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1.
J Pers Med ; 13(8)2023 Jul 31.
Article in English | MEDLINE | ID: mdl-37623470

ABSTRACT

PURPOSE: For people with hearing implants (HI), magnetic resonance imaging (MRI) still presents some difficulties due to the built-in magnet. Radiologists often have concerns regarding complications associated with HIs. The aim of this study was to record the experiences of HI users during and after MRI examinations. METHOD: A survey including 15 questions regarding MRI specifics, namely changes in hearing ability, hearing/sound impressions, pain, uncomfortable feelings, etc., were mailed to our patients. RESULTS: Overall, 79 patients with HI had a total of 159 MR examinations in our institute. A total of 45 HI recipients reported back: 35% stated that they had been rejected by an MRI Institute because of their HI. Their feelings/impression ratings during the measurements were not present and therefore were not rated for the majority (49%), 42% of the HI users rated the pain with 0 (no pain), 2% with 1 (very light pain), 4% with 5 (acceptable pain), and 2% rated the pain with 7, which is between acceptable and strong pain. One examination resulted in a dislocation of the magnet of a cochlear implant (CI 512 Cochlear Limited). No adverse events were reported for MED-EL HI users in the survey (none of the contacted AB users answered the questionnaire). The reported mean daily wearing time was 11.6 ± 4.6 h per day for 6.3 ± 1.7 days per week. CONCLUSIONS: Based on these results and our experience we conclude that MRI examinations with HI are safe given that the measurements are performed according to the safety policies and procedures released by the manufacturers.

2.
Toxins (Basel) ; 13(2)2021 01 22.
Article in English | MEDLINE | ID: mdl-33499402

ABSTRACT

The mycotoxin zearalenone (ZEN) is a frequent contaminant of animal feed and is well known for its estrogenic effects in animals. Cattle are considered less sensitive to ZEN than pigs. However, ZEN has previously been shown to be converted to the highly estrogenic metabolite α-zearalenol (α-ZEL) in rumen fluid in vitro. Here, we investigate the metabolism of ZEN in the reticulorumen of dairy cows. To this end, rumen-fistulated non-lactating Holstein Friesian cows (n = 4) received a one-time oral dose of ZEN (5 mg ZEN in 500 g concentrate feed) and the concentrations of ZEN and ZEN metabolites were measured in free rumen liquid from three reticulorumen locations (reticulum, ventral sac and dorsal mat layer) during a 34-h period. In all three locations, α-ZEL was the predominant ZEN metabolite and ß-zearalenol (ß-ZEL) was detected in lower concentrations. ZEN, α-ZEL and ß-ZEL were eliminated from the ventral sac and reticulum within 34 h, yet low concentrations of ZEN and α-ZEL were still detected in the dorsal mat 34 h after ZEN administration. In a second step, we investigated the efficacy of the enzyme zearalenone hydrolase ZenA (EC 3.1.1.-, commercial name ZENzyme®, BIOMIN Holding GmbH, Getzersdorf, Austria) to degrade ZEN to the non-estrogenic metabolite hydrolyzed zearalenone (HZEN) in the reticulorumen in vitro and in vivo. ZenA showed a high ZEN-degrading activity in rumen fluid in vitro. When ZenA was added to ZEN-contaminated concentrate fed to rumen-fistulated cows (n = 4), concentrations of ZEN, α-ZEL and ß-ZEL were significantly reduced in all three reticulorumen compartments compared to administration of ZEN-contaminated concentrate without ZenA. Upon ZenA administration, degradation products HZEN and decarboxylated HZEN were detected in the reticulorumen. In conclusion, endogenous metabolization of ZEN in the reticulorumen increases its estrogenic potency due to the formation of α-ZEL. Our results suggest that application of zearalenone hydrolase ZenA as a feed additive may be a promising strategy to counteract estrogenic effects of ZEN in cattle.


