Background Osteoporosis is a widespread chronic disease characterized by low bone density. There is currently no gold standard treatment for osteoporosis. The aim of this study was to explore the role and mechanism of Astragaloside on osteogenic differentiation of MC3T3-E1 cells. Methods MC3T3-E1 cells were divided into control and different dose of Astragaloside (10, 20, 40, 50, and 60 μg/ml). Then, ALP and ARS staining were performed to identify the effects of Astragaloside for early and late osteogenic capacity of MC3T3-E1 cells, respectively. Real-time PCR and western blot were performed to assess the ALP, OCN, and OSX expression. PI3K/Akt signaling pathway molecules were then assessed by Western blot. Finally, PI3K inhibitor, LY294002, was implemented to assess the mechanism of Astragaloside in promoting osteogenic differentiation of MC3T3-E1 cells. Results Astragaloside significantly increased the cell viability than the control group. Moreover, Astragaloside enhanced the ALP activity and calcium deposition than the control groups. Compared with the control group, Astragaloside increased the ALP, OCN, and OSX expression in a dose-response manner. Western blot assay further confirmed the real-time PCR results. Astragaloside could significantly increase the p-PI3K and p-Akt expression than the control group. LY294002 partially reversed the promotion effects of Astragaloside on osteogenic differentiation of MC3T3-E1 cells. LY294002 partially reversed the promotion effects of Astragaloside on ALP, OCN, and OSX of MC3T3-E1 cells. Conclusion The present study suggested that Astragaloside promoted osteogenic differentiation of MC3T3-E1 cells through regulating PI3K/Akt signaling pathway.

Background. Diabetic retinopathy (DR) is a prevalent microvascular complication of diabetes, and the levels of chemerin were associated with the severity of DR. However, there is no research on chemerin in the development of proliferative diabetic retinopathy (PDR). Therefore, our study aimed to explore the relationship between chemerin and PDR. Methods. The levels of chemerin/chemokine-like receptor (CMKLR1), proinflammatory cytokines, and vascular endothelial growth factor (VEGF) in 90 cases of PDR and nonproliferative diabetic retinopathy (NPDR) patients and in high glucose (HG) stimulated human retinal pigment epithelium cells (ARPE-19) were evaluated by ELISA. Moreover, chemerin was added into HG-induced ARPE-19 cells to assess its effect on proinflammatory cytokines and VEGF. Results. The levels of chemerin/CMKLR1 were higher in PDR patients than NPDR ones, and chemerin was positively correlated with CMKLR1 in PDR patients. Compared to NPDR, the secretions of proinflammatory cytokines and VEGF were increased in PDR patients and positively correlated with chemerin/CMKLR1. Additionally, chemerin activated CMKLR1 and aggravated HG-induced cell injury, inflammatory responses, and VEGF expressions in ARPE-19 cells. Conclusion. Our study demonstrated that chemerin/CMKLR1 axis aggravated the progression of PDR, which suggested that inhibition of chemerin might serve as a new therapeutic approach to treat PDR.

This study aimed to explore the relationship between diabetic retinopathy (DR) and diabetic foot ulcers (DFUs) to provide evidence for the prevention of diabetic complications. PubMed, EMBASE, Web of Science, Cochrane Library, China National Knowledge Infrastructure, Chinese Biomedical Literature Database and Wanfang Data databases were searched from their inception until March 2023 for studies on the relationship between DR and DFU. Two researchers independently screened the literature and extracted data according to the inclusion and exclusion criteria. The meta‐analysis was performed using the RevMan 5.3 software. Eleven articles referring to 10 208 patients were included, of whom 2191 patients had DFU and 8017 patients did not have DFU. The meta‐analysis results showed that DR significantly increased the incidence of DFU (47.94% vs. 16.38%; OR, 4.13; 95% CI, 2.33–7.33; p < 0.001). The results of this study suggest that patients with DR have a higher risk of developing DFU, highlighting the importance of regular screening for these two complications to prevent serious adverse outcomes of diabetes. However, further high‐quality studies are required to validate the conclusions of the present study.

Objective. The objective is to investigate the relationship and correlation between PEDF and TGF-β in aqueous humor and serum and high myopia CNV lesions. Methods. For each group of patients (namely, group A: patients with high myopia CNV (mCNV); group B: patients with high myopia without CNV; group C: patients with CNV caused by other eye diseases; and group D (control group): patients with simple cataract (without CNV and high myopia)), 20 patients were collected. A total of 40 patients have been collected since the beginning of the study in December 2020, including 7 patients in group A, 13 patients in group B, 10 patients in group C, and 10 patients in group D. Serum and aqueous humor samples were collected, and PEDF and TGF-β levels in serum and aqueous humor were detected by enzyme-linked immunosorbent assay (ELISA). SPSS 26.0 statistical software was used to process the data. Independent sample t-test was used to compare the data of the same factor in the same group between serum and aqueous humor. Comparisons of the same factors between different groups were performed using a one-way analysis of variance (ANOVA). Correlation analysis was conducted by the Pearson correlation coefficient test. P < 0.05 indicated that the difference was statistically significant. Results. There were no significant differences in age, gender, and course of disease among all groups ( P > 0.05 ). The concentration of PEDF in aqueous humor in group A and group C was higher than that in group B and group D. There was no significant correlation between serum PEDF content and the above-mentioned diseases. The concentration of TGF-β in aqueous humor in groups A, B, and C was significantly higher than that in group D. However, there was no significant correlation between TGF-β content in serum and the above-mentioned diseases. There was no significant correlation between aqueous humor and serum PEDF. There was no significant correlation between the content of TGF-β in aqueous humor and serum. Conclusion. TGF-β in aqueous humor may be involved in the development of high myopia and intraocular CNV disease. However, PEDF in aqueous humor may be involved in the development of intraocular CNV disease and has no significant correlation with high myopia. At the same time, TGF-β and PEDF in serum had no significant correlation with high myopia and intraocular CNV disease. There was no significant correlation between the concentrations of TGF-β and PEDF in aqueous humor and serum.

Leptin is over-secreted in many autoimmune diseases, which can promote dendritic cells (DCs) maturation and up-regulate the expression of inflammatory cytokines, but the underlying mechanisms are not fully elucidated. Considering the major role of leptin in maintaining energy balance and the significant role of glycolysis in DCs activation, our study aims to investigate whether leptin promotes the activation of DCs via glycolysis and its underlying mechanisms. We demonstrated that leptin promoted the activation of DCs, including up-regulating the expression of co-stimulatory molecules and inflammatory cytokines, enhancing the proliferation and T helper 17 (Th17) cell ratio in peripheral blood mononuclear cells (PBMC) co-cultured with leptin-stimulated DCs. Leptin also enhanced DCs glycolysis with increased glucose consumption, lactate production, and the expression of hexokinase 2 (HK2). In addition, the activation of DCs stimulated by leptin could be inhibited by the glycolysis inhibitor 2-DG. To explore the signaling pathways involved in leptin-induced HK2 expression, we observed that only the inhibitors of STAT3 (NSC74859) could repress the enhancement of HK2 triggered by leptin stimulation. Therefore, our results indicated that leptin promoted glycolytic metabolism to induce DCs activation via STAT3-HK2 pathway.