Molecular Cloning and Expression of Ferritin mRNA in Heavy Metal-Poisoned<i>Xenopus laevis</i>Cells

Muller, Jean-Pierre; Vedel, Michèle; Monnot, M J; Touzet, Nicole; Wegnez, Maurice

doi:10.1089/dna.1991.10.571

Cited by 15 publications

(6 citation statements)

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“…Semiquantitative RT-PCR revealed that the transcriptional level of AlFER was the highest in the intestine, followed by the respiratory tree, perisoma and muscle strips, with no mRNA detected in the gonad. It is noteworthy that the intestine of A. leucoprocta is always fi lled with mud and therefore is potentially challenged by bacteria and metal ions that may cause up-regulation of ferritin expression (Muller et al, 1991;Zhang et al, 2006). The absence of ferritin in gonad coincides with reports on Haliotis rufescens and H .…”

Section: Discussionsupporting

confidence: 79%

Construction of a cDNA library for sea cucumber Acaudina leucoprocta and differential expression of ferritin peptide

Zhou

Hou²,

et al. 2016

Chin. J. Ocean. Limnol.

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Acaudina leucoprocta is an edible sea cucumber of economic interest that is widely distributed in China. Little information is available concerning the molecular genetics of this species although such knowledge would contribute to a better understanding of the optimal conditions for its aquaculture and its mechanisms of defense against disease. Therefore, we constructed a cDNA library and, based on bioinformatics analysis of the sequences, the functions of 75% of the cDNAs were identifi ed, including those involved in cell structure, energy metabolism, mitochondrial function, and signal transduction pathways. Approximately 25% of genes in the library were unmatched. The gene for A. leucoprocta ferritin was also cloned. The predicted amino-acid sequence of ferritin displayed signifi cant homology with other sea-cucumber counterparts but indicated that it was a new member of the ferritin family. Semiquantitative real-time RT-PCR indicated the highest levels of ferritin mRNA expression in the intestine. A polyclonal antibody of ferritin was also produced. These data provide a set of molecular tools essential for further studies of the functions of ferritin protein in A. leucoprocta .

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Section: Discussionsupporting

confidence: 79%

Construction of a cDNA library for sea cucumber Acaudina leucoprocta and differential expression of ferritin peptide

Zhou

Hou²,

et al. 2016

Chin. J. Ocean. Limnol.

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“…In contrast, the heme‐free ferritin encoded by cj0612c involved in intracellular iron storage was upregulated. Ferritin is involved in the primary detoxification response to heavy metals including Cd 2+ in Xenopus laevis cells [53]. The principal function of ferritins is to store iron inside cells in the ferric form; a secondary function could be detoxification of iron or protection against O 2 and its reactive products.…”

Section: Resultsmentioning

confidence: 99%

Molecular responses of Campylobacter jejuni to cadmium stress

2008

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Cadmium ions (Cd 2+ ) are a potent carcinogen in animals, and cadmium is a toxic metal of significant environmental and occupational importance for humans [1][2][3][4][5]. Cadmium ions are very toxic even at low concentrations, but the basis for their toxicity is not fully understood. Cadmium is not a redox-active metal and does not participate in Fenton-type reactions. Moreover, it does not bind to DNA or interact with DNA in a stable manner [1,2].Several mechanisms have been proposed to explain how bacteria and lower eukaryotes protect themselves against cadmium toxicity. These include accumulation of intracellular Zn 2+ , reduction of Cd 2+ uptake, enhanced expression of the low-molecular weight cysteine-rich protein metallothionein that sequesters cadmium, binding of cadmium ions by other heavy metal-associated proteins, and an increase in intracellular disulfide content that contributes to effective binding of cadmium [6].Disulfide reductases are responsible for the modulation of intracellular disulfide concentrations. They are essential enzymes in the antioxidant mechanisms of Cadmium ions are a potent carcinogen in animals, and cadmium is a toxic metal of significant environmental importance for humans. Response curves were used to investigate the effects of cadmium chloride on the growth of Camplyobacter jejuni. In vitro, the bacterium showed reduced growth in the presence of 0.1 mm cadmium chloride, and the metal ions were lethal at 1 mm concentration. Two-dimensional gel electrophoresis combined with tandem mass spectrometry analysis enabled identification of 67 proteins differentially expressed in cells grown without and with 0.1 mm cadmium chloride. Cellular processes and pathways regulated under cadmium stress included fatty acid biosynthesis, protein biosynthesis, chemotaxis and mobility, the tricarboxylic acid cycle, protein modification, redox processes and the heat-shock response. Disulfide reductases and their substrates play many roles in cellular processes, including protection against reactive oxygen species and detoxification of xenobiotics, such as cadmium. The effects of cadmium on thioredoxin reductase and disulfide reductases using glutathione as a substrate were studied in bacterial lysates by spectrophotometry and nuclear magnetic resonance spectroscopy, respectively. The presence of 0.1 mm cadmium ions modulated the activities of both enzymes. The interactions of cadmium ions with oxidized glutathione and reduced glutathione were investigated using nuclear magnetic resonance spectroscopy. The data suggested that, unlike other organisms, C. jejuni downregulates thioredoxin reductase and upregulates other disulfide reductases involved in metal detoxification in the presence of cadmium.Abbreviations GSH, reduced glutathione; GSSG, oxidized glutathione; MTA, 5¢-methylthioadenosine; SAH, S-adenosylhomocysteine; TCA, tricarboxylic acid.

