Ag/ZnO/PMMA nanocomposites for efficient water reuse

This work attempts to produce photocatalytic surfaces for large-scale applications by depositing nanostructured coatings on polymeric substrates. ZnO/poly(methyl methacrylate) (PMMA) composites were prepared by low-temperature atomic layer deposition (ALD) of ZnO on PMMA substrates. In addition, to increase the photocatalytic and antibacterial activities of ZnO films, Ag nanoparticles were added on ZnO surfaces using plasma-enhanced ALD. The morphology, crystallinity, and chemical composition of the specimens were meticulously examined by scanning and transmission electron microscopies, energy-dispersive X-ray spectroscopy, and X-ray diffraction analyses. The noteworthy photocatalytic activity of the nanocomposites was proved by the degradation of the following organic pollutants in aqueous solution: methylene blue, paracetamol, and sodium lauryl sulfate. The antibacterial properties of the samples were tested using Escherichia coli as a model organism. Moreover, the possible toxic effects of the specimens were checked by biological tests. The present results unambiguously indicate the Ag/ZnO/PMMA nanocomposite as a powerful tool for an advanced wastewater treatment technology.peer-reviewe

Monoamine oxidase A and B activities in embryonic chick hepatocytes: differential regulation by retinoic acid

Monoamine oxidases (MAOs) A and B are two isoenzymes involved in the degradation of many biological amines in the nervous system and in peripheral organs. In the present work hepatocytes isolated from 14-day-old chick embryos were used as a model system to determine whether retinoic acid (RA) is capable of modulating the activity of the two MAO forms. RA is a retinoid that, by binding with nuclear receptors, interferes with the expression of specific genes in many differentiation processes. Enzymic activity was measured with a radiochemical method using serotonin and beta-phenylethylamine as preferential substrates for MAO A and MAO B, respectively. The specific activity of the two forms was measured in hepatocytes cultured for 24, 48 and 72 h in the presence and the absence of serum. RA stimulated MAO B but not MAO A activity, in a dose- and time-dependent way, and only in the presence of serum. Maximum stimulation (about 3.5-fold) was obtained after treatment with 5 mum RA for 72 h. Kinetic analysis of MAO B activity showed an increase in V-max in treated hepatocytes (5 muM RA for 72 h) with no change in K-m. In conclusion, the present work shows that RA selectively elicits MAO B activity in cultured chick embryonic hepatocytes, this stimulation requires the presence of some factors present in the serum and is probably due to an increase in the number of enzyme molecules. Copyright (C) 2001 John Wiley Sons, Ltd

Molecular characterization of monoamine oxidase in zebrafish (Danio rerio)

Monoamine oxidase (MAO) is responsible for the degradation of a number of neurotransmitters and other biogenic amines. In terrestrial vertebrates, two forms of the enzyme, named MAO A and B, were found in which mammals are coded by two similar but distinct genes. In teleosts, the biochemical data obtained so far indicate that enzyme activity is due to a single form, whose sequence, obtained for trout, displays 70% identity with mammal MAO A and B. In this paper, we carried out an investigation of zebrafish MAO (Z-MAO) to shed further light on the nature of the MAO form present in aquatic vertebrates. Sequencing studies have revealed an open reading frame 522-amino-acids long with MW 58.7 kDa, displaying 84% identity with trout MAO and about 70% identity with mammal MAO A and MAO B. Analysis of the sequence and of the predicted secondary structure shows that also in Z-MAO principal domains characterizing the MAOs are present. The domain linking the FAD is very well conserved, while the transmembrane domain sequence linking the enzyme to the external mitochondrial membrane does not appear to be conserved even with respect to trout MAO. Comparison with the amino acids which, according to the human MAO B and rat MAO A models, line the substrate-binding site shows that in Z-MAO, several residues (V172, N173, F200, L327) differ from MAO B but are similar or identical to the corresponding ones present in rat MAO A, as well as in trout MAO. A three-dimensional model is reported of the substrate-binding site of Z-MAO obtained by comparative modeling. Our observations support the hypothesis that the MAO form present in aquatic vertebrates is a MAO A-like form. Experiments performed to test the effect of selective MAO A (clorgyline) and MAO B (deprenyl) inhibitors on the enzyme's activity in liver and brain confirm the presence of a single form of MAO in zebrafish. (C) 2004 Elsevier Inc. All rights reserved

Effect of Short-Time Exposures to Nickel and Lead on Brain Monoamine Oxidase from Danio rerio and Poecilia reticulata

The aim of this work was to verify, in two small size freshwater teleosts Danio rerio and Poecilia reticulata, the effects of short-time exposures (24 and 72 h) to a sublethal dose (500 mu g/L) of nickel and lead, on brain monoamine oxidase (MAO), an important neural enzyme. The 24-h treatment using both metals caused a strong reduction of MAO activity in D. rerio brain, whereas causing a slight MAO activity stimulation in P reticulata brain. The same treatment in both species did not affect the brain MAO mRNA production as showed by RT-PCR. Extending the duration of treatment as far as 72 h, partly (D. rerio) or completely (P. reticulata) reversed the metal effects on brain MAO activity suggesting that mechanisms to neutralize the metals had been activated. (C) 2008 Wiley Periodicals, Inc. Environ Toxicol 24: 309-313, 2009

Biologia dello Sviluppo

Il capitolo riguarda lo sviluppo del pesce zebra, sia sotto gli aspetti morfologici che molecolari