共查询到20条相似文献,搜索用时 15 毫秒
1.
Zahida Zahoor Angela J. Davies Ruth S. Kirk David Rollinson Anthony John Walker 《Cell stress & chaperones》2010,15(5):639-650
Synthesis of heat shock proteins (HSPs) following cellular stress is a response shared by many organisms. Amongst the HSP
family, the ∼70 kDa HSPs are the most evolutionarily conserved with intracellular chaperone and extracellular immunoregulatory
functions. This study focused on the effects of larval excretory-secretory products (ESPs) from the parasite Schistosoma mansoni on HSP70 protein expression levels in haemocytes (defence cells) from its snail intermediate host Biomphalaria glabrata. S. mansoni larval stage ESPs are known to interfere with haemocyte physiology and behaviour. Haemocytes from two different B. glabrata strains, one which is susceptible to S. mansoni infection and one which is resistant, both showed reduced HSP70 protein levels following 1 h challenge with S. mansoni ESPs when compared to unchallenged controls; however, the reduction observed in the resistant strain was less marked. The
decline in intracellular HSP70 protein persisted for at least 5 h in resistant snail haemocytes only. Furthermore, in schistosome-susceptible snails infected by S. mansoni for 35 days, haemocytes possessed approximately 70% less HSP70. The proteasome inhibitor, MG132, partially restored HSP70
protein levels in ESP-challenged haemocytes, demonstrating that the decrease in HSP70 was in part due to intracellular degradation.
The extracellular signal-regulated kinase (ERK) signalling pathway appears to regulate HSP70 protein expression in these cells,
as the mitogen-activated protein-ERK kinase 1/2 (MEK1/2) inhibitor, U0126, significantly reduced HSP70 protein levels. Disruption
of intracellular HSP70 protein expression in B. glabrata haemocytes by S. mansoni ESPs may be a strategy employed by the parasite to manipulate the immune response of the intermediate snail host. 相似文献
2.
Wheeler DS Dunsmore KE Wong HR 《Biochemical and biophysical research communications》2003,301(1):54-59
Heat shock protein 70 (HSP70) is an intracellular stress protein that confers cytoprotection to a variety of cellular stressors. Several lines of evidence have suggested that augmentation of the heat shock response by increasing the expression of HSP70 represents a potential therapeutic strategy for the treatment of critically ill patients. The Tat protein of human immunodeficiency virus 1 (HIV-1) has been used previously to deliver functional cargo proteins intracellularly when added exogenously to cultured cells. We generated a Tat-HSP70 fusion protein using recombinant methods and treated HSF -/- cells with either Tat-HSP70 or recombinant HSP70 prior to exposure to hyperoxia or lethal heat shock. We showed that biologically active, exogenous HSP70 can be delivered into cells using the HIV-1 Tat protein, and that the Tat-mediated delivery of HSP70 confers cytoprotection against thermal stress and hyperoxia and may represent a novel approach to augmenting intracellular HSP70 levels. 相似文献
3.
4.
Jacques Oberson Andr Rawyler Roland Brndle Giorgio Canevascini 《Fungal genetics and biology : FG & B》1999,26(3):178
Three features of the heat shock response, reorganization of protein expression, intracellular accumulation of trehalose, and alteration in unsaturation degree of fatty acids were investigated in the thermophilic fungus Chaetomium thermophile and compared to the response displayed by a closely related mesophilic species, C. brasiliense. Thermophilic heat shock response paralleled the mesophilic response in many respects like (i) the temperature difference observed between normothermia and the upper limit of translational activity, (ii) the transient nature of the heat shock response at the level of protein expression including both the induction of heat shock proteins (HSPs) as well as the repression of housekeeping proteins, (iii) the presence of representatives of high-molecular-weight HSPs families, (iv) intracellular accumulation of trehalose, and finally (v) modifications in fatty acid composition. On the other hand, a great variability between the two organisms was observed for the proteins expressed during stress, in particular a protein of the HSP60 family that was only observed in C. thermophile. This peptide was also present constitutively at normal temperature and may thus fulfil thermophilic functions. It is shown that accumulation of trehalose does not play a part in thermophily but is only a stress response. C. thermophile contains less polyunsaturated fatty acids at normal temperature than C. brasiliense, a fact that can be directly related to thermophily. When subjected to heat stress, both organisms tended to accumulate shorter and less unsaturated fatty acids. 相似文献
5.
