Synthesis, characterization, antioxidant activity and neuroprotective effects of selenium polysaccharide from Radix hedysari.

Beta-amyloid (Aß) peptide, the hallmark of Alzheimer's disease, invokes oxidative damage to neurons and eventually leads to neuronal death. Selenylation modification of polysaccharide obtained from Radix hedysari (RHP) was studied to access antioxidant activities and neuroprotective effects against oxidative stress and apoptosis induced by Aß25-35 in vitro. A series of the selenylation derivatives of RHP (Se-RHP) was synthesized using nitric acid-sodium selenite (HNO3-Na2SeO3) method. The organic selenium content of Se-RHP increased from 1.04 to 3.29 mg/g. However, compared with the weight-average molecular mass (Mw) of RHP, Mw of Se-RHP showed a significant decrease, and varied from 27.7 kDa to 62.7 kDa. FT-IR spectra and (13)C NMR spectra indicated the selenite groups had been introduced mainly at the C-6 positions of RHP. Compared with RHP, Se-RHP showed greater antioxidant activities in vitro. Furthermore, both RHP and Se-RHP3 had neuroprotective effects against Aß25-35-induced oxidative stress and apoptosis in SH-SY5Y human neuroblastoma cells, which might be a potential therapeutic agent for preventing or treating neurodegenerative diseases.

Proteomic analysis of the effect of triterpenes from Patrinia heterophylla on leukemia K562 cells.

For centuries, Patrinia heterophylla had been used in China to treat many diseases including tumor. Triterpenes has been identified as the major active constituents in Patrinia heterophylla. To elucidate the antitumor mechanism of triterpenes from Patrinia heterophylla1 (TPH), a proteomic analysis is carried out with TPH treatment in K562 cells. The total proteins extracted from TPH treated K562 cells are analyzed by two dimensional gel electrophoresis (2-DE) and compared with those untreated K562 cells. Mass spectrometry is applied to identify the differentially expressed proteins. Twenty-three differentially expressed significant proteins are discovered. Eight proteins are later identified by mass spectrometry (MALDI-TOF-MS) and Mascot software. Among them, four proteins are up-regulated (Aldolase A, Glyceraldehyde-3-phosphate dehydrogenase, Flavin reductase and Hemoglobin subunit) and four proteins were down-regulated (Heat-shock protein 90 〈Alpha〉 (HSP90-〈Alpha〉), Eukaryotic translation initiation factor 5A, Moesin, tublin) by TPH treatment in K562 cells. The identified proteins are associated with energy metabolism, oxidative stress, apoptosis, signal transduction, differential induction, and protein biosynthesis. These findings might provide valuable insights into the antitumor mechanism of TPH in K562 cells.