Thermal stress accelerates mercury chloride toxicity in Oreochromis niloticus via up-regulation of mercury bioaccumulation and HSP70 mRNA expression

Although fumonisins are identified as responsible for alterations in weight gain, little information is available on their effects on expression of growth-related genes, especially for Nile tilapia (Oreochromis niloticus) fingerlings. In this study, Nile tilapia fingerlings were treated with increasing levels of fumonisin B1 (FB1) and fumonisin B2 (FB2) (diets of 0, 20, 40, and 60 mg/kg) to evaluate their effects on weight gain (WG), feed intake (FI), feed efficiency (FE), growth hormone receptor (GHR) and insulin growth factor 1 (IGF-1) mRNA expression in liver of this fish. All variables were evaluated at 15 and 30 days of treatment. Diet containing 0 mg fumonisin/kg was used as control treatment. Treatment with 20, 40, and 60 mg fumonisin/kg of diet significantly reduced WG (P<0.0001) and FE (P<0.0001), while GHR and IGF-1 mRNA expression was reduced both at 15 and 30 days of treatment. Feed intake was not affected by diets in any of the evaluated periods. These results indicate that fumonisins (FB1 + FB2) affect the growth of Nile tilapia fingerlings through mechanisms that involve reduction of GHR and IGF-1 expression.

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Regulation of human heme oxygenase-1 gene expression under thermal stress

Blood ◽

10.1182/blood.v87.12.5074.bloodjournal87125074 ◽

1996 ◽

Vol 87 (12) ◽

pp. 5074-5084 ◽

Cited By ~ 99

Author(s):

S Okinaga ◽

K Takahashi ◽

K Takeda ◽

M Yoshizawa ◽

H Fujita ◽

...

Keyword(s):

Gene Expression ◽

Thermal Stress ◽

Heat Shock ◽

Transient Expression ◽

Reporter Gene ◽

Heme Oxygenase ◽

Gene Promoter ◽

Heme Oxygenase 1 ◽

Heat Shock Element ◽

Hsp70 Mrna

Heme oxygenase-1 is an essential enzyme in heme catabolism, and its human gene promoter contains a putative heat shock element (HHO-HSE). This study was designed to analyze the regulation of human heme oxygenase-1 gene expression under thermal stress. The amounts of heme oxygenase-1 protein were not increased by heat shock (incubation at 42 degrees C) in human alveolar macrophages and in a human erythroblastic cell line, YN-1–0-A, whereas heat shock protein 70 (HSP70) was noticeably induced. However, heat shock factor does bind in vitro to HHO-HSE and the synthetic HHO-HSE by itself is sufficient to confer the increase in the transient expression of a reporter gene upon heat shock. The deletion of the sequence, located downstream from HHO-HSE, resulted in the activation of a reporter gene by heat shock. These results suggest that HHO-HSE is potentially functional but is repressed in vivo. Interestingly, heat shock abolished the remarkable increase in the levels of heme oxygenase-1 mRNA in YN-1–0-A cells treated with hemin or cadmium, in which HSP70 mRNA was noticeably induced. Furthermore, transient expression assays showed that heat shock inhibits the cadmium-mediated activation of the heme oxygenase-1 promoter, whereas the HSP70 gene promoter was activated upon heat shock. Such regulation of heme oxygenase-1 under thermal stress may be of physiologic significance in erythroid cells.

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