Interactions between starch source and gelatinisation degree on performance and small intestinal digestion in broiler chickens.

1. A 2 × 2 factorial arrangement was used to test the hypothesis that, in pelleted diets, legume starch is digested less rapidly and to a lesser extent than cereal starch, and that increased gelatinisation through extrusion would eliminate the differences between the starch sources. In addition, the trial examined whether a lower ratio of starch to nitrogen disappearance rate (SNDR) could improve feed conversion ratio (FCR).2. At 17 d of age, male broilers were randomly distributed among four dietary treatments, consisting of either wheat or faba bean starch-rich fraction (FBS) as the sole starch source and pelleting or extrusion as processing methods. Each treatment had 10 replicate pens containing five birds each.3. Extrusion resulted in a more extensive starch gelatinisation compared to pelleting, as expected.4. No difference in weight gain at 29 d of age was observed between birds fed starch sources. However, birds fed wheat tended (P = 0.080) to have better FCR than those fed FBS, while the effect of processing methods was insignificant. Thus, there was no interaction between starch source and processing method on FCR.5. In pelleted diets, FBS had lower and slower starch digestibility compared to wheat in all intestinal segments (P < 0.05). The interaction between starch source and processing method in all intestinal segments (P < 0.001) demonstrated that FBS responded more to gelatinisation through extrusion than did wheat. Thus, differences in starch digestibility between the wheat and FBS were eliminated with extrusion.6. Feeding extruded diets significantly increased the upper jejunal expression of GLUT1, GLUT2 and SGLT1 compared to pelleted diets, which suggested that glucose absorption was less likely to be a limiting factor for starch utilisation.7. Pelleting resulted in a lower ratio (P < 0.001) of SNDR compared to extrusion (on average 1.4-fold) but did not improve FCR.

Passage rate through the anterior digestive tract of broiler chickens fed on diets with ground and whole wheat.

1. Birds were fed diets containing ground or whole wheat and titanium dioxide for 10 min, followed by dissection of 4 birds per treatment after 30, 60, 90, 120, 150 and 180 min. 2. The crop, proventriculus and gizzard, duodenum, jejunum, and ileum from each bird were dried and combusted, and titanium content in each section was determined. 3. Significant amounts of titanium were found in the small intestine of the birds as soon as 30 min after being given feed containing titanium, and significant amounts had passed the small intestine after 120 to 150 min. 4. Titanium contents equivalent to approximately 5 g feed were eliminated from the gizzard per hour independently of whether ground or whole wheat was used. Thus, a hypothesis that the use of whole grain would slow down passage rate through the upper digestive tract was not supported by the current results.

Effect of highly purified porcine gut glucagon-like immunoreactivity (glicentin) on glucose release from isolated rat hepatocytes.

We studied the effect of the highly purified gut peptide glicentin on the glucose production and cyclic AMP accumulation of isolated rat hepatocytes. Glicentin at 2.10(-7) mol/l had the same effect on glucose production as maximally effective concentrations of glucagon, but did not stimulate cyclic AMP to the same extent; furthermore, glicentin apparently had only 1/100 of the potency of glucagon on glucose production. During incubation with hepatocytes glicentin was degraded to low molecular weight fragments one of which were chromatographically very similar to fragments of glucagon. It is suggested that glicentin exerts its glucagon-like effects on hepatocytes only after degradation to glucagon-like fragments. The results also demonstrate that the coupling between cyclic AMP accumulation and glucose production depends on the nature of the stimulatory peptide.

Glicentin immunoreactive cells: their relationship to glucagon-producing cells.

The cellular and subcellular localization of one of the gut glucagon-like immunoreactants (GLI-1 or glicentin) and the relative distribution of glicentin- and glucagon-containing cells were investigated by immunocytochemistry. By immunofluorescence, the antiglicentin serum, which does not react with glucagon, revealed positive cells in the islets of Langerhans and in the gut mucosa, particularly in the terminal ileum and colon. In the intestinal mucosa, it was proven ultrastructurally that the glicentin immunoreactive cells correspond to the L cell and that the secretory granules represent the storage compartment of the immunoreactive material. In pancreatic islets, consecutive semithin sections treated with antiglicentin and specific antiglucagon sera showed that the same A cell population reacted with both sera, while immunoperoxidase staining on thin sections revealed that the immunoreactive material was confined to the secretory granules. The same results were obtained on dog oxyntic mucosa, where the glicentin- and glucagon-containing cells were identified as the gastric A cell. The immunocytochemical demonstration of a common glicentin-like material in the A and L cells together with the known presence of a common immunoreactant in glicentin and glucagon strongly support the idea that the A and L cells are ontogenetically related and synthesize their secretory product via a glicentin-like precursor which, by specific cleavage, could yield glucagon and gut glucagon-like immunoreactants.

Sequence analysis of porcine gut GLI-1.

A protein from porcine gut with 100 amino acid residues (porcine gut GLI-1) and having glucagon-like immunoreactivity has been characterized by partial sequences. The sequence of the C-terminal amino acid residues is -Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala and includes the C-terminal amino acid residue sequence (-Met-Asn-Thr) of porcine glucagon. Evidence is presented that the glucagon sequence -Thr-Ser-Asp-Tyr-Ser-Lys-Tyr- is found in the gut GLI-1 as well. The data support the theory that gut GLI-1 contains the full glucagon sequence and that gut GLI-1 and glucagon are formed from a common precursor.

Purification and characterization of a protein from porcine gut with glucagon-like immunoreactivity.

A protein with glucagon-like immunoreactivity has been isolated from porcine intestine in a highly purified form. The isoelectric point is 6.8-6.9, and the molecular weight is 11,625, as calculated from its amino acid composition: this estimate has been confirmed by S.D.S. gel electrophoresis. The partial sequence so far elucidated is from the N-terminal: Arg-Ser-Leu-Gin-Asn-Thr-Glx-Glx-Lys-Ala-Arg-Ser-Phe-, and from the C-terminal: -Ile-Ala, both differing from those of porcine pancreatic glucagon. On a molar basis the protein has the same immunoreactivity as porcine glucagon when assayed with some anti-glucagon sera, while the activity is less than 0.2% using other anti-glucagon sera.