Erythrocyte Hemolysis by Organic Tin and Lead Compounds

Kleszcyńska, H; Hładyszowski, Jerzy; Pruchnik, Hanna; Przestalski, S.

doi:10.1515/znc-1997-1-212

Cited by 31 publications

(21 citation statements)

References 6 publications

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“…Alkyl compounds of tin are particularly toxic, and the more methyl groups they contain, the more harmful they are. Among their other effects, organic compounds of tin inhibit the process of oxidative phosporylation and accelerate the hemolysis of erythrocytes [1][2][3]. They also change the physical properties of lipid model membranes.…”

Section: Introductionmentioning

confidence: 99%

The influence of tin compounds on the dynamic properties of liposome membranes: A study using the ESR method

Man

Podolak

Engel

2006

Cellular and Molecular Biology Letters

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Abstract:The influence of organic and inorganic compounds of tin on the dynamic properties of liposome membranes obtained in the process of dipalmitoylphosphatidylcholine (DPPC) sonication in distilled water was investigated. This was carried out by means of the spin ESR probe method. The probes were selected in such a way as to penetrate different areas of the membrane (a TEMPO probe, 5-DOXYL stearic acid, 16-DOXYL stearic acid). Four compounds of tin were chosen: three organic ones, (CH 3 ) 4 Sn, (C 2 H 5 ) 4 Sn and (C 3 H 7 ) 3 SnCl, and one inorganic one, SnCl 2 . The investigated compounds were added to a liposome dispersion, which was prepared prior to that. The concentration of the admixture was changed within the values from 0 to 10%-mole in proportion to DPPC. The studies indicated that the chlorides of tin display the highest activity in their interaction with liposome membranes. Since these compounds have ionic form in a water solution, the obtained result can mean that this form of admixture has a considerable influence on its activity. Furthermore, it was found that there is a slightly stronger influence of tin compounds with a longer hydrocarbon chain on changes in the probes' spectroscopic parameters.

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Section: Introductionmentioning

confidence: 99%

The influence of tin compounds on the dynamic properties of liposome membranes: A study using the ESR method

Man

Podolak

Engel

2006

Cellular and Molecular Biology Letters

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“…In our hands these compounds showed marked toxicity at 100 mM (data not shown). Compounds 6, 7, and 8 are non-drug-like; compounds 6 and 8 are organolead and organotin molecules, respectively, which as a general class of molecules are considered to be neurotoxins (Chang, 1990) and cause erythrocyte lysis (Kleszcy nska et al, 1997). Compound 7 (trichopolyn I) is a structurally complex 10-residue lipopeptide isolated from the fungus Trichoderma polysporum that belongs to the trichogin class of lipopeptaibols antibiotics whose mechanism of action is thought to be pore formation in bacterial cell membranes (de Zotti et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Experimental Evaluation of Proposed Small-Molecule Inhibitors of Water Channel Aquaporin-1

et al. 2016

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The aquaporin-1 (AQP1) water channel is a potentially important drug target, as AQP1 inhibition is predicted to have therapeutic action in edema, tumor growth, glaucoma, and other conditions. Here, we measured the AQP1 inhibition efficacy of 12 putative small-molecule AQP1 inhibitors reported in six recent studies, and one AQP1 activator. Osmotic water permeability was measured by stopped-flow light scattering in human and rat erythrocytes that natively express AQP1, in hemoglobin-free membrane vesicles from rat and human erythrocytes, and in plasma membrane vesicles isolated from AQP1-transfected Chinese hamster ovary cell cultures. As a positive control, 0.3 mM HgCl 2 inhibited AQP1 water permeability by .95%. We found that none of the tested compounds at 50 mM significantly inhibited or increased AQP1 water permeability in these assays. Identification of AQP1 inhibitors remains an important priority.

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“…These results are in agreement with earlier reports. 19 The distribution of Me 3 SnCl and Ph 3 SnCl in erythrocyte systems can be explained by the hydrophilic nature of trimethyltin (which is responsible for its relatively poor haemolytic activity) and the hydrophobic character of triphenyltin and tripropyltin (which shows a highly haemolytic action). This, in turn, suggests that the high-affinity binding site of triphenyltin is located in a very hydrophobic region of the erythrocyte membrane systems.…”

Section: Discussionmentioning

confidence: 99%

Molecular mechanism of haemolysis induced by triphenyltin chloride

Burda

Lekki

Cieślak

et al. 2002

Applied Organom Chemis

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Organometals are known to cause lysis of cells, but the molecular mechanism of their action is not recognized. In this work, we have examined the interaction of triphenyltin with erythrocyte membranes. We determined the order of haemolytic activity of the investigated organometal species as being: triphenyllead > tripropyltin = triphenyltin > triethyllead > trimethyltin. Such an order suggests that the haemolytic activity increases with the increasing hydrophobicity of the organic ligands. Compounds containing lead are more toxic than the respective complexes of tin. Triphenyltin chloride (Ph 3 SnCl) is very effective in lysis of erythrocytes. Using 119 Sn Mo È ssbauer spectroscopy we showed that triphenyltin interacts with the protein components of pig erythrocyte membranes in a highly specific way, but we did not detect any interaction of triphenyltin with pig haemoglobin. The Mo È ssbauer spectrum was fitted with a single doublet characterized by hyperfine parameters that differ considerably from those reported for other organotin compounds in membranes of red blood cells. Applying the point charge model of the electric field gradient for the analysis of the environment of tin bonds from the quadrupole splitting, we could indicate N het from histidine and/or S thiol from cysteine as the only possible ligands of Ph 3 Sn(IV). We expect that protein components of erythrocyte membranes having similar cysteine and histidine arrangement, such as in cat or rat haemoglobins, which provide high-affinity binding sites for organotins, can bind triphenyltin with high affinity. We give some arguments that ankyrin and b-spectrin are the most probable targets of Ph 3 Sn(IV) action and indicate its potential binding sites within the proteins. The highly specific interaction of triphenyltin with the membrane cytoskeleton components, postulated by us, should already influence the rigidity of red blood cells at the stage preceding the lysis of erythrocytes. To support this hypothesis, we carried out scanning force microscopy measurements of red blood cells elasticity. We have observed a lower stiffness for erythrocytes treated with concentrations of Ph 3 SnCl that caused less than 20% of haemolysis.

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Erythrocyte Hemolysis by Organic Tin and Lead Compounds

Cited by 31 publications

References 6 publications

The influence of tin compounds on the dynamic properties of liposome membranes: A study using the ESR method

The influence of tin compounds on the dynamic properties of liposome membranes: A study using the ESR method

Experimental Evaluation of Proposed Small-Molecule Inhibitors of Water Channel Aquaporin-1

Molecular mechanism of haemolysis induced by triphenyltin chloride

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