ABSTRACT
The determination of bisphenol A (BPA) and/or bisphenol A diglycidyl ether (BADGE) in foods sold in Japanese markets and in water leached from six epoxy resin cans with similar diameters was carried out using high-performance liquid chromatography (HPLC) with electrochemical detection (LC/ECD), LC-mass spectrometric detection (LC/MS) and LC-tandem mass spectrometric detection (LC/MS/MS). BPA concentrations were 0-842 ng g(-1) for 48 canned foods, 0-14 ng g(-1) for 23 foods in plastic containers, and 0-1 ng g(-1) for 16 foods in paper containers. No BADGE was detected in three canned foods. There was no difference in leaching concentrations of BPA into glycine buffers at pHs 8 and 11, and water. The amounts of BPA leached into water from six epoxy resin cans held at 121 degrees C for 20 min were almost the same as the cans' contents and were much higher than the amounts leached from cans held at or below 80 degrees C for 60 min. The amount leached depended on the type of can, but not on the amount of BADGE leached from the cans. Considerably more BPA than BADGE leached to water from six cans. Two cans whose contents had high concentrations of BPA showed no BADGE leaching even at 121 degrees C, suggesting the different kinds of epoxy resin can linings from others. The results imply that the main source of human exposure to BPA is food from cans with linings that contain high percentages of BPA as an additive or an unforeseen contaminant.
Subject(s)
Estrogens, Non-Steroidal/analysis , Food Contamination/analysis , Food Packaging , Phenols/analysis , Benzhydryl Compounds , Chromatography, High Pressure Liquid/methods , Chromatography, Liquid/methods , Epoxy Compounds/analysis , Epoxy Resins/chemistry , Food Analysis/methods , Food Preservation , Humans , Japan , Mass Spectrometry/methodsABSTRACT
PURPOSE: Multifocal electroretinograms (multifocal ERGs) were performed to evaluate retinal function in patients with diabetic macular edema. MATERIALS & METHODS: Eight eyes of 5 patients underwent pars plana vitrectomy for diabetic macular edema. Multifocal ERGs, fundus examinations, and fluorescent angiographies were done both before and after the operation. RESULTS: Post-operative visual acuity was improved by two or more lines in 3 eyes. In multifocal ERGs, the amplitude of the positive wave (P1) from the macular area decreased transiently after surgery (p < 0.05), but it improved with the passage of time. The P1 amplitude from the peripheral area was decreased throughout the observation period of six months (p < 0.05). For both areas, the P1 latency was increased significantly (p < 0.05) at one month post-operatively, and then decreased. CONCLUSION: These findings are consistent with the possibility that the surgical method, especially removal of the posterior cortical vitreous, can cause retinal damage.
Subject(s)
Diabetic Retinopathy/physiopathology , Diabetic Retinopathy/surgery , Edema/physiopathology , Edema/surgery , Electroretinography , Vitrectomy , Electroretinography/methods , Female , Humans , Male , Middle AgedABSTRACT
The kinetics of inflammatory cytokines in sensory retina of mice with corneal alkali-burned eyes were examined. Retinal samples were collected from ICR mice with unburned and alkali-burned eyes from day 3 to day 14. Enzyme-linked immunosorbent assay was used to quantitate the expression levels of interleukin-1 alpha (IL-1 alpha), IL-1 beta and IL-6. Concentrations of IL-1 beta and IL-6 were significantly elevated at day 3 after alkali burn, and reduced to normal level by day 7. The concentration of IL-1 alpha was below assay sensitivity at all times. A significant elevation of IL-1 beta and IL-6 in the sensory retina may contribute to the retinal inflammatory response in the alkali-burned eyes. This is the first report suggesting that the retina is involved in the damage process of alkali burn.
