Long-term heat stress at final gestation: physiological and heat shock responses of Saanen goats

2021 ◽  
Author(s):  
Henrique Barbosa Hooper ◽  
Priscila dos Santos Silva ◽  
Sandra Aparecida de Oliveira ◽  
Giovana Krempel Fonseca Merighe ◽  
Cristiane Gonçalves Titto ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Responses

scholarly journals Heat Stress Activates Fission Yeast Spc1/StyI MAPK by a MEKK-Independent Mechanism

1998 ◽  
Vol 9 (6) ◽  
pp. 1339-1349 ◽  
Author(s):  
Kazuhiro Shiozaki ◽  
Mitsue Shiozaki ◽  
Paul Russell
Keyword(s):  
Oxidative Stress ◽  
Heat Stress ◽  
Heat Shock ◽  
Fission Yeast ◽  
Phosphorylation Sites ◽  
High Osmolarity ◽  
Mapk Kinase ◽  
Independent Mechanism ◽  
Heat Shock Responses ◽  
And Oxidative Stress

Fission yeast Spc1/StyI MAPK is activated by many environmental insults including high osmolarity, oxidative stress, and heat shock. Spc1/StyI is activated by Wis1, a MAPK kinase (MEK), which is itself activated by Wik1/Wak1/Wis4, a MEK kinase (MEKK). Spc1/StyI is inactivated by the tyrosine phosphatases Pyp1 and Pyp2. Inhibition of Pyp1 was recently reported to play a crucial role in the oxidative stress and heat shock responses. These conclusions were based on three findings: 1) osmotic, oxidative, and heat stresses activate Spc1/StyI in wis4 cells; 2) oxidative stress and heat shock activate Spc1/StyI in cells that express Wis1AA, in which MEKK consensus phosphorylation sites were replaced with alanine; and 3) Spc1/StyI is maximally activated in Δpyp1 cells. Contrary to these findings, we report: 1) Spc1/StyI activation by osmotic stress is greatly reduced in wis4 cells; 2)wis1-AA and Δwis1 cells have identical phenotypes; and 3) all forms of stress activate Spc1/StyI inΔpyp1 cells. We also report that heat shock, but not osmotic or oxidative stress, activate Spc1 in wis1-DDcells, which express Wis1 protein that has the MEKK consensus phosphorylation sites replaced with aspartic acid. Thus osmotic and oxidative stress activate Spc1/StyI by a MEKK-dependent process, whereas heat shock activates Spc1/StyI by a novel mechanism that does not require MEKK activation or Pyp1 inhibition.

scholarly journals Evolutionary and acclimation-induced variation in the heat-shock responses of congeneric marine snails (genus Tegula) from different thermal habitats: implications for limits of thermotolerance and biogeography

1999 ◽  
Vol 202 (21) ◽  
pp. 2925-2936 ◽  
Author(s):  
L. Tomanek ◽  
G.N. Somero
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Gulf Of California ◽  
Gill Tissue ◽  
Absolute Temperature ◽  
Temperate Zone ◽  
Cellular Damage ◽  
Intertidal Species ◽  
Marine Snails ◽  
Heat Shock Responses

Heat stress sufficient to cause cellular damage triggers the heat-shock response, the enhanced expression of a group of molecular chaperones called heat-shock proteins (hsps). We compared the heat-shock responses of four species of marine snails of the genus Tegula that occupy thermal niches differing in absolute temperature and range of temperature. We examined the effects of short-term heat stress and thermal acclimation on the synthesis of hsps of size classes 90, 77, 70 and 38 kDa by measuring incorporation of (35)S-labeled methionine and cysteine into newly synthesized proteins in gill tissue. Temperatures at which enhanced synthesis of hsps first occurred (T(on)), temperatures of maximal induction of hsp synthesis (T(peak)) and temperatures at which hsp synthesis was heat-inactivated (T(off)) were lowest in two low-intertidal to subtidal species from the temperate zone, T. brunnea and T. montereyi, intermediate in a mid- to low-intertidal species of the temperate zone, T. funebralis, and highest in a subtropical intertidal species from the Gulf of California, T. rugosa. Synthesis of hsps and other classes of protein by T. brunnea and T. montereyi was heat-inactivated at temperatures commonly encountered by T. funebralis during low tides on warm days. In turn, protein synthesis by T. funebralis was blocked at the upper temperatures of the habitat of T. rugosa. Acclimation of snails to 13 degrees C, 18 degrees C and 23 degrees C shifted T(on) and T(peak) for certain hsps, but did not affect T(off). The heat-shock responses of field-acclimatized snails were generally reduced in comparison with those of laboratory-acclimated snails. Overall, despite the occurrence of acclimatory plasticity in their heat-shock responses, genetically fixed differences in T(on), T(peak) and T(off) appear to exist that reflect the separate evolutionary histories of these species and may play important roles in setting their thermal tolerance limits and, thereby, their biogeographic distribution patterns.

scholarly journals Are the Effects of Heat on Physiology Due to Heat Shock Proteins?