For a variety of species, changes in the expression of heat shock proteins (HSP) have been linked to key developmental changes,
i.e., gametogenesis, embryogenesis, and metamorphosis. Many marine invertebrates are known to have a biphasic life cycle where
pelagic larvae go through settlement and metamorphosis as they transition to the benthic life stage. A series of experiments
were run to examine the expression of heat shock protein 70 (HSP 70) during larval and early spat (initial benthic phase)
development in the Eastern oyster, Crassostrea virginica. In addition, the impact of thermal stress on HSP 70 expression during these early stages was studied. C. virginica larvae and spat expressed three HSP 70 isoforms, two constitutive, HSC 77 and HSC 72, and one inducible, HSP 69. We found
differences in the expression of both the constitutive and inducible forms of HSP 70 among larval and early juvenile stages
and in response to thermal stress. Low expression of HSP 69 during early larval and spat development may be associated with
the susceptibility of these stages to environmental stress. Although developmental regulation of HSP 70 expression has been
widely recognized, changes in its expression during settlement and metamorphosis of marine invertebrates are still unknown.
The results of the current study demonstrated a reduction of HSP 70 expression during settlement and metamorphosis in the
Eastern oyster, C. virginica. 相似文献
6.
AsHSP17, a creeping bentgrass small heat shock protein modulates plant photosynthesis and ABA‐dependent and independent signalling to attenuate plant response to abiotic stress
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Xinbo Sun Chunyu Sun Zhigang Li Qian Hu Liebao Han Hong Luo 《Plant, cell & environment》2016,39(6):1320-1337
Heat shock proteins (HSPs) are molecular chaperones that accumulate in response to heat and other abiotic stressors. Small HSPs (sHSPs) belong to the most ubiquitous HSP subgroup with molecular weights ranging from 12 to 42 kDa. We have cloned a new sHSP gene, AsHSP17 from creeping bentgrass (Agrostis stolonifera) and studied its role in plant response to environmental stress. AsHSP17 encodes a protein of 17 kDa. Its expression was strongly induced by heat in both leaf and root tissues, and by salt and abscisic acid (ABA) in roots. Transgenic Arabidopsis plants constitutively expressing AsHSP17 exhibited enhanced sensitivity to heat and salt stress accompanied by reduced leaf chlorophyll content and decreased photosynthesis under both normal and stressed conditions compared to wild type. Overexpression of AsHSP17 also led to hypersensitivity to exogenous ABA and salinity during germination and post‐germinative growth. Gene expression analysis indicated that AsHSP17 modulates expression of photosynthesis‐related genes and regulates ABA biosynthesis, metabolism and ABA signalling as well as ABA‐independent stress signalling. Our results suggest that AsHSP17 may function as a protein chaperone to negatively regulate plant responses to adverse environmental stresses through modulating photosynthesis and ABA‐dependent and independent signalling pathways. 相似文献
7.
Not changes in membrane fluidity but proteotoxic stress triggers heat shock protein expression in Chlamydomonas reinhardtii
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Sylvia Thoms Juliane Schurig Felix Willmund Michael Schroda 《Plant, cell & environment》2017,40(12):2987-3001
A conserved reaction of all organisms exposed to heat stress is an increased expression of heat shock proteins (HSPs). Several studies have proposed that HSP expression in heat‐stressed plant cells is triggered by an increased fluidity of the plasma membrane. Among the main lines of evidence in support of this model are as follows: (a) the degree of membrane lipid saturation was higher in cells grown at elevated temperatures and correlated with a lower amplitude of HSP expression upon a temperature upshift, (b) membrane fluidizers induce HSP expression at physiological temperatures, and (c) membrane rigidifier dimethylsulfoxide dampens heat‐induced HSP expression. Here, we tested whether this holds also for Chlamydomonas reinhardtii. We show that heat‐induced HSP expression in cells grown at elevated temperatures was reduced because they already contained elevated levels of cytosolic HSP70A/90A that apparently act as negative regulators of heat shock factor 1. We find that membrane rigidifier dimethylsulfoxide impaired translation under heat stress conditions and that membrane fluidizer benzyl alcohol not only induced HSP expression but also caused protein aggregation. These findings support the classical model for the cytosolic unfolded protein response, according to which HSP expression is induced by the accumulation of unfolded proteins. Hence, the membrane fluidity model should be reconsidered. 相似文献
8.
