title: Overexpression of heat shock protein 70 and its relationship to intestine under acute heat stress in broilers: 2. Intestinal oxidative stress.
abstract: Oxidative stress injury is one important factor in intestinal mucosal barrier damage. Expression of heat shock protein (HSP)70 is an endogenous mechanism by which living cells adapt to stress. This study was undertaken to investigate the protective effects of HSP70 on intestinal oxidative stress. Two hundred and forty broilers were injected intraperitoneally with HSP70 inducer l-(1)-glutamine or with the inhibitor quercetin. Twenty-four hours later, they were heat stressed for 0, 2, 3, 5, and 10 h, respectively, at 36 ± 1°C. The l-(1)-glutamine significantly increased HSP70 expression (P < 0.001). At 2 h or 3 h of heat stress, the HSP70 expression obviously elevated (P < 0.001). Levels of corticosterone and the heterophil:lymphocyte ratio significantly increased when HSP70 expression was inhibited (P < 0.0001). Serum corticosterone was negatively correlated with the HSP70 expression at 3 h of heat stress (P = 0.0015; R = -0.6537). Heat shock protein 70 significantly protected the integrity of the intestinal mucosa from heat stress, with significantly decreased lactic dehydrogenase when HSP70 expression was enhanced (P < 0.001). In addition, heat-stress time significantly affected the lactic dehydrogenase release (P < 0.001). Furthermore, HSP70 significantly elevated antioxidant enzyme activities (such as superoxide dismutase, glutathione peroxidase, and total antioxidant capacity) and inhibited lipid peroxidation to relieve intestinal mucosal oxidative injury (P < 0.001). These results suggest that HSP70 is capable of protecting the intestinal mucosa from heat-stress injury by improving antioxidant capacity of broilers and inhibiting the lipid peroxidation production.
authors.affiliation: State Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, China. guxianhong@vip.sina.com
authors.forename: X H
authors.initials: XH
authors.lastname: Gu
authors.forename: Y
authors.initials: Y
authors.lastname: Hao
authors.forename: X L
authors.initials: XL
authors.lastname: Wang
mesh_terms: D000818:Animals; D000975:Antioxidants / Q000032:analysis; D002645:Chickens / Q000502:physiology*; D003345:Corticosterone / Q000097:blood; D005973:Glutamine / Q000494:pharmacology*; D005979:Glutathione Peroxidase / Q000032:analysis; D006098:Granulocytes / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000166:cytology / Q000378:metabolism*; D007583:Jejunum / Q000166:cytology / Q000378:metabolism; D007770:L-Lactate Dehydrogenase / Q000032:analysis; D015227:Lipid Peroxidation; D008214:Lymphocytes / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism; D008297:Male; D008315:Malondialdehyde / Q000032:analysis; D018384:Oxidative Stress; D011794:Quercetin / Q000494:pharmacology*; D011897:Random Allocation; D013482:Superoxide Dismutase / Q000032:analysis
chemical_list: D000975:Antioxidants; D018840:HSP70 Heat-Shock Proteins; D005973:Glutamine; D008315:Malondialdehyde; D011794:Quercetin; D007770:L-Lactate Dehydrogenase; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D003345:Corticosterone