Correction: Beneficial bacteria inhibit cachexia.

[This corrects the article DOI: 10.18632/oncotarget.7730.

Dietary supplementation of encapsulated organic acids enhances performance and modulates immune regulation and morphology of jejunal mucosa in piglets.

The aim of the study was to test two encapsulated regimens containing organic acids and/or zinc oxide (ZnO) on weaned piglet performance and jejunal mucosa morphology and immunity. For that, weaned piglets were allocated to treatments including control, supplemented with encapsulated organic acids (ACID group), and supplemented with organic acids and ZnO, both encapsulated (ACIDplus group). Antibiotics were used at similar concentrations in all groups during the first two weeks, but withdrawn from the ACIDplus group during the last three weeks of the experiment.

Inactivation of CYLD in intestinal epithelial cells exacerbates colitis-associated colorectal carcinogenesis - a short report.

Purpose: CYLD is a tumor suppressor that has been linked to the development of various human malignancies, including colon cancer. The tumor-suppressing function of CYLD is associated with its deubiquitinating activity, which maps to the carboxyl-terminal region of the protein. In the present study we evaluated the role of intestinal epithelial CYLD in colitis-associated cancer using a conditional mouse CYLD inactivation model.

Beneficial bacteria inhibit cachexia.

Muscle wasting, known as cachexia, is a debilitating condition associated with chronic inflammation such as during cancer. Beneficial microbes have been shown to optimize systemic inflammatory tone during good health; however, interactions between microbes and host immunity in the context of cachexia are incompletely understood. Here we use mouse models to test roles for bacteria in muscle wasting syndromes.

Evaluation of the possible transmission of BSE and scrapie to gilthead sea bream (Sparus aurata).

In transmissible spongiform encephalopathies (TSEs), a group of fatal neurodegenerative disorders affecting many species, the key event in disease pathogenesis is the accumulation of an abnormal conformational isoform (PrP(Sc)) of the host-encoded cellular prion protein (PrP(C)). While the precise mechanism of the PrP(C) to PrP(Sc) conversion is not understood, it is clear that host PrP(C) expression is a prerequisite for effective infectious prion propagation. Although there have been many studies on TSEs in mammalian species, little is known about TSE pathogenesis in fish.