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Hereditary gingival fibromatosis (HGF) is a rare oral condition that may appear as an isolated entity or as part of a genetic disease or syndrome. Molecular and biochemical mechanisms that trigger this pathologic process are not completely understood. In this article, we present a rare case of hereditary gingival fibromatosis in conjunction with a syndromic phenotype, associated with a rare missense mutation of the KCNK4 gene. This mutation induces a change in the structure of the TRAAK channel belonging to the 2-pore potassium channels. The gain of function promoted by the mutation could represent the pathogenetic basis of gingival fibromatosis.

Sheep develop clinical diseases after 3-5 years after infection with Mycobacterium avium subsp. paratuberculosis (MAP). Clinical symptoms of paratuberculosis include persistent diarrhea and weight loss due to a chronic inflammation of the small intestine. Tissue alterations in the areas of the ileo-cecal junction are often observed. Here, we investigate the molecular processes underlying tissue damages in intestinal mucosa of 14 sheep showing either tuberculoid or lepromatous form of MAP enteritis. We found that E-cadherins, alpha-catenin and beta1-integrins were present at significant low levels in tissues of sheep affected by lepromatous form and that this pattern was associated with high expression of TGF-beta, IL-10, IL-1beta, and TNF-alpha and with a modest increase of CD4+ and CD25+ T cells. Tissues of sheep with the tuberculoid form showed high expression of IFNgamma, IL-12, and MCP-1 and a significant presence of CD4+ and CD25+ T cells. Finally, anti-transglutaminase (tTG) IgG1 antibodies were detected in sera of infected animal belonging to both groups, as already described for human inflammatory bowel diseases. Our results further stress the similarities in the clinical and histological features between ruminant paratuberculosis and human intestinal inflammatory diseases.

Donkey’s milk may be considered a valid alternative, for infant nutrition, to powdered milks, soybean milk or other formulas, since its composition in lipids and proteins is very close to human milk. The aim of the present study is to characterize “donkey’s milk” product, especially with regard to the protein fractions. Three different chromatographic approaches for donkey’s milk proteins separation are described, based on their different isoelectric points, hydrophobicity and molecular mass. The proteins obtained were further separated by sodium dodecyl sulphate polyacrylamide gel electrophoresis and identified by N-terminal sequencing. α S1 - and β-caseins, lysozyme, α-lactalbumin, β-lactoglobulin were identified. Furthermore, the content of α-lactalbumin, β-lactoglobulin, and lysozyme in donkey’s milk was determined by a reversed-phase HPLC method. The β-lactoglobulin and α-lactalbumin content was 3.75 and 1.8 mg/ml, respectively (mean values). The present study showed the nutritional properties of donkey’s milk characterized by low casein and high lysozyme content (1.0 mg/ml) compared with other kinds of milks.