32
views
0
recommends
+1 Recommend
1 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Influence of long-term thermal stress on the 
 in vitro maturation on embryo development and Heat Shock Protein abundance in zebu cattle

      research-article

      Read this article at

      ScienceOpenPublisherPMC
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The objective of this study was to investigate the influence of long-term temperature stress during the in vitro maturation (IVM) of oocytes on the in vitro embryo production (IVP) and the abundance of HSP70 and HSP90 in zebu cattle. Viable cumulus-oocyte complexes (COCs) were incubated for 24 h at 37 °C, 38.5 °C, or 40 °C for the low-, physiological, and high-temperature stress treatments, respectively. Thereafter, they were subjected to in vitro fertilization and culture. Temperature did not affect the polar body extrusion. However, IVP was adversely affected when IVM took place at 37 °C and 40 °C. The highest abundance of HSP70 was observed in cumulus cells after maturation of COCs at 40 °C. In contrast, HSP70 was more abundant in oocytes at both 37 °C and 40 °C; however, at 40 °C, the difference to the control group (38.5 °C) was not significant. In contrast, the highest abundance of HSP90 was observed in oocytes and cumulus cells at 37 °C. It appears that HSP70 and HSP90 respond to cold and heat stress in different ways. In conclusion, moderately high (40 °C) and low (37 °C) thermal stress for 24 h during IVM is detrimental to the developmental competence of oocyte and is accompanied by changes in the abundances of HSP70 and HSP90, especially in cumulus cells.

          Related collections

          Most cited references42

          • Record: found
          • Abstract: found
          • Article: not found

          Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.

          The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90. Both sequences end with the motif EEVD. The crystal structures of the TPR-peptide complexes show the peptides in an extended conformation, spanning a groove in the TPR domains. Peptide binding is mediated by electrostatic interactions with the EEVD motif, with the C-terminal aspartate acting as a two-carboxylate anchor, and by hydrophobic interactions with residues upstream of EEVD. The hydrophobic contacts with the peptide are critical for specificity. These results explain how TPR domains participate in the ordered assembly of Hsp70-Hsp90 multichaperone complexes.
            • Record: found
            • Abstract: found
            • Article: not found

            Invited review: Effects of heat and cold stress on mammalian gene expression.

            This review examines the effects of thermal stress on gene expression, with special emphasis on changes in the expression of genes other than heat shock proteins (HSPs). There are approximately 50 genes not traditionally considered to be HSPs that have been shown, by conventional techniques, to change expression as a result of heat stress, and there are <20 genes (including HSPs) that have been shown to be affected by cold. These numbers will likely become much larger as gene chip array and proteomic technologies are applied to the study of the cell stress response. Several mechanisms have been identified by which gene expression may be altered by heat and cold stress. The similarities and differences between the cellular responses to heat and cold may yield key insights into how cells, and by extension tissues and organisms, survive and adapt to stress.
              • Record: found
              • Abstract: found
              • Article: not found

              Effect of bovine sperm separation by either swim-up or Percoll method on success of in vitro fertilization and early embryonic development.

              The objectives of these experiments were to characterize separation of frozen-thawed bovine spermatozoa on a Percoll gradient and then to compare sperm separation by either a swim-up or Percoll gradient procedure for the ability of spermatozoa to fertilize oocytes in vitro. The Percoll gradient was a 45 and 90% discontinuous gradient. Initial experiments found that centrifugation of semen on the Percoll gradient for 15 min at 700 g was sufficient to obtain optimal recovery of motile spermatozoa. Most of the nonmotile spermatozoa were recovered at the interface of the 45 and 90% Percoll layers, while the motile spermatozoa were primarily in the sperm pellet at the bottom of the gradient. When frozen-thawed semen from each of 7 bulls was separated by swimup, a mean +/- SEM of 9% +/- 1 of the motile spermatozoa were recovered after the procedure. In contrast, more spermatozoa were recovered after Percoll gradient separation (P 0.05). A carry over of Percoll into the fertilization medium with the Percoll separated spermatozoa was found not the cause for the decreased penetration of oocytes by these spermatozoa. In 2 of 3 bulls tested, the decreased penetration of oocytes by Percoll separated spermatozoa could be overcome by increasing the sperm concentration during fertilization from 1 x 10(6) to 5 x 10(6)/ml. When development of embryos fertilized by either swim-up or Percoll separated spermatozoa was compared for the semen from 2 bulls, a difference in cleavage rate was found in favor of swim-up separated spermatozoa (P 0.05). The disadvantages of the Percoll procedure could easily be overcome and the procedure was faster and yielded a six-fold greater recovery of motile spermatozoa than the swim-up method.

                Author and article information

                Journal
                Anim Reprod
                Anim Reprod
                ar
                Animal Reproduction
                Colégio Brasileiro de Reprodução Animal - CBRA
                1806-9614
                1984-3143
                27 August 2020
                2020
                : 17
                : 3
                : e20190085
                Affiliations
                [1 ] originalInstitute of Reproductive Biology, Leibniz Institute for Farm Animal Biology, Dummerstorf, Germany
                [2 ] originalPrograma de Pós-graduação em Ciência Animal, Universidade Estadual de Londrina, Londrina, PR, Brasil
                [3 ] originalNational Dairy Research Institute, Animal Biotechnology Centre, Karnal, Haryana, India
                [4 ] originalPrograma de Pós-graduação em Ciência Animal, Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brasil
                [5 ] originalPrograma de Pós-graduação em Ciências Veterinárias, Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brasil
                [6 ] originalPrograma de Pós-graduação em Zootecnia, Universidade Estadual de Mato Grosso do Sul, Aquidauana, MS, Brasil
                Author notes
                [* ]Corresponding author: fabiana.sterza@ 123456uems.br

                Conflicts of interest: The authors have no conflict of interest to declare.

                RP: Conceptualization, Funding acquisition, Supervision, Writing – review & editing; MBSC performed the experiments, Formal analysis, Methodology, Writing – original draft; TKD: Conceptualization; JV: Methodology; MIMM: helped supervise the project; WALS: helped the formal analysis; CJTC: Methodology; FAMS: Conceptualization, Funding acquisition, Data curation, Supervision, Writing – review & editing.

                Author information
                http://orcid.org/0000-0003-2521-6126
                http://orcid.org/0000-0002-7846-7685
                http://orcid.org/0000-0003-2426-8901
                http://orcid.org/0000-0001-7374-4615
                http://orcid.org/0000-0001-8416-2450
                http://orcid.org/0000-0001-6579-9982
                http://orcid.org/0000-0001-7815-3339
                http://orcid.org/0000-0002-0597-9663
                Article
                arAO20190085 00203
                10.1590/1984-3143-AR2019-0085
                7534571
                33029207
                79ab73e0-01cc-4ae4-abfd-5f7557542a93
                Copyright @

                Copyright © The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 22 June 2019
                : 07 August 2020
                Page count
                Figures: 1, Tables: 2, Equations: 0, References: 46
                Funding
                Funded by: CAPES
                Award ID: 88881.068117/2014-01
                Funded by: CAPES
                Award ID: 001
                Financial support: This study was funded by the Coordination of Improvement of Higher Education Personnel - Brazil (CAPES - 88881.068117/2014-01) and the Foundation for the Development of Teaching, Science, and Technology in Mato Grosso do Sul (FUNDECT). Ph.D. students received a grant from CAPES (001).
                Categories
                Original Article

                oocytes,hsp70,hsp90,bovine
                oocytes, hsp70, hsp90, bovine

                Comments

                Comment on this article

                Related Documents Log