Cells of Bacillus megaterium 27 were challenged by a 30-min heat shock at 45 degrees C during various sporulation stages and then shifted back to a temperature permissive for sporulation (27 degrees C), at which they developed spores. Heat shock applied at 120 min after the end of the exponential phase induced synthesis of heat shock proteins (HSPs) in the sporangia and delayed the inactivation of spores at 85 degrees C. Several HSPs, mainly HSP 70, could be detected in the cytoplasm of these spores. An analogous HSP, the main HSP induced by increased temperature during growth, belongs to the GroEL group according to its N-terminal sequence. The identity of this protein was confirmed by Western blot (immunoblot) analysis with polyclonal antibodies against B. subtilis GroEL. Sporangia treated by heat shock immediately or 240 min after exponential phase also synthesized HSPs, but none of them could be detected in the spores in an appreciable amount. These spores showed only a slightly increased heat resistance.

• MeSH
• autoradiografie MeSH
• Bacillus megaterium růst a vývoj   metabolismus   fyziologie   MeSH
• bakteriální proteiny biosyntéza   izolace a purifikace   MeSH
• časové faktory MeSH
• chaperon hsp60 MeSH
• cytoplazma metabolismus   MeSH
• elektroforéza v polyakrylamidovém gelu MeSH
• kinetika MeSH
• molekulární sekvence - údaje MeSH
• molekulová hmotnost MeSH
• proteiny teplotního šoku biosyntéza   izolace a purifikace   MeSH
• radioizotopy síry MeSH
• sekvence aminokyselin MeSH
• sírany metabolismus   MeSH
• spory bakteriální fyziologie   MeSH
• vysoká teplota MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• bakteriální proteiny MeSH
• chaperon hsp60 MeSH
• proteiny teplotního šoku MeSH
• radioizotopy síry MeSH
• sírany MeSH
• sodium sulfate MeSH Prohlížeč

Heat-shock proteins (Hsps) are thought to play a role in the development of cancer and to modulate tumor response to cytotoxic therapy. In this study, Hsp27, Hsp60, Hsp90α, and HspBP1 gene expression was investigated in human leukemia cell lines as well as in leukemia cells derived from patients with the onset of the disease. Hsp70 membrane expression and expression of Hsp27, Hsp60, Hsp70, Hsp90α, and HspBP1 genes were also tested in samples from leukemia patients. Relative Hsps gene expression was examined in human leukemia cell lines and also in patients, using real-time quantitative reverse-transcriptase polymerase chain reaction (RT-PCR). Hsp70 cell surface expression was studied in patients with leukemia onset using flow cytometry. All tested cell lines showed significantly increased expression of Hsp60, Hsp90α, and HspBP1 genes compared with a cohort of healthy controls; additionally there was increased Hsp27 expression except for Jurkat and CCRF cells. Significantly higher gene expression of Hsp27, Hsp60, Hsp90α, and HspBP1 was observed in the peripheral blood of patients compared with bone marrow and healthy control samples, while Hsp70 expression was without any significant difference among cohorts. Hsp70 cell surface expression was found on defrosted and cultured leukemia cells but not on unprocessed biological samples from patients. Leukemia cells showed a heterogeneous pattern of Hsp gene expression among leukemia cell lines as well as in peripheral blood and bone marrow of patients.

