scholarly journals Corrigendum: Heat Shock Protein HSP24 Is Involved in the BABA-Induced Resistance to Fungal Pathogen in Postharvest Grapes Underlying an NPR1-Dependent Manner

2021 ◽  
Vol 12 ◽  
Author(s):  
Chunhong Li ◽  
Shifeng Cao ◽  
Kaituo Wang ◽  
Changyi Lei ◽  
Nana Ji ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Induced Resistance ◽  
Fungal Pathogen ◽  
Dependent Manner

Progesterone enhances target gene transcription by receptor free of heat shock proteins hsp90, hsp56, and hsp70

1991 ◽  
Vol 11 (10) ◽  
pp. 4998-5004
Author(s):  
M K Bagchi ◽  
S Y Tsai ◽  
M J Tsai ◽  
B W O'Malley
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Transcriptional Activation ◽  
Target Gene ◽  
Steroid Hormone ◽  
Receptor Activation ◽  
Target Cells ◽  
Dependent Manner ◽  
Shock Proteins

Steroid receptors regulate transcription of target genes in vivo and in vitro in a steroid hormone-dependent manner. Unoccupied progesterone receptor exists in the low-salt homogenates of target cells as a functionally inactive 8 to 10S complex with several nonreceptor components such as two molecules of 90-kDa heat shock protein (hsp90), a 70-kDa heat shock protein (hsp70), and a 56-kDa heat shock protein (hsp56). Ligand-induced dissociation of receptor-associated proteins such as hsp90 has been proposed as the mechanism of receptor activation. Nevertheless, it has not been established whether, beyond release of heat shock proteins, the steroidal ligand plays a role in modulating receptor activity. To examine whether the release of these nonreceptor proteins from receptor complex results in a constitutively active receptor, we isolated an unliganded receptor form essentially free of hsp90, hsp70, and hsp56. Using a recently developed steroid hormone-responsive cell-free transcription system, we demonstrate for the first time that the dissociation of heat shock proteins is not sufficient to generate a functionally active receptor. This purified receptor still requires hormone for high-affinity binding to a progesterone response element and for efficient transcriptional activation of a target gene. When an antiprogestin, Ru486, is bound to the receptor, it fails to promote efficient transcription. We propose that in the cell, in addition to the release of receptor-associated inhibitory proteins, a distinct hormone-mediated activation event must precede efficient gene activation.

scholarly journals Heat Shock Protein 70 Is Able to Prevent Heat Shock-Induced Resistance of Target Cells to CTL

2000 ◽  
Vol 164 (5) ◽  
pp. 2362-2371 ◽  
Author(s):  
Ralf Dressel ◽  
Leslie Elsner ◽  
Thomas Quentin ◽  
Lutz Walter ◽  
Eberhard Günther
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Induced Resistance ◽  
Heat Shock Protein 70 ◽  
Target Cells

scholarly journals Urocortin increases the expression of heat shock protein 90 in rat cardiac myocytes in a MEK1/2-dependent manner

2002 ◽  
Vol 172 (2) ◽  
pp. 283-293 ◽  
Author(s):  
BK Brar ◽  
J Railson ◽  
A Stephanou ◽  
RA Knight ◽  
DS Latchman
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cardiac Myocytes ◽  
Primary Cultures ◽  
Heat Shock Protein 90 ◽  
Mitogen Activated Protein Kinase ◽  
Dependent Manner ◽  
Maximal Increase ◽  
Mitogen Activated Protein ◽  
Hsp90 Protein

We have previously demonstrated that urocortin protects cultured cardiac myocytes from ischaemic and reoxygenation injury and decreases the infarct size in the rat heart exposed to regional ischaemia and reperfusion. Urocortin-mediated cardioprotection is via activation of the mitogen-activated protein kinase (MAP kinase, MEK1/2) pathway. In addition, it is well documented that heat shock protein (hsp) 70 and hsp90 are cardioprotective against lethal stress. In this study we show, for the first time, that urocortin induces the expression of hsp90 but not hsp70 in primary cultures of rat neonatal cardiac myocytes. Levels of hsp90 protein increase by 1.5-fold over untreated cells within 10 min of urocortin treatment and are sustained for 24 h with a maximal increase of 2.5-fold at 60 min (P<0.05 at all time points). The increase in hsp90 expression by urocortin was not inhibited by actinomycin D, and urocortin failed to increase hsp90 promoter activity. Urocortin induction of hsp90 was inhibited by the MEK1/2 inhibitor PD98059 (P<0.001) and by cycloheximide, and both inhibitors abrogate urocortin-mediated cardioprotection (P<0.05 for cycloheximide, P<0.001 for PD98059). Hence, MEK1/2 and protein synthesis are involved in the cardioprotective effect of urocortin against hypoxic-mediated cell death, possibly due to an increase in expression of hsp90 protein. This is the first report of heat shock protein induction by urocortin or any other member of the corticotrophin-releasing hormone family.

