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1.
Environ Sci Pollut Res Int ; 29(11): 16758-16761, 2022 Mar.
Article in English | MEDLINE | ID: mdl-35025042

ABSTRACT

This study gives a depiction of what are the general directions taken by international institutions so to tackle the current health emergency and the most pressing environmental issues, such as climate change and COVID-19 (Schaltegger, 2020; Adebayo et al., 2021).The role of companies is crucial under disruptive events, such as a crisis or, more in line with the present time, a pandemic, and the pursue of the shareholder value cannot be the essence and the only objective in doing business anymore, since also ESG (i.e., environmental, social, and governance) dynamics have to be taken in due consideration. Moreover, an adequate and effective corporate governance should lead to higher disclosure quality, which subsequently should help protect the entire planet and ecosystems as well. In this context, the principal role of accounting and corporate reporting activities should be oriented towards making emerge what is and what is not done by companies in their business operations, and the disclosure of financial information is currently deemed inappropriate for pursuing a sustainable growth in the medium and long run (Schaltegger, J Account Org Change 16:613-619, 2020; Kirikkaleli & Adebayo, Sustain Dev 29:583-594, 2020; Tettamanzi, Venturini & Murgolo Wider corporate reporting: La possibile evoluzione della Relazione sulla Gestione Bilancio e Revisione, IPSOA - Wolters Kluwer, Philadelphia, 2021). Thus, the objective of this study is to investigate what international and European institutions have planned to do in order to align corporate objectives with environmental and societal needs in the coming years (Biondi et al., Meditari Account Res 28:889-914, 2020; Songini L et al. Integrated reporting quality and BoD characteristics: an empirical analysis. J Manag Govern, 2021).As of today, our analysis finds that IFRS Foundation (at global level) and EFRAG (at European one) have been taking steps toward the aforementioned issues so to propose disclosure standards more in line with sustainability and environmental needed improvements. In fact, we tried to give a depiction of what are the actual and future strategies that both these institutions are going to put in place: this snapshot will give scientists, engineers, lawyers, and business people an overview of what should be like the corporate world of the near future, from a corporate reporting/accounting perspective (so to better understand what will be expected from companies of all the industries worldwide).


Subject(s)
Ecosystem , Industry , Sustainable Growth
2.
J Comp Neurol ; 520(2): 364-83, 2012 Feb 01.
Article in English | MEDLINE | ID: mdl-21800313

ABSTRACT

Nitric oxide synthase (NOS) has been characterized in several opistobranchs and pulmonates but it was much less investigated in prosobranchs, which include more than 20,000 species and account for most of the gastropod diversity. Therefore, new data from this large group are needed for a better knowledge of the molecular evolution of NOS enzymes in molluscs. This study focused on NOS expressed in the nervous system of the prosobranch neogastropod Stramonita haemastoma. In this study we report compelling evidence on the expression of a constitutive Ca(2+) /CaM-dependent neuronal NOS in the central and peripheral nervous system. The prevailing neuronal localization of NADPHd activity was demonstrated by NADPHd histochemistry in both central and peripheral nervous system structures. L-arginine/citrulline assays suggested that Stramonita NOS is a constitutive enzyme which is both cytosolic and membrane-bound. Molecular cloning of the full-length Stramonita NOS (Sh-NOS) by reverse-transcription polymerase chain reaction (RT-PCR) followed by 5' and 3' RACE showed that Sh-NOS is a protein of 1,517 amino acids, containing a PDZ domain at the N-terminus and sharing similar regulatory domains to the mammalian neuronal NOS (nNOS). Regional expression of the Sh-NOS gene was evaluated by RT-PCR. This analysis showed different expression levels in the nerve ring, the osphradium, the cephalic tentacles, the buccal tissues, and the foot, whereas NOS expression was not found in the salivary glands and the gland of Leiblein. The present data provide a solid background for further studies addressing the specific functions of NO in neogastropods.


