ABSTRACT
Necrotizing sialometaplasia (NS) is a benign self-limiting inflammatory disease of mucus-secreting glands, mainly involving the minor salivary glands. This lesion can mimic a malignant neoplasm, as more frequently it manifests as a submucosal swelling or as an ulcer of the palate. Awareness of the disease is crucial to avoid undue surgical treatment. We herewith report MR findings in a histologically proven case of NS.
Subject(s)
Granulomatosis with Polyangiitis/diagnosis , Oral Ulcer/diagnosis , Sialometaplasia, Necrotizing/diagnosis , Adult , Diagnosis, Differential , Female , Humans , Magnetic Resonance ImagingABSTRACT
Antiserum against homogeneous hog kidney D-amino-acid oxidase (D-amino-acid: oxygen oxidoreductase (deaminating), EC 1.4.3.3) was elicited in rabbits, and monospecific antibodies were prepared by affinity chromatography. The antibodies inhibited up to 90% of hog D-amino-acid oxidase activity, and 100% of the enzyme could be immunoprecipitated. The antibodies inhibited both holoenzyme and reconstituted apoprotein to a similar degree, indicating that they did not interfere with the FAD-binding site of the protein. The antibodies inhibited D-amino-acid oxidase activity from other mammalian species to a similar degree, while the enzyme activities from birds, amphibians, fishes and yeast were inhibited and immunoprecipitated to lower extents. In immunoblotting experiments, after SDS-polyacrylamide gel electrophoresis, the antibodies recognized a single band of about 40 kDa in all the species analyzed, and the entity of the signal was inversely related to the phylogenetic distance from mammals. The antibodies did not inhibit D-alanine dehydrogenase activity from Escherichia coli, but gave positive bands in immunoblotting.
Subject(s)
Antibodies/immunology , D-Amino-Acid Oxidase/immunology , Kidney/enzymology , Amphibians , Animals , Birds , D-Amino-Acid Oxidase/metabolism , Electrophoresis, Polyacrylamide Gel , Epitopes/immunology , Escherichia coli/enzymology , Fishes , Immunoassay , Immunosorbent Techniques , Kinetics , Mammals , Rhodotorula/enzymology , Species Specificity , SwineABSTRACT
The intracellular localization of D-amino acid oxidase in rat kidney and liver has been investigated using the indirect immunogold postembedding technique. Different fixation and embedding conditions for optimal preservation of antigenicity and fine structure have been tested. Immunolabelling was possible only in tissues embedded in polar resins (glycol methacrylate and Lowicryl K4M). In kidney the enzyme was demonstrable only in the peroxisomes of the proximal tubule, where it was associated with the peroxisome core. The enzyme was present in all the peroxisomes of the proximal tubule and appeared to be codistributed with catalase. Control experiments and quantitative analysis confirmed the specificity of the D-amino acid oxidase immunolocalization. All the other cells in kidney failed to demonstrate any labelling. In liver, the immunolabelling was present in the matrix of the hepatocyte peroxisomes, whereas no traces of the enzyme were found in the nucleoid. The intensity of the immunolabelling in liver peroxisomes was lower than in kidney. No specific labelling was observed in cells other than hepatocytes.