scholarly journals Mitochondrial small heat shock protein mediates seed germination via thermal sensing

2019 ◽  
Vol 116 (10) ◽  
pp. 4716-4721 ◽  
Author(s):  
Wei Ma ◽  
Xueying Guan ◽  
Jie Li ◽  
Ronghui Pan ◽  
Luyao Wang ◽  
...  
Keyword(s):  
Heat Shock ◽  
Seed Germination ◽  
Heat Shock Protein ◽  
Critical Factor ◽  
Small Heat Shock Protein ◽  
Ros Generation ◽  
Dependent Manner ◽  
Temperature Dependent ◽  
Transport Chain ◽  
Thermal Sensing

Seed germination is an energy demanding process that requires functional mitochondria upon imbibition. However, how mitochondria fine tune seed germination, especially in response to the dynamics of environmental temperature, remains largely unknown at the molecular level. Here, we report a mitochondrial matrix-localized heat shock protein GhHSP24.7, that regulates seed germination in a temperature-dependent manner. Suppression ofGhHSP24.7renders the seed insensitive to temperature changes and delays germination. We show that GhHSP24.7 competes with GhCCMH to bind to the maturation subunit protein GhCcmFcto form cytochrome C/C1(CytC/C1) in the mitochondrial electron transport chain. GhHSP24.7 modulates CytC/C1production to induce reactive oxygen species (ROS) generation, which consequently accelerates endosperm rupture and promotes seed germination. Overexpression ofGhHSP24.7’s homologous genes can accelerate seed germination inArabidopsisand tomato, indicating its conserved function across plant species. Therefore,HSP24.7is a critical factor that positively controls seed germination via temperature-dependent ROS generation.

scholarly journals A constitutive 70 kDa heat-shock protein is localized on the fibres of spindles and asters at metaphase in an ATP-dependent manner: a new chaperone role is proposed

2001 ◽  
Vol 360 (2) ◽  
pp. 413 ◽  
Author(s):  
Cecilia AGUELI ◽  
Fabiana GERACI ◽  
Giovanni GIUDICE ◽  
Laura CHIMENTI ◽  
Domenico CASCINO ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Dependent Manner

RNAi Silencing of TEL-AML1 Reveals a Heat Shock Protein Dependent Mechanism in the Development of Leukemia.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 2844-2844
Author(s):  
Christofer Diakos ◽  
Christopher Gerner ◽  
Andrea Inthal ◽  
Helmut Gadner ◽  
Renate Panzer-Grümayer
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Fusion Gene ◽  
Leukemic Cell ◽  
Leukemia Cell Line ◽  
Cell Phenotype ◽  
Dependent Manner ◽  
Leukemic Clone ◽  
Shock Proteins

Abstract The t(12;21) chromosomal translocation generating the TEL-AML1 fusion product is the most frequent genetic aberration of childhood acute lymphoblastic leukemia. This translocation has been shown to occur in utero and thus represents an early or even initiating event in leukemia development. However, additional molecular changes are necessary for the clinical manifestation of the disease. Despite increasing knowledge on TEL and AML1, the role of the TEL-AML1 fusion gene and its contribution to the malignant transformation is largely unknown. In particular, the mechanisms by which TEL-AML1 influences the biology of the affected cell, and thus survival and expansion, are yet to be defined. The aim of this study was to investigate the functional contribution of TEL-AML1 to the leukemic cell phenotype. We particularly sought to search for TEL-AML1 dependent genes as well as for pathways that function in a fusion gene dependent manner. The t(12;21) positive B cell precursor leukemia cell line REH was used as model system and RNA interference technology, a new and highly specific approach, was employed to block the expression of the TEL-AML1 fusion gene. The successful silencing of TEL-AML1 was demonstrated by Western blot analysis. In order to gain a broad overview of the impact of TEL-AML1 silencing upon the leukemic cell, RNA was isolated and subjected to Affymetrix gene chip analysis. In addition, we studied the proteome by high-resolution 2D electrophoresis. Expression profiling resulted in a specific pattern of differentially regulated genes after TEL-AML1 suppression with a particular emphasis on genes involved in the control of apoptosis. Genes with anti-apoptotic properties were down regulated after TEL-AML1 silencing while those that contribute to apoptosis were largely unaffected. Among the affected anti-apoptotic genes were the heat shock proteins, the most prominent representatives of which were HSP90 and HSP70. Their changes were observed at the mRNA but also at the protein level. This is of special interest, since both heat shock proteins interfere with the intrinsic as well as the extrinsic pathway of apoptosis and hence provide a powerful anti-apoptotic signal. These first data support a model in which TEL-AML1, as an early event, is functionally linked to an anti-apoptotic network and especially to the members of the heat shock protein family. Engagement of these mechanisms might rescue a cell from apoptosis and in consequence give rise to the development of a pre-leukemic clone, a reservoir for the acquisition of further mutations that might eventually give rise to leukemia. Thus, decreasing the apoptosis defence by silencing TEL-AML1 or by inhibiting the heat shock proteins might sensitize TEL-AML1 positive cells to apoptosis. This would not only be an option for future therapy of leukemias but also for the eradication of the pre-leukemic clone as a proposed source of relapse.

