Objective:To establish a method for the determination of nimesulide granules by HPLC. Methods:An Inertsil ODS-SP C18 column(250 mm × 4. 6 mm,5 μm) was used, and the mobile phase was 0. 01 mol·L-1 potassium hydrogen phosphate anhy-drous-acetonitrile(55∶45)[adjusting pH to (7. 2 ± 0. 05) with phosphoric acid]. The detection wavelength was set at 399nm and the flow rate was 1.0 ml·min-1. The injection volume was 20 μl. Results: The linear range of nimesulide was 0.044-0.222 μg(r=0. 999 9), the average recovery was 99. 22% and RSD was 0. 46%(n=6). Conclusion:The method is simple, accurate with promis-ing sensitivity and reproducibility, and can be used in the determination of nimesulide granules .

Objective To investigate the effects of peptide-binding domain (PBD) of heat shock protein (HSP) 72 on epithelial to mesenchymal transition (EMT) in rat renal tubular epithelial cells.Methods The expressions of wild-type HSP72,mutant of HSP72 lacking peptide binding domain (HSP72-△PBD) and HSP72-PBD were induced by plasmid transfection.NRK-52E ceils were stimulated by TGF-β1 for 48 h.The expressions of α-smooth muscle actin (α-SMA),E-cadherin,HSP72 and Smad3/p-Smad3 were detected by Western blot and immunofluorescence.Results After NRK-52E cells were stimulated by TGF-β 1 (10 μg/L) for 48 h,the expression of α-SMA was increased and the protein level of E-cadherin was decreased.Western blotting and immunofluorescence showed that over-expression of both HSP72 and PBD inhibited TGF-β1-induced up-regulation of protein α-SMA expression,down-regulation of protein E-cadherin.However,overexpression of HSP72-△PBD did not change the protein level of E-cadherin and α-SMA.In addition,over-expression of HSP72 and PBD significantly inhibited the phosphorylation of Smad3.Conclusion Inhibition of Smad3 activation and EMT by HSP72 is associated with the function of PBD.

Numerous studies have reported that the resistance of biofilm bacteria to antibiotics can be up to 10-1 000 fold higher than that of planktonic bacteria. Bacterial biofilms are reported to be responsible for more than 80% of human microbial infection, posing great challenges to the healthcare sector. Many studies have reported that plant extracts and their active ingredients can inhibit the formation and development of bacterial biofilms, including reducing biofilm biomass and the number of viable bacteria in biofilms, as well as eradicating mature biofilms. This review summarized the plant extracts and their active ingredients that are inhibitory to bacterial biofilms, and analyzed the underpinning mechanisms. This review may serve as a reference for the development of plant drugs to prevent and treat biofilm infections.
Anti-Bacterial Agents/pharmacology* ; Bacteria ; Biofilms ; Humans ; Plant Extracts/pharmacology* ; Quorum Sensing

Hereditary gingival fibromatosis (HGF) is a rare inherited condition with fibromatoid hyperplasia of the gingival tissue that exhibits great genetic heterogeneity. Five distinct loci related to non-syndromic HGF have been identified; however, only two disease-causing genes, SOS1 and REST, inducing HGF have been identified at two loci, GINGF1 and GINGF5, respectively. Here, based on a family pedigree with 26 members, including nine patients with HGF, we identified double heterozygous pathogenic mutations in the ZNF513 (c.C748T, p.R250W) and KIF3C (c.G1229A, p.R410H) genes within the GINGF3 locus related to HGF. Functional studies demonstrated that the ZNF513 p.R250W and KIF3C p.R410H variants significantly increased the expression of ZNF513 and KIF3C in vitro and in vivo. ZNF513, a transcription factor, binds to KIF3C exon 1 and participates in the positive regulation of KIF3C expression in gingival fibroblasts. Furthermore, a knock-in mouse model confirmed that heterozygous or homozygous mutations within Zfp513 (p.R250W) or Kif3c (p.R412H) alone do not led to clear phenotypes with gingival fibromatosis, whereas the double mutations led to gingival hyperplasia phenotypes. In addition, we found that ZNF513 binds to the SOS1 promoter and plays an important positive role in regulating the expression of SOS1. Moreover, the KIF3C p.R410H mutation could activate the PI3K and KCNQ1 potassium channels. ZNF513 combined with KIF3C regulates gingival fibroblast proliferation, migration, and fibrosis response via the PI3K/AKT/mTOR and Ras/Raf/MEK/ERK pathways. In summary, these results demonstrate ZNF513 + KIF3C as an important genetic combination in HGF manifestation and suggest that ZNF513 mutation may be a major risk factor for HGF.
Animals ; Humans ; Mice ; Fibromatosis, Gingival/pathology* ; Gingiva ; Kinesins/genetics* ; Mutation/genetics* ; Phosphatidylinositol 3-Kinases/genetics*