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1.
International Eye Science ; (12): 193-197, 2023.
Article de Chinois | WPRIM | ID: wpr-960934

RÉSUMÉ

AIM: To elucidate the effect of histone deacetylase(HDAC)inhibitor suberoylanilide hydroxamic acid(SAHA)on the proliferation of choroidal melanoma(CM)cell line C918 and to explore the related mechanism.METHODS: Inverted fluorescence microscope was used to observe the effect of different concentrations of SAHA(0.625, 1.25 or 2.5 μmol/L)on the morphology of C918 cell. The cell viability was detected by cholecystokinin octapeptide(CCK-8)assay. Plate clone formation assay and EdU staining were carried out to measure the effect of SAHA on the cell proliferation. Meanwhile, the expressions of cell proliferation-related proteins including c-Myc, CyclinA2 and CDK2, and histone deacetylase 7(HDAC7)and fibroblast growth factor 18(FGF18)were detected by Western blot.RESULTS: Compared with the control group, the cell density was reduced in SAHA. SAHA could also promote cell shrinkage, and the inhibition on cell was in a concentration-dependent manner. CCK-8 assay showed that SAHA treatment decreased cell viability in a dose-dependent manner and the inhibition rate was 80% when SAHA at 2.5 μmol/L. Compared with the control group, Western blot showed that SAHA could suppress the expression of cell proliferation proteins including c-Myc, CyclinA2 and CDK2 in a dose-dependent manner. In addition, 1.25 μmol/L SAHA significantly decreased the numbers of EdU staining positive cells and cell clones. More importantly, SAHA could dose-dependently decrease the expression of HDAC7 and FGF18 compared with control group.CONCLUSION: SAHA could inhibit the proliferation of CM cell line C918 by inhibiting the HDAC7/FGF18 signaling pathway.

2.
Zhonghua ganzangbing zazhi ; Zhonghua ganzangbing zazhi;(12): 569-571, 2006.
Article de Chinois | WPRIM | ID: wpr-341299

RÉSUMÉ

<p><b>OBJECTIVE</b>To further study the binding character of hepatitis B surface antigen (HBsAg) and beta 2-glycoprotein I (beta2GP I) and to explore whether beta2GP I plays an important role in the hepatotropism of hepatitis B virus.</p><p><b>METHODS</b>Using Western blot technique, we observed the binding character of the HBsAg with reduced and non-reduced beta2GP I.</p><p><b>RESULTS</b>rHBsAgs with reduced and non-reduced beta2GP I showed identical binding activity.</p><p><b>CONCLUSIONS</b>The binding activity of HBsAg is dependent on tandem residues, but not on conformational structures of beta2GP I. There is a specific binding between HBV and beta2GP I, which may play an important role in HBV infection and is one of the reasons of hepatotropism of HBV.</p>


Sujet(s)
Humains , Hépatite B , Virologie , Antigènes de surface du virus de l'hépatite B , Métabolisme , Virus de l'hépatite B , Virulence , Protéines de l'enveloppe virale , Sang , bêta 2-Glycoprotéine I , Sang
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