Spindle oscillations are generated in the dorsal thalamus and modulated by the thalamic reticular nucleus

Spindle waves occur during the early stage of slow wave sleep and are thought to arise in the thalamic reticular nucleus (TRN), causing inhibitory postsynaptic potential spindle-like oscillations in the dorsal thalamus that are propagated to the cortex. We have found that thalamocortical neurons exhibit membrane oscillations that have spindle frequencies, consist of excitatory postsynaptic potentials, and co-occur with electroencephalographic spindles. TRN lesioning prolonged oscillations in the medial geniculate body (MGB) and auditory cortex (AC). Injection of GABA~A~ antagonist into the MGB decreased oscillation frequency, while injection of GABA~B~ antagonist increased spindle oscillations in the MGB and cortex. Thus, spindles originate in the dorsal thalamus and TRN inhibitory inputs modulate this process, with fast inhibition facilitating the internal frequency and slow inhibition limiting spindle occurrence

The Individual and Combined Effects of Deoxynivalenol and Aflatoxin B1 on Primary Hepatocytes of Cyprinus Carpio

Aflatoxin B1 (AFB1) and deoxynivalenol (DON) are important food-borne mycotoxins that have been implicated in animal and human health. In this study, individual and combinative effects of AFB1 and DON were tested in primary hepatocytes of Cyprinus carpio. The results indicated that the combinative effects of AFB1 and DON (0.01 μg/mL AFB1 and 0.25 μg/mL DON; 0.02 μg/mL AFB1 and 0.25 μg/mL DON; 0.02 μg/mL AFB1 and 0.5 μg/mL DON) were higher than that of individual mycotoxin (P < 0.05). The activity of AST, ALT and LDH in cell supernatant was higher than that of control group (P < 0.05) when the mycotoxins were exposed to primary hepatocytes for 4 h. The decreased cell number was observed in tested group by inverted light microscopy. The mitochondrial swelling, endoplasmic reticulum dilation and a lot of lipid droplets were observed in primary hepatocytes by transmission electron microscope. Therefore, this combination was classified as an additive response of the two mycotoxins

Amyloid-like aggregates of neuronal tau induced by formaldehyde promote apoptosis of neuronal cells

BACKGROUND: The microtubule associated protein tau is the principle component of neurofibrillar tangles, which are a characteristic marker in the pathology of Alzheimer's disease; similar lesions are also observed after chronic alcohol abuse. Formaldehyde is a common environmental contaminant and also a metabolite of methanol. Although many studies have been done on methanol and formaldehyde intoxication, none of these address the contribution of protein misfolding to the pathological mechanism, in particular the effect of formaldehyde on protein conformation and polymerization. RESULTS: We found that unlike the typical globular protein BSA, the natively-unfolded structure of human neuronal tau was induced to misfold and aggregate in the presence of ~0.01% formaldehyde, leading to formation of amyloid-like deposits that appeared as densely staining granules by electron microscopy and atomic force microscopy, and bound the amyloid-specific dyes thioflavin T and Congo Red. The amyloid-like aggregates of tau were found to induce apoptosis in the neurotypic cell line SH-SY5Y and in rat hippocampal cells, as observed by Hoechst 33258 staining, assay of caspase-3 activity, and flow cytometry using Annexin V and Propidium Iodide staining. Further experiments showed that Congo Red specifically attenuated the caspase-3 activity induced by amyloid-like deposits of tau. CONCLUSION: The results suggest that low concentrations of formaldehyde can induce human tau protein to form neurotoxic aggregates, which could play a role in the induction of tauopathies

{N,N-Dimethyl-N′-[phen­yl(2-pyrid­yl)methyl­ene]ethane-1,2-diamine-κ3 N,N′,N′′}dithio­cyanato-κN,κS-copper(II)

In the title complex, [Cu(NCS)2(C16H19N3)], the CuII atom is coordinated by a total of four N atoms; three from one tridentate Schiff base ligand and one from one of the NCS− ions. The S atom from the other NCS− ion completes the distorted square-pyramidal coordination

Bis(N′-benzoyl­pyridine-4-carbohydrazide)(1,10-phenanthroline)copper(II) dinitrate

In the title complex, [Cu(C13H11N3O2)2(C12H8N2)](NO3)2, the CuII atom (site symmetry 2) is coordinated by four N atoms from one 1,10-phenanthroline and two hydrazine ligands, respectively. The hydrazine ligands coordinate to the CuIIatom by a pyridine N atom. These four atoms form a slightly distorted square-planar N4 donor set. In the packing, two additional Cu⋯O inter­actions occur [Cu⋯O = 2.462 (2) Å], resulting in a typical Jahn–Teller-distorted octahedral environment around the Cu atom. N—H⋯O hydrogen bonds result in a three-dimensional network. The O atoms of the anion are disordered over two positions in a 0.68 (2):0.32 (2) ratio