Heat shock protein 70 gene expression and stress response of red-spotted (Epinephelus akaara) and hybrid (E. akaara female × E. lanceolatus male) groupers to heat and cold shock exposure

The stress response is a highly conserved cellular defense mechanism defined by the rapid and specific expression of stress proteins, with concomitant transient inhibition of nonstress protein gene expression. The stress proteins mediate cellular and tissue protection against diverse cytotoxic stimuli. Among the many classes of stress proteins, heat shock protein 70 and heme oxygenase-1 are the best characterized with respect to lung biology. A potential role for stress proteins in human lung disease is inferred from studies demonstrating stress protein expression in the lungs of patients with cancer, asthma, and acute lung injury. Several examples of stress protein-mediated cytoprotection exist in cell and animal models of acute lung injury. Stress protein induction protects rats against acute lung injury caused by either systemic administration of endotoxin or intratracheal administration of phospholipase A1. In vitro, increased expression of stress proteins protects lung cells against endotoxin-mediated apoptosis and oxidant injury. The mechanisms of stress response-mediated cytoprotection may involve the enzymatic and molecular chaperone properties of stress proteins. Alternatively, the stress response may protect by modulating lung proinflammatory responses. Data from extrapulmonary systems suggest that stress response-associated factors (heat shock protein 70 and heat shock factor) are directly involved in modulation of proinflammatory gene expression. Recent evidence also demonstrates interactions between the stress response and the I-kappa B/nuclear factor-kappa B pathway in cultured lung cells. Increased understanding about the role of stress proteins in lung biology may support efforts to selectively increase expression of one or more stress proteins to provide protection against human acute lung injury.

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Heat Shock Protein 70 Improves In Vitro Embryo Yield and Quality from Heat Stressed Bovine Oocytes

Animals ◽

10.3390/ani11061794 ◽

2021 ◽

Vol 11 (6) ◽

pp. 1794

Author(s):

Konstantina Stamperna ◽

Themistoklis Giannoulis ◽

Eleni Dovolou ◽

Maria Kalemkeridou ◽

Ioannis Nanas ◽

...

Keyword(s):

Gene Expression ◽

Heat Shock ◽

Heat Shock Protein ◽

Heat Shock Protein 70 ◽

Cumulus Cells ◽

Intramolecular Interactions ◽

Developmental Competence ◽

Embryo Yield ◽

Bovine Oocytes

Heat shock protein 70 (HSP70) is a chaperon that stabilizes unfolded or partially folded proteins, preventing inappropriate inter- and intramolecular interactions. Here, we examined the developmental competence of in vitro matured oocytes exposed to heat stress with or without HSP70. Bovine oocytes were matured for 24 h at 39 °C without (group C39) or with HSP70 (group H39) and at 41 °C for the first 6 h, followed by 16 h at 39 °C with (group H41) or without HSP70 (group C41). After insemination, zygotes were cultured for 9 days at 39 °C. Cleavage and embryo yield were assessed 48 h post insemination and on days 7, 8, 9, respectively. Gene expression was assessed by RT-PCR in oocytes, cumulus cells and blastocysts. In C41, blastocysts formation rate was lower than in C39 and on day 9 it was lower than in H41. In oocytes, HSP70 enhanced the expression of three HSP genes regardless of incubation temperature. HSP70 at 39 °C led to tight coordination of gene expression in oocytes and blastocysts, but not in cumulus cells. Our results imply that HSP70, by preventing apoptosis, supporting signal transduction, and increasing antioxidant protection of the embryo, protects heat stressed maturing bovine oocyte and restores its developmental competence.

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Effect of heat shock protein 70 homologue DNAK on gene expression of penaeidins, serine proteinase, prophenoloxidase and transglutaminase in hemocytes of Litopenaeus vannamei

Fish & Shellfish Immunology ◽

10.1016/j.fsi.2013.03.068 ◽

2013 ◽

Vol 34 (6) ◽

pp. 1656

Author(s):

B Hu ◽

P Sorgeloos ◽

P Bossier

Keyword(s):

Gene Expression ◽

Heat Shock ◽

Heat Shock Protein ◽

Litopenaeus Vannamei ◽

Heat Shock Protein 70 ◽

Serine Proteinase

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Effects of Ascorbic Acid and β-1,3-Glucan on Survival, Physiological Response and Flesh Quality of Cultured Tiger Grouper (Epinephelus fuscoguttatus) during Simulated Transport in Water

Biology ◽

10.3390/biology9020037 ◽

2020 ◽

Vol 9 (2) ◽

pp. 37 ◽

Cited By ~ 1

Author(s):

Bo Wu ◽

Qi Wang ◽

Jie Cao ◽

Jun Mei ◽

Jing Xie

Keyword(s):

Ascorbic Acid ◽

Survival Rate ◽

Stress Response ◽

Heat Shock ◽

Heat Shock Protein ◽

Heat Shock Protein 70 ◽

Flesh Quality ◽

Epinephelus Fuscoguttatus ◽

Tiger Grouper

Transport in water is the most common method for achieving high survival rates when transporting cultured fish in China; yet, transport success relies on proper water quality and conditions. This research was designed to explore the effects of ascorbic acid and β-1,3-glucan on survival, physiological responses, and flesh quality of farmed tiger grouper (Epinephelus fuscoguttatus) during simulated transport. The transport water temperature for live tiger grouper was 15 °C, which had the highest survival rate, the lowest stress response, and metabolic rate, and this will reduce the susceptibility to diseases. It is stated that β-1,3-glucan influences the changes of cortisol content, heat shock protein 70, IL-1β, and IgM transcription levels during simulated transport. Rather than using ascorbic acid alone (the A-group), β-1,3-glucan (3.2 mg/L) in the presence of ascorbic acid (25 mg/L) can effectively reduce the increase of transport-induced serum cortisol content, heat shock protein 70, and IL-1β, but stimulated IgM. 25 mg/L ascorbic acid and 3.2 mg/L β-1,3-glucan had no obvious effect on the nutritional indexes and flavor of live tiger grouper; however, these can effectively reduce the stress response, improve the innate immune activity, and ensure a higher survival rate.

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