Assessment of Disease Activity in Small Bowel Crohn's Disease: Comparison between Endoscopy and Magnetic Resonance Enterography Using MRIA and Modified MRIA Score.

Objectives. To retrospectively compare the results of the MRIA (magnetic resonance index of activity) with a modified MRIA (mMRIA), which was calculated excluding from MRIA formula the data of relative contrast enhancement (RCE). Materials and Methods. MR-E and corresponding endoscopic records of 100 patients were reviewed. MRIA, mMRIA, and SES endoscopic index were calculated for all the patients. Namely, MRIA was calculated as follows: (1.5 × wall thickening + 0.02 × RCE + 5 × intramural edema + 10 × ulcers), while mMRIA was calculated with the modified formula (1.5 × wall thickening + 5 × intramural edema + 10 × ulcers). Results. Mean MRIA and mMRIA values were 19.3 and 17.68, respectively (p < 0.0001). A significant correlation (p < 0.0001) was observed between MRIA and mMRIA scores and between both MR indexes and SES (p < 0.0001). Conclusions. mMRIA was comparable to MRIA in the evaluation of disease activity in Crohn's disease.

Residue analysis of glucocorticoids in bovine milk by liquid chromatography-tandem mass spectrometry.

A sensitive liquid chromatography-tandem mass spectrometry (LC-MS/MS) method for the simultaneous determination of 13 steroidal anti-inflammatory drugs in bovine milk is presented. Due to their weakly acid nature, analytes were separated by ion suppression reversed phase chromatography and detected in positive-ion mode by a high flow electrospray source. Dexamethasone-d4 was used as internal standard. The sample preparation was simple and reliable; it included acidic deproteinization of milk followed by sample enrichment and clean-up, utilizing a C18 solid phase extraction cartridge. Recoveries exceeded 70% with an intra-day precision not larger than 12%. The efficiency of the sample clean-up and internal standardization rendered negligible the matrix effect, estimated by comparing standard and matrix-matched calibration curves. A small-scale reconnaissance was carried out on several raw and whole fresh milk samples. A large number of analyzed samples showed a chromatographic peak, in the retention time window of cortisol, at levels included between its decision limit (CCalpha) and detection capability (CCbeta). As a result of a heat-induced transformation, an isomeric product of triamcinolone was observed during the extract evaporation. Since this rearrangement might occur during the milk pasteurization process, LC-MS/MS and (1)H-NMR investigations were performed out to conclusively differentiate the two isomers. One- and two-dimensional proton NMR spectra were able to identify the transformation product as 9a-fluoro-11b,16a-trihydroxy-17b-hydroxymethyl-D-homoandrosta-1,4-diene-3,17a-dione.

Specific adducts formed through a radical reaction between peptides and contact allergenic hydroperoxides.

The first step in the development of contact allergy (allergic contact dermatitis) includes the penetration of an allergy-causing chemical (hapten) into the skin, where it binds to macromolecules such as proteins. The protein-hapten adduct is then recognized by the immune system as foreign to the body. For hydroperoxides, no relevant hapten target proteins or protein-hapten adducts have so far been identified. In this work, bovine insulin and human angiotensin I were used as model peptides to investigate the haptenation mechanism of three hydroperoxide haptens: (5R)-5-isopropenyl-2-methyl-2-cyclohexene-1-hydroperoxide (Lim-2-OOH), cumene hydroperoxide (CumOOH), and 1-(1-hydroperoxy-1-methylethyl) cyclohexene (CycHexOOH). These hydroperoxides are expected to react via a radical mechanism, for which 5,10,15,20-tetraphenyl-21H,23H-porphine iron(III) chloride (Fe(III)TPPCl) was used as a radical initiator. The reactions were carried out in 1:1 ethanol/10 mM ammonium acetate buffer pH 7.4, for 3 h at 37 degrees C, and the reaction products were either enzymatically digested or analyzed directly by MALDI/TOF-MS, HPLC/MS/MS, and 2D gel electrophoresis. Both hydroperoxide-specific and unspecific reaction products were detected, but only in the presence of the iron catalyst. In the absence of catalyst, the hydroperoxides remained unreacted. This suggests that the hydroperoxides can enter into the skin and remain inert until activated. Through the detection of a Lim-2-OOH adduct bound at the first histidine (of two) of angiotensin I, it was confirmed that hydroperoxides have the potential to form specific antigens in contact allergy.