Subject(s)
Central Nervous System/anatomy & histology , Central Nervous System/enzymology , Gastropoda/anatomy & histology , Gastropoda/enzymology , Nitric Oxide Synthase/metabolism , Amino Acid Sequence , Animals , Enzyme Inhibitors/metabolism , Ganglia, Invertebrate/anatomy & histology , Humans , Molecular Sequence Data , NADPH Dehydrogenase/metabolism , Neurons/cytology , Neurons/enzymology , Nitric Oxide/metabolism , Nitric Oxide Synthase/classification , Nitric Oxide Synthase/genetics , Phylogeny , Sequence Alignment , Tissue Distribution
3.
Nitric Oxide ; 23(2): 94-100, 2010 Sep 15.
Article in English | MEDLINE | ID: mdl-20638951

ABSTRACT

The presence of nitric oxide (NO) pathway has been well demonstrated in the main invertebrate groups, showing parallel findings on the role of NO in vertebrates and invertebrates. Noteworthy is the example of the role played by the nitrergic pathway in the sensorial functions, mainly in olfactory-like systems. On the other hand, the emerging molecular information about NOSs from lower metazoans (Porifera, cnidarians up to higher invertebrates) suggests that NO pathways might represent examples of a parallel evolution of the NOS prototypes in different animal lineages. Nevertheless, increasing evidence suggests that NO is one of the earliest and most widespread signaling molecules in living organisms. Here, we attempt to provide a survey of current knowledge of the synthesis and possible roles of NO and the related signaling pathway in lower metazoans (i.e., Porifera and Cnidaria), two phyla forming a crucial bridge spanning the evolutionary gap between the protozoans and higher metazoans. From the literature data here reported, it emerges that future research on the biological roles of NO in basal metazoans is likely to be very important for understanding the evolution of signaling systems.


Subject(s)
Cnidaria/metabolism , Cyclic GMP/metabolism , Nitric Oxide/metabolism , Porifera/metabolism , Animals , Cnidaria/genetics , Cyclic GMP/chemistry , Evolution, Molecular , Hydra/genetics , Hydra/metabolism , Nitric Oxide/chemistry , Porifera/genetics
4.
Nitric Oxide ; 21(3-4): 164-70, 2009.
Article in English | MEDLINE | ID: mdl-19635580

ABSTRACT

Recent data have shown that a functional NO-cGMP signalling system plays an important role during development and seems to be operative early during the differentiation of embryonic stem cells. The intriguing possibility exists that this role can be evolutionarily conserved between vertebrates and invertebrates. In this paper, we have analyzed the effect of NO-cGMP pathway on the regeneration process in Hydra vulgaris, the most primitive invertebrate possessing a nervous system. Our results indicate that NO production increased during Hydra regeneration. The NOS inhibitor L-NAME reduced the regenerative process and the same effect was obtained by treatment with either the specific guanylate cyclase inhibitor ODQ or the protein kinase G (PKG) inhibitor KT-5823. In contrast, the regeneration process was increased by treating decapitated Hydra with the NO donor NOC-18. Furthermore, we found that cell proliferation was also increased by treating decapitated Hydra with the NO donor NOC-18 and reduced by treatment with the NOS inhibitor L-NAME. Our results strongly suggest that the NO-cGMP-PKG pathway is involved in the control of the proliferative-differentiative patterns of developing and regenerating structures in cnidarians as well as bilaterians.


Subject(s)
Hydra/physiology , Nitric Oxide/physiology , Regeneration , Animals , Carbazoles/pharmacology , Cyclic GMP-Dependent Protein Kinases/antagonists & inhibitors , Enzyme Inhibitors/pharmacology , Head , Hydra/drug effects , Hydra/enzymology , NG-Nitroarginine Methyl Ester/pharmacology , Nitric Oxide/biosynthesis , Nitric Oxide Donors/pharmacology , Nitric Oxide Synthase/antagonists & inhibitors , Nitric Oxide Synthase/metabolism , Nitroso Compounds/pharmacology
5.
Int J Radiat Oncol Biol Phys ; 72(2): 562-7, 2008 Oct 01.
Article in English | MEDLINE | ID: mdl-18793958

