ABSTRACT
Three new compounds, i.e. stenophyllols A-C (1-3), were isolated from the rhizome of Boesenbergia stenophylla. The structures were determined by spectroscopic analysis (UV, IR, NMR and HRESIMS). In-vitro neuroblastoma cell viability assay showed stenophyllol A (1) was able to reduce the N2A cell viability to 20% within 24 h.
Subject(s)
Antineoplastic Agents, Phytogenic/pharmacology , Zingiberaceae , Animals , Antineoplastic Agents, Phytogenic/isolation & purification , Cell Line, Tumor , Cell Survival , Mice , Molecular Structure , Phytochemicals/isolation & purification , Phytochemicals/pharmacology , Plant Extracts , Rhizome/chemistry , Zingiberaceae/chemistryABSTRACT
Two new bisanthraquinones, glabraquinone A and B (1-2) were isolated from the root of Prismatomeris glabra (Korth.) Valeton. In addition to the new glabraquinones, six known anthraquinones, that is, 1-hydroxy-2-methoxy-6-methylanthraquinone (3), 1,2-dimethoxy-7-methylanthraquinone (4), lucidin (5), nordamnacanthal (6), damnacanthal (7) and 2-carboxaldehyde-3-hydroxyanthraquinone (8)) and an aromatic compound, that is, catechol diethyl ether (9) were isolated and characterized in this study. Compounds 1, 4 and 9 showed mild activity, reducing N2A cell viability to 77%, 82% and 77%, respectively, in anti-neuroblastoma assay.
ABSTRACT
Our current understanding on brain death remains limited despite its clinical importance. This study evaluated whether the proteome expressed in the rat rostral ventrolateral medulla (RVLM), a neural substrate that our laboratory identified previously to be intimately related to brain death, is uniquely different from other brain areas, using the cerebral cortex, which is defunct under persistent vegetative state for comparison. We found that a group of antioxidant proteins, including members of the peroxiredoxin (Prx) family (Prx-1, Prx-2, Prx-5, Prx-6), thioredoxin and mitochondrial manganese superoxide dismutase, exhibited significantly higher protein and mRNA expression levels in RVLM when compared to cerebral cortex. Tissue oxygen, ATP contents and ATP synthase subunits α and ß in RVLM were also significantly elevated. On the other hand, protein and mRNA levels of members of the ubiquitin-proteasome system, including proteasome subunit α type-1, ubiquitin, uniquitin-conjugating enzyme E2 N, ubiquitin carboxyl-terminal hydrolase isozyme L1 and L3, were comparable in both brain regions. We conclude that a significantly elevated level of antioxidant proteins and mRNA in RVLM is consistent with the exhibition of higher tissue oxygen tension and metabolic energy production in this neural substrate, which together constitute a safeguard mechanism against brain death.
Subject(s)
Brain Death/metabolism , Brain/metabolism , Medulla Oblongata/metabolism , Proteome/metabolism , Adenosine Triphosphate/metabolism , Animals , Cerebral Cortex/metabolism , Gene Expression Regulation , Male , Oxygen/metabolism , Proteome/analysis , Proteome/genetics , Proteomics , RNA, Messenger/genetics , Rats , Rats, Sprague-DawleyABSTRACT
A family of bis(2-pyridyl)amino-modified poly(amidoamine) dendrimer Cu complexes was prepared, and their chemical nuclease activities and binding affinity (Kb) levels for DNA plasmid were investigated. The Kb values of the G2 to G6 apodendrimers for DNA plasmid were found to be 7.4, 23, 48, 70, and 280 µM-1, respectively, using ethidium bromide (EtBr) displacement experiments. The chemical nuclease activities of the corresponding complexes were determined by gel electrophoresis, and a clear positive dendritic effect was observed. Further analysis indicated a linear correlation between the Kb values of the G2 to G5 apodendrimers and the nuclease activity of the corresponding complexes. This observation indicated the importance of substrate binding affinity for macromolecular nuclease activity. In addition, an experiment using 3'-(p-hydroxyphenyl) fluorescein suggested that hydroxyl radicals formed under the tested conditions. Subsequently performed inhibition studies indicated that the hydroxyl radical was the active species responsible for the plasmid cleavage.