Abstract

Heat shock (HS) protein 70 (HSP70), a well-known HS-induced protein, acts as an intracellular chaperone to protect cells against stress conditions. Although HS induces HSP70 expression to confer stress resistance to cells, HS causes cell toxicity by increasing reactive oxygen species (ROS) levels. Recently, a standardized extract of Asparagus officinalis stem (EAS), produced from the byproduct of asparagus, has been shown to induce HSP70 expression without HS and regulate cellular redox balance in pheochromocytoma cells. However, the effects of EAS on reproductive cell function remain unknown. Here, we investigated the effect of EAS on HSP70 induction and oxidative redox balance in cultured bovine cumulus-granulosa (CG) cells. EAS significantly increased HSP70 expression; however, no effect was observed on HSP27 and HSP90 under non-HS conditions. EAS decreased ROS generation and DNA damage and increased glutathione (GSH) synthesis under both non-HS and HS conditions. Moreover, EAS synergistically increased HSP70 and HSF1 expression and increased progesterone levels in CG cells. Treatment with an HSP70 inhibitor significantly decreased GSH level, increased ROS level, and decreased HSF1, Nrf2, and Keap1 expression in the presence of EAS. Furthermore, EAS significantly increased progesterone synthesis. Thus, EAS improves HSP70-mediated redox balance and cell function in bovine CG cells.

Highlights

  • Heat shock (HS) protein 70 (HSP70), a well-known HS-induced protein, acts as an intracellular chaperone to protect cells against stress conditions

  • To determine the concentration of extract of Asparagus officinalis stem (EAS) required to induce the expression of HSP27, HSP70, and HSP90 in bovine CG cells, we examined various concentrations of EAS (0.5, 1, and 5 mg/mL)

  • Since HSPs are induced by HS, we evaluated the effect of EAS on HSP expression after 6 h of HS (41 °C) treatment in comparison with that under non-HS conditions in bovine CG cells

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Summary

Introduction

Heat shock (HS) protein 70 (HSP70), a well-known HS-induced protein, acts as an intracellular chaperone to protect cells against stress conditions. We investigated the effect of EAS on HSP70 induction and oxidative redox balance in cultured bovine cumulus-granulosa (CG) cells. The balance between ROS and GSH levels can reduce DNA damage by altering the cellular redox status, improving cell survival. Asparagine has been found to increase HSP70 mRNA levels in a human promyelocytic leukemia cell ­line[20] This evidence suggests that EAS is a potential inducer of HSP70, which may regulate the balance between GSH and ROS generation. Several products, such as paeoniflorin, geranylgeranylacetone, and bimoclomol, have been found to stimulate ­HSP7021,22. These data showed that the HSP70 inducer has a synergistic effect under HS on HSP70 expression

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