• MeSH
• buněčná membrána metabolismus   MeSH
• chaperon hsp60 genetika   metabolismus   MeSH
• dospělí MeSH
• kohortové studie MeSH
• kojenec MeSH
• leukemie genetika   metabolismus   patologie   MeSH
• lidé středního věku MeSH
• lidé MeSH
• messenger RNA genetika   MeSH
• mladiství MeSH
• mladý dospělý MeSH
• molekulární chaperony MeSH
• nádorové buňky kultivované MeSH
• polymerázová řetězová reakce s reverzní transkripcí MeSH
• předškolní dítě MeSH
• prognóza MeSH
• proteiny tepelného šoku HSP27 genetika   metabolismus   MeSH
• proteiny tepelného šoku HSP70 genetika   metabolismus   MeSH
• proteiny tepelného šoku HSP90 genetika   metabolismus   MeSH
• proteiny teplotního šoku MeSH
• průtoková cytometrie MeSH
• senioři MeSH
• studie případů a kontrol MeSH
• Check Tag
• dospělí MeSH
• kojenec MeSH
• lidé středního věku MeSH
• lidé MeSH
• mladiství MeSH
• mladý dospělý MeSH
• mužské pohlaví MeSH
• předškolní dítě MeSH
• senioři MeSH
• ženské pohlaví MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• srovnávací studie MeSH
• Názvy látek
• chaperon hsp60 MeSH
• HSP90AA2P protein, human MeSH Prohlížeč
• HSPB1 protein, human MeSH Prohlížeč
• messenger RNA MeSH
• molekulární chaperony MeSH
• proteiny tepelného šoku HSP27 MeSH
• proteiny tepelného šoku HSP70 MeSH
• proteiny tepelného šoku HSP90 MeSH
• proteiny teplotního šoku MeSH

The heat shock response of growing and fully-grown pig oocytes was analyzed in vitro by determining heat shock protein70 (HSP70) synthesis under both normal conditions (39 degrees C; 0 and 6h) and after heat shock (43 degrees C; 1, 4 and 6h). The expression of HSP70 in oocytes was detected by immunoblotting analysis. Growing oocytes measuring 80-99 microm synthesized a high number of HSP70 without heat shock effect, and these were capable of increasing the synthesis of HSP70 after heat shock to a maximum after 1h. Growing oocytes measuring 100-115 microm also synthesized HSP70 without heat shock and after it, but the HSP70 synthesis was not statistically changed by increasing duration of heat shock. In fully-grown oocytes, great amounts of HSP70 were found without heat shock treatment, and the contents of HSP70 significantly decreased after heat shock. These results indicate that growing oocytes are able to synthesize HSP70 after heat shock. This ability declines at the end of the growth period, and fully-grown oocytes are unable to induce HSP70 synthesis after heat shock. HSP70 is synthesized and stored during oocyte growth. The high HSP70 synthesis in non-heat-treated growing oocytes and a great amount of HSP70 in fully-grown oocytes support the hypothesis that HSP70 is important for oocyte growth and maturation.

• MeSH
• oocyty chemie   růst a vývoj   MeSH
• prasata * MeSH
• proteiny tepelného šoku HSP70 analýza   MeSH
• vysoká teplota * MeSH
• western blotting MeSH
• zvířata MeSH
• Check Tag
• ženské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• proteiny tepelného šoku HSP70 MeSH

Heat shock proteins (HSPs) HSP27, HSP70 and HSP90 are molecular chaperones; their expression is increased after exposure of cells to conditions of environmental stress, including heat shock, heavy metals, oxidative stress, or pathologic conditions, such as ischemia, infection, and inflammation. Their protective function is to help the cell cope with lethal conditions. The HSPs are a class of proteins which, in normal cells, are responsible for maintaining homeostasis, interacting with diverse protein substrates to assist in their folding, and preventing the appearance of folding intermediates that lead to misfolded or damaged molecules. They have been shown to interact with different key apoptotic proteins and play a crucial role in regulating apoptosis. Several HSPs have been demonstrated to directly interact with various components of tightly regulated caspase-dependent programmed cell death. These proteins also affect caspase-independent apoptosis by interacting with apoptogenic factors. Heat shock proteins are aberrantly expressed in hematological malignancies. Because of their prognostic implications and functional role in leukemias, HSPs represent an interesting target for antileukemic therapy. This review will describe different molecules interacting with anti-apoptotic proteins HSP70 and HSP90, which can be used in cancer therapy based on their inhibition.

