Effects of short-term copper exposure on gill structure, metallothionein and hypoxia-inducible factor-1α (HIF-1α) levels in rainbow trout (Oncorhynchus mykiss)

Heerden, Daléne van; Vosloo, André; Nikinmaa, Mikko

doi:10.1016/j.aquatox.2004.06.002

Cited by 104 publications

(63 citation statements)

References 24 publications

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“…Cell proliferation with thickening of gill filament epithelium is one histological change found in fish exposed to copper by several authors (Arellano 1999, De Boeck et al 2001, van Heerden et al 2004, and may lead to the lamellar fusion observed in this study. These results also were found in fish exposed to other pollutants (Randi et al 1996, Van den Heuvel et al 2000, Rosety-Rodríguez et al 2002.…”

Section: Discus Discus Discus Discus Discussion Sion Sion Sion Sionmentioning

confidence: 79%

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Histopathological changes in liver and gill epithelium of Nile tilapia, Oreochromis niloticus, exposed to waterborne copper

et al. 2007

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Nile tilapia, Oreochromis niloticus, of both sexes were reared in freshwater and exposed to 0.5, 1.0 and 2.5mg L-1 of waterborne copper for a period of 21 days. Liver and gill samples were collected after 21 days of exposure to copper and lesions were analyzed by light microscopy. The main histopathological changes observed in gills exposed to the highest concentration were edema, lifting of lamellar epithelia and an intense vasodilatation of the lamellar vascular axis. Although less frequent, lamellar fusion caused by the filamentar epithelium proliferation and some lamellar aneurisms were also found. The liver of control group exhibited a quite normal architecture, while the fish exposed to copper showed vacuolation and necrosis. These hepatic alterations were more evident in fish exposed to 1.0 and 2.5mg L-1 copper concentrations. The number of hepatocytes nucleus per mm² of hepatic tissue decreased with the increase of copper concentration. In contrast, the hepatic somatic index was high in fish exposed at 2.5mg L-1 of copper. In short, this work advance new knowledge as influence of copper in the gill and liver histology of O. niloticus and demonstrated that their effects could be observed at different concentrations.

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confidence: 79%

“…The edema, epithelial lifting as well as lamellar fusion also are defence mechanisms that reduce the branchial superficial area in contact with the external milieu. These mechanisms also increase the diffusion barrier to the pollutant (Laurèn & McDonald 1985, Van Heerden et al 2004.…”

Section: Discus Discus Discus Discus Discussion Sion Sion Sion Sionmentioning

confidence: 99%

Histopathological changes in liver and gill epithelium of Nile tilapia, Oreochromis niloticus, exposed to waterborne copper

et al. 2007

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“…The environmental copper load was adequate to cause significant structural changes in the fish tissues (Heerden et al, 2004). This electron microscopic study, after 24 h Cu exposure, showed that the initial alteration of gills appeared in the mucosal cells of the lamellar epithelium.…”

Section: Discussionmentioning

confidence: 94%

Toxicity of copper in butterfish (Poronotus triacanthus): Tissues accumulation and ultrastructural changes

Jiraungkoorskul

Sahaphong

Kangwanrangsan

2007

Environmental Toxicology

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The present study investigated the accumulation of copper in various tissues and ultrastructural alterations in butterfish, Poronotus triacanthus. In acute toxicity test, butterfish were exposed to 250 g/L copper for 24 h. In subacute toxicity test, fish were exposed to 25 g/L copper for 7 days and then returned to normal water for 48 h. The levels of copper accumulation in the tissues were determined by using an atomic absorption spectrometer. After the 7 day exposure, the highest level of copper was found in the liver, followed by kidney, gills, and muscle tissues (3.64, 0.62, 0.59, and 0.34 g/L, respectively). The recovery group has shown some reduction in copper level in these tissues when compared with those of the 7 day exposure group (3.09, 0.34, 0.30, and 0.27 g/L, respectively). In gills, the major changes such as filament cell proliferation, increase in intercellular spaces, epithelial lifting, and thickening of the filament and lamellar epithelium were observed. In liver, the major changes such as swollen mitochondria, fragmented in rough endoplasmic reticulum, increases in number and size of lysosomes and lipid droplets. Infiltration of leukocytes, increasing hepatocyte size with pyknotic nuclei, and presence of vacuoles were also observed. In kidney, the changes included alterations of the first proximal tubules, as well as vacuolization of the cytoplasm, proliferation of lysosomes and mitochondria, dilation of endoplasmic reticulum, and finally, cell necrosis. The transmission electron microscopic analysis revealed that the 7 day exposure group had more severe effect in tissue alterations than the 24 h exposure group. Tissue regeneration was also observed in the 48 h recovery group. # 2007 Wiley Periodicals, Inc. Environ Toxicol 22: 92-100, 2007.

