Expression of heat shock protein 60 in the tissues of transported piglets

Abstract

In this study, we sought to determine the distribution and expression of heat shock protein 60 (Hsp60) in the tissues of transported piglets. A total of 24 Chinese Erhualian piglets with an average body weight of 20±1 kg were assessed under both 2-h transported and normal housing conditions. Results of enzymatic analysis showed that the serum creatine kinase and aspartate aminotransferase concentrations were significantly increased in the 2-h transported piglets. Acute cellular lesions characterized by granular and vacuolar degeneration of the parenchyma cells in the tested heart, liver, and kidney were also confirmed by histopathological test after 2 h transportation. These results indicate that transport stress induces tissue damage to heart, liver, and kidney. Hsp60-positive immunostaining was consistently detected in the cytoplasm of myocardial cells, hepatocytes, renal tubular epithelial cells, and epithelial cells of fundic gland. However, results of enzyme-linked immunosorbent assay indicated that Hsp60 expression was only significantly elevated in the stomach, with lower expression in the heart and a nonsignificant trend of increased liver and kidney expression of Hsp60. These results indicate that different tissues had different sensitivities to transport stress, possibly resulting in varying levels of cytoprotection by Hsp60 in the different tissues. The expression of Hsp60 following 2 h transportation coincided with deterioration of cardiac cytoprotection in the heart and protection in the stomach. However, the direct role of Hsp60 in cytoprotection of heart and stomach tissues needs further investigation.

Hsp110 expression changes in rat primary myocardial cells exposed to heat stress in vitro

“…All Hsp110 loss-of-function or deletion mutants listed in the Drosophila deletion project database are lethal (Easton et al, 2000). However, contrary to our finding of Hsp110 protecting myocardial cells from damage, Hsp110 expression is induced by cadmium exposure but is dispensable for cell survival of mouse NIH3T3 fibroblasts (Ridley et al, 2010), suggesting that the regulation of Hsp110 may have cellular and tissue specificity in disparate organisms (Zhu et al, 2009;Yue et al, 2010).…”

Differential stress responses among newly received calves: variations in reductant capacity and Hsp gene expression

“…Bao et al (2008) reported an attenuation of four cardiac Hsp members, in response to 6 h road transportation. In accordance with this study, Zhu et al (2009) found more than 60% reduction in cardiac Hsp60 of piglets, following 2 h transportation. Most interestingly, the authors report a tissue-specific Hsp response; in addition to the decrease in cardiac Hsp, a significant increase and nonchanged levels of Hsp60 were detected for the stomach, liver and kidney, respectively.…”

“…Recently, it has been reported that elevated levels of intracellular Hsp60 may confer a tissue-dependent cytoprotection in 2-h transported piglets (Zhu et al, 2009). Studies during the last decade indicated that extracellular Hsp, being released from stressed cells, promoted proinflammatory cytokine production and local inflammation through activation of the innate immune system.…”

Heat shock protein 70 is upregulated in the intestine of intrauterine growth retardation piglets

“…Frozen intestinal mucosa samples were homogenized in cold solution (200 mg tissues per milliliter) containing 0.15 M NaCl, 20 mM Tris-HCl (pH 8.0), 1 mM EDTA, 1 mM phenylmethylsulfonyl fluoride, 0.1 μM E-46, 0.08 μM aprotinin, 0.1 μM leupeptin, and 0.1% NP-40 (Salokhe et al 2006;Zhu et al 2009) using Ultra-Turrax homogenizer on ice. The homogenate was centrifuged at 1,200×g, 15 min at 4°C.…”