Search bioRxiv⌕ Search

Biology subjects

Leonenko, Z.

Publications and source records attributed to Leonenko, Z..

5 recordsLinked to original sources

Giant and Opposite Lithium Isotope Effects on Rat Hippocampus Synaptic Activity Revealed by Multi-Electrode Array Electrophysiology

INTRODUCTORY SUMMARYLithium (Li) has been a frontline medication for the treatment of bipolar disorder for decades, but its mechanism of action remains poorly understood1,2. While clinically prescribed Li salts consist of a mixture of two stable isotopes, 6Li and 7Li, the neurobiological effects of each isotope are only beginning to receive attention. Recent theoretical proposals have suggested that the Li isotopes may exert unique effects in the brain, stemming from quantum phenomena linked to their distinct nuclear spin properties3-5. However, aside from earlier observations of isotope-dependent variations in animal behavior6,7, direct experimental evidence is lacking. We used multi-electrode array electrophysiology to probe field excitatory post-synaptic potentials (fEPSPs) in rat brain slices and demonstrated that 6Li and 7Li have large and opposite effects on synaptic transmission and lead to smaller, but still distinct, differences in synaptic plasticity, particularly, paired-pulse facilitation and the early stages of long-term potentiation. Our results provide direct experimental evidence that Li isotopes exert remarkably different neurological effects, while avoiding many of the interpretive challenges associated with behavioural studies. These findings lay the groundwork for future investigations of quantum phenomena in neuronal activity and promote the idea that Li isotopes are pharmacologically distinct agents.

neuroscience↗

Effects of Natural Lithium and Lithium Isotopes on Voltage Gated Sodium Channel Activity in SH-SY5Y and IPSC Derived Cortical Neurons

Although lithium (Li) is a widely used treatment for bipolar disorder, its exact mechanisms of action remain elusive. Research has shown that the two stable Li isotopes, which differ in their mass and nuclear spin, can induce distinct effects in both in vivo and in vitro studies. Since sodium (Na+) channels are the primary pathway for Li+ entry into cells, we examined how Li+ affects the current of Na+ channels using whole-cell patch-clamp techniques on SH-SY5Y neuroblastoma cells and human iPSC-derived cortical neurons. Our findings indicate that mammalian Na+ channels in both neuronal models studied here display no selectivity between Na+ and Li+, unlike previously reported bacterial Na+ channels. We observed differences between the two neuronal models in three measured parameters (Vhalf, Gmax,z). We saw no statistically significant differences between any ions in SHSY-5Y cells, but small differences in the half-maximum activation potential (Vhalf) between Na+ and 6Li+ and between 7Li+ and 6Li+ were found in iPSC-derived cortical neurons. Although Na+ channels are widely expressed and important in neuronal function, the very small differences observed in this work suggest that Li+ regulation through Na+ channels is likely not the primary mechanism underlying Li+ isotope differentiation.

neuroscience↗

Contact mode high-speed AFM of phase separated lipid bilayers to study amyloid-β interactions

Cellular membranes are an essential feature of life, the composition and structure of which is important in governing cellular processes and is linked to multiple disorders. Of particular interest is the role that the lipid membrane plays in amyloidogenic diseases such as Alzheimers disease (AD), including the role of lipid composition and cholesterol in mediating amyloid toxicity. To mimic neuronal membranes, we used 3-component (DPPC/DOPC/Chol) and 5-component (DPPC/POPC/Chol/sphingomyelin/GM1) model membranes. Atomic force microscopy (AFM) is a key tool in studying the structures of lipid membranes and their interactions with amyloid. Recent advances in contact mode high-speed AFM (HS-AFM) have made it possible to capture dynamic processes at video rate. We used a unique custom-built contact mode HS-AFM to image model lipid membranes and study amyloid-{beta} interactions in liquid. We demonstrate the advantage of using HS-AFM coupled with spatiotemporal variability analysis to capture the dynamic interaction of A{beta} 1-42 monomers and oligomers with phase separated lipid bilayers to elucidate the role of nanoscale domains in amyloid-membrane interactions. We show that amyloid oligomer complexes induce greater dynamic instability than monomers, and that low cholesterol membranes are more susceptible to destabilization. Overall, we demonstrate the advantage of HS-AFM to image biological processes on biologically relevant soft samples and discuss tip-sample interactions at high-speed operation in contact mode on lipid membrane models in liquid environment. Graphical Abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=62 SRC="FIGDIR/small/633021v2_ufig1.gif" ALT="Figure 1"> View larger version (26K): org.highwire.dtl.DTLVardef@8a7da2org.highwire.dtl.DTLVardef@3e39d5org.highwire.dtl.DTLVardef@1470050org.highwire.dtl.DTLVardef@658f19_HPS_FORMAT_FIGEXP M_FIG C_FIG

