Arthrospira platensis is one of the candidates expected to replace antibiotics by its immunostimulatory effects in broiler industry, but the evaluation aimed at field applications is not enough. Here, we measured general immunological indicators such as specific antibody responses against sheep red blood cell and Brucella abortus, serum immunoglobulin concentrations and monocyte phagocytic capacity of broiler chickens, which assigned to four dietary treatment groups: A. platensis at 0, 0.01, 0.1 and 1% was added to their normal feed. Then, the 0.01 to 1% groups were compared to the 0% group. In specific antibody responses, the 0.1% group maintained a higher antibody titer against sheep red blood cells, while the 0.01% group did against Brucella abortus after the secondary response. Regarding serum immunoglobulin concentrations, IgG levels of the 0.1 and 1% groups were significantly higher, while IgA levels showed no significant differences. In the phagocytosis assay, each supplemented group showed an increase of the phagocytic capacity of blood monocytes. In several tests, the 1% group presented heteroscedasticity, i.e., some individuals showed high responses, while others presented poor responses. These observations indicate that dietary A. platensis enhances not systemic but some particular immune responses in broiler chickens and a high level of supplementation may inhibit this effect. Therefore, a dietary supplementation of 0.1% of A. platensis with some immunomodulatory substances that enhance mucosal immunity is suitable for upregulating the systemic immune response in broiler chickens.
We studied the binding and catabolic function of adherent monocytes from patients with rheumatoid arthritis (RA) and normal subjects using stable, heat aggregates of IgG125I (A-IgG) as a model for soluble immune complexes. Scatchard plots of 4 degrees C binding data showed that RA monocytes had increased binding avidity and higher maximal binding capacity for A-IgG compared with monocytes from normal subjects. These data suggest that RA monocytes have increased numbers of Fc receptors for IgG, although a concomitant increase in the avidity of individual Fc receptors could not be excluded. At 37 degrees C, RA monocytes; kinetic analysis suggested that increases in catabolized A-IgG were due to increased binding of A-IgG with no change in the fractional rates of catabolism. Latex titers of RA patients correlated with the number of Fc receptors detected on RA monocytes. Mononuclear phagocytes from RA patients are often exposed to endