Comparison of the monovalent cation complexes of monensin, nigericin, and dianemycin

Steinrauf, L. K.; Czerwinski, Edmund W.; Pinkerton, Mary

doi:10.1016/0006-291x(71)90156-2

Cited by 32 publications

(11 citation statements)

References 4 publications

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“…We next investigated whether Bak is critically involved in the maintenance of autophagic flux during cell death induced by agents that have properties similar to those of nigericin. The structure and properties of nigericin are similar to those of monensin, although monensin has a preference for Na ϩ instead of K ϩ (25,38). Like nigericin, monensin treatment disrupts lysosomal function (27,39).…”

Section: Characterization Of Nigericin-induced Mn9d Neuronal Cellmentioning

confidence: 71%

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Nigericin-induced Impairment of Autophagic Flux in Neuronal Cells Is Inhibited by Overexpression of Bak

Lim

Lee

Kim

et al. 2012

Journal of Biological Chemistry

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Section: Characterization Of Nigericin-induced Mn9d Neuronal Cellmentioning

confidence: 71%

“…Nigericin is an ionophore and acts as an antiporter of K ϩ /H ϩ and raises the pH of acidic compartments (25). In image-based screens for autophagy inducers, nigericin was identified as one of the candidates that increase LC3 spots following treatment (26).…”

Section: Bak Is a Prototypic Pro-apoptoticmentioning

confidence: 99%

Nigericin-induced Impairment of Autophagic Flux in Neuronal Cells Is Inhibited by Overexpression of Bak

Lim

Lee

Kim

et al. 2012

Journal of Biological Chemistry

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“…Unlike monensin, these larger polyethers also show direct coordination of a carboxylic acid atom to the cation, as does grisoxin (30-dehydroxynigericin) in which the equivalent of the O-11 atom in monensin A is missing [33]. These differences have been ascribed to the increasing flexibility of the ligand in the larger polyethers, which also permits them to coordinate a wider selection of cations [34]. …”

Section: Resultsmentioning

confidence: 99%

Intermediates in monensin biosynthesis: A late step in biosynthesis of the polyether ionophore monensin is crucial for the integrity of cation binding

Hüttel

Spencer

Leadlay

2014

Beilstein J. Org. Chem.

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SummaryPolyether antibiotics such as monensin are biosynthesised via a cascade of directed ring expansions operating on a putative polyepoxide precursor. The resulting structures containing fused cyclic ethers and a lipophilic backbone can form strong ionophoric complexes with certain metal cations. In this work, we demonstrate for monensin biosynthesis that, as well as ether formation, a late-stage hydroxylation step is crucial for the correct formation of the sodium monensin complex. We have investigated the last two steps in monensin biosynthesis, namely hydroxylation catalysed by the P450 monooxygenase MonD and O-methylation catalysed by the methyl-transferase MonE. The corresponding genes were deleted in-frame in a monensin-overproducing strain of Streptomyces cinnamonensis. The mutants produced the expected monensin derivatives in excellent yields (ΔmonD: 1.13 g L−1 dehydroxymonensin; ΔmonE: 0.50 g L−1 demethylmonensin; and double mutant ΔmonDΔmonE: 0.34 g L−1 dehydroxydemethylmonensin). Single crystals were obtained from purified fractions of dehydroxymonensin and demethylmonensin. X-ray structure analysis revealed that the conformation of sodium dimethylmonensin is very similar to that of sodium monensin. In contrast, the coordination of the sodium ion is significantly different in the sodium dehydroxymonensin complex. This shows that the final constitution of the sodium monensin complex requires this tailoring step as well as polyether formation.

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“…X-ray diffraction studies of nigericin and its metal complexes (Steinrauf et al, 1971) have demonstrated that potassium complexes of nigericin have cyclic structure in contrast to the nondissociated form of the antibiotic which is linear in configuration. This structural difference accounts for different mobilities of the hydrogen and potassium complexes and dimers.…”

Section: Discussionmentioning

confidence: 98%

Nigericin-induced charge transfer across membranes

et al. 1975

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The electric properties of the bilayer lecithin membranes have been studied in the presence of the antibiotic nigericin. When the antibiotic concentration is about 10(-7) ohm-1 cm-2. The potassium ion concentration gradient gives rise to a transmembrane potential of the order of 40 mV per 10-fold concentration gradient with the side of the higher potassium concentration negative. The transmembrane potential produced by the hydrogen ion concentration gradient is a function of the potassium ion concentration which is equal on both sides of the membrane. For low potassium ion concentrations the hydrogen potential has the expected polarity with the solution having higher concentration of protons negative. For potassium ion concentrations exceeding 0.03 M the hydrogen potential has the reverse polarity. This unexpected result cannot be accounted for in terms of the available simple hypotheses about the charge transport mechanism for nigericin in BLM. In order to account for the experimental results obtained, a theoretical approach has been developed based on the assumption that charge is transported across the membrane by nigericin dimers. The theoretical predicitons are in satisfactory agreement with the experimental results. The model also yields some predictions which may be verified in future experiments.

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Comparison of the monovalent cation complexes of monensin, nigericin, and dianemycin

Cited by 32 publications

References 4 publications

Nigericin-induced Impairment of Autophagic Flux in Neuronal Cells Is Inhibited by Overexpression of Bak

Nigericin-induced Impairment of Autophagic Flux in Neuronal Cells Is Inhibited by Overexpression of Bak

Intermediates in monensin biosynthesis: A late step in biosynthesis of the polyether ionophore monensin is crucial for the integrity of cation binding

Nigericin-induced charge transfer across membranes

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