Decreased temperature as a signal for regulation of heat shock protein expression in anoxic brain and heart: focus on “Expression of heat shock proteins in anoxic crucian carp (Carassius carassius): support for cold as a preparatory cue for anoxia”

2010 ◽  
Vol 298 (6) ◽  
pp. R1496-R1498 ◽  
Author(s):  
Howard M. Prentice
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Crucian Carp ◽  
Carassius Carassius ◽  
Heat Shock Protein Expression ◽  
Shock Proteins ◽  
Crucian Carp Carassius Carassius

Expression of heat shock proteins in anoxic crucian carp (Carassius carassius): support for cold as a preparatory cue for anoxia

2010 ◽  
Vol 298 (6) ◽  
pp. R1499-R1508 ◽  
Author(s):  
Kåre-Olav Stensløkken ◽  
Stian Ellefsen ◽  
Helene Kile Larsen ◽  
Jarle Vaage ◽  
Göran E. Nilsson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Function ◽  
Crucian Carp ◽  
Cellular Damage ◽  
Winter Period ◽  
Carassius Carassius ◽  
Shock Proteins ◽  
The Brain ◽  
Crucian Carp Carassius Carassius

The crucian carp ( Carassius carassius ) tolerates anoxia for days to months depending on temperature. During episodes of stress, heat shock proteins (HSPs) are important for limiting cellular damage, mainly by ensuring protein function. Accordingly, we hypothesized that anoxia would change the expression of HSPs and that this response would be temperature dependent. Real-time RT-PCR was used to investigate the effects of 1 and 7 days anoxia (A1 and A7) on the expression of HSP70a, HSP70b, HSC70, HSP90, and HSP30 in the brain and heart of 8°C- and 13°C-acclimated crucian carp. In general, the expression of all HSPs changed in response to anoxia, although varying in size and direction, and with organ and temperature. HSP70a expression increased drastically (∼10-fold) in A7 brains and hearts at 13°C but not at 8°C. HSC70 and HSP90 expression decreased in A7 brains (by 60–70%), but not in A7 hearts. HSC70 expression increased in A1 brains and hearts at both temperatures (by 60–160%), and HSP30 expression decreased in A7 brains and hearts at both temperatures (by 50–80%). Notably, normoxic fish showed 7- and 11-fold higher HSP70a expression in the brain and heart at 8°C compared with 13°C. This difference disappeared during anoxia, suggesting that cold may function as a cue for preconditioning the crucian carp's HSP70a expression to the approaching anoxic winter period.

The effect of heat stress on bull sperm quality and related HSPs expression

2016 ◽  
Vol 66 (3-4) ◽  
pp. 321-333 ◽  
Author(s):  
Yunyun Cheng ◽  
Songcai Liu ◽  
Ying Zhang ◽  
Dan Su ◽  
Gang Wang ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Molecular Mechanisms ◽  
Sperm Quality ◽  
Heat Shock Protein Expression ◽  
Shock Proteins

Heat stress dramatically decreases bull sperm quality and has recently received more attention due to the warmer global climate and more intensive production. However, no data exist regarding sperm quality or the related molecular mechanisms under heat stress. Recent studies showed that inducible heat shock proteins (HSPs) play an important role in the dairy heat stress regulation. In this article, to investigate the impacts of heat stress on sperm quality and the associated molecular mechanisms, sperm quality and enzyme activities concerning acrosome reaction were assessed in Simmental, Limousin and Yanbian bulls under heat stress. Subsequently, changes in heat shock protein expression profiles of Simmental bulls were observed, because we observed that sperm quality of these bulls was most sensitive to heat stress. Finally, the relationship between sperm quality and heat shock protein expression under heat stress was analyzed. The results show that summer heat stress decreased the sperm quality of the three bull breeds significantly. Moreover, different levels of heat stimulation induced various enzyme activity changes, among which the activity change in acrosomal enzyme was the most remarkable. Furthermore, the expression of heat shock proteins in the sperm was influenced by the imposed heat stress, among which the expression levels of HSP60 and HSP70 were increased while HSP90 decreased. In summary, our data show that heat stress seriously affects sperm quality and that HSP90 was most sensitive, although it should be noted that seasonal effects may confound these results. This change in heat shock protein expression may be the major factor that affected the sperm quality of the bulls. The findings may provide a new hypothesis for how heat stress impacts reproduction mechanistically.

scholarly journals Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96.

1995 ◽  
Vol 182 (3) ◽  
pp. 885-889 ◽  
Author(s):  
D Arnold ◽  
S Faath ◽  
H Rammensee ◽  
H Schild
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Tumor Cells ◽  
Mhc Class I ◽  
Donor Cell ◽  
Class I ◽  
Heat Shock Protein Gp96 ◽  
Shock Proteins

Vaccination of mice with heat shock proteins isolated from tumor cells induces immunity to subsequent challenge with those tumor cells the heat shock protein was isolated from but not with other tumor cells (Udono, H., and P.K. Srivastava. 1994. J. Immunol. 152:5398-5403). The specificity of this immune response is caused by tumor-derived peptides bound to the heat shock proteins (Udono., H., and P.K. Srivastava. 1993. J. Exp. Med. 178:1391-1396). Our experiments show that a single immunization with the heat shock protein gp96 isolated from beta-galactosidase (beta-gal) expressing P815 cells (of DBA/2 origin) induces cytotoxic T lymphocytes (CTLs) specific for beta-gal, in addition to minor H antigens expressed by these cells. CTLs can be induced in mice that are major histocompatibility complex (MHC) identical to the gp96 donor cells (H-2d) as well as in mice with a different MHC (H-2b). Thus gp96 is able to induce "cross priming" (Matzinger, P., and M.J. Bevan. 1977. Cell. Immunol. 33:92-100), indicating that gp96-associated peptides are not limited to the MHC class I ligands of the gp96 donor cell. Our data confirm the notion that samples of all cellular antigens presentable by MHC class I molecules are represented by peptides associated with gp96 molecules of that cell, even if the fitting MHC molecule is not expressed. In addition, we extend previous reports on the in vivo immunogenicity of peptides associated gp96 molecules to two new groups of antigens, minor H antigens, and proteins expressed in the cytosol.

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 Ocean warming lead to heat shock protein expression and decrease in the feeding rate of the Patagonian sea star Anasterias minuta

2022 ◽  
Vol 546 ◽  
pp. 151661
Author(s):  
Lorena P. Arribas ◽  
José E.F. Alfaya ◽  
M. Gabriela Palomo ◽  
Sebastian Giulianelli ◽  
Rocío A. Nieto Vilela ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Feeding Rate ◽  
Ocean Warming ◽  
Sea Star ◽  
Heat Shock Protein Expression
Sign in / Sign up

Export Citation Format

Share Document