ABSTRACT

PURPOSE: Boron neutron capture therapy (BNCT) is a radiotherapeutic modality based on (10)B(n,alpha)(7)Li reaction, for the treatment of malignant gliomas. One of the main limitations for BNCT effectiveness is the insufficient intake of (10)B nuclei in the tumor cells. This work was aimed at investigating the use of L-DOPA as a putative enhancer for (10)B-drug 4-dihydroxy-borylphenylalanine (BPA) uptake in the C6-glioma model. The investigation was first performed in vitro and then extended to the animal model. METHODS AND MATERIALS: BPA accumulation in C6-glioma cells was assessed using radiowave dielectric spectroscopy, with and without L-DOPA preloading. Two L-DOPA incubation times (2 and 4 hours) were investigated, and the corresponding effects on BPA accumulation were quantified. C6-glioma cells were also implanted in the brain of 32 rats, and tumor growth was monitored by magnetic resonance imaging. Rats were assigned to two experimental branches: (1) BPA administration; (2) BPA administration after pretreatment with L-DOPA. All animals were sacrificed, and assessments of BPA concentrations in tumor tissue, normal brain, and blood samples were performed using high-performance liquid chromatography. RESULTS: L-DOPA preloading induced a massive increase of BPA concentration in C6-glioma cells only after a 4-hour incubation. In the animal model, L-DOPA pretreatment produced a significantly higher accumulation of BPA in tumor tissue but not in normal brain and blood samples. CONCLUSIONS: This study suggests the potential use of L-DOPA as enhancer for BPA accumulation in malignant gliomas eligible for BNCT. L-DOPA preloading effect is discussed in terms of membrane transport mechanisms.


Subject(s)
Boron Compounds/pharmacokinetics , Boron Neutron Capture Therapy/methods , Brain Neoplasms/metabolism , Dopamine Agents/administration & dosage , Glioma/metabolism , Levodopa/administration & dosage , Phenylalanine/analogs & derivatives , Animals , Boron Compounds/blood , Boron Compounds/therapeutic use , Brain/metabolism , Brain Neoplasms/blood , Brain Neoplasms/radiotherapy , Dopamine Agents/pharmacology , Glioma/blood , Glioma/radiotherapy , Levodopa/pharmacology , Male , Phenylalanine/blood , Phenylalanine/pharmacokinetics , Phenylalanine/therapeutic use , Rats
6.
Mech Ageing Dev ; 127(6): 544-51, 2006 Jun.
Article in English | MEDLINE | ID: mdl-16530251

ABSTRACT

We present here a brief description of the relationships among metals, nitric oxide metabolism, and ageing. In particular, we will discuss the interactions occurring between redox (copper, iron) and non-redox (zinc) metals and nitric oxide, the metal- and nitric oxide-catalyzed formation of thiol adducts (nitrosothiols, mixed disulphides) and the possible involvement of these species in the ageing process.


Subject(s)
Aging/metabolism , Metals, Heavy/metabolism , Nitric Oxide/metabolism , Aged , Animals , Glutathione/metabolism , Humans , Nitroso Compounds/metabolism , Oxidation-Reduction , Sulfhydryl Compounds/metabolism
7.
Neurosci Lett ; 384(3): 254-9, 2005 Aug 26.
Article in English | MEDLINE | ID: mdl-15923083

ABSTRACT

Nitric oxide (NO) regulates key aspects of cell metabolism through reversible inhibition of cytochrome c oxidase (CcOX), the terminal electron acceptor (complex IV) of the mitochondrial respiratory chain, in competition with oxygen. Recently, a constitutive mitochondrial NOS corresponding to a neuronal NOS-I isoform (mtNOS-I) has been identified in several tissues. The role of this enzyme might be to generate NO close enough to its target without a significant overall increase in cellular NO concentrations. An effective, selective, and specific NO action might be guaranteed further by a physical interaction between mtNOS-I and CcOX. This possibility has never been investigated. Here we demonstrate that mtNOS-I is associated with CcOX, as proven by electron microscopic immunolocalization and co-immunoprecipitation studies. By affinity chromatography, we found that association is due to physical interaction of mtNOS-I with the C-terminal peptide of the Va subunit of CcOX, which displays a consensus sequence for binding to the PDZ domain of mtNOS-I previously unreported for CcOX. The molecular details of the interaction have been analyzed by means of molecular modeling and molecular dynamics simulations. This is the first evidence of a protein-protein interaction mediated by PDZ domains involving CcOX.


Subject(s)
Cerebellar Cortex/metabolism , Electron Transport Complex IV/metabolism , Mitochondria/enzymology , Models, Molecular , Nerve Tissue Proteins/metabolism , Neurons/metabolism , Nitric Oxide Synthase/metabolism , Protein Interaction Mapping/methods , Animals , Cerebellar Cortex/ultrastructure , Computer Simulation , Female , Male , Mice , Mitochondria/ultrastructure , Nerve Tissue Proteins/ultrastructure , Neurons/ultrastructure , Nitric Oxide Synthase/ultrastructure , Nitric Oxide Synthase Type I , Protein Binding , Tissue Distribution
8.
Brain Behav Evol ; 62(1): 43-55, 2003.
Article in English | MEDLINE | ID: mdl-12907859

