Effect of graded inclusion of dietary soybean meal on nutrient digestibility, health, and metabolic indices of adult dogs.

Two studies were conducted using adult dogs to evaluate the effect of increasing the inclusion of soybean meal (SBM) in an adult dog food on body composition, hematological and biochemical blood analyses, and total tract nutrient digestibility. Nutritionally complete and balanced diets were formulated with commercial-grade SBM (48% CP) to replace 0, 10, 20, or 30% of the protein provided by dried chicken protein resulting in final SBM inclusion of 0, 6.0, 11.5, and 17.0% (as-fed basis), respectively. In study 1, diets were fed during a 24-wk feeding trial using 36 female (spayed), adult hounds to evaluate food intake, BW, body composition, and blood measurements. There were no diet-related differences in food intake or BW. Body composition responded in a quadratic manner to increased dietary SBM inclusion with the percentage (%) of lean mass responding positively (P < 0.05) and absolute amounts of fat mass and percent body fat responding negatively (P < 0.05). All diagnostic blood components remained within normal physiological ranges for healthy, adult dogs. Serum concentrations of C-reactive protein and IGF-1 were similar among diets. In study 2, diets were evaluated in a digestibility study using 12 adult dogs in a 4 × 4 Latin square design. Increased SBM inclusion was associated with linear increases in the digestibility of CP (P < 0.05) and fat (P < 0.05) and CP retention (P < 0.05). Linear reductions in fecal DM content (P < 0.01) and increased fecal output (P < 0.05) were noted with increased SBM inclusion. All diets were similar in DE and ME content, but a quadratic trend was noted with increased SBM inclusion when DE (P = 0.083) and ME (P = 0.062) were expressed per unit of metabolic body size. Overall, it can be inferred from these results that the partial replacement of dried chicken protein with SBM in a nutritionally complete and balanced diet does not compromise the nutritional status and long-term health of adult dogs.

Sgk1 enhances RANBP1 transcript levels and decreases taxol sensitivity in RKO colon carcinoma cells.

The serum- and glucocorticoid-regulated kinase (Sgk1) is essential for hormonal regulation of epithelial sodium channel-mediated sodium transport and is involved in the transduction of growth factor-dependent cell survival and proliferation signals. Growing evidence now points to Sgk1 as a key element in the development and/or progression of human cancer. To gain insight into the mechanisms through which Sgk1 regulates cell proliferation, we adopted a proteomic approach to identify up- or downregulated proteins after Sgk1-specific RNA silencing. Among several proteins, the abundance of which was found to be up- or downregulated upon Sgk1 silencing, we focused our attention of RAN-binding protein 1 (RANBP1), a major effector of the GTPase RAN. We report that Sgk1-dependent regulation of RANBP1 has functional consequences on both mitotic microtubule activity and taxol sensitivity of cancer cells.

Functional analysis of R75Q mutation in the gene coding for Connexin 26 identified in a family with nonsyndromic hearing loss.

Mutations in the gene (GJB2) coding for Connexin 26 (Cx26) are responsible for genetic forms of sensorineural hearing loss. This article describes a family characterized by congenital profound hearing loss, inherited in an autosomal dominant fashion and associated to a R75Q substitution in Cx26. Cell transfection and fluorescence imaging, dye transfer experiments and dual patch clamp recording showed that the mutant completely prevents the formation of functional channels despite assembling into junctional plaques, in communication incompetent HeLa cells. The disease is not associated with palmar and plantar keratosis in any of the family members, suggesting that R75Q substitution is not sufficient for the development of the complete syndromic phenotype. The association of palmar and plantar keratosis with profound hearing loss may be dependent on genetic background, requiring a functional interaction between the mutated Cx26 and other epidermally expressed connexins.