HortScience ◽  
1996 ◽  
Vol 31 (4) ◽  
pp. 691c-691
Author(s):  
Robert E. Paull ◽  
Chris B. Watkins
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Responses ◽  
Critical Role ◽  
Chilling Injury ◽  
Heat Treatments ◽  
Adaptation To Heat ◽  
Heat Shock Responses ◽  
Shock Proteins

Production of heat shock proteins (HSP) in response to high temperatures are a highly recognizable feature of plant and animal systems. It is thought that such proteins play a critical role in survival under supraoptimal temperature conditions. The use of heat treatments has been examined extensively, especially for disinfestation of fruit and disease control. Heat treatments can affect physiological responses, such as ethylene production, softening, and other ripening factors, as well as reducing physiological disorders, including chilling injury. HSPs have been implicated in a number of stress responses, but the extent that they are involved, especially in amelioration of chilling injury, is a subject of debate. In a number of cases, heat shock proteins do not appear to be involved, and HSPs do not explain long-term adaptation to heat; other systems for which we do not have models may be at work. Resolution of these issues may require the use of transgenic plants with modified heat shock responses.

scholarly journals Effect of long term heat stress and dietary restriction on the expression of small heat shock protein (sHSP) genes in rat liver tissue

2016 ◽  
Vol 32 (3) ◽  
pp. 161-161
Author(s):  
Faruk Bozkaya ◽  
Mehmet Osman Atlı ◽  
Aydin Guzeloglu ◽  
Seyit Ali Kayis ◽  
Mehmet Salih Kaya ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Rat Liver ◽  
Dietary Restriction ◽  
Liver Tissue ◽  
Small Heat Shock Protein

Intracellular growth and pathogenesis of Leishmania parasites

2011 ◽  
Vol 51 ◽  
pp. 81-95 ◽  
Author(s):  
Thomas Naderer ◽  
Malcolm J. McConville
Keyword(s):  
Amino Acids ◽  
Heat Shock ◽  
Carbon Sources ◽  
Surface Expression ◽  
Parasite Survival ◽  
Heat Shock Responses ◽  
Shock Proteins ◽  
Intracellular Amastigote ◽  
Leishmania Parasites

Parasitic protozoa belonging to the genus Leishmania are the cause of a spectrum of diseases in humans, as well as chronic long-term infections. These parasites exhibit a remarkable capacity to survive and proliferate within the phagolysosome compartment of host macrophages. Studies with defined Leishmania mutants in mouse models of infection have highlighted processes that are required for parasite survival in macrophages. Parasite mutants have been identified that (i) are poorly virulent when the insect (promastigote) stage is used to initiate infection, but retain wild-type virulence following transformation to the obligate intracellular amastigote stage, (ii) are highly attenuated when either promastigotes or amastigotes are used, and (iii) are unable to induce characteristic lesion granulomas, but can persist within macrophages in other tissues. From these analyses it can be concluded that promastigote stages of some species require the surface expression of lipophosphoglycan, but not other surface components. Survival and subsequent proliferation of Leishmania in macrophages requires the activation of heat-shock responses (involving the up-regulation and/or phosphorylation of heat-shock proteins), the presence of oxidative and nitrosative defence mechanisms, and uptake and catabolism of carbon sources (glycoproteins, hexoses and amino acids) and essential nutrients (purines, amino acids and vitamins). Parasite mutants with defects in specific kinase/phosphatase-dependent signalling pathways are also severely attenuated in amastigote virulence, highlighting the potential importance of post-translational regulatory mechanisms in parasite adaptation to this host niche.

scholarly journals Heat Stress Responses and Thermotolerance in Maize

2021 ◽  
Vol 22 (2) ◽  
pp. 948
Author(s):  
Zhaoxia Li ◽  
Stephen H. Howell
Keyword(s):  
Transcription Factors ◽  
Heat Stress ◽  
Stress Response ◽  
Heat Shock ◽  
Stress Responses ◽  
Rna Splicing ◽  
Optimal Growth ◽  
Heat Stress Response ◽  
Genes Encoding ◽  
Heat Shock Responses

High temperatures causing heat stress disturb cellular homeostasis and impede growth and development in plants. Extensive agricultural losses are attributed to heat stress, often in combination with other stresses. Plants have evolved a variety of responses to heat stress to minimize damage and to protect themselves from further stress. A narrow temperature window separates growth from heat stress, and the range of temperatures conferring optimal growth often overlap with those producing heat stress. Heat stress induces a cytoplasmic heat stress response (HSR) in which heat shock transcription factors (HSFs) activate a constellation of genes encoding heat shock proteins (HSPs). Heat stress also induces the endoplasmic reticulum (ER)-localized unfolded protein response (UPR), which activates transcription factors that upregulate a different family of stress response genes. Heat stress also activates hormone responses and alternative RNA splicing, all of which may contribute to thermotolerance. Heat stress is often studied by subjecting plants to step increases in temperatures; however, more recent studies have demonstrated that heat shock responses occur under simulated field conditions in which temperatures are slowly ramped up to more moderate temperatures. Heat stress responses, assessed at a molecular level, could be used as traits for plant breeders to select for thermotolerance.

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