Abstract
Simple SummaryThe impact of heat stress is a major challenge causing economical losses to the poultry industry. Heat stress exerts a damaging effect on physiological responses such as immunity, oxidative stress, and intestinal and muscular functions. In this review, we highlight the potential cytoprotective effects of heat-shock proteins to antagonize the adverse effects of heat shock, and how we can modulate their functions with pharmacological and nutritional interventions.Heat stress is one of the most challenging environmental stresses affecting domestic animal production, particularly commercial poultry, subsequently causing severe yearly economic losses. Heat stress, a major source of oxidative stress, stimulates mitochondrial oxidative stress and cell dysfunction, leading to cell damage and apoptosis. Cell survival under stress conditions needs urgent response mechanisms and the consequent effective reinitiation of cell functions following stress mitigation. Exposure of cells to heat-stress conditions induces molecules that are ready for mediating cell death and survival signals, and for supporting the cell’s tolerance and/or recovery from damage. Heat-shock proteins (HSPs) confer cell protection against heat stress via different mechanisms, including developing thermotolerance, modulating apoptotic and antiapoptotic signaling pathways, and regulating cellular redox conditions. These functions mainly depend on the capacity of HSPs to work as molecular chaperones and to inhibit the aggregation of non-native and misfolded proteins. This review sheds light on the key factors in heat-shock responses for protection against cell damage induced by heat stress in chicken.
Highlights
The relentless stresses imposed by high ambient temperatures and the associated oxidative stress exacerbate several health problems in domestic animals, primarily commercial chicken
There is the enhancement of cell survival-related gene expression, and the early activation of some molecules that work as molecular chaperones and contribute to cell survival processes during heat stress, such as heat-shock factors (HSFs) and heat-shock proteins (HSPs) [3,4,5]
The interaction between HSP27 and AKT can form a complex with p38 mitogen-activated protein kinase (MAPK), which mediates the phosphorylation of HSP27 that binds to AKT and works as a scaffold protein to allow for the phosphorylation of AKT
Summary
The relentless stresses imposed by high ambient temperatures and the associated oxidative stress exacerbate several health problems in domestic animals, primarily commercial chicken. The cell has developed adaptive and effective mechanisms to counteract cellular insult induced by heat stress Among these mechanisms, there is the enhancement of cell survival-related gene expression, and the early activation of some molecules that work as molecular chaperones and contribute to cell survival processes during heat stress, such as heat-shock factors (HSFs) and heat-shock proteins (HSPs) [3,4,5]. The induction of HSPs is an essential endogenous protection mechanism The upregulation of these molecules enhances cell stability and develops thermotolerance during heat-stress conditions. Kamboh et al reported that flavonoid supplementation (genistein and hesperidin) downregulated HSP70 mRNA in the skeletal muscle of heat-stressed broilers [14] They suggested that this downregulation might be due to the structural and functional resemblance of genistein with estrogens. Naturalplant-derived compounds might modulate HSP expression by tuning their induction during stress conditions through their biological and pharmacological activities, including antioxidant, detoxification, and anti-inflammatory activities [15,16]
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