• MeSH
• apoptóza MeSH
• leukemie patologie   MeSH
• lidé MeSH
• proteiny tepelného šoku HSP27 fyziologie   MeSH
• proteiny tepelného šoku HSP70 antagonisté a inhibitory   chemie   fyziologie   MeSH
• proteiny tepelného šoku HSP90 antagonisté a inhibitory   chemie   fyziologie   MeSH
• proteiny teplotního šoku fyziologie   MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• přehledy MeSH
• Názvy látek
• proteiny tepelného šoku HSP27 MeSH
• proteiny tepelného šoku HSP70 MeSH
• proteiny tepelného šoku HSP90 MeSH
• proteiny teplotního šoku MeSH

• MeSH
• chaperon hsp60 analýza   MeSH
• Echinococcus chemie   MeSH
• echinokokóza jater parazitologie   veterinární   MeSH
• imunoblotting MeSH
• nemoci ovcí parazitologie   MeSH
• ovce MeSH
• proteiny tepelného šoku HSP70 analýza   MeSH
• teplota MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• chaperon hsp60 MeSH
• proteiny tepelného šoku HSP70 MeSH

Heat shock proteins (HSP) are produced in response to various stress stimuli to prevent cell damage. We evaluated the involvement of nitric oxide (NO) and reactive oxygen species (ROS) in the accumulation of Hsp70 proteins in tomato leaves induced by abiotic and biotic stress stimuli. A model system of leaf discs was used with two tomato genotypes, Solanum lycopersicum cv. Amateur and Solanum chmielewskii, differing in their resistance to fungal pathogen Oidium neolycopersici. Leaf discs were exposed to stress factors as heat shock and pathogen infection alone or in a combination, and treated with substances modulating endogenous NO and ROS levels. Two proteins of Hsp70 family were detected in stressed tomato leaf discs: a heat-inducible 72 kDa protein and a constitutive 75 kDa protein. The pathogenesis and mechanical stress influenced Hsp75 accumulation, whereas heat stress induced mainly Hsp72 production. Treatment with NO donor and NO scavenger significantly modulated the level of Hsp70 in variable manner related to the genotype resistance. Hsp70 accumulation correlated with endogenous NO level in S. lycopersicum and ROS levels in S. chmielewskii. We conclude NO and ROS are involved in the regulation of Hsp70 production and accumulation under abiotic and biotic stresses in dependence on plant ability to trigger its defence mechanisms.

• MeSH
• Ascomycota fyziologie   MeSH
• nemoci rostlin mikrobiologie   MeSH
• oxid dusnatý metabolismus   MeSH
• proteiny tepelného šoku HSP70 metabolismus   MeSH
• reakce na tepelný šok MeSH
• reaktivní formy kyslíku metabolismus   MeSH
• Solanum lycopersicum genetika   mikrobiologie   fyziologie   MeSH
• Solanum genetika   mikrobiologie   fyziologie   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• oxid dusnatý MeSH
• proteiny tepelného šoku HSP70 MeSH
• reaktivní formy kyslíku MeSH

The review concerns heat shock proteins and their significance in immune reactions. It focuses on problems of physiological and pathological interactions in etiology and duration of autoimmune diseases and infection processes, especially fungal infections. New trends are described in exploitation of heat shock proteins for preparation of specific protective vaccines.

• MeSH
• autoimunitní nemoci imunologie   patofyziologie   MeSH
• infekce imunologie   mikrobiologie   patofyziologie   MeSH
• lidé MeSH
• mykózy imunologie   patofyziologie   MeSH
• proteiny teplotního šoku metabolismus   MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Názvy látek
• proteiny teplotního šoku MeSH

A hyperthermic shock (43 degrees C/30 min) enhances in somite stages of the chick embryo development the activity of the caudal morphogenetic system, manifested by intensive growth of the embryonic trunk. The exposure also induced the synthesis of heat shock proteins (HSP 70). A single administration of a bioflavonoid quercetin dissolved in DMSO to chick embryos in stages HH 10-11 (10-14 somites) prior to heat exposure inhibited both the growth acceleration and the HSP induction.

