Gluten is the main storage protein in grains and consists of gliadin and glutenin occurring in the same ratio. Persons suffering from intolerances, including celiac disease, must avoid foods containing gluten or products containing wheat, barley, and rye. Accordingly, gluten detection is of high interest for the food safety of celiac patients. This study was designed to determine the concentrations of gluten in foods labeled "gluten free" available in the United States. Seventy-eight samples labeled gluten free were collected and analyzed using a gliadin competitive enzyme-linked immunosorbent assay. The gluten content was calculated based on the assumption of the same ratio between gliadin and glutenin. Forty-eight (61.5%) of the 78 samples contained less than the limit of quantification of 10 mg/kg for gluten. In addition, 14 (17.9%) of the 78 samples labeled gluten free contained less gluten than the guidelines established by the Codex Alimentarius for gluten-free labeling (20 mg/kg). However, 16 samples (20.5%) did contain gluten levels of ≥20 mg/kg, ranging from 20.3 to 60.3 mg/kg. In particular, five of eight breakfast cereal samples showed gluten contents higher than 20 mg/kg. These results may be of concern, as gluten sensitivity is known to vary among celiac disease patients.

Ochratoxin A (OTA) is a widespread mycotoxin produced by several species of the genera Aspergillus and Penicillium. OTA exists in a variety of foods, including rice, oats, and coffee and is hepatotoxic, with a similar mode of action as aflatoxin B1. The precise mechanism of cytotoxicity is not yet known, but oxidative damage is suspected to contribute to its cytotoxic effects. In this study, human hepatocyte HepG2 cells were treated with various concentrations of OTA (5–500 nM) for 48 h. OTA triggered oxidative stress as demonstrated by glutathione depletion and increased reactive oxygen species, malondialdehyde level, and nitric oxide production. Apoptosis was observed with 500 nM OTA treatment. OTA increased both the mRNA and protein expression of phase I and II enzymes. The same results were observed in an in vivo study using ICR mice. Furthermore, the relationship between phase I and II enzymes was demonstrated by the knockdown of the aryl hydrocarbon receptor (AhR) and NF-E2-related factor 2 (Nrf2) with siRNA. Taken together, our results show that OTA induces oxidative stress through the phase I reaction regulated by AhR and induces apoptosis, and that the phase II reaction is activated by Nrf2 in the presence of oxidative stress.