1999
DOI: 10.1016/s0162-0134(99)00121-x
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Interference of aluminium on iron metabolism in erythroleukaemia K562 cells

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Cited by 27 publications
(22 citation statements)
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“…Taking together the present and previous findings, it is conceivable that fucoidan-binding Al may move into the S-phase nucleus. A number of studies of a variety of cultured cell lines have shown that Al loading resulted in abnormal Fe accumulation and compartmentalization [31][32][33]. Co-localization of Al and Fe has been found in hepatocytes of dialysis patients [34].…”
Section: Discussionmentioning
confidence: 99%
“…Taking together the present and previous findings, it is conceivable that fucoidan-binding Al may move into the S-phase nucleus. A number of studies of a variety of cultured cell lines have shown that Al loading resulted in abnormal Fe accumulation and compartmentalization [31][32][33]. Co-localization of Al and Fe has been found in hepatocytes of dialysis patients [34].…”
Section: Discussionmentioning
confidence: 99%
“…As Al and Fe share numerous common physicochemical features, it is not surprising that Fe metabolism is severely affected during Al stress (Morgan and Redgrave, 1998). Al is known to impede proteins/enzymes that are dependent on Fe to function in an effective manner due to their similar trivalent state; Al can readily substitute for Fe especially in environments where the former is easily accessible (Perez et al, 1999). However, its inability to undergo any redox manipulation compels Al to be associated with these essential biomolecules; hence, rendering them ineffective (Zatta et al, 2003;Middaugh et al, 2005).…”
Section: Al Interferes With Fe Homeostasismentioning
confidence: 99%
“…The dissociation constants for transferrin binding to iron and aluminum are within the same order of magnitude: 1.75 · 10 À9 M À1 and 1.37 · 10 À9 M À1 , respectively [49]. Cells cultured in the presence of Al 3+ were found to have an increased number of tranferrin receptors, so Fe 3+ uptake values were not altered [49]. In fluids where the concentrations of transferrin and citrate are low, Al 3+ binds nucleoside di-and triphosphates, and is found to displace Mg 2+ from the nucleotides [6].…”
Section: Introductionmentioning
confidence: 72%
“…About 90% of the Al 3+ in the blood is bound by the iron-transport protein transferrin [6,48]. The dissociation constants for transferrin binding to iron and aluminum are within the same order of magnitude: 1.75 · 10 À9 M À1 and 1.37 · 10 À9 M À1 , respectively [49]. Cells cultured in the presence of Al 3+ were found to have an increased number of tranferrin receptors, so Fe 3+ uptake values were not altered [49].…”
Section: Introductionmentioning
confidence: 99%