• MeSH
• kuřecí embryo MeSH
• proteiny tepelného šoku HSP70 metabolismus   MeSH
• quercetin farmakologie   MeSH
• reakce na tepelný šok MeSH
• zvířata MeSH
• Check Tag
• kuřecí embryo MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• proteiny tepelného šoku HSP70 MeSH
• quercetin MeSH

OBJECTIVE: The purpose of this study was to determinate the changes of amniotic fluid HSP 70 concentrations in patiens with preterm premature rupture of the membranes, and in the presence of intraamniotic infection and histological changes of inflammations. DESIGN: Prospective study. SETTING: Department of Obstetrics and Gynecology Medical Faculty Charles University Hradec Králové. METHODS: We studied 30 women between 24 and 36 weeks of gestation with preterm premature rupture of the membranes. Samples of amniotic fluid were collected by transabdominal amniocentesis. These patients were divided into 2 groups. In group 1 were patiens with intraamniotic infection. In group 2 were patiens without intraamniotic infection. Among 76% (35/30) patients placenta were collected and assessed for presence or absence acute inflammatory lesions. HSP70 concentration in amniotic fluid were determined using a sensitive and specific diagnostic kit Hsp 70- ELISA kit manufactered Assay Desings, USA. RESULTS: There was no significant difference in the median amniotic fluid HSP70 concentration between patients with preterm rupture of the membranes with IAI and without IAI (patients with IAI: median 5.12 ng/ml, range 3.01-90.37 ng/ml vs. patients without IAI: median 4.68 ng/ml, range 0.58-84.28 ng/ml; p = 0.56). There was no significant difference in the median amniotic fluid HSP70 concentration between patients with preterm rupture of the membranes with presence and absence histological of acute inflammatory lesions in the placenta and membranes (patients with presence: median 6.97 ng/ml, range 2.61-90.37 ng/ml vs. patients with absence: median 4.63 ng/ml, range 0.58-84.28 ng/ml; p = 0.68). CONCLUSION: Intraamniotic levels HSP70 were not associated with intraamniotic infection and acute inflammatory lessions in the placenta and membranes.

• MeSH
• bakteriální infekce metabolismus   MeSH
• chorioamnionitida metabolismus   MeSH
• dospělí MeSH
• infekční komplikace v těhotenství metabolismus   MeSH
• lidé MeSH
• mladiství MeSH
• mladý dospělý MeSH
• plodová voda chemie   MeSH
• předčasný odtok plodové vody metabolismus   MeSH
• proteiny tepelného šoku HSP70 analýza   MeSH
• těhotenství MeSH
• Check Tag
• dospělí MeSH
• lidé MeSH
• mladiství MeSH
• mladý dospělý MeSH
• těhotenství MeSH
• ženské pohlaví MeSH
• Publikační typ
• anglický abstrakt MeSH
• časopisecké články MeSH
• Názvy látek
• proteiny tepelného šoku HSP70 MeSH

In this study, lipoic acid and heat shock treatments were applied to C(2)C(12) myotubes and Sprague-Dawley rats to investigate changes in the heat shock protein 70 (HSP70) and glucose transporter 4 (GLUT4) in 4 different skeletal muscle groups. The results of western blotting indicated that treatment of lipoic acid for 24 h, heat-shock and combined lipoic acid and heat-shock which all increased the level of HSP70 substantially in C(2)C(12) myotubes. However, either lipoic acid or heat-shock did not increase the level of GLUT4 in C(2)C(12) myotubes. In an in vitro migration assay, lipoic acid increased wound migration only when it was applied for 3 h. Moreover, our in vivo results revealed that lipoic acid did not increase HSP70 and GLUT4 in all 4 different skeletal muscles. Furthermore, heat-shock increased HSP70 in all 4 different muscle groups, and heat-shock treatment alone increased the GLUT4 in the soleus muscle only, suggesting that the GLUT4 increased by heat-shock was slow-twitch muscle specific. Collectively, our results indicated that heat-shock is critical factor that modulates GLUT4 and HSP70 in the skeletal muscle of rats.

• MeSH
• buněčné linie MeSH
• kosterní svaly fyziologie   MeSH
• krysa rodu Rattus MeSH
• potkani Sprague-Dawley MeSH
• přenašeč glukosy typ 4 metabolismus   MeSH
• proteiny tepelného šoku HSP70 metabolismus   MeSH
• reakce na tepelný šok fyziologie   MeSH
• svalová vlákna typu I fyziologie   MeSH
• zvířata MeSH
• Check Tag
• krysa rodu Rattus MeSH
• mužské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• přenašeč glukosy typ 4 MeSH
• proteiny tepelného šoku HSP70 MeSH
• Slc2a4 protein, rat MeSH Prohlížeč