Dry but Not Humid Thermal Processing of Aloe vera Gel Promotes Cytotoxicity on Human Intestinal Cells HT-29.

Aloe vera products, both in food and cosmetics, are becoming increasingly popular due to their claimed beneficial effects, which are mainly attributed to the active compound acemannan. Usually, these end products are based on powdered starting materials. High temperatures during the drying process to obtain the starting materials have several advantages, like shortening the drying time, eliminating toxic aloin and reducing bacterial contamination. Nevertheless, there are two major drawbacks: first, at temperatures of 80 °C or higher, structural changes in acemannan, especially its deacetylation (>46%), are triggered, which does not happen at lower temperatures (14% at 60 °C); secondly, a toxic principle is formed at higher temperatures, resulting in a higher cytotoxicity. Thus, two temperature-dependent but opposing effects cause with a median cytotoxic concentration of CC50 = 0.4× a peak of cytotoxicity at 80 °C; at 60 °C this cytotoxic substance is not formed and at 100 °C aloin is more readily eliminated, resulting in a CC50 = 1.1× and CC50 = 1.4×, respectively. The cytotoxic substance generated by dry heat at 80 °C is not a modified polysaccharide because its polysaccharide-enriched alcohol-insoluble fraction is with CC50 = 0.9× less cytotoxic. Moreover, this substance is polar enough to be washed away with ethanol. Additionally, when Aloe gel is heated at 80 °C under humid conditions (pasteurization), the cytotoxicity does not increase (CC50 = 1.6×). Finally, to produce powdered starting materials from Aloe gel, it is recommended to use temperatures of around 60 °C in order to preserve the acemannan structure (and thus biological activity) and the low cytotoxicity.

In Vitro Bioactivity of Methanolic Extracts from Amphipterygium adstringens (Schltdl.) Schiede ex Standl., Chenopodium ambrosioides L., Cirsium mexicanum DC., Eryngium carlinae F. Delaroche, and Pithecellobium dulce (Roxb.) Benth. Used in Traditional Medicine in Mexico.

Seven out of eight methanolic extracts from five plants native to Mexico were inactive against ten bacterial strains of clinical interest. The fruit extract of Chenopodium ambrosioides inhibited the bacteria Enterococcus faecalis (MIC = 4375 µg/ml), Escherichia coli (MIC = 1094 µg/ml), and Salmonella typhimurium (MIC = 137 µg/ml). The fruit extract of C. ambrosioides was with CC50 = 45 µg/ml most cytotoxic against the cell-line Caco-2, followed by the leaf extract from Pithecellobium dulce (CC50 = 126 µg/ml); interestingly, leaves of C. ambrosioides (CC50 = 563 µg/ml) and bark of P. dulce (CC50 = 347 µg/ml) extracts were much less cytotoxic. We describe for the first time the cytotoxic effect from extracts of the aerial parts and the flowers of Cirsium mexicanum (CC50 = 323 µg/ml and CC50 = 250 µg/ml, resp.). Phytochemical analysis demonstrated for both extracts high tannin and saponin and low flavonoid content, while terpenoids were found in the flowers. For the first time we report a cytotoxicological study on an extract of Eryngium carlinae (CC50 = 356 µg/ml) and likewise the bark extract from Amphipterygium adstringens (CC50 = 342 µg/ml). In conclusion the fruit extract of C. ambrosioides is a potential candidate for further biological studies.

Functional analysis of the Arabidopsis PLDZ2 promoter reveals an evolutionarily conserved low-Pi-responsive transcriptional enhancer element.

Plants have evolved a plethora of responses to cope with phosphate (Pi) deficiency, including the transcriptional activation of a large set of genes. Among Pi-responsive genes, the expression of the Arabidopsis phospholipase DZ2 (PLDZ2) is activated to participate in the degradation of phospholipids in roots in order to release Pi to support other cellular activities. A deletion analysis was performed to identify the regions determining the strength, tissue-specific expression, and Pi responsiveness of this regulatory region. This study also reports the identification and characterization of a transcriptional enhancer element that is present in the PLDZ2 promoter and able to confer Pi responsiveness to a minimal, inactive 35S promoter. This enhancer also shares the cytokinin and sucrose responsive properties observed for the intact PLDZ2 promoter. The EZ2 element contains two P1BS motifs, each of which is the DNA binding site of transcription factor PHR1. Mutation analysis showed that the P1BS motifs present in EZ2 are necessary but not sufficient for the enhancer function, revealing the importance of adjacent sequences. The structural organization of EZ2 is conserved in the orthologous genes of at least eight families of rosids, suggesting that architectural features such as the distance between the two P1BS motifs are also important for the regulatory properties of this enhancer element.