Pinicolol B from Antrodia cinnamomea induces apoptosis of nasopharyngeal carcinoma cells.

ETHNOPHARMACOLOGICAL RELEVANCE: The medicinal mushroom Antrodia cinnamomea possesses anticancer properties but the active compounds responsible for these effects are mostly unknown. AIM OF THE STUDY: We aimed to identify novel A. cinnamomea compounds that produce cytotoxic effects on cancer cells. MATERIALS AND METHODS: Using ethanol extraction and chromatography, we isolated the lanostanoid compound lanosta-7,9(11),24-trien-3ß,15α,21-triol (1) from cultured A. cinnamomea mycelium. Cytotoxicity and pro-apoptotic effects of compound 1 were evaluated using the MTS assay and flow cytometry analysis, respectively. RESULTS: Compound 1 produced cytotoxic effects on the nasopharyngeal carcinoma cell lines TW02 and TW04, with IC50 values of 63.3 and 115.0µM, respectively. On the other hand, no cytotoxic effects were observed on non-tumorigenic nasopharyngeal epithelial cells (NP69). In addition, compound 1 induced apoptosis in TW02 and TW04 cells as revealed by flow cytometry analysis. CONCLUSIONS: Our results demonstrate for the first time the presence of pinicolol B in A. cinnamomea mycelium and suggest that this compound may contribute to the anticancer effects of A. cinnamomea.

Functional studies of soybean (Glycine max L.) seed LEA proteins GmPM6, GmPM11, and GmPM30 by CD and FTIR spectroscopy.

The protein and mRNA levels of late embryogenesis abundant (LEA) genes may be linked to osmotic stresses. Here, we characterized three soybean hydrophilic LEA proteins--GmPM11 (LEA I), GmPM6 (LEA II), and GmPM30 (LEA III)--by circular dichroism and Fourier transform infrared spectroscopy. Structural analysis revealed that the LEA proteins adopted high amounts of disordered conformations in solution and underwent conformational changes with hydrophobicity and desiccation induction. Macromolecular interaction studies revealed that the GmPM proteins interact with non-reducing sugars and phospholipids. GmPM6 and GmPM30 but not GmPM11 could prevent beta-aggregation of poly-L-lysine after slow drying. We discuss the possible functions of hydrophilic LEA proteins in maturing seeds.