coumestrol and naringenin

Spatholobus sinensis is a plant of the Spatholobus genus (Leguminosae family). Its caulis are used as "ji-xue-teng" regionally. However, to our knowledge, no phytochemical investigation on S. sinensis has been reported to date. In this study, eight compounds were isolated from the ethanol extract of the caulis of S. sinensis, by solvents extraction and column chromatography methods. By analysis of their physic-chemical constants and spectral data, the structures of 8 compounds were identified as spatholosineside A (1), 2',4',5,7-tetrahydroxyisoflavone (2), isoliquiritigenin (3), lupinalbin A (4), coumestrol (5), naringenin (6), protocatechuic acid (7), leonuriside A (8). Compound 1 is a new compound.

Topics: Chalcones; Coumestrol; Fabaceae; Flavanones; Glycosides; Molecular Structure; Plant Stems; Plants, Medicinal

The study investigated the ability of 34 natural and synthetic chemicals to compete with [3H]17beta-estradiol (E2) for binding to bacterially expressed glutathione-S-transferase (GST)-estrogen receptors (ER) fusion proteins from five different species. Fusion proteins consisted of the ER D, E and F domains of human alpha (GST-hERalphadef), mouse alpha (GST-mERalphadef), chicken (GST-cERdef), green anole (GST-aERdef) and rainbow trout ERs (GST-rtERdef). All five fusion proteins displayed high affinity for E2 with dissociation constants (K(d)) ranging from 0.3 to 0.9 nM. Although, the fusion proteins exhibited similar binding preferences and binding affinities for many of the chemicals, several differences were observed. For example, alpha-zearalenol bound with greater affinity to GST-rtERdef than E2, which was in contrast to other GST-ERdef fusion proteins examined. Coumestrol, genistein and naringenin bound with higher affinity to the GST-aERdef, than to the other GST-ERdef fusion proteins. Many of the industrial chemicals examined preferentially bound to GST-rtERdef. Bisphenol A, 4-t-octylphenol and o,p' DDT bound with approximately a ten-fold greater affinity to GST-rtERdef than to other GST-ERdefs. Methoxychlor, p,p'-DDT, o,p'-DDE, p,p'-DDE, alpha-endosulfan and dieldrin weakly bound to the ERs from the human, mouse, chicken and green anole. In contrast, these compounds completely displaced [3H]E2 from GST-rtERdef. These results demonstrate that ERs from different species exhibit differential ligand preferences and relative binding affinities for estrogenic compounds and that these differences may be due to the variability in the amino acid sequence within their respective ER ligand binding domains.

Topics: Amino Acid Sequence; Animals; Binding, Competitive; Chickens; Cloning, Molecular; Coumestrol; Dieldrin; Estrogen Receptor Modulators; Estrogens; Estrogens, Non-Steroidal; Flavanones; Flavonoids; Genistein; Humans; Isoflavones; Lizards; Methoxychlor; Mice; Molecular Sequence Data; Mycotoxins; Oncorhynchus mykiss; Phytoestrogens; Plant Preparations; Receptors, Estrogen; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Species Specificity