Modulation of Heat-Shock Proteins Mediates Chicken Cell Survival against Thermal Stress

Simple Summary The 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.