Work-related health problems among resident immigrant workers in Italy and Spain

Background: in both Spain and Italy the number of immigrants has strongly increased in the last 20 years, currently representing more than the 10% of workforce in each country. The segregation of immigrants into unskilled or risky jobs brings negative consequences for their health. The objective of this study is to compare prevalence of work-related health problems between immigrants and native workers in Italy and Spain. Methods: data come from the Italian Labour Force Survey (n=65 779) and Spanish Working Conditions Survey (n=11 019), both conducted in 2007. We analyzed merged datasets to evaluate whether interviewees, both natives and migrants, judge their health being affected by their work conditions and, if so, which specific diseases. For migrants, we considered those coming from countries with a value of the Human Development Index lower than 0.85. Logistic regression models were used, including gender, age, and education as adjusting factors. Results: migrants reported skin diseases (Mantel-Haenszel pooled OR=1.49; 95%CI: 0.59-3.74) and musculoskeletal problems among those employed in agricultural sector (Mantel-Haenszel pooled OR=1.16; 95%CI: 0.69-1.96) more frequently than natives; country-specific analysis showed higher risks of musculoskeletal problems among migrants compared to the non-migrant population in Italy (OR=1.17; 95% CI: 0.48-1.59) and of respiratory problems in Spain (OR=2.02; 95%CI: 1.02-4.0). In both countries the risk of psychological stress was predominant among national workers. Conclusions: this collaborative study allows to strength the evidence concerning the health of migrant workers in Southern European countries.

Muscle-Type Nicotinic Receptor Blockade by Diethylamine, the Hydrophilic Moiety of Lidocaine

Lidocaine bears in its structure both an aromatic ring and a terminal amine, which can be protonated at physiological pH, linked by an amide group. Since lidocaine causes multiple inhibitory actions on nicotinic acetylcholine receptors (nAChRs), this work was aimed to determine the inhibitory effects of diethylamine (DEA), a small molecule resembling the hydrophilic moiety of lidocaine, on Torpedo marmorata nAChRs microtransplanted to Xenopus oocytes. Similarly to lidocaine, DEA reversibly blocked acetylcholine-elicited currents (IACh) in a dose-dependent manner (IC50 close to 70 μM), but unlike lidocaine, DEA did not affect IACh desensitization. IACh inhibition by DEA was more pronounced at negative potentials, suggesting an open-channel blockade of nAChRs, although roughly 30% inhibition persisted at positive potentials, indicating additional binding sites outside the pore. DEA block of nAChRs in the resting state (closed channel) was confirmed by the enhanced IACh inhibition when pre-applying DEA before its co-application with ACh, as compared with solely DEA and ACh co-application. Virtual docking assays provide a plausible explanation to the experimental observations in terms of the involvement of different sets of drug binding sites. So, at the nAChR transmembrane (TM) domain, DEA and lidocaine shared binding sites within the channel pore, giving support to their open-channel blockade; besides, lidocaine, but not DEA, interacted with residues at cavities among the M1, M2, M3, and M4 segments of each subunit and also at intersubunit crevices. At the extracellular (EC) domain, DEA and lidocaine binding sites were broadly distributed, which aids to explain the closed channel blockade observed. Interestingly, some DEA clusters were located at the α-γ interphase of the EC domain, in a cavity near the orthosteric binding site pocket; by contrast, lidocaine contacted with all α-subunit loops conforming the ACh binding site, both in α-γ and α-δ and interphases, likely because of its larger size. Together, these results indicate that DEA mimics some, but not all, inhibitory actions of lidocaine on nAChRs and that even this small polar molecule acts by different mechanisms on this receptor. The presented results contribute to a better understanding of the structural determinants of nAChR modulation.