Glycinebetaine enhances the tolerance of tomato plants to high temperature during germination of seeds and growth of seedlings 总被引:3,自引:0,他引:3
Li S Li F Wang J Zhang W Meng Q Chen TH Murata N Yang X 《Plant, cell & environment》2011,34(11):1931-1943
Tomato (Lycopersicon esculentum cv. 'Moneymaker') was transformed with a codA gene, from Arthrobacter globiformis, for choline oxidase that had been modified to allow targeting to both chloroplasts and the cytosol. Glycinebetaine (GB) accumulated in seeds of transformed plants up to 1 μmol g(-1) dry weight (DW), while no detectable GB was found in wild-type (WT) seeds. The codA-transgenic seeds germinated faster and at higher frequency than WT seeds with high temperature treatment. After heat stress, levels of expression of a mitochondrial small heat-shock protein (MT-sHSP), heat-shock protein 70 (HSP70) and heat-shock cognate 70 (HSC70) were higher in transgenic seeds than in WT seeds during heat stress, and the accumulation of HSP70 was more prominent in codA-transgenic seeds than in WT seeds. Addition of GB to the germination medium or imbibition of seeds in a solution of GB enhanced the tolerance of WT seeds to high temperatures. WT seeds treated with exogenous GB also expressed heat-shock genes at elevated levels and accumulated more HSP70 than controls. Our results suggest that GB, either applied exogenously or accumulated in vivo in codA-transgenic seeds, enhanced the expression of heat-shock genes in and improved the tolerance to high temperature of tomato seeds during germination. 相似文献
9.
Cara JB Aluru N Moyano FJ Vijayan MM 《Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology》2005,142(4):426-431
Heat shock proteins (HSPs) expression is commonly used as indicators of cellular stress in animals. However, very little is known about either the expression patterns of HSPs or their role in the stress-tolerance phenomenon in early life stages of fish. To this end, we examined the impact of food-deprivation (12 h), reduced oxygen levels (3.5 mg/L for 1 h) and heat shock (HS: + 5 °C for 1 h) on HSP70 and HSP90 protein expression in early life stages of the gilthead sea bream (Sparus aurata), a warm-water aquaculture species. Also, we investigated HSP70 and HSP90 response to food-deprivation (7 days) in early life stages of rainbow trout (Oncorhynchus mykiss), a cool-water aquaculture species, and the tolerance of this larvae to heat shock (either + 5 or + 10 °C for 1 h). Our results clearly demonstrate that food-deprivation enhances HSP70 and HSP90 protein expression in larvae of both species. In gilthead sea bream larvae, the stressors-induced HSP70 and HSP90 (only in the reduced oxygen group) protein expression returned to unstressed levels after 24 h recovery. In fed trout larvae, a + 5 °C heat shock did not elevate HSP70 and HSP90 expression, whereas 100% mortality was evident with a + 10 °C HS. However, food-deprived trout larvae, which had higher HSP70 and HSP90 protein content, survived HS and showed HS-dependent increases in HSP70, but not HSP90 expression. Overall, HSP70 and HSP90 protein expression in early life stages of fish have the potential to be used as markers of nutritional stress, while elevation of the tissue HSPs content may be used as a means to increase stress tolerance during larval rearing. 相似文献
10.
