementry Material)." Current Cancer Drug Targets 9, no. 5 (2009): 675–89. http://dx.doi.org/10.2174/156800909789057024.

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37

Raju, Vulapalli S., and Mahin D. Maines. "Coordinated expression and mechanism of induction of HSP32 (heme oxygenase-1) mRNA by hyperthermia in rat organs." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1217, no. 3 (1994): 273–80. http://dx.doi.org/10.1016/0167-4781(94)90286-0.

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38

Kiemer, Alexandra K., Tobias Gerwig, Alexander L. Gerbes, Herbert Meißner, Manfred Bilzer, and Angelika M. Vollmar. "Kupffer-cell specific induction of heme oxygenase 1 (hsp32) by the atrial natriuretic peptide — role of cGMP." Journal of Hepatology 38, no. 4 (2003): 490–98. http://dx.doi.org/10.1016/s0168-8278(03)00056-4.

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39

Tredget, E. E., Areta E. Kowal-Vern, Joanna E. Goral, Richard L. Gamelli, and Victoria L. McGill. "hsp70, hsp32, and grp78 are increased in thermally injured skin with and without antithrombin(human) concentrate infusion." Journal of Burn Care & Rehabilitation 021, no. 3 (2000): 213–19. http://dx.doi.org/10.1067/mbc.2000.105085.

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40

Kowal-Vern, Areta, Joanna Goral, Richard L. Gamelli, Victoria McGill, and John Clancy. "hsp70, hsp32, and grp78 Are Increased in Thermally Injured Skin With and Without Antithrombin (Human) Concentrate Infusion." Journal of Burn Care & Rehabilitation 21, no. 3 (2000): 213–19. http://dx.doi.org/10.1097/00004630-200021030-00006.

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41

Stahnke, T., C. Richter-Landsberg, C. Stadelmann, A. Netzler, and W. Brück. "Differential upregulation of heme oxygenase-1 (HSP32) in glial cells after oxidative stress and in demyelinating disorders." Journal of Molecular Neuroscience 32, no. 1 (2007): 25–37. http://dx.doi.org/10.1007/s12031-007-0005-8.

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42

Chiu, Jen-Hwey, Ya-Fang Cheng, Jir-You Wang, and Cheng-Fong Hsu. "Remote pharmacological preconditioning on median nerve territory increases Hsp32 expression and attenuates ischemia–reperfusion injury in rat heart." Life Sciences 90, no. 17-18 (2012): 629–36. http://dx.doi.org/10.1016/j.lfs.2012.02.007.

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43

Yu, Alice L., Jerome Moriniere, Marco Birke та ін. "Reactivation of Optic Nerve Head Astrocytes by TGF-β2 and H2O2Is Accompanied by Increased Hsp32 and Hsp47 Expression". Investigative Opthalmology & Visual Science 50, № 4 (2009): 1707. http://dx.doi.org/10.1167/iovs.08-1961.

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44

V. Kurian, M., J. M. Mullins, L. R. Hamilton, P. M. Mehl та J. K. Keevan. "Elevated Levels of Stress Proteins (Hsp32 and Hsp70i) in H9c2 Cells Exposed to 60Hz, 120礣 Magnetic Field". Molecular & Cellular Biomechanics 3, № 4 (2006): 217–18. http://dx.doi.org/10.32604/mcb.2006.003.217.

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45

Bergeron, Marcelle, Donna M. Ferriero, Hendrik J. Vreman, David K. Stevenson, and Frank R. Sharp. "Hypoxia-Ischemia, but Not Hypoxia Alone, Induces the Expression of Heme Oxygenase-1 (HSP32) in Newborn Rat Brain." Journal of Cerebral Blood Flow & Metabolism 17, no. 6 (1997): 647–58. http://dx.doi.org/10.1097/00004647-199706000-00006.

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Heme oxygenase (HO) is the rate-limiting enzyme in the degradation of heme to produce bile pigments and carbon monoxide. The HO-1 isozyme is induced by a variety of agents such as heat, heme, and hydrogen peroxide. Evidence suggests that the bile pigments serve as antioxidants in cells with compromised defense mechanisms. Because hypoxia-ischemia (HI) increases the level of oxygen free radicals, the induction of HO-1 expression in the brain during ischemia could modulate the response to oxidative stress. To study the possible involvement of HO-1 in neonatal hypoxia-induced ischemic tolerance, we examined the brains of newborn rat pups exposed to 8% O2 (for 2.5 to 3 hours), and the brain of chronically hypoxic rat pups with congenital cardiac defects (Wistar Kyoto; WKY/ NCr). Heme oxygenase-1 immunostaining did not change after either acute or chronic hypoxia, suggesting that HO-1 is not a good candidate for explaining hypoxia preconditioning in newborn rat brain. To study the role of HO-1 in neonatal HI, 1-week-old rats were subjected to right carotid coagulation and exposure to 8% O2/92% N2 for 2.5 hours. Whereas HO enzymatic activity was unchanged in ipsilateral cortex and subcortical regions compared with the contralateral hemisphere or control brains, immunocytochemistry and Western blot analysis showed increased HO-1 staining in ipsilateral cortex, hippocampus, and striatum at 12 to 24 hours up to 7 days after HI. Double fluorescence immunostaining showed that HO-1 was expressed mostly in ED-1 positive macrophages. Because activated brain macrophages have been associated with the release of several cytotoxic molecules, the presence of HO-1 positive brain macrophages may determine the tissue vulnerability after HI injury.

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46

Kelly, S. E., and I. L. Cartwright. "Perturbation of chromatin architecture on ecdysterone induction of Drosophila melanogaster small heat shock protein genes." Molecular and Cellular Biology 9, no. 1 (1989): 332–35. http://dx.doi.org/10.1128/mcb.9.1.332.

