In this study, the major antioxidant components of rose flower were identified. An aqueous extract of rose flowers was chromatographed on CM-cellulose in ammonium acetate buffer (10 mM, pH 4.5) to yield three un-adsorbed peaks F1, F2 and F3. Each of these peaks was subjected to gel filtration on Sephadex G75. F1 yielded two peaks, whereas both F2 and F3 gave rise to only a single peak. Spectroscopic studies using NMR and FTIR revealed that F3 is a gallic acid derivative. It exhibited the highest antioxidative potency. F1-a derived from F1 by gel filtration is mainly a polysaccharide-peptide complex with less potent antioxidative activity. F2 is a polysaccharide also with reduced antioxidant activity. This study demonstrates, for the first time, the presence of both gallic acid derivatives and polysaccharides as major antioxidant principles of the aqueous extract of rose flowers.

Hepatitis B virus X protein (HBx) plays critical roles in the pathogenesis of hepatocellular carcinoma (HCC). Here, we were interested in knowing whether the oncogene Lin28A and its homolog Lin28B are involved in the hepatocarcinogenesis mediated by HBx. We showed that the expression levels of Lin28A and Lin28B were increased in clinical HCC tissues, HepG2.2.15 cell line and liver tissues of p21-HBx transgenic mice. Interestingly, the expression levels of HBx were positively associated with those of Lin28A/Lin28B in clinical HCC tissues. Moreover, the overexpression of HBx resulted in the upregulation of Lin28A/Lin28B in hepatoma HepG2/H7402 cell lines by transient transfection, suggesting that HBx was able to upregulate Lin28A and Lin28B. Then, we examined the mechanism by which HBx upregulated Lin28A and Lin28B. We identified that the promoter region of Lin28A regulated by HBx was located at nt -235/-66 that contained Sp-1 binding element. Co-immunoprecipitation showed that HBx was able to interact with Sp-1 in HepG2-X cells. Moreover, chromatin immunoprecipitation (ChIP) demonstrated that HBx could bind to the promoter of Lin28A, which failed to work when Sp-1 was silenced. Electrophoretic mobility shift assay (EMSA) further identified that HBx was able to interact with Sp-1 element in Lin28A promoter via transcription factor Sp-1. In addition, we found that c-Myc was involved in the activation of Lin28B mediated by HBx. In function, Lin28A/Lin28B played important roles in HBx-enhanced proliferation of hepatoma cells in vitro and in vivo. In conclusion, HBx activates Lin28A/Lin28B through Sp-1/c-Myc in hepatoma cells. Lin28A/Lin28B serves as key driver genes in HBx-induced hepatocarcinogenesis.

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