Modulation of heat shock protein 70 (HSP70) gene expression ex vivo in response to heat stress in chicken.

The present study was conducted to assess the effect of exposure to heat stress on the HSP70 gene expression pattern ex vivo in chickens. The adult healthy birds (n = 15) grouped into three replicates of n = 5 each were used to isolate peripheral blood mononuclear cells (PBMCs). The PBMCs were subjected to heat stress at 42 °C for 1 h, and cells without heat stress (NHS) were taken as control. The cells were seeded in 24 well plates and incubated in a humidified incubator at 37 °C under 5% CO2 for recovery. HSP70 expression kinetics were evaluated at 0, 2, 4, 6, and 8 h of the recovery period. Compared with NHS, the expression pattern of HSP70 was upregulated gradually from 0 to 4 h with peak (p < 0.05) expression recorded at 4 h of recovery time. mRNA expression of HSP70 escalated in a time-dependent manner from 0 to 4 h of heat exposure and thereafter exhibited a gradually decreasing pattern till 8 h of the recovery period. The findings from this study highlight the protective role of HSP70 against the deleterious effects of heat stress in chicken PBMCs. Further, the study demonstrates the possible use of PBMCs as a cellular system in assessing the heat stress effect in chickens ex vivo.

Untranslated regions (UTRs) orchestrate translation reprogramming in cellular stress responses.

Stress is the result of an organism's interaction with environmental challenges. Regulations of gene expression including translation modulations are critical for adaptation and survival under stress. Untranslated regions (UTRs) of the transcripts play significant roles in translation regulation and continue to raise many intriguing questions in our understanding of cellular stress physiology. IRES (Internal ribosome entry site) and uORF (upstream open reading frame) mediated alternative translation initiations are emerging as unique mechanisms. Recent studies have revealed novel means of mRNAs stabilization in stress granules and their reversible modifications. Differential regulation of select transcripts is possible by the interplay between the adenine/uridine-rich elements (AREs) in 3'UTR with their binding proteins (AUBP) and by microRNA-mediated effects. Coordination of these various mechanisms control translation and thereby enables appropriate responses to environmental stress. In this review, we focus on the role of sequence signatures both at 5' and 3'UTRs in translation reprogramming during cellular stress responses.