biophysics↗

Melatonin alters fluid phase co-existence in POPC/DPPC/cholesterol membranes

The structure and biophysical properties of lipid biomembranes are important for normal function of plasma and organelle membranes, which is essential for proper functioning of living cells. In Alzheimers disease (AD) the structure of neuronal membranes becomes compromised by the toxic effect of amyloid-{beta} (A{beta}) protein which accumulates at neuron synapses, resulting in membrane perforation and dysfunction, oxidative stress and cell death. Melatonin is an important pineal gland hormone that has been shown to be protective against A{beta} toxicity in cellular and animal studies, but the molecular mechanism of this protection is not well understood. It has been shown that melatonin can interact with model lipid membranes and alter the membrane biophysical properties, such as membrane molecular order and dynamics. This effect of melatonin has been previously studied in simple model bilayers with one or two lipid components, we consider a more complex ternary lipid mixture as our membrane model. In this study, we used 2H-NMR to investigate the effect of melatonin on lipid phase behaviour of a three-component model lipid membranes composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and cholesterol. We used deuterium labelled palmitoyl-d31 in POPC-d31 and DPPC-d62 separately, to probe the changes in hydrocarbon chain order as a function of temperature and varying concentrations of melatonin. We found that melatonin concentration influences phase separation in these ternary mixtures somewhat differently depending on whether POPC-d31 or DPPC-d62was used. At 5 mol% melatonin we observed phase separation in samples with POPC-d31, but not with DPPC-d62. However, at 10 mol% melatonin phase separation was observed in both samples with either POPC-d31 or DPPC-d62. These results indicate that melatonin can have a strong effect on membrane structure and physical properties, which may provide some clues to understanding how melatonin protects against A{beta}. SIGNIFICANCEMelatonin has been shown to be protective against A{beta} pathology in animal and cellular studies. Although the mechanism of this protection is not well-understood, melatonins membrane-active properties may be important in this regard. In this work solid-state deuterium nuclear magnetic resonance was used to study the effect of melatonin on the POPC/DPPC/cholesterol model membranes. Specifically, we showed that melatonin modifies lipid hydrocarbon chain order to promote phase separation. This knowledge helps to explain the role of melatonin in lipid domain formation and may provide a deeper understanding of the mechanism of melatonin neuroprotection in AD.

biophysics↗

C subunit of the ATP synthase is an amyloidogenic channel-forming peptide: possible implications in mitochondrial pathogenesis

The c subunit is an inner mitochondrial membrane (IMM) protein and is an integral part of the F0 complex of the ATP synthase. Under physiological conditions, this short 75 residue-long peptide folds into an -helical hairpin and forms oligomers spanning the lipid bilayer. In addition to its physiological role, the c subunit has been proposed as a key participant in stress-induced IMM permeabilization by the mechanism of calcium-induced permeability transition. However, the molecular mechanism of the c subunit participation in IMM permeabilization is not completely understood. Here we used fluorescence spectroscopy, atomic force microscopy and black lipid membrane methods to gain insights into the structural and functional properties of c subunit protein that make it relevant to mitochondrial toxicity. We discovered that c subunit is an amyloidogenic peptide that can spontaneously fold into {beta}-sheets and self-assemble into fibrils and oligomers. C subunit oligomers exhibited ion channel activity in lipid membranes. We propose that the toxic effects of c subunit might be linked to its amyloidogenic properties and are driven by mechanisms similar to those of neurodegenerative polypeptides such as A{beta} and -synuclein.

biophysics↗