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“…Several Fe(II)-dependent enzymes, such as the HIF-prolyl hydroxylase (PHD 1-3) and asparagine hydroxylase (FIH-1), regulate HIF-1α stability and activation. Numerous studies have shown that HIF-1α is not only regulated by oxygen tension, but also by various other stimuli, such as transition metals, which can mimic hypoxia to stabilize HIF-1α protein in cultured cells (Horiguchi et al, 1996;Oshiro et al, 1998;Chun et al, 2000;Hossain et al, 2000;Gao et al, 2002bGao et al, , 2004Yuan et al, 2003;Hwang et al, 2004;van Heerden et al, 2004;Zhao et al, 2004). Since Fe(II) is an important cofactor for these hydroxylases and loosely bound to two histidine sites in these enzymes, non-iron metal ions may decrease the activity of these enzymes by either decreasing cellular iron level or directly replacing iron in the enzymes that hydroxylate HIF.…”

Section: Discussionmentioning

confidence: 99%

Effects of 12 metal ions on iron regulatory protein 1 (IRP-1) and hypoxia-inducible factor-1 alpha (HIF-1α) and HIF-regulated genes

Chen

Huang

et al. 2006

Toxicology and Applied Pharmacology

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Several metal ions that are carcinogenic affect cellular iron homeostasis by competing with iron transporters or iron-regulated enzymes. Some metal ions can mimic a hypoxia response in cells under normal oxygen tension, and induce expression of HIF-1α-regulated genes. This study investigated whether 12 metal ions altered iron homeostasis in human lung carcinoma A549 cells as measured by an activation of IRP-1 and ferritin level. We also studied hypoxia signaling by measuring HIF-1α protein levels, hypoxia response element (HRE)-driven luciferase reporter activity, and Cap43 protein level (an HIF-1α responsive gene). Our results show the following: (i) Ni(II), Co(II), V(V), Mn(II), and to a lesser extent As(III) and Cu(II) activated the binding of IRP-1 to IRE after 24 h, while the other metal ions had no effect; (ii) 10 of 12 metal ions induced HIF-1α protein but to strikingly different degrees. Two of these metal ions, Al(III) and Cd(II), did not induce HIF-1α protein; however, as indicated below, only Ni(II), Co (II), and to lesser extent Mn(II) and V(V) activated HIF-1α-dependent transcription. The combined effects of both [Ni(II) + As(III)] and [Ni (II) + Cr(VI)] on HIF-1α protein were synergistic; (iii) Addition of Fe(II) with Ni(II), Co(II), and Cr (VI) attenuated the induction of HIF-1α after 4 h treatment; (iv) Ni(II), Co(II), and Mn(II) significantly decrease ferritin level after 24 h exposure; (v) Ni(II), Co(II), V (V), and Mn(II) activated HRE reporter gene after 20 h treatment; (vi) Ni(II), Co(II), V(V), and Mn(II) increased the HIF-1-dependent Cap43 protein level after 24 h treatment. In conclusion, only Ni (II), Co (II), and to a lesser extent Mn(II) and V(V) significantly stabilized HIF-1α protein, activated IRP, decreased the levels of ferritin, induced the transcription of HIF-dependent reporter, and increased the expression of Cap43 protein levels (HIF-dependent gene). The mechanism for the significant stabilization and elevation of HIF-1α protein which drives these other parameters was previously shown by us and others to involve a loss of cellular Fe as well as inhibition of HIF-1α-dependent prolyl hydroxylases which target the binding of VHL ubiquitin ligase and degrade HIF-1α. Even though there were small effects of some of the other metals on IRP and HIF-1α, downstream effects of HIF-1α activation and therefore robust hypoxia signaling were only observed with Ni(II), Co(II), and to much lesser extents with Mn(II) and V(V) in human A549 lung cells. It is of interest that the metal ions that were most effective in activating hypoxia signaling were the ones that were poor inducers of metallothionein protein and also decreased Ferritin levels, since both of these proteins can bind metal ions and protect the cell against toxicity in human lung cells. It is important to study effects of these metals in human lung cells since this represents a major route of human environmental and occupational exposure to these metal ions.

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Effects of short-term copper exposure on gill structure, metallothionein and hypoxia-inducible factor-1α (HIF-1α) levels in rainbow trout (Oncorhynchus mykiss)

Cited by 104 publications

References 24 publications

Histopathological changes in liver and gill epithelium of Nile tilapia, Oreochromis niloticus, exposed to waterborne copper

Histopathological changes in liver and gill epithelium of Nile tilapia, Oreochromis niloticus, exposed to waterborne copper

Toxicity of copper in butterfish (Poronotus triacanthus): Tissues accumulation and ultrastructural changes

Effects of 12 metal ions on iron regulatory protein 1 (IRP-1) and hypoxia-inducible factor-1 alpha (HIF-1α) and HIF-regulated genes

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