ABSTRACT

In the present study, we have analyzed the expression of nitric oxide synthase (NOS) in the preoptic-hypothalamo-hypophyseal system of the teleost Oreochromis niloticus. The assay for enzyme activity demonstrated that a constitutive NOS activity is present both in soluble and particulate fractions of the homogenates of diencephalons. Western blot analysis using an antibody against the N-terminus of human nNOS revealed two bands both in the supernatant and in the pellet. One band co-migrates at approximately 150 kDa with that detected in the rat cerebellum homogenates and presumably corresponds to neuronal NOS (nNOS) of mammals. The additional band, which migrates at approximately 180 kDa, might be attributed to an alternatively spliced nNOS isoform. Using NADPH diaphorase (NADPHd) histochemistry in combination with NOS immunohistochemistry, nNOS expression has been detected in preoptic nuclei, hypophysiotrophic nuclei of the ventral hypothalamus, and the pituitary gland. Various degrees of dissociation of NADPHd activity and nNOS immunoreactivity have been detected that could be attributed to the expression of different subtypes of nNOS in the preoptic/hypothalamo/hypophysial system of tilapia. In this paper, we also investigated the colocalization of nNOS with arginine-vasotocin (AVT) by means of immunolabeling of consecutive sections. Results suggest that NO may be colocalized with AVT in a subpopulation of neurosecretory neurons. Present findings suggest that nitric oxide (NO) is implicated in the modulation of hormone release in teleosts in a similar way to mammals.


Subject(s)
Hypothalamo-Hypophyseal System/enzymology , Nitric Oxide Synthase/metabolism , Pituitary-Adrenal System/enzymology , Preoptic Area/enzymology , Animals , Blotting, Western/methods , Cerebellum/metabolism , Electric Fish , Fixatives/metabolism , Hypothalamo-Hypophyseal System/cytology , Immunohistochemistry/methods , Kinetics , NADPH Dehydrogenase/metabolism , Nitric Oxide Synthase Type I , Pituitary-Adrenal System/cytology , Pituitary-Adrenal System/metabolism , Preoptic Area/cytology , Preoptic Area/metabolism , Subcellular Fractions/metabolism , Time Factors , Vasotocin/metabolism
9.
Antimicrob Agents Chemother ; 47(7): 2303-6, 2003 Jul.
Article in English | MEDLINE | ID: mdl-12821483

ABSTRACT

The activity of NCX 972, a new molecule obtained by adding a nitric oxide (NO) moiety to metronidazole, was tested against six isolates of Entamoeba histolytica in xenic cultures. NCX 972 released NO into trophozoite cells and enhanced killing of amoebas in a dose- and time-dependent manner compared to metronidazole.


Subject(s)
Antitrichomonal Agents/pharmacology , Entamoeba histolytica/drug effects , Metronidazole/pharmacology , Nitric Oxide/chemistry , Animals , Antitrichomonal Agents/chemistry , Dose-Response Relationship, Drug , Drug Design , In Vitro Techniques , Metronidazole/chemistry
10.
FASEB J ; 16(14): 1970-2, 2002 Dec.
Article in English | MEDLINE | ID: mdl-12397094

ABSTRACT

The amyloid peptides Abeta1-42 and Abeta25-35 strongly inhibited the activity of constitutive neuronal and endothelial nitric oxide synthases (i.e., NOS-I and NOS-III, respectively) in cell-free assays. The molecular mechanism of NOS inhibition by Ab fragments was studied in detail with Abeta25-35. The inhibitory ability was mostly NADPH-dependent and specific for the soluble form of Abeta25-35. Optical, fluorescence, and NMR spectroscopy showed that the soluble, but not aggregated, Abeta25-35 interacted with NADPH, thus suggesting that a direct recruitment of NADPH may result in diminished availability of the redox cofactor for NOS functioning. To assess the physiological relevance of our findings, rat neuronal-like PC12 and glioma C6 cell lines were used as cellular models. After Abeta25-35 internalization into cells was verified, the activity of constitutive NOS was measured using the DAF-2DA detection system and found to be severely impaired upon Abeta25-35 uptake. Consistent with previous results on the molecular cross-talk between NOS isoforms, repression of constitutive NOS by Abeta25-35 resulted in enhanced expression of inducible NOS (NOS-II) mRNA in C6 cells. Our results represent the first evidence that amyloid fragments impair constitutive NOS activity in cell-free and cellular systems, providing a possible molecular mechanism for the onset and/or maintenance of Alzheimer's disease.


