[Differences of B cells, plasma cells, and related cytokines expression in gingival tissues between periodontitis and periodontal healthy subjects].

OBJECTIVE: This study aimed to compare the differences of B cells, plasma cells, and related cytokines expression in gingival tissues between periodontitis and periodontal healthy subjects. METHODS: Gingival tissues were collected from periodontal healthy subjects (periodontal healthy group, n=12) and periodontitis patients (periodontitis group, n=15). Hematoxylin-eosin (HE) staining was used for histopathological examination. Immunohistochemical staining (CD19, CD38, and CD138) was applied to detect the expression of B cells and plasma cells. B cell-activating factor (BAFF) and soluble receptor activator of nuclear factor-κB ligand (sRANKL) were detected by enzyme-linked immunosorbent assay. RESULTS: Extensive inflam-matory cell infiltration was found in the gingival tissues of the periodontitis group. The number of CD19(+), CD38(+), and CD138(+) cells of the periodontitis group was significantly higher than that of the periodontal healthy group (P<0.000 1). BAFF and sRANKL levels of the periodontitis group were higher than those of the periodontal healthy group (P<0.01, P<0.001, respectively). CONCLUSIONS: The expression of B cells, plasma cells, and their related BAFF and sRANKL cytokines were significantly higher in periodon-titis patients than those in the periodontal healthy subjects, sug-gesting that B cells and plasma cells may be involved in the development of periodontitis.

[Matrix metalloproteinase 8 and 9 regulations of polymorphonuclear leukocytes stimulated by Porphyromonas gingivalis with different fimA genotypes].

OBJECTIVE: To investigate the pathogenicity of matrix metalloproteinase 8, 9 (MMP-8, MMP-9) regulations of polymorphonuclear leukocytes (PMNs) by challenge of Porphyromonas gingivalis (P. gingivalis) with different fimA genotypes. METHODS: The studies mainly adopt the isopycnic sedimentation separation to separate the PMNs from human peripheral blood. P. gingivalis ATCC 33277 (type I), WCSP 115 (type II), WCSP 1.5 (type III), W83 (type IV), WCSP 559 (type IV) were assessed for their inductions of MMP-8, MMP-9 expression in PMNs. MMP-8, MMP-9 protein levels in culture supernatant were determined by ELISA at different time intervals (5 min, 30 min, 1 h, 2 h) following continuous co-culture of bacteria with PMNs. RESULTS: MMP-8 and MMP-9 protein levels produced by PMNs co-culture with the I fimA-IV fimA P. gingivalis were significantly stronger than unsimulated group. The velocity and quantity of MMP-8 produced by PMNs co-culture with the II fimA P. gingivalis and IV fimA P. gingivalis were more than III fimA, IVfimA P. gingivalis. The MMP-9 protein levels produced by PMNs co-culture with the I fimA, II fimA, IV fimA P. gingivalis was significantly stronger than III fimA and IV fimA P. gingivalis. CONCLUSION: II fimA and IV fimA P. gingivalis have stronger pathogenicity relatively, which indicate that fimA genotype is associated with pathogenesis of P. gingivalis.

[Monocyte chemoattractant protein-1 regulations of human gingival fibroblasts by Porphyromonas gingivalis with different fimA genotypes].

OBJECTIVE: To investigate the mechanism of monocyte chemoattractant protein-1 (MCP-1) regulations of human gingival fibroblasts (HGF) by challenge of Porphyromonas gingivalis (Pg) with different fimA genotypes. METHODS: Pg ATCC 33277 (type I), WCSP115 (type II), WCSP1.5 (type III), W83 (type IV) were assessed for their inductions of MCP-1 expression in HGF. MCP-1 mRNA levels of HGF were determined by real-time RT-PCR and MCP-1 protein levels in culture supernatant by ELISA at different time intervals (1 h, 3h, 6h and 12h) following continuous co-culture of bacteria with HGF. RESULTS: MCP-1 mRNA and protein levels were both up-regulated when HGF co-cultured with different Pg fimA genotypes. Type II was stronger than other fimA genotypes, HGF expressed significantly great amount of MCP-1 mRNA [(25.75 +/- 3.12)-(326.69 +/- 35.35)] and protein [(178.20 +/- 46.20)-(443.46 82.19) ng/L] for different time periods; While Type III was weaker than other fimA genotypes, and the level of MCP-1 mRNA was [ (4.16 +/- 0.82)-(94.17 +/- 18.56)] and protein [(86.95 +/- 23.90)-(264.01 +/- 28.59) ng/L](P < 0.05). CONCLUSIONS: fimA genotypes of Pg are related with the inductions of MCP-1, which might indicate fimA genotype is associated with pathogenesis of Pg.

[Matrix metalloproteinases regulations of human gingival fibroblasts by Porphyromonas gingivalis with different fimA genotypes].

OBJECTIVE: To investigate the mechanism of matrix metalloproteinases (MMP) regulations of human gingival fibroblasts (HGF) by challenge of Porphyromonas gingivalis (Pg) with different fimA genotypes. METHODS: Pg ATCC 33277 (type I), WCSP115 (type II), WCSP1.5 (type III), W83 (type IV) were assessed for their inductions of MMP-1 and MMP-2 expression in HGF. MMP mRNA levels of HGF were determined by real-time RT-PCR and MMP protein levels in culture supernatant were determined by ELISA at different time intervals (1, 3, 6 and 12 h) following continuous co-culture of bacteria with HGF. RESULTS: When co-cultured with Pg, the MMP-1 and MMP-2 mRNA and protein expression of HGF significantly increased compared with the negative control group (P < 0.01). The group of type II showed greater up-regulated than other fimA genotypes in the mRNA and protein expressions of MMP-1 and MMP-2, MMP-1 mRNA [(28.88 +/- 3.12) - (231.01 +/- 24.99)] and protein [(1.35 +/- 0.17) - (3.08 +/- 1.20)] microg/L; MMP-2 mRNA [(20.42 +/- 2.21) - (188.34 +/- 37.37)] and protein [(2.57 +/- 0.76) - (18.08 +/- 1.15)] microg/L for different time periods; While the group of type III was weaker than other fimA genotypes, the level of MMP-1 mRNA was [(5.11 +/- 0.55) - (72.84 +/- 8.84)] and protein [(0.68 +/- 0.13) - (1.46 +/- 0.94)] microg/L, MMP-2 mRNA [(4.55 +/- 0.55) - (25.75 +/- 3.12)] and protein [(2.28 +/- 0.93) - (11.22 +/- 2.46)] microg/L (P < 0.05). CONCLUSIONS: Pg could induce HGF to over-express MMP, and fimA genotypes of Pg may be related to this pathogenicity, which might indicate fimA genotype is associated with pathogenesis of Pg.