Malignant H1299 tumour cells preferentially internalize iron-bound inositol hexakisphosphate
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چکیده
منابع مشابه
Malignant H1299 tumour cells preferentially internalize iron-bound inositol hexakisphosphate
In colon enterocytes and in well-differentiated colon cancer CaCo-2 cells, InsP6 (inositol hexakisphosphate) inhibits iron uptake by forming extracellular insoluble iron/InsP6 complexes. In this study, we confirmed that CaCo-2 cells are not able to take up iron/InsP6 but, interestingly, found that the cells are able to internalize metal-free and Cr3+-bound InsP6. Thus, the inability of CaCo-2 c...
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Inositols (myo-inositol and inositol hexakisphosphate) exert a wide range of critical activities in both physiological and pathological settings. Deregulated inositol metabolism has been recorded in a number of diseases, including cancer, where inositol modulates different critical pathways. Inositols inhibit pRB phosphorylation, fostering the pRB/E2F complexes formation and blocking progressio...
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This review assesses the authenticity of inositol hexakisphosphate (InsP(6)) being a wide-ranging regulator of many important cellular functions. Against a background in which the possible importance of localized InsP(6) metabolism is discussed, there is the facile explanation that InsP(6) is merely an "inactive" precursor for the diphosphorylated inositol phosphates. Indeed, many of the propos...
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We report the crystal structure of the catalytic domain of human ADAR2, an RNA editing enzyme, at 1.7 angstrom resolution. The structure reveals a zinc ion in the active site and suggests how the substrate adenosine is recognized. Unexpectedly, inositol hexakisphosphate (IP6) is buried within the enzyme core, contributing to the protein fold. Although there are no reports that adenosine deamina...
متن کاملInhibition of iron-catalysed hydroxyl radical formation by inositol polyphosphates: a possible physiological function for myo-inositol hexakisphosphate.
1. The ability of myo-inositol polyphosphates to inhibit iron-catalysed hydroxyl radical formation was studied in a hypoxanthine/xanthine oxidase system [Graf, Empson and Eaton (1987) J. Biol. Chem. 262, 11647-11650]. Fe3+ present in the assay reagents supported some radical formation, and a standard assay, with 5 microM Fe3+ added, was used to investigate the specificity of compounds which cou...
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ژورنال
عنوان ژورنال: Bioscience Reports
سال: 2013
ISSN: 0144-8463,1573-4935
DOI: 10.1042/bsr20130079