Subject(s)
Amyloid beta-Peptides/pharmacology , Enzyme Inhibitors/pharmacology , NADP/pharmacology , Nitric Oxide Synthase/metabolism , Amyloid beta-Peptides/chemistry , Amyloid beta-Peptides/metabolism , Animals , Magnetic Resonance Spectroscopy , Models, Biological , NADP/chemistry , Neuroglia/enzymology , Nitric Oxide Synthase/biosynthesis , Nitric Oxide Synthase/genetics , Nitric Oxide Synthase Type I , Nitric Oxide Synthase Type II , Nitric Oxide Synthase Type III , PC12 Cells , Peptide Fragments/chemistry , Peptide Fragments/metabolism , Peptide Fragments/pharmacology , RNA, Messenger/biosynthesis , Rats , Spectrometry, Fluorescence , Tumor Cells, Cultured
11.
Eur J Biochem ; 269(3): 884-92, 2002 Feb.
Article in English | MEDLINE | ID: mdl-11846789

ABSTRACT

The product of agmatine oxidation catalyzed by Pisum sativum L. copper amine oxidase has been identified by means of one- and two-dimensional (1)H-NMR spectroscopy to be N-amidino-2-hydroxypyrrolidine. This compound inhibits competitively rat nitric oxide synthase type I and type II (NOS-I and NOS-II, respectively) and bovine trypsin (trypsin) activity, values of Ki being (1.1 +/- 0.1) x 10(-5) m (at pH 7.5 and 37.0 degrees C), (2.1 +/- 0.1) x 10(-5) m (at pH 7.5 and 37.0 degrees C), and (8.9 +/- 0.4) x 10(-5) m (at pH 6.8 and 21.0 degrees C), respectively. Remarkably, the affinity of N-amidino-2-hydroxypyrrolidine for NOS-I, NOS-II and trypsin is significantly higher than that observed for agmatine and clonidine binding. Furthermore, N-amidino-2-hydroxypyrrolidine and agmatine are more efficient than clonidine in displacing [(3)H]clonidine (= 1.0 x 10(-8) m) from specific binding sites in heart rat membranes, values of IC50 being (1.3 +/- 0.4) x 10(-9) m and (2.2 +/- 0.4) x 10(-8) m, respectively (at pH 7.4 and 37.0 degrees C).


Subject(s)
Agmatine/metabolism , Amine Oxidase (Copper-Containing)/metabolism , Pyrrolidines/metabolism , Agmatine/chemistry , Agmatine/pharmacology , Animals , Binding, Competitive , Clonidine/metabolism , Clonidine/pharmacology , Humans , Imidazoline Receptors , Inhibitory Concentration 50 , Magnetic Resonance Spectroscopy , Male , Membranes/drug effects , Membranes/metabolism , Models, Molecular , Nitric Oxide Synthase/antagonists & inhibitors , Nitric Oxide Synthase/chemistry , Nitric Oxide Synthase/metabolism , Nitric Oxide Synthase Type I , Nitric Oxide Synthase Type II , Oxidation-Reduction , Pisum sativum/enzymology , Pyrrolidines/chemistry , Rats , Rats, Wistar , Receptors, Drug/metabolism , Trypsin/chemistry , Trypsin/drug effects , Trypsin/metabolism
12.
Int J Mol Med ; 9(2): 131-4, 2002 Feb.
Article in English | MEDLINE | ID: mdl-11786922

ABSTRACT

Nitric oxide (NO) has emerged as an important cytotoxic and cytostatic effector for a number of pathogens, including viruses, bacteria, fungi, and parasites. When the microbicidal effect of NO occurs, the NO-mediated S-nitrosylation of cysteine containing proteins (e.g., cysteine proteases) appears to be a common and widespread mechanism. This overview concerns parasitic cysteine proteases as NO targets, providing molecular bases for the parasiticidal effect of NO.


Subject(s)
Antiparasitic Agents/chemistry , Antiparasitic Agents/metabolism , Nitric Oxide/chemistry , Nitric Oxide/metabolism , Parasites/metabolism , Animals , Cysteine/metabolism , Cysteine Endopeptidases/chemistry , Cysteine Endopeptidases/metabolism , Humans , Models, Molecular , Nitric Oxide Donors/metabolism , Parasites/enzymology , Protein Conformation , Protozoan Proteins
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