Dataset Information

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

ABSTRACT: 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.

SUBMITTER: Stamperna K

PROVIDER: S-EPMC8235242 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature

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

Stamperna Konstantina K Giannoulis Themistoklis T Dovolou Eleni E Kalemkeridou Maria M Nanas Ioannis I Dadouli Katerina K Moutou Katerina K Mamuris Zissis Z Amiridis Georgios S GS

Animals : an open access journal from MDPI 20210616 6

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 ...[more]

PMID: 34208520

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Project description:The aim of this work was to evaluate the impacts of feeding different levels of postbiotic RI11 on antioxidant enzyme activity, physiological stress indicators, and cytokine and gut barrier gene expression in broilers under heat stress. A total of 252 male broilers Cobb 500 were allocated in cages in environmentally controlled chambers. All the broilers received the same basal diet from 1 to 21 d. On day 22, the broilers were weighed and grouped into 7 treatment groups and exhibited to cyclic high temperature at 36 ± 1°C for 3 h per day until the end of the experiment. From day 22 to 42, broilers were fed with one of the 7 following diets: negative control, basal diet (0.0% RI11) (NC group); positive control, NC diet + 0.02% (w/w) oxytetracycline (OTC group); antioxidant control, NC diet + 0.02% (w/w) ascorbic acid. The other 4 other groups were as follows: NC diet + 0.2% cell-free supernatant (postbiotic RI11) (v/w), NC diet + 0.4% cell-free supernatant (postbiotic RI11) (v/w), NC diet + 0.6% cell-free supernatant (postbiotic RI11) (v/w), and NC diet + 0.8% cell-free supernatant (postbiotic RI11) (v/w). Supplementation of different levels (0.4, 0.6, and 0.8%) of postbiotic RI11 increased plasma glutathione peroxidase, catalase, and glutathione enzyme activity. Postbiotic RI11 groups particularly at levels of 0.4 and 0.6% upregulated the mRNA expression of IL-10 and downregulated the IL-8, tumor necrosis factor alpha, heat shock protein 70, and alpha-1-acid glycoprotein levels compared with the NC and OTC groups. Feeding postbiotic RI11, particularly at the level of 0.6%, upregulated ileum zonula occludens-1 and mucin 2 mRNA expressions. However, no difference was observed in ileum claudin 1, ceruloplasmin, IL-6, IL-2, and interferon expression, but downregulation of occludin expression was observed as compared with the NC group. Supplementation of postbiotic RI11 at different levels quadratically increased plasma glutathione peroxidase, catalase and glutathione, IL-10, mucin 2, and zonula occludens-1 mRNA expression and reduced plasma IL-8, tumor necrosis factor alpha, alpha-1-acid glycoprotein, and heat shock protein 70 mRNA expression. The results suggested that postbiotics produced from Lactiplantibacillus plantarum RI11 especially at the level of 0.6% (v/w) could be used as an alternative to antibiotics and natural sources of antioxidants in poultry feeding.

Dataset Information

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

Publications

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

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