Variability within a pea core collection of LEAM and HSP22, two mitochondrial seed proteins involved in stress tolerance
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MARIE‐HÉLÈNE AVELANGE‐MACHEREL NICOLE PAYET DAVID LALANNE MARTINE NEVEU DIMITRI TOLLETER JUDITH BURSTIN DAVID MACHEREL 《Plant, cell & environment》2015,38(7):1299-1311
LEAM, a late embryogenesis abundant protein, and HSP22, a small heat shock protein, were shown to accumulate in the mitochondria during pea (Pisum sativum L.) seed development, where they are expected to contribute to desiccation tolerance. Here, their expression was examined in seeds of 89 pea genotypes by Western blot analysis. All genotypes expressed LEAM and HSP22 in similar amounts. In contrast with HSP22, LEAM displayed different isoforms according to apparent molecular mass. Each of the 89 genotypes harboured a single LEAM isoform. Genomic and RT‐PCR analysis revealed four LEAM genes differing by a small variable indel in the coding region. These variations were consistent with the apparent molecular mass of each isoform. Indels, which occurred in repeated domains, did not alter the main properties of LEAM. Structural modelling indicated that the class A α‐helix structure, which allows interactions with the mitochondrial inner membrane in the dry state, was preserved in all isoforms, suggesting functionality is maintained. The overall results point out the essential character of LEAM and HSP22 in pea seeds. LEAM variability is discussed in terms of pea breeding history as well as LEA gene evolution mechanisms. 相似文献
11.
Tohru Takata Sun Nyunt Wai Akemi Takade Yoshiro Sawae Junko Ono Kazunobu Amako 《Microbiology and immunology》1995,39(9):639-645
From plate cultures of Campylobacter jejuni grown in room air a particulate protein of 62 kDa was isolated by ion-exchange chromatography. The protein had a square shape from the side view but when viewed from the top it had a star-shaped structure. The molecular size of the whole particle determined by gel filtration was 850 kDa which suggested the presence of 14 subunits of 62 kDa in each particle. The N-terminal 37 amino residues showed more than 80% homology with the sequence of these heat shock protein (HSP) 60 homologs of Chlamydia trachomatis, Helicobacter pylori, and Escherichia coli (GroEL). This protein is immunologically cross-reactive with the antiserum for the 60-kDa HSP of Yersinia enterocolitica. Production of the 62-kDa protein increased under heat stress and growth in an aerobic atmospheric environment. From these observations we concluded that the 62-kDa protein is a Campylobacter stress protein (Cj62) which belongs to the HSP 60 family. 相似文献
12.
The success of any organism depends not only on niche adaptation but also the ability to survive environmental perturbation
from homeostasis, a situation generically described as stress. Although species-specific mechanisms to combat “stress” have
been described, the production of heat shock proteins (HSPs), such as HSP70, is universally described across all taxa. Members
of the HSP70 gene family comprising the constitutive (HSC70) and inducible (HSP70) members, plus GRP78 (glucose-regulated
protein, 78 kDa), a related HSP70 family member, were cloned using degenerate polymerase chain reaction (PCR) from two evolutionary
divergent Antarctic marine molluscs (Laternula elliptica and Nacella concinna), a bivalve and a gastropod, respectively. The expression of the HSP70 family members was surveyed via quantitative PCR after
an acute 2-h heat shock experiment. Both species demonstrated significant up-regulation of HSP70 gene expression in response
to increased temperatures. However, the temperature level at which these responses were induced varied with the species (+6–8°C
for L. elliptica and +8–10°C for N. concinna) compared to their natural environmental temperature). L. elliptica also showed tissue-specific expression of the genes under study. Previous work on Antarctic fish has shown that they lack
the classical heat shock response, with the inducible form of HSP70 being permanently expressed with an expression not further
induced under higher temperature regimes. This study shows that this is not the case for other Antarctic animals, with the
two molluscs showing an inducible heat shock response, at a level probably set during their temperate evolutionary past. 相似文献
13.
L. Luo Z. Li M. Y. Tang B. Z. Cheng W. H. Zeng Y. Peng G. Nie X. Q. Zhang 《Plant biology (Stuttgart, Germany)》2020,22(5):794-804
- Heat stress decreases crop growth and yield worldwide. Spermidine (Spd) is a small aliphatic amine and acts as a ubiquitous regulator for plant growth, development and stress tolerance.
