MicroRNA-210 Regulates Endoplasmic Reticulum Stress and Apoptosis in Porcine Embryos

Muhammad Rosyid Ridlo1,2, Eui Hyun Kim1, Geon A Kim3

  • 1Department of Theriogenology and Biotechnology, Research Institute for Veterinary Science, College of Veterinary Medicine, Seoul National University, Seoul 08826, Korea.

Insights

In vitro embryo production is hindered by endoplasmic reticulum (ER) stress. Inhibiting microRNA-210 (miR-210) improves embryo development by reducing ER stress and apoptosis.

Area of Science:

  • Reproductive Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • Endoplasmic reticulum (ER) stress impedes in vitro embryo production and survival.
  • MicroRNA-210 (miR-210) is implicated in cellular stress adaptation and inflammation.

Purpose of the Study:

  • To investigate the role of miR-210 in porcine in vitro embryo development.
  • To determine the effects of miR-210 on ER stress and apoptosis during early embryonic development.

Main Methods:

  • Microinjection of miR-210 inhibitor or mimic into parthenogenetically activated porcine embryos.
  • Assessment of embryo developmental rates (cleavage and blastocyst formation).
  • Quantification of total cell number (TCN) in blastocysts.
  • Analysis of gene expression related to ER stress (XBP1, uXBP1, sXBP1, ATF4, PTPN1), apoptosis (Caspase 3), and pluripotency (NANOG, SOX2).

Main Results:

  • miR-210 inhibition significantly improved cleavage rates, blastocyst formation, and TCN, while reducing XBP1 expression.
  • Inhibition of miR-210 decreased ER stress markers (uXBP1, sXBP1, ATF4, PTPN1), apoptosis (Caspase 3), and increased pluripotency markers (NANOG, SOX2).
  • Conversely, miR-210 mimic injection impaired embryo development, downregulated ER stress and apoptosis markers, and reduced pluripotency markers.

Conclusions:

  • miR-210 plays a critical role in regulating porcine in vitro embryo development.
  • Inhibiting miR-210 can alleviate ER stress and reduce apoptosis, thereby enhancing in vitro embryo production outcomes.

Related Concept Videos

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.8K
MicroRNAs01:22

MicroRNAs

MicroRNA (miRNA) are short, regulatory RNA transcribed from introns (non-coding regions of a gene) or intergenic regions (stretches of DNA present between genes). Several processing steps are required to form biologically active, mature miRNA. The initial transcript, called primary miRNA (pri-mRNA), base-pairs with itself, forming a stem-loop structure. Within the nucleus, an endonuclease enzyme, called Drosha, shortens the stem-loop structure into hairpin-shaped pre-miRNA. After the pre-miRNA...
3.4K
MicroRNAs01:22

MicroRNAs

MicroRNA (miRNA) are short, regulatory RNA transcribed from introns—non-coding regions of a gene—or intergenic regions—stretches of DNA present between genes. Several processing steps are required to form biologically active, mature miRNA. The initial transcript, called primary miRNA (pri-mRNA), base-pairs with itself forming a stem-loop structure. Within the nucleus, an endonuclease enzyme, called Drosha, shortens the stem-loop structure into hairpin-shaped pre-miRNA. After...
23.2K
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
5.9K