The in vitro antiproliferative and antioxidant effects of different fractions of Rosa canina hips on human colon cancer cell lines (Caco-2) was studied. The compounds tested were total extract (fraction 1), vitamin C (fraction 2), neutral polyphenols (fraction 3) and acidic polyphenols (fraction 4). All the extracts showed high cytotoxicity after 72 h, both low and high concentrations. The flow cytometric analysis revealed that all the fractions produce disturbances in the cell cycle resulting in a concomitant cell death by an apoptotic pathway. Changes in the redox status of Caco-2 cells in response to Rosa canina hips were determined. Cells were exposed to hydrogen peroxide in presence of plant fractions and the production of Reactive Oxygen Species (ROS) was significantly decreased. Therefore, our data demonstrate that rosehip extracts are a powerful antioxidant that produces an antiproliferative effect in Caco-2 cells. Therefore, these results predict a promising future for Rosa canina as a therapeutic agent. Thus, this natural plant could be an effective component of functional foods addressed towards colorectal carcinoma.

The alkynyl gold(I) derivative [Au(C≡CPh)(PTA)] (PTA=1,3,5-triaza-7-phosphaadamantane) induces apoptosis in colorectal carcinoma tumour cells (Caco-2) without affecting to normal enterocytes. [Au(C≡CPh)(PTA)] is a slight lipophilic drug, stable in PBS (Phosphate Buffered Saline) and able to bind BSA (Bovin Serum Albumin) by hydrophobic interactions. Once inside the cell, [Au(C≡CPh)(PTA)] targets seleno proteins such as Thioredoxin Reductase 1, increasing ROS (Reactive Oxygen Species) levels, reducing cell viability and proliferation and inducing mitochondrial apoptotic pathway, pro-apoptotic and anti-apoptotic protein imbalance, loss of mitochondrial membrane potential, cytochrome c release and activation of caspases 9 and 3. Moreover, unlike other metal-based drugs such as cisplatin, [Au(C≡CPh)(PTA)] does not target nucleic acid, reducing the risk of side mutation in the DNA. In consequence, our results predict a promising future for [Au(C≡CPh)(PTA)] as a chemotherapeutic agent for colorectal carcinoma.

Three main ethnic groups live in the South American country of Ecuador: Mestizos, Amerindian natives, and African-derived populations, or Afro-Ecuadorans. Mestizos and Afro-Ecuadorans can be considered trihybrid populations containing genes originating in the Americas, Europe, and Africa, as is the case with equivalent populations in other Latin American countries. The proportion and the dynamics of the admixture process remain unknown. However, a certain sex asymmetry of the admixture process can be expected for historical reasons. We typed 11 Y-chromosome short tandem repeats (STRs) in these three ethnic groups to provide adequate allele and haplotype frequencies for forensic genetic purposes and to quantify admixture proportions in male lineages. In addition, a data set of 15 autosomal STRs in the same samples were reanalyzed for the same purpose. Contributions to Mestizo Y chromosomes were estimated to be 70% European, 28% Amerindian, and 2% African, whereas in autosomes the contributions were 19%, 73%, and 8%, respectively, which underlines the sexual asymmetry in mating, with Europeans contributing mostly males. European Y-chromosome haplotypes in Mestizos were similar to those in Spain. Moreover, about 10% of European Y chromosomes were found in the Amerindian Kichwa. As for Afro-Ecuadorans, their contributions to the male line are 44% African, 31% European, and 15% Native American; the last value is the highest percentage reported so far for an African-derived American group. Autosomal admixture was estimated as 56% African, 16% European, and 28% Amerindian.

A reversible carbon catabolite inactivation step is described for isocitrate lyase from Saccharomyces cerevisiae. This reversible inactivation step of isocitrate lyase is similar to that described for fructose 1,6-bisphosphatase. Addition of 2,4-dinitrophenol, nystatin or glucose to cultures, grown in ethanol as carbon source, caused a rapid loss of the isocitrate lyase and fructose 1,6-bisphosphatase activities at pH 5.5 but not at pH 7.5. These results suggest that intracellular acidification and thus a cAMP increase is involved in the catabolite inactivation mechanism of both enzymes. From results obtained by addition of glucose to yeast cultures at pH 7.5 it was concluded that others factors than cAMP can play a role in the catabolite inactivation mechanism of both enzymes.