- Objectives of this study were to determine effects of exogenous Spd on changes in endogenous polyamine (PA) and γ‐aminobutyric acid (GABA) metabolism, oxidative damage, senescence and heat shock protein (HSP) expression in white clover subjected to heat stress. Physiological and molecular methods, including colorimetric assay, high performance liquid chromatography and qRT‐PCR, were applied.
- Results showed that exogenous Spd significantly alleviated heat‐induced stress damage. Application of Spd not only increased endogenous putrescine, Spd, spermine and total PA accumulation, but also accelerated PA oxidation and improved glutamic acid decarboxylase activity, leading to GABA accumulation in leaves under heat stress. The Spd-pretreated white clover maintained a significantly higher chlorophyll (Chl) content than untreated plants under heat stress, which could be related to the roles of Spd in up‐regulating genes encoding Chl synthesis (PBGD and Mg‐CHT) and maintaining reduced Chl degradation (PaO and CHLASE) during heat stress. In addition, Spd up‐regulated HSP70, HSP70B and HSP70‐5 expression, which might function in stabilizing denatured proteins and helping proteins to folding correctly in white clover under high temperature stress.
- In summary, exogenous Spd treatment improves the heat tolerance of white clover by altering endogenous PA and GABA content and metabolism, enhancing the antioxidant system and HSP expression and slowing leaf senescence related to an increase in Chl biosynthesis and a decrease in Chl degradation during heat stress.
14.
Areum Lee Hyun Ji Park Seung Hee Jo Haemyeong Jung Hyun-Soon Kim Hyo-Jun Lee Youn-Sung Kim Choonkyun Jung Hye Sun Cho 《植物学报(英文版)》2023,65(5):1113-1133
Peptidyl-prolyl isomerase-like 1(PPIL1) is associated with the human spliceosome complex. However, its function in pre-mRNA splicing remains unclear. In this study, we show that Arabidopsis thaliana CYCLOPHILIN 18-2(AtCYP18-2), a PPIL1 homolog,plays an essential role in heat tolerance by regulating pre-mRNA splicing. Under heat stress conditions,AtCYP18-2 expression was upregulated in mature plants and GFP-tagged AtCYP18-2 redistributed to nuclear and cytoplasmic puncta. We determined that AtCYP... 相似文献
15.
Biliana Grigorova Irina I. Vaseva Klimentina Demirevska Urs Feller 《Acta Physiologiae Plantarum》2011,33(5):2041-2049
Drought and heat stress are among the abiotic factors causing the most severe damage on plant crops. Their combination is
quite common in dry and semi-dry regions worldwide and little is known about its effect on heat shock protein (HSP) profile
in wheat plants. The expression of four HSP genes (Hsp 17.8, Hsp 26.3, Hsp 70 and Hsp 101b) in Triticum aestivum L. plants subjected to individually applied water deprivation or high temperature and their combination was monitored via
one-step RT-PCR analysis. Changes in the expression levels of small HSPs (smHSPs), HSP70 and HSP100 were established also
by SDS-PAGE. The combination of drought and heat induced HSP expression more effectively than the individually applied stresses.
The induction of HSPs displayed greater rate in the drought-tolerant wheat variety Katya than in the drought-sensitive cv.
Sadovo. The results obtained in wheat plants suggested that the effect of separately applied drought and heat shock cannot
be extrapolated to their combination. 相似文献
16.