Heat induction of heat shock protein 25 requires cellular glutamine in intestinal epithelial cells

2006 ◽  
Vol 291 (2) ◽  
pp. C290-C299 ◽  
Author(s):  
Kittiporn Phanvijhitsiri ◽  
Mark W. Musch ◽  
Mark J. Ropeleski ◽  
Eugene B. Chang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Heat Shock ◽  
Epithelial Cells ◽  
Heat Shock Protein ◽  
Cellular Response ◽  
Intestinal Epithelial Cells ◽  
Dependent Manner ◽  
Intestinal Epithelial ◽  
Heat Induction

Glutamine is considered a nonessential amino acid; however, it becomes conditionally essential during critical illness when consumption exceeds production. Glutamine may modulate the heat shock/stress response, an important adaptive cellular response for survival. Glutamine increases heat induction of heat shock protein (Hsp) 25 in both intestinal epithelial cells (IEC-18) and mesenchymal NIH/3T3 cells, an effect that is neither glucose nor serum dependent. Neither arginine, histidine, proline, leucine, asparagine, nor tyrosine acts as physiological substitutes for glutamine for heat induction of Hsp25. The lack of effect of these amino acids was not caused by deficient transport, although some amino acids, including glutamate (a major direct metabolite of glutamine), were transported poorly by IEC-18 cells. Glutamate uptake could be augmented in a concentration- and time-dependent manner by increasing either media concentration and/or duration of exposure. Under these conditions, glutamate promoted heat induction of Hsp25, albeit not as efficiently as glutamine. Further evidence for the role of glutamine conversion to glutamate was obtained with the glutaminase inhibitor 6-diazo-5-oxo-l-norleucine (DON), which inhibited the effect of glutamine on heat-induced Hsp25. DON inhibited phosphate-dependent glutaminase by 75% after 3 h, decreasing cell glutamate. Increased glutamine/glutamate conversion to glutathione was not involved, since the glutathione synthesis inhibitor, buthionine sulfoximine, did not block glutamine’s effect on heat induction of Hsp25. A large drop in ATP levels did not appear to account for the diminished Hsp25 induction during glutamine deficiency. In summary, glutamine is an important amino acid, and its requirement for heat-induced Hsp25 supports a role for glutamine supplementation to optimize cellular responses to pathophysiological stress.

scholarly journals Tissue-dependent expression of heat shock factor 2 isoforms with distinct transcriptional activities.

1995 ◽  
Vol 15 (10) ◽  
pp. 5288-5293 ◽  
Author(s):  
M L Goodson ◽  
O K Park-Sarge ◽  
K D Sarge
Keyword(s):  
Gene Expression ◽  
Alternative Splicing ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mammalian Cells ◽  
Protein Gene ◽  
Heat Shock Factor ◽  
Dependent Manner ◽  
Heat Shock Protein Gene ◽  
Mouse Tissues

Heat shock factor 2 (HSF2) functions as a transcriptional regulator of heat shock protein gene expression in mammalian cells undergoing processes of differentiation and development. Our previous studies demonstrated high regulated expression and unusual constitutive DNA-binding activity of the HSF2 protein in mouse testes, suggesting that HSF2 functions to regulate heat shock protein gene expression in spermatogenic cells. The purpose of this study was to test whether HSF2 regulation in testes is associated with alterations in the HSF2 polypeptide expressed in testes relative to other mouse tissues. Our results show that mouse cells express not one but two distinct HSF2 proteins and that the levels of these HSF2 isoforms are regulated in a tissue-dependent manner. The testes express predominantly the 71-kDa HSF2-alpha isoform, while the heart and brain express primarily the 69-kDa HSF2-beta isoform. These isoforms are generated by alternative splicing of HSF2 pre-mRNA, which results in the inclusion of an 18-amino-acid coding sequence in the HSF2-alpha mRNA that is skipped in the HSF2-beta mRNA. HSF2 alternative splicing is also developmentally regulated, as our results reveal a switch in expression from the HSF2-beta mRNA isoform to the HSF2-alpha isoform during testis postnatal developmental. Transfection analysis shows that the HSF2-alpha protein, the predominant isoform expressed in testis cells, is a more potent transcriptional activator than the HSF2-beta isoform. These results reveal a new mechanism for the control of HSF2 function in mammalian cells, in which regulated alternative splicing is used to modulate HSF2 transcriptional activity in a tissue-dependent manner.

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