Exigência de treonina digestível para suínos machos castrados dos 15 aos 30 kg

Dois experimentos com o objetivo de determinar a exigência de treonina digestível verdadeira para suínos machos castrados dos 15 aos 30 kg foram realizados. No primeiro (ensaio de digestibilidade) foram usados oito suínos machos castrados, com peso médio inicial de 30,3 kg PV, previamente submetidos à cirurgia de anastomose íleo retal, distribuídos em delineamento em blocos ao acaso, com dois tratamentos, quatro repetições e um animal por unidade experimental. Os tratamentos consistiram de uma dieta basal, com 15,7% de proteína bruta (PB) e 0,49% de treonina total, e uma dieta isenta de proteína, para determinar o coeficiente de digestibilidade ileal verdadeira da treonina da dieta basal. No segundo experimento, 40 suínos mestiços, machos castrados, com peso inicial médio de 15,3 kg PV, foram distribuídos em delineamento experimental de blocos ao acaso, com cinco tratamentos (0,49; 0,54; 0,59; 0,64; e 0,69% de treonina total), quatro repetições e dois animais por unidade experimental. Por meio das características de desempenho e teor de uréia no soro sangüíneo e do modelo quadrático e, ou, o descontínuo LRP, foi obtido o valor de 0,63% como a exigência de treonina total para suínos machos castrados dos 15 aos 30 kg. Ao considerar o coeficiente de digestibilidade ileal verdadeira da treonina da dieta basal (84,6%) determinado no ensaio de digestibilidade e o coeficiente de digestibilidade de 100% para a treonina sintética suplementada na ração, foi obtido o valor de 0,56% como exigência de treonina digestível verdadeira.Two studies were conducted to determine the true digestible threonine requirement for barrows from 15 to 30 kg live weight (LW). In the first (digestibility trial) were used eight barrows, averaging 30,3 kg LW initial weight, submitted previous to the ileum-rectal anastomosis surgery, were allotted to a randomized block design, with two treatments, four replicates and one animal per experimental unit. The treatments consisted of a basal diet, with 15.7% of crude protein (CP) and .49% of total threonine, and one a protein free diet, to determine the coefficient of true ileal digestibility of threonine in the basal diet. In the second experiment, 40 crossbred pigs, barrows, averaging 15.3 kg initial weight were allotted to a randomized block design, with five treatments (.49, .54, .59, .64, e .69% of total threonine), four replicates and two animals per experimental unit. Using performance traits and serum urea level and applying the quadratic and/or the broken line models, a requirement value of .63% total threonine for 15 to 30 kg barrows was obtained . Considering the threonine basal diet coefficient of true ileal digestibility (84.6%) and the supplemented crystalline threonine digestibility coefficient of 100%, a requirement value of .56% true digestible threonine was obtained

Selective adherence of IgA to murine Peyer's patch M cells: evidence for a novel IgA receptor.

M cells represent the primary route by which mucosal Ags are transported across the intestinal epithelium and delivered to underlying gut-associated lymphoid tissues. In rodents and rabbits, Peyer's patch M cells selectively bind and endocytose secretory IgA (SIgA) Abs. Neither the nature of the M cell IgR nor the domains of SIgA involved in this interaction are known. Using a mouse ligated ileal loop assay, we found that monoclonal IgA Abs with or without secretory component, but not IgG or IgM Abs, bound to the apical surfaces of Peyer's patch M cells, indicating that the receptor is specific for the IgA isotype. Human serum IgA and colostral SIgA also bound to mouse M cells. The asialoglycoprotein receptor or other lectin-like receptors were not detected on the apical surfaces of M cells. We used recombinant human IgA1 and human IgA2 Abs and domain swapped IgA/IgG chimeras to determine that both domains Calpha1 and Calpha2 are required for IgA adherence to mouse Peyer's patch M cells. This distinguishes the M cell IgA receptor from CD89 (FcalphaI), which binds domains Calpha2-Calpha3. Finally, we observed by immunofluorescence microscopy that some M cells in the human ileum are coated with IgA. Together these data suggest that mouse, and possibly human, M cells express an IgA-specific receptor on their apical surfaces that mediates the transepithelial transport of SIgA from the intestinal lumen to underlying gut-associated organized lymphoid tissues

Functional protective role for mucin glycosylated repetitive domains

Mucins carry out a number of protective roles, some of which are more easily studied than others. One mucin function is believed to be the protection of the mucosal epithelium against acidic and proteolytic damage in the stomach and intestines. In the present work, a portion of stomach mucin tandem repeat sequence (Muc6) was joined to the catalytic domain of a reporter enzyme [human milk cholesterol esterase (CE)] to determine whether the former can protect the latter protein from damage. This Muc6 domain replaced a unique series of glycosylated C-terminal repeats normally present in CE. The chimeric protein (CE/Muc6) was expressed in two different cell lines and its properties compared to recombinant full-length CE and a truncated version of CE which contained only the catalytic domain (CE/trunc). Results showed that both CE and CE/Muc6 were resistant to denaturation by acid and to proteolysis by pepsin at low pH values or by pancreatic proteases compared to CE/trunc. Thus, a stomach Muc6 domain is sufficient to confer stability on the CE catalytic domain, demonstrating a protective effect by a glycosylated mucin sequence