Effects of coated sodium butyrate on growth performance, intestinal morphology, and caecal short-chain fatty acids of growing Pekin ducks.

1. A dose‒response experiment with six supplemental levels of coated sodium butyrate (CSB) (0, 250, 500, 750, 1,000, and 1,250 mg/kg) was conducted to investigate its effects on growth performance, intestinal morphology, and caecal short-chain fatty acids of growing Pekin ducks aged 14 to 35 d. A total of 288 male 14-d-old Pekin ducks were randomly allocated to six dietary treatments. Each treatment had eight replicate pens of six ducks per pen.2. The daily weight gain, daily feed intake, and feed/gain of ducks from 14 to 35 d of age were not influenced by increasing CSB levels. The relative weight and length of the duodenum, jejunum, and caecum increased linearly or quadratically as supplemental CSB increased (P < 0.05).3. For the ileum and caecum, the villus height and height/crypt depth increased linearly or quadratically, and the villus crypt depth decreased linearly as the supplemental CSB increased (P < 0.05). As supplemental CSB increased, the goblet cell numbers of the ileum increased and decreased and changed quadratically (P < 0.05), but caecal goblet cell number increased quadratically (P < 0.05). Increasing the CSB level linearly or quadratically elevated the concentrations of propionic acid and butyric acid in the caecum (P < 0.05).4. It was concluded that CSB can be used as a safe and effective feed additive to promote the intestinal integrity of growing ducks by improving intestinal morphology and increasing the concentration of caecal short-chain fatty acids.

Expression of P-cadherin in gastric carcinomas and its reduction in tumor progression.

The expression of P-cadherin, one of the Ca(2+)-dependent cell-cell adhesion molecules, in human gastric carcinomas was examined by Northern blotting, Western blotting and immunohistochemistry. P-cadherin mRNA was expressed in all the gastric carcinoma tissues examined, whereas no message was detected in non-neoplastic mucosa. By Western-blot analysis, P-cadherin protein was expressed in 83% and 29% of the well-differentiated and poorly differentiated gastric adenocarcinomas, respectively, the incidence being significantly different. Immunohistochemically, P-cadherin immunoreactivity was localized on the cell surface or the cell-to-cell borders of well-differentiated adenocarcinomas. P-cadherin was not detected in Borrmann's type-4 or scirrhous carcinomas where the tumor cells proliferate diffusely with productive fibrosis. The level of P-cadherin expression in stage-2 carcinomas was significantly higher than in stage-I carcinomas. In the case of patients in stages 2 to 4, however, the level of P-cadherin expression decreased as the stage progressed, the difference between stages 2 and 3 and between stages 3 and 4 being significant. Our findings suggest that P-cadherin might play an important role in the development of well-differentiated gastric adenocarcinomas and the decreased expression of P-cadherin might be responsible for the infiltrative growth and progression of gastric carcinomas.

Expression of transforming growth factor alpha in human tissues: immunohistochemical study and northern blot analysis.

The expression of transforming growth factor alpha (TGF-alpha) was examined in various human tissues and the fetus, using immunohistochemistry and Northern blot analysis. TGF-alpha immunoreactivity was detected mainly in the epithelial cells of the digestive tract, liver, pancreas, kidney, thyroid, adrenal, skin, mammary gland and genital organs. In the digestive tract, epithelial cells with regenerative change or hyperplastic change showed strong immunoreactivity to TGF-alpha. Peripheral nerve, vessels, megakaryocytes and macrophages in the lung and spleen were also positive for TGF-alpha. By Northern blot analysis the expression of TGF-alpha mRNA was confirmed in the digestive tract, salivary gland, thyroid, kidney and mammary gland. In the human fetus, the nerve tissues, liver, adrenal and kidney were positive for TGF-alpha. Strong immunoreactivity to TGF-alpha was observed in the hepatocytes of the fetus. These findings indicate that TGF-alpha is produced by a variety of non-neoplastic cells in both adult and fetal tissues.

An electron microscopic, immunogold analysis of glutamate and glutamine in terminals of rat spinocerebellar fibers.

A semiquantitative, electron microscopic immunocytochemical procedure based on the use of colloidal gold particles as markers was employed to analyze the subcellular distribution of glutamate and glutamine, a major glutamate precursor, in a subpopulation of spinocerebellar mossy fiber terminals. These terminals were identified by anterograde transport of a horseradish peroxidase-wheat germ agglutinin conjugate, injected in the thoracic spinal cord. Gold particles signalling glutamate-like immunoreactivity were enriched over clusters of synaptic vesicles relative to organelle-free cytoplasmic matrix, and there was a strong positive correlation between gold particle and synaptic vesicle densities (correlation coefficient 0.94). Gold particles indicating glutamine-like immunoreactivity showed a much weaker correlation with vesicle density (correlation coefficient 0.36) and were about equally concentrated over cytoplasmic matrix as over clusters of synaptic vesicles. Compared with the mossy fibers, the putative GABAergic Golgi cell terminals exhibited a lower level of glutamate-like immunoreactivity, which was very weakly correlated with the vesicle density (correlation coefficient 0.27). The level of glutamine-like immunoreactivity in the Golgi cell terminals was similar to that in mossy fibers, but much lower than that in glial cells. The anterogradely labelled mossy fiber terminals were not enriched in immunoreactivities for aspartate or GABA. These results suggest that the level and subcellular distribution of glutamate in presumed glutamatergic terminals differs from that in terminals in which glutamate only serves metabolic or precursor roles, and that these differences can be exploited in immunocytochemical studies aimed at identifying glutamate-using neurons. In contrast, glutamine immunocytochemistry does not seem to be generally useful in this regard.