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“…1983, Goudard et al 1991, Milcent et al 1996. Thus, some authors have suggested that ferritin may be a general metal detoxicant protein carrier (Joshi & Zimmerman 1988, Joshi et al 1989, Muller et al 1991. Taking into consideration these observations, the binding of 2'0Po by ferritin in fish liver is, therefore, not surprising.…”

Section: Discussionmentioning

confidence: 98%

210Po binding to metallothioneins and ferritin in the liver of teleost marine fish

Durand¹,

Carvalho²,

Goudard³

et al. 1999

Mar. Ecol. Prog. Ser.

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The subcellular distribution of the naturally occurring radionuclide "' PO was investigated in the Liver of the Atlantic mackerel Scomber scombrus. The majority of the 2'0Po was found in the cytosol of the liver cells. Fractionation of the cytosol proteins by high performance size-exclusion and ion-exchange chromatography indicated that about 30% of 210Po was bound to ferritin and approximately 28% to metallothioneins. The affinity of 210Po for these proteins was confirmed by a similar binding of the artificial Z08Po isotope incubated in vitro with the cytosolic proteins. Two other proteins, likely selenium-and zinc-containing enzymes, may also bind smaller amounts of 210Po, about 8 % each. The extensive binding of 'lOPo to ferritin and metallothioneins is not accompanied by a similar strong binding of 21uPb, the radioactive grandparent of "OPo, which explains the generally very high 210Po:210Pb ratio observed in fish tissues and, in particular, fish liver KEY WORDS: Polonium. Fish. Metallothionein. Ferritin INTRODUCTIONPolonium-210, a high energy D-particle emitter in the uranium decay chain, is the major source of internal radiation dose to marine organisms (Cherry & Heyraud 1982, Carvalho 1988. This naturally occurring radionuclide is also responsible for a significant proportion of the radiation exposure of humans to background radiation, in particular, through consumption of seafood (Parfenov 1974, Hunt & Allington 1993, Yamamoto et al. 1994, Carvalho 1995a. 210Po is naturally occurring and ubiquitous in our environment, but, due to its radiotoxic properties, special attention has been paid to the possible enhancement of 210Po environmental concentrations which may occur from the inputs of effluents of phosphate-ore processing industries (Germain et al. 1992, Pennders et al. 1992, Carvalho 1995b, Swift et al. 1995.It is well known that 210Po is accumulated particularly by marine organisms and transferred through 'E-mail: jpdurandmnat svt sciences.univ-nantes.fr marine food chains (Heyraud & Cherry 1979, Carvalho 19881, with ingestion being the major route of entry (Carvalho & Fowler 1994). The tissues of some organisms, such as the hepatopancreas of crustaceans and fish liver may contain particularly high concentrations of 210Po. Furthermore, they display 210Po:2'0Pb ratios of 10' to 103 (Carvalho 1988), which correspond to an enhanced ratio in the food chain compared to the 210Po:210Pb ratio in sea water, which is around unity (Heyraud & Cherry 1979). The reason for an elevated 210Po:210Pb ratio in marine food chains is not known. Furthermore, several studies have suggested that the subcellular localization of 2'0Po, in particular in the cell nucleus, may have important implications with respect to the genetic radiotoxic effects of the 210Po U particles (Howell et al. 1990).Some attempts have been made previously to establish the subcellular localization of 2'0Po in tissues of marine invertebrates and small mammals. The aim of this study was to investigate the subcellular distribution of 210Po a...

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Molecular Cloning and Expression of Ferritin mRNA in Heavy Metal-PoisonedXenopus laevisCells

Cited by 15 publications

References 47 publications

Construction of a cDNA library for sea cucumber Acaudina leucoprocta and differential expression of ferritin peptide

Construction of a cDNA library for sea cucumber Acaudina leucoprocta and differential expression of ferritin peptide

Molecular responses of Campylobacter jejuni to cadmium stress

210Po binding to metallothioneins and ferritin in the liver of teleost marine fish

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