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Alterations in the pattern of DNase I hypersensitivity were observed on ecdysterone-stimulated transcription of Drosophila melanogaster small heat shock protein genes. Perturbations were induced near hsp27 and hsp22, coupled with an extensive domain of chromatin unfolding in the intergenic region between hsp23 and the developmentally regulated gene 1. These regions represent candidates for ecdysterone regulatory interactions.

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47

Kelly, S. E., and I. L. Cartwright. "Perturbation of chromatin architecture on ecdysterone induction of Drosophila melanogaster small heat shock protein genes." Molecular and Cellular Biology 9, no. 1 (1989): 332–35. http://dx.doi.org/10.1128/mcb.9.1.332-335.1989.

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Alterations in the pattern of DNase I hypersensitivity were observed on ecdysterone-stimulated transcription of Drosophila melanogaster small heat shock protein genes. Perturbations were induced near hsp27 and hsp22, coupled with an extensive domain of chromatin unfolding in the intergenic region between hsp23 and the developmentally regulated gene 1. These regions represent candidates for ecdysterone regulatory interactions.

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48

Amin, J., R. Mestril, and R. Voellmy. "Genes for Drosophila small heat shock proteins are regulated differently by ecdysterone." Molecular and Cellular Biology 11, no. 12 (1991): 5937–44. http://dx.doi.org/10.1128/mcb.11.12.5937.

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Genes for small heat shock proteins (hsp27 to hsp22) are activated in late third-instar larvae of Drosophila melanogaster in the absence of heat stress. This regulation has been simulated in cultured Drosophila cells in which the genes are activated by the addition of ecdysterone. Sequence elements (HERE) involved in ecdysterone regulation of the hsp27 and hsp23 genes have been defined by transfection studies and have recently been identified as binding sites for ecdysterone receptor. We report here that the hsp27 and hsp23 genes are regulated differently by ecdysterone. The hsp27 gene is activated rapidly by ecdysterone, even in the absence of protein synthesis. In contrast, high-level expression of the hsp23 gene begins only after a lag of about 6 h, is dependent on the continuous presence of ecdysterone, and is sensitive to low concentrations of protein synthesis inhibitors. Transfection experiments with reporter constructs show that this difference in regulation is at the transcriptional level. Synthetic hsp27 or hsp23 HERE sequences confer hsp27- or hsp23-type ecdysterone regulation on a basal promoter. These findings indicate that the hsp27 gene is a primary, and the hsp23 gene is mainly a secondary, hormone-responsive gene. Ecdysterone receptor is implied to play a role in the regulation of both genes.

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49

Amin, J., R. Mestril, and R. Voellmy. "Genes for Drosophila small heat shock proteins are regulated differently by ecdysterone." Molecular and Cellular Biology 11, no. 12 (1991): 5937–44. http://dx.doi.org/10.1128/mcb.11.12.5937-5944.1991.

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Abstract:

Genes for small heat shock proteins (hsp27 to hsp22) are activated in late third-instar larvae of Drosophila melanogaster in the absence of heat stress. This regulation has been simulated in cultured Drosophila cells in which the genes are activated by the addition of ecdysterone. Sequence elements (HERE) involved in ecdysterone regulation of the hsp27 and hsp23 genes have been defined by transfection studies and have recently been identified as binding sites for ecdysterone receptor. We report here that the hsp27 and hsp23 genes are regulated differently by ecdysterone. The hsp27 gene is activated rapidly by ecdysterone, even in the absence of protein synthesis. In contrast, high-level expression of the hsp23 gene begins only after a lag of about 6 h, is dependent on the continuous presence of ecdysterone, and is sensitive to low concentrations of protein synthesis inhibitors. Transfection experiments with reporter constructs show that this difference in regulation is at the transcriptional level. Synthetic hsp27 or hsp23 HERE sequences confer hsp27- or hsp23-type ecdysterone regulation on a basal promoter. These findings indicate that the hsp27 gene is a primary, and the hsp23 gene is mainly a secondary, hormone-responsive gene. Ecdysterone receptor is implied to play a role in the regulation of both genes.

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50

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

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The molecular chaperone Hsp33 inEscherichia coliresponds to oxidative stress conditions with the rapid activation of its chaperone function. On its activation pathway, Hsp33 progresses through three major conformations, starting as a reduced, zinc-bound inactive monomer, proceeding through an oxidized zinc-free monomer, and ending as a fully active oxidized dimer. While it is known that Hsp33 senses oxidative stress through its C-terminal four-cysteine zinc center, the nature of the conformational changes in Hsp33 that must take place to accommodate this activation process is largely unknown. To investigate these conformational rearrangements, we constructed constitutively monomeric Hsp33 variants as well as fragments consisting of the redox regulatory C-terminal domain of Hsp33. These proteins were studied by a combination of biochemical and NMR spectroscopic techniques. We found that in the reduced, monomeric conformation, zinc binding stabilizes the C terminus of Hsp33 in a highly compact, α-helical structure. This appears to conceal both the substrate-binding site as well as the dimerization interface. Zinc release without formation of the two native disulfide bonds causes the partial unfolding of the C terminus of Hsp33. This is sufficient to unmask the substrate-binding site, but not the dimerization interface, rendering reduced zinc-free Hsp33 partially active yet monomeric. Critical for the dimerization is disulfide bond formation, which causes the further unfolding of the C terminus of Hsp3 and allows the association of two oxidized Hsp33 monomers. This then leads to the formation of active Hsp33 dimers, which are capable of protecting cells against the severe consequences of oxidative heat stress.

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