Reactivity of Al(III) with membrane phospholipids: a NMR approach

Zambenedetti, Pamela; Tisato, Francesco; Corain, Benedetto; Zatta, Paolo

doi:10.1007/bf00149555

Cited by 16 publications

(3 citation statements)

References 19 publications

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“…However, the evidence presented above shows that exposure of both soluble and membrane-bound enzymes to AICI3 and Al-citrate (0-100 μΜ), causes no changes in enzymatic activity. These findings, in addition to reports that Al affects vesicle fusion and alters membrane permeability [35,36], indicates that the plasma membrane and not enzymatic binding domains is the most likely site of Al toxicity in plants.…”

Section: It Is Likely That Alsupporting

confidence: 53%

Aluminum interaction with plasma membrane lipids and enzyme metal binding sites and its potential role in Al cytotoxicity

Jones¹,

Kochian²

1997

FEBS Letters

145

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The trivalent cation aluminum can cause chronic cytotoxicity in plants, animals and microorganisms. It has been suggested that Al interaction with cell membranes and enzyme metal binding sites may be involved in Al cytotoxicity. In this study, the binding of Al to microsomes and liposomes was found to be lipid dependent with the signal transduction element phosphatidylinositol-4,5-bisphosphate having the highest affinity for Al with an Al:lipid stoichiometry of 1:1. Al binding was only reduced in the presence of high concentrations of Ca 2+ (> 1 ηιΜ). Both citrate and, to a lesser extent, malate were capable of preventing Al lipid binding, which is consistent with the involvement of these organic acids in a recently described Al detoxification mechanism in plants. The effects of AICI3, Alcitrate and Z11SO4 on metal-dependent enzyme activities (enolase, pyruvate kinase, H + -ATPase, myosin, Calpain, proteinase K, phospholipase A2 and arginase) was assayed in vitro. While Zn 2+ was capable of inhibiting all the enzymes except the H+-ATPase, AICI3 and Al-citrate had minimal effects except for with phospholipase A 2 where an interaction with AICI3 occurred. However, this could be negated by the addition of citrate. The results indicate that, contrary to current hypotheses, the toxic mode of Al is not through an interaction with enzymatic catalytic metal binding sites but may be through the interaction with specific membrane lipids.

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Section: It Is Likely That Alsupporting

confidence: 53%

Aluminum interaction with plasma membrane lipids and enzyme metal binding sites and its potential role in Al cytotoxicity

Jones¹,

Kochian²

1997

FEBS Letters

145

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“…These metals can damage intracellular proteins and DNA, can interfere with enzymatic activity, and through redox changes may alter Fe–S clusters. ,, Aluminum can alter the outer membrane by three known mechanisms: binding to phosphate functional groups in the membrane, displacing Mg, and promoting lipid peroxidation. ,,, Aluminum has a strong preference for oxygen donors, which makes phosphate molecules, a major component of phospholipids, ideal targets for Al binding. Bound to phospholipids, Al alters protein interactions, , promotes aggregation of phosphorylated chains, and may cause misfolding of proteins …”

Section: Resultsmentioning

confidence: 99%

Antibacterial Activity of Aluminum in Clay from the Colombian Amazon

Londono

Hartnett

Williams

2017

Environ. Sci. Technol.

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The problems of antibiotic overuse compel us to seek alternative antibacterial agents. Some clays have been shown to kill antibiotic-resistant human pathogens and may provide an alternative to known antibiotics. Here we show that Al toxicity plays a central role in the antibacterial action of a kaolin-rich clay from the Colombian Amazon (AMZ). Antibacterial susceptibility testing shows minimum inhibitory concentrations of 80 mg/mL against a model Escherichia coli (ATCC 25922). The clay buffered the media pH to ∼4.6 and Eh values to +360 mV. Chemical analysis of AMZ and bacteria showed that Al, P, and transition metals (Fe, Cu, Mn, and Zn) were exchanged during incubation at 37 °C. Only Al derived from the clay exceeded the minimum inhibitory concentrations for E. coli under acidic conditions. Ion imaging showed elevated Al levels in the bacterial membrane, and high intracellular Fe levels, relative to those of untreated controls. Phosphorus depletion in E. coli after reaction with AMZ, together with evidence of membrane permeabilization, suggests that Al reacts with membrane phospholipids, enhancing intracellular transport of metals. These results highlight the importance of dissolved Al for amplifying the toxicity of transition metals to human pathogens.

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“…It also reduced the Mg 2+ -ATPase activity in Zea mays L. microsomal fractions [ 69 ]. Al binding to membrane phospholipids altered lipid-protein interaction and modified their transport in human erythrocytes [ 70 ]. Since significantly more Al bound to CIAT899 than to B3 membrane, we propose that this is responsible for membrane damage and consequently the higher leakage of ATP from Al-treated CIAT899 than B3 cells.…”

Section: Discussionmentioning

confidence: 99%

The Cell Membrane of a Novel Rhizobium phaseoli Strain Is the Crucial Target for Aluminium Toxicity and Tolerance

Wekesa

John

Reichelt

et al. 2022

Cells

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Soils with low pH and high aluminium (Al) contamination restrict common bean production, mainly due to adverse effects on rhizobia. We isolated a novel rhizobium strain, B3, from Kenyan soil which is more tolerant to Al stress than the widely used commercial strain CIAT899. B3 was resistant to 50 µM Al and recovered from 100 µM Al stress, while CIAT899 did not. Calcein labeling showed that less Al binds to the B3 membranes and less ATP and mScarlet-1 protein, a cytoplasmic marker, leaked out of B3 than CIAT899 cells in Al-containing media. Expression profiles showed that the primary targets of Al are genes involved in membrane biogenesis, metal ions binding and transport, carbohydrate, and amino acid metabolism and transport. The identified differentially expressed genes suggested that the intracellular γ-aminobutyric acid (GABA), glutathione (GSH), and amino acid levels, as well as the amount of the extracellular exopolysaccharide (EPS), might change during Al stress. Altered EPS levels could also influence biofilm formation. Therefore, these parameters were investigated in more detail. The GABA levels, extracellular EPS production, and biofilm formation increased, while GSH and amino acid level decreased. In conclusion, our comparative analysis identified genes that respond to Al stress in R. phaseoli. It appears that a large portion of the identified genes code for proteins stabilizing the plasma membrane. These genes might be helpful for future studies investigating the molecular basis of Al tolerance and the characterization of candidate rhizobial isolates that perform better in Al-contaminated soils than commercial strains.

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Reactivity of Al(III) with membrane phospholipids: a NMR approach

Cited by 16 publications

References 19 publications

Aluminum interaction with plasma membrane lipids and enzyme metal binding sites and its potential role in Al cytotoxicity

Aluminum interaction with plasma membrane lipids and enzyme metal binding sites and its potential role in Al cytotoxicity

Antibacterial Activity of Aluminum in Clay from the Colombian Amazon

The Cell Membrane of a Novel Rhizobium phaseoli Strain Is the Crucial Target for Aluminium Toxicity and Tolerance

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