Corrigendum to “Adelmidrol, a palmitoylethanolamide analogue, as a new pharmacological treatment for the management of acute and chronic inflammation” [Biochem. Pharmacol. 119 (2016) 27–41, (S0006295216302611), (10.1016/j.bcp.2016.09.001)]

The [Formula presented]-Actin and A/C Lamin loading controls of the Western Blots shown in Fig.4A and 4B were erroneously inserted in the Fig.4. The correct loading controls are shown here below:[Formula presented] Figure 4: The effects of adelmidrol on CAR-induced nuclear NF-κBp65 translocation and IkB-α degradation, iNOS and COX-2 expressions. Representative western blots showing the effects of adelmidrol on IκB-α degradation (A), nuclear NF-κBp65 translocation (B), iNOS expression (C) and COX-2 expression (D) after CAR injection. Adelmidrol treatment reduced IκB-α degradation (A), nuclear NF-κBp65 translocation (B), iNOS (C) and COX-2 (D) expressions. Pretreatment with GW9662 was not able to reduce nuclear NF-κBp65 translocation, IκB-α degradation, iNOS and COX-2 expressions (A, B, C, D). The loading control for A, C, D ([Formula presented]-actin) is the same (see details in 2.7. section). A representative blot of lysates obtained from 20 animals/group is shown, and densitometry analysis of all animals is reported. The results in A, B C and D are expressed as means ± SD of 20 animals for each group. *p < 0.05 vs sham; **p < 0.01 vs sham, ***p < 0.01 vs sham, °p < 0.05 vs CAR; °°p < 0.01 vs CAR, °°°p < 0.01 vs CAR. 2.7 Western blots for IkB-α, COX-2, iNOS and nuclear NF-kBp65 Western blot analysis was performed as previously described [15]. The following primary antibodies were used: anti-IkB- α (Santa Cruz Biotechnology, 1:1000; D.B.A. s.r.l. Milan Italy), anti-NF-kBp65 (1:1000; Santa Cruz Biotechnology; D.B.A. s.r.l. Milan Italy), anti-COX-2 (1:500; Santa Cruz Biotechnology), anti-iNOS (1:500; Santa Cruz Biotechnology; D.B.A. s.r.l. Milan Italy) in 1 x PBS, 5 %. w/v non-fat dried milk, 0.1 % Tween-20 overnight at 4 °C. Anti-[Formula presented]-actin or anti-lamin A/C antibody (1:1000; Santa Cruz Biotechnology; D.B.A. s.r.l. Milan Italy) was used as internal control. The membranes were stripped by agitation with 2 % glycine, pH 2, blocked in 5 % non-fat dried milk/PBS for 1 h at RT and re-incubated several times with different antibodies to optimize the detection of the proteins minimizing the number of gels and transfers. For this reason, the loading control for the figure 4 A, C, D ([Formula presented]-actin) is the same. The relative expression of the protein bands of IkB- α (37 kDa), nuclear NF-kBp65 (65 kDa), iNOS (130 kDa), COX-2 (50 kDa) was detected with an enhanced chemiluminescence (ECL) system (Thermo, USA) and visualized with the Chemi Doc XRS (Bio-Rad, USA) and analyzed by using Image Lab 3.0 software (Bio-Rad, USA). The authors sincerely apologize for any inconvenience caused by this error and assure the readers of this article of their commitment to upholding the integrity and accuracy of their research findings. Daniela Impellizzeri: Data Curation, Writing- original draft, Methodology. Rosanna Di Paola: Data Curation, Writing- original draft. Marika Cordaro: Formal analysis, Methodology. Enrico Gugliandolo: Investigation, Methodology. Giovanna Casili: Investigation, Methodology. Valeria Maria Morittu: Formal analysis. Domenico Britti: Writing-review &editing. Emanuela Esposito: Conceptualizzation, Supervision. Salvatore Cuzzocrea: Conceptualizzation, Writing-review &editing, Supervision.