Association of Americium with Ferritin in the Canine Liver

Stover, Betsy J.; Bruenger, F. W.; Stevens, Wallace

doi:10.2307/3572868

Cited by 28 publications

(18 citation statements)

References 7 publications

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“…For example, in studies carried out on the hepatopancreas of marine invertebrates, 210Po was found mainly associated with the microsomal pellet and with an unidentified high molecular weight fraction (Cherry et al 1979, Finger & Smith 1987, Heyraud et al 1987. We noted that some authors have shown that ferritin, which may reach a molecular weight of about 850 kDa, is able to precipitate with the microsomal fraction during centrifugation (Stover et al 1970, Bruenger et al 1971, whereas other authors have reported that ferritin may also be an integral component of the microsomal fraction (Minotti 1989). Whichever the case, our chromatographic results clearly show that there is an extensive binding of 'lOPo by ferritin, which might explain earlier reports on the high 210Po content of the microsomal fraction in invertebrates.…”

Section: Discussionmentioning

confidence: 72%

“…However, ferritin can also combine with other metals such as Cd, Zn, Cu, Ni, CO, Mn, Mg, Pb, Be, T1 and A1 (Treffy & Harrison 1984, Wardeska et al 1986, Fleming & Joshi 1991. Pead et al 1995, and it has also been shown that transuranium elements such as Am, Cm, Cf and Pu are associated with the cytosolic ferritin in mammals and in marine invertebrates (Stover et al 1970, Bruenger et al 1976, Galey e t al. 1983, Goudard et al 1991, Milcent et al 1996.…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 72%

Section: Discussionmentioning

confidence: 99%

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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“…(5) The association of Am(II1) with ferritin in the cytosol of canine liver has been reported by STOVER et uZ. (18) who consider that ferritin is the major binding species for Am(II1) in canine liver. In the rat liver both Am(II1) and Cm(II1) have been shown to become associated with ferritin in the cytosol within 1 hr of their intravenous injection in soluble form.…”

Section: Binding Of Transuranic Elements To Proteinsmentioning

confidence: 83%

Interactions Between Transuranium Elements and the Components of Cells and Tissues

Taylor¹

1972

Health Physics

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Comparative studies of the interactions of plutonium, americium and curium with serum proteins from various species, with proteins isolated from the organic matrix of bone, and with some other proteins have all shown that plutonium is bound very much more firmly by protein than either americium or curium. Investigations of the sub-cellular distribution patterns of these elements in liver and testes have shown that all three elements become associated with lysosomal structures and that different mechanisms of lysosomal uptake are involved for polymeric and monomeric plutonium, americium and curium. The implications of these findings are discussed in relation to the types of biological damage which has been observed in experimental animals.

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“…Additional roles have been described for this storing molecule. Indeed, early studies on subcellular distribution of transuranic elements such as 238 Pu and 241 Am in mammals tissues have shown also that this iron-carrier systems (ferritin and transferrin) have an important function in the transport and fixation of these radionuclides (Stover et al, 1970;Lehmann et al, 1983) as well as in accumulation of the natural radionuclide 210 Po in marine organisms (Durand et al, 1999(Durand et al, , 2002. Ferritin has also been suggested as being an acute phase protein responding to a nonlethal injury to the organism.…”

Section: Introductionmentioning

confidence: 97%

Crassostrea gigas ferritin: cDNA sequence analysis for two heavy chain type subunits and protein purification

Durand

Goudard

Pieri

et al. 2004

Gene

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Ferritin has been shown as being the principal iron storage in the majority of living organisms. In marine species, ferritin is also involved in high-level accumulation of (210)Po. As part of our work on the investigation of these radionuclides' concentration in natural environment, ferritin was searched at the gene and protein level. Ferritin was purified from the visceral mass of the oyster Crassostrea gigas by ion-exchange chromatography and HPLC. SDS-PAGE revealed one band of 20 kDa. An Expressed Sequence Tag (EST) library was screened and led to the identification of two complementary DNA (cDNA) involved in ferritin subunit expression. The complete coding sequences and the untranslated regions (UTRs) of the two genes were obtained and a 5' Rapid Amplification of cDNA Ends (RACE) was used to obtain the two iron-responsive elements (IREs) with the predicted stem-loop structures usually present in the 5'-UTR of ferritin mRNA. Sequence alignment in amino acid of the two new cDNA showed an identity with Pinctada fucata (85.4-88.3%), Lymnaea stagnalis (79.3-82.2%) and Helix pomatia (79.1-79.1%). The residues responsible for the ferroxidase center, conserved in all vertebrate H-ferritins, are present in the two oyster ferritin subunits. Oyster ferritins do not present the special characteristics of other invertebrate ferritins like insect ferritins but have some functional similarities with the vertebrate H chains ferritin.

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Association of Americium with Ferritin in the Canine Liver

Cited by 28 publications

References 7 publications

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

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

Interactions Between Transuranium Elements and the Components of Cells and Tissues

Crassostrea gigas ferritin: cDNA sequence analysis for two heavy chain type subunits and protein purification

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