Subject(s)
Burns, Chemical/etiology , Corneal Injuries , Eye Burns/chemically induced , Interleukin-1/metabolism , Interleukin-6/metabolism , Retina/metabolism , Animals , Cornea/drug effects , Enzyme-Linked Immunosorbent Assay , Female , Mice , Mice, Inbred ICR , Sodium HydroxideABSTRACT
Deleterious effects of isopropyl unoprostone (PG-F2 alpha) on the ocular surface were evaluated using the in vivo barrier function assay of corneal epithelial cells and the proliferation assay of human corneal epithelial cells in vitro. The barrier function of corneal epithelial cells in vivo was not impaired by treatment with PGF2 alpha, but it was significantly suppressed by timolol. The result of cell proliferation assay of human corneal cells showed that the 0.12% PGF2 alpha ophthalmic solution caused greater suppression of cell proliferation and acuter cell toxicity than 0.5% timolol ophthalmic solution. Further study showed that not the vehicle but the PGF2 alpha itself was responsible for these deleterious effects. We conclude that the 0.12% PGF2 alpha ophthalmic solution affects cell migration and proliferation but not the barrier effects of the ocular surface. These results suggest that the corneal epithelial defect of glaucoma patients may be caused by these two independent mechanisms, namely suppression of cell proliferation by PGF2 alpha and the destruction of the barrier function of the ocular surface by timolol.
Subject(s)
Corneal Diseases/chemically induced , Dinoprost/analogs & derivatives , Epithelium, Corneal/drug effects , Adrenergic beta-Antagonists/administration & dosage , Adrenergic beta-Antagonists/adverse effects , Adult , Aged , Cell Division/drug effects , Cells, Cultured , Dinoprost/administration & dosage , Dinoprost/adverse effects , Epithelium, Corneal/cytology , Female , Humans , Male , Middle Aged , Ophthalmic Solutions , Timolol/administration & dosage , Timolol/adverse effectsABSTRACT
An oxygen electrode method for determining residual hydrogen peroxide in foods has been further improved. Pretreatment, which includes extraction and neutralization, is done in a hydrogen peroxide extraction apparatus with nitrogen gas bubbling. The hydrogen peroxide concentration of the sample is corrected by subtracting the sample blank value, obtained for the sample through catalase treatment. Bubbling with nitrogen gas effectively minimized the sample blank value, making this method suitable for accurate determination of trace amounts of hydrogen peroxide in foods. Recoveries of hydrogen peroxide added at 1-10 micrograms/g were 77.8-107.1% by the present method. These recoveries are similar to or higher than those by the Japanese standard method and by another modified oxygen electrode method. Concentrations of naturally occurring hydrogen peroxide in solid foods were < 0.87 microgram/g by the present method, lower than those by either the standard method or another modified oxygen electrode method.
Subject(s)
Beverages/analysis , Coffee/chemistry , Food Additives/analysis , Hydrogen Peroxide/analysis , Electrodes , Food Analysis , Nitrogen , OxygenSubject(s)
Fluorides, Topical/metabolism , Age Factors , Child , Female , Fluorides/analysis , Humans , Male , Saliva/analysis , Sex Factors , TabletsSubject(s)
Community Dentistry , Public Health Dentistry , Fluorides, Topical , Health Services Needs and Demand , Humans , JapanSubject(s)
Cholesterol/biosynthesis , Liver/metabolism , Panax , Plants, Medicinal , Saponins/pharmacology , Animals , In Vitro Techniques , Liver/drug effects , Male , RatsABSTRACT
Absorption beta-alanine, anserine or carnosine from rat intestine was studied in vivo by a force feeding method and in vitro using an everted sac method. Possibility of anserine and carnosine hydrolysis prior to intestinal absorption was also investigated using a glycylleucine dipeptidase-containing fraction prepared from rat intestine. The following results were obtained. 1) Anserine and carnosine were absorbed as they were from rat small intestine. 2) Both anserine and carnosine were partially hydrolyzed in vitro by the glycylleucine dipeptidase-containing fraction. Carnosine was hydrolyzed faster than anserine. The above rather conflicting results suggest that physiological amounts of anserine and carnosine might be absorbed from rat small intestine in dipeptide forms.
