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AIM: To investigate the effects of the compound ANBP on wound healing in diabetic rats and explore its mechanism of action. METHODS: Ninety male SD rats were randomly divided into blank, model, compound ANBP, Beifuxin, and nicotinamide mononucleotide (NMN) groups, with 16 rats in each group. Wound healing in each group was observed and samples were taken on days 3, 7 and 14 to analyze the wound healing rate. Local histopathological changes were observed using HE and Masson staining. The expressions of pyruvate dehydrogenase E1 subunit alpha 1 (PDHAl), citrate synthase (CS), isocitrate dehydrogenase (IDH1) and oxoglutarate dehydrogenase (OGDH) were detected through immunofluorescence and Western blot. The number and morphology of mitochondria in the wound tissue were observed using transmission electron microscopy. RESULTS: Histomorphological changes revealed significant improvement in diabetic wound healing in the blank and compound ANBP groups compared to that of the model group. The wound healing rates of the blank, compound ANBP, Beifuxin, and NMN groups were significantly increased on days 3, 7, and 14 (P<0. 01). Compared to the model group, granulation tissue generation was higher in the other groups, covering the wound defect and producing abundant collagen fibers. At 3, 7, and 14 days after intervention, the blank, compound ANBP, Beifuxin, and NMN groups showed significantly enhanced fluorescence intensities of TCA cycling-related enzymes PDHA1, CS, IDH1, and OGDH indicating increased expression of these enzymes. The levels of the TCA cycling-related enzymes were significantly increased (P<0. 01) in the compound ANBP, Beifuxin and NMN groups but were significantly decreased (P<0. 01) in the model group. An increase in the number and density of mitochondria and a decrease in the cavitation rate of mitochondria with improved morphology (P<0. 05) was observed in the group treated with compound ANBP. CONCLUSION: Compound ANBP may increase the number of mitochondria, improve mitochondrial morphology and function, upregulate the expression levels of PDHA1, CS, IDH1, and OGDH proteins, and accelerate the regeneration of wound granulation tissue, thus promoting the healing of diabetic wounds in rats. [ABSTRACT FROM AUTHOR]

Regulating the metal–support interaction is essential for obtaining highly efficient catalysts for the catalytic oxidation of volatile organic compounds (VOCs). In this work, CuO-TiO2(coll) and CuO/TiO2(imp) with different metal–support interactions were prepared via colloidal and impregnation methods, respectively. The results demonstrated that CuO/TiO2(imp) has higher low-temperature catalytic activity, with a 50% removal of toluene at 170 °C compared to CuO-TiO2(coll). Additionally, the normalized reaction rate (6.4 × 10−6 mol·g−1·s−1) at 160 °C over CuO/TiO2(imp) was almost four-fold higher than that over CuO-TiO2(coll) (1.5 × 10−6 mol·g−1·s−1), and the apparent activation energy value (27.9 ± 2.9 kJ·mol−1) was lower. Systematic structure and surface analysis results disclosed that abundant Cu2+ active species and numerous small CuO particles were presented over CuO/TiO2(imp). Owing to the weak interaction of CuO and TiO2 in this optimized catalyst, the concentration of reducible oxygen species associated with the superior redox property could be enhanced, thus significantly contributing to its low-temperature catalytic activity for toluene oxidation. This work is helpful in exploring the influence of metal–support interaction on the catalytic oxidation of VOCs and developing low-temperature catalysts for VOCs catalytic oxidation. [ABSTRACT FROM AUTHOR]

The development of superior low-temperature catalytic performance and inexpensive catalysts for the removal of volatile organic compounds (VOCs) is crucial for their industrial application. Herein, CuO/Ce0.6Zr0.4O2 catalysts calcinated at different temperatures (Cu/CZ-X, X represented calcination temperature) were prepared and used to eliminate toluene. It can be found that Cu/CZ-550 presented the highest low-temperature catalytic activity, with the lowest temperature (220 °C) 50% conversion of toluene, the highest normalized reaction rate (3.1 × 10−5 mol·g−1·s−1 at 180 °C) and the lowest apparent activation energy value (86.3 ± 4.7 kJ·mol−1). Systematically, the surface properties analysis results showed that the optimum redox property, abundant oxygen vacancies, and plentiful surface Ce3+ species over Cu/CZ-550 were associated with the strong interaction between Cu and support could significantly favor the adsorption and activation of toluene, thus resulting in its superior catalytic performance. [ABSTRACT FROM AUTHOR]

Background: The association between S100 calcium-binding protein A8 (S100A8) and angiogenesis has been reported in previous reports. This study focuses on the roles of S100A8 in the angiogenesis of human dermal microvascular endothelial cells (HDMECs) and in cutaneous wound healing in mice., Methods: Candidate genes related to angiogenesis activity were screened using a GSE83582 dataset. The overexpression DNA plasmid of S100A8 was transfected into HDMECs to analyze its effect on cell proliferation, migration, and angiogenesis. Full-thickness skin wounds were induced on mice, followed by adenovirus treatments to analyze the function of gene alteration in wound healing and pathological changes. The upstream regulator of S100A8 was predicted by bioinformatics analysis and verified by luciferase and immunoprecipitation assays. The role of the forkhead box A1 (FOXA1)-S100A8 interaction in p38 MAPK activation and angiogenesis were validated by rescue experiments., Results: S100A8 was identified as a gene significantly correlated with angiogenesis. The S100A8 upregulation promoted the proliferation, migration, and angiogenesis of HDMECs, and it promoted p38 MAPK phosphorylation. Treatment of SB203580, a p38 MAPK inhibitor, blocked the promoting effect of S100A8. FOXA1 was identified as an upstream factor of S100A8 promoting its transcription. FOXA1 overexpression in HDMECs increased p38 MAPK phosphorylation and enhanced the activity of cells, which were blocked by the S100A8 inhibition. Similar results were reproduced in vivo where FOXA1 overexpression accelerated whereas the S100A8 knockdown retarded the cutaneous wound healing in mice., Conclusion: FOXA1 mediates the phosphorylation of p38 MAPK through transcription activation of S100A8, thereby inducing angiogenesis and promoting cutaneous wound healing.