Subject(s)
Dietary Supplements , Hydrolases/administration & dosage , Rumen/enzymology , Zearalenone/metabolism , Animal Feed , Animals , Cattle , Dairying , Female , Food Microbiology , Hydrolases/metabolism , Hydrolysis , Inactivation, Metabolic , Kinetics , Male , Zeranol/analogs & derivatives , Zeranol/metabolism
3.
AMB Express ; 3(1): 62, 2013 Oct 22.
Article in English | MEDLINE | ID: mdl-24148308

ABSTRACT

The target of the present study was to quantify the capacity of different commercially available yeast derivatives to bind E. coli F4 and Salmonella Typhimurium. In addition, a correlation analysis was performed for the obtained binding numbers and the mannan-, glucan- and protein contents of the products, respectively. In a subsequent experiment, different yeast strains were fermented and treated by autolysis or French press to obtain a concentrated yeast cell wall. The capacity of yeast cell wall products to bind E. coli F4 and Salmonella Typhimurium was assessed with a quantitative microbiological microplate-based assay by measuring the optical density (OD) as the growth parameter of adhering bacteria. Total mannan and glucan were determined by HPLC using an isocratic method and a Refractive Index (RI) Detector. Total protein was determined by Total Kjeldahl Nitrogen (TKN). Statistical analyses were performed with IBM SPSS V19 using Spearman correlation and Mann Whitney U Test.Different yeast derivatives show different binding numbers, which indicate differences in product quality.Interestingly, the binding numbers for Salmonella Typhimurium are consistently higher (between one and two orders of magnitude) than for E. coli F4.We could demonstrate some statistical significant correlations between the mannan- and glucan content of different yeast derivatives and pathogen binding numbers; however, for the different yeast strains fermented under standardized laboratory conditions, no statistically significant correlations between the mannan- and glucan content and the binding numbers for E. coli and Salmonella Typhimurium were found.Interestingly, we could demonstrate that the yeast autolysis had a statistically significant difference on E. coli binding in contrast to the French press treatment. Salmonella binding was independent of these two treatments.As such, we could not give a clear statement about the binding factors involved. We propose that many more factors apart from mannan- and glucan content, such as cell wall structure, strain diversity, structural diversity, structural surroundings, and non-specific interactions play important roles in pathogen immobilization.

4.
J Microbiol Methods ; 83(2): 168-74, 2010 Nov.
Article in English | MEDLINE | ID: mdl-20826190

ABSTRACT

Yeast cell wall fractions have been proposed to bind enteropathogenic bacteria. The aim of this study was to develop a quantitative assay by measuring the optical density as growth parameter of adhering bacteria. The exponential growth phase of adhering bacteria was determined by optical density reading and compared with the colony count (CFU/mL). A linear regression was compiled and the bacterial number bound to the yeast cell wall product could be determined. Further focus was the investigation of a yeast cell wall from strain Trichosporon mycotoxinivorans (MTV) for its ability to bind gram negative Salmonella, E. coli and Campylobacter strains and gram positive probiotic bacteria of the genera lactobacilli and bifidobacteria as well as gram positive Clostridium perfringens quantitatively. The gram negative probiotic strain E. coli Nissle 1917 was also investigated. Seven out of 10 S. Typhimurium and S. Enteritidis strains adhered to the cell wall product with an amount between 10(3) and 10(4) CFU/10 µg. Four out of 7 E. coli strains showed an average binding capability (10(2) CFU/10 µg) whereas 4×10(3) E. coli F4 cells bound per 10 µg yeast cell wall. E. coli 0149 K91, E. coli 0147 K89, C. jejuni and C. perfringens as well the genera lactobacilli and bifidobacteria did not bind to the yeast cell wall. E. coli Nissle 1917 was bound with 2×10(2) CFU/10 µg. These results demonstrate that cell wall from MTV can be used to differentially bind E. coli spp. and Salmonella spp. up to 8×10(4) CFU/10 µg. Thus certain yeast cell walls may prevent enteric infections caused by selective bacteria. This methodical approach would be an accurate tool in the feed industry for quality control of yeast cell wall products.


Subject(s)
Bacterial Adhesion , Cell Wall/chemistry , Fungal Proteins/isolation & purification , Fungal Proteins/metabolism , Gram-Negative Bacteria/physiology , Trichosporon/chemistry , Animals , Biomass , Colony Count, Microbial , Gram-Negative Bacteria/isolation & purification , Gram-Negative Bacteria/metabolism , Gram-Positive Bacteria/isolation & purification , Gram-Positive Bacteria/metabolism , Gram-Positive Bacteria/physiology , Poultry/microbiology , Protein Binding , Spectrophotometry , Swine/microbiology
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