Mitochondrial Oxidative Damage in Chicken Skeletal Muscle Induced by Acute Heat Stress

Abstract

Mitochondria have long been known to play a critical role in maintaining bioenergetic status under physiological conditions. Our previous studies have shown that acute heat stress increases production of mitochondrial reactive oxygen species (ROS) in the skeletal muscle of chickens. This increased ROS production may lead to nonspecific modification of lipids and proteins, which may then result in bioenergetic dysfunctions. If increased mitochondrial ROS production in heat-stressed chickens causes oxidative damage, changes in mitochondrial peroxidized lipids and oxidatively modified proteins can be detected. To study this, --week-old male broiler chickens (nῌ.ῌ2) were exposed to acute heat stress (-.῍ for +2 h) while control chickens were kept at thermoneutral condition (,/῍). Skeletal muscle subsarcolemmal mitochondria were isolated and used to study mitochondrial malondialdehyde (MDA) and protein carbonyl groups. Mitochondrial thiobarbituric acid reactive substances (TBARS) formation was measured colorimetrically with *.*+ῌ butylated hydroxytoluene (BHT) and expressed as MDA equivalent. To detect oxidation-sensitive mitochondrial proteins, polypeptides resolved by two-dimensional (,D) electrophoresis were immunostained with DNP-specific antibodies for carbonylated proteins using Western blotting. In heat-stressed chickens, mitochondrial MDA was ,.1-fold higher, and 2, mitochondrial proteins were oxidized when compared to that of control chickens. These results suggest that in heat-stressed chickens, increased mitochondrial ROS production leads to oxidative damage to mitochondrial lipids and proteins.

Sequential changes in superoxide production, anion carriers and substrate oxidation in skeletal muscle mitochondria of heat‐stressed chickens

“…Indeed we have already provided direct evidence of mitochondrial superoxide generation using both electron spin resonance (ESR) spectroscopy, with 5,5-dimethyl-1-pyrroline N-oxide as a spin trap agent, and lucigenin-derived chemiluminescence (LDCL) in skeletal muscle of acute heat-stressed chickens [7]. It was also shown that the acute heat treatments exhibited oxidative damage to mitochondrial proteins and lipids in chicken skeletal muscle [8]. However, the mechanism underlying acute heat stress-induced in vivo overproduction of mitochondrial superoxide in chicken skeletal muscle is not still clear.…”

Role of Heat Shock Proteins in Livestock Adaptation to Heat Stress

“…11,18 HS was shown to raise both of Thiobarbituric acid-reactive species (TBARS) and malondialdehyde (MDA) levels in broilers, buffalos and dairy cows which are the major products of lipid peroxidation. 19,20 Antioxidant enzymes activities, namely superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX) were observed to increase in HS in livestock. 11 Elevated concentration of SOD and GPX concentration was observed in prepartum cows with peaks around calving during summer month.…”

Improvement in Egg Production of PD 3 Chicken Line with Histopathological Conditions of the Jejunum up on Supplementation of Fermented Yeast Culture during and Post Summer Season

“…Azad et al, (2013) observed that in chronic heat exposed chickens, ROS production increased and was found until d9 of HS and not thereafter, which means that chickens became acclimatized to the heat stress. In 18 h heat stressed chickens, plasma and mitochondrial malondialdehyde (MDA) was 2.1-and 2.7-fold higher (Mujahid et al, 2007). Even though the role of appetite regulating hormones like Leptin, Ghrelin on feed intake, functions of liver is known (Song et al, 2012), their role on physiological and metabolic functions of chickens experiencing heat stress during summer season is lacking.…”