Heat stress-induced H2O2 is required for effective expression of heat shock genes in Arabidopsis 总被引:5,自引:0,他引:5
The mechanisms of sensing and signalling of heat and oxidative stresses are not well understood. The central question of this
paper is whether in plant cells oxidative stress, in particular H2O2, is required for heat stress- and heat shock factor (HSF)-dependent expression of genes. Heat stress increases intracellular
accumulation of H2O2 in Arabidopsis cell culture. The accumulation was greatly diminished using ascorbate as a scavenger or respectively diphenyleneiodonium
chloride (DPI) as an inhibitor of reactive oxygen species production. The mRNA of heat shock protein (HSP) genes, exemplified
by Hsp17.6, Hsp18.2, and the two cytosolic ascorbate peroxidase genes Apx1, Apx2, reached similar levels by moderate heat stress (37°C) or by treatment with H2O2, butylperoxide and diamide at room temperature. The heat-induced expression levels were significantly reduced in the presence
of ascorbate or DPI indicating that H2O2 is an essential component in the heat stress signalling pathway. Rapid (15 min) formation of heat shock promoter element
(HSE) protein-binding complex of high molecular weight in extracts of heat-stressed or H2O2-treated cells and the inability to form this complex after ascorbate treatment suggests that oxidative stress affects gene
expression via HSF activation and conversely, that H2O2 is involved in HSF activation during the early phase of heat stress. The heat stress induction of a high mobility HSE-binding
complex, characteristic for later phase of heat shock response, was blocked by ascorbate and DPI. H2O2 was unable to induce this complex suggesting that H2O2 is involved only in the early stages of HSF activation. Significant induction of the genes tested after diamid treatment
and moderate expression of the sHSP genes in the presence of 50 mM ascorbate at 37°C occurred without activation of HSF, indicating
that other mechanisms may be involved in stress signalling.
Electronic Supplementary Material Supplementary material is available for this article at http//dx.doi.org/10.1007/s11103-006-0045-4
Roman A. Volkov and Irina I. Panchuk contributed equally 相似文献
17.
18.
Wang S Xie W Rylander MN Tucker PW Aggarwal S Diller KR 《Biotechnology and bioengineering》2008,99(1):146-154
The direct correlation between levels of heat shock protein expression and efficiency of its tissue protection function motivates this study of how thermal doses can be used for an optimal stress protocol design. Heat shock protein 70 (HSP70) expression kinetics were visualized continuously in cultured bovine aortic endothelial cells (BAECs) on a microscope heating stage using green fluorescent protein (GFP) as a reporter. BAECs were transfected with a DNA vector, HSP(p)-HSP70-GFP which expresses an HSP70-GFP fusion protein under control of the HSP70 promoter. Expression levels were validated by western blot analysis. Transfected cells were heated on a controlled temperature microscope stage at 42 degrees C for a defined period, then shifted to 37 degrees C for varied post-heating times. The expression of HSP70-GFP and its sub-cellular localization were visualized via fluorescence microscopy. The progressive expression kinetics were measured by quantitative analysis of serial fluorescence images captured during heating protocols from 1 to 2 h and post-heating times from 0 to 20 h. The results show two sequential peaks in HSP70 expression at approximately 3 and 12 h post-heat shock. A progressive translocation of HSP70 from the cytoplasm to the nucleus was observed from 6 to 16 h. We conclude that we have successfully combined molecular cloning and optical imaging to study HSP70 expression kinetics. The kinetic profile for HSP70-GFP fusion protein is consistent with the endogenous HSP70. Furthermore, information on dynamic intracellular translocation of HSP70 was extracted from the same experimental data. 相似文献
19.
E. G. Rikhvanov I. V. Fedoseeva D. V. Pyatrikas G. B. Borovskii V. K. Voinikov 《Russian Journal of Plant Physiology》2014,61(2):141-153
Mild heat stress induces the expression of heat shock proteins (HSPs) that protect plants from death during damaging heat treatments. It was assumed that the appearance in the cell of denatured proteins triggers the expression of HSP; however, recent results show that protein denaturation is not a prerequisite for this process. In this work we discuss a hypothetical mechanism for activation under heat stress of HSP expression promoted by short-term elevation of cytosolic Ca2+ level. According to our hypothesis, a prolonged elevation of Ca2+ has a negative influence on HSP expression. Therefore, calcium is transported from the cytosol into intracellular compartments, including mitochondria. The Ca2+ entry into mitochondria is accompanied by hyperpolarization of the inner mitochondrial membrane and by the increased production of reactive oxygen species (ROS). The increased ROS production contributes to the activation of HSP expression under mild heat stress but leads to plant death under severe heat shock. Thus, mitochondria and, possibly, other organelles play the crucial role in determining life or death fate of heat-treated plant cells by controlling the cytosolic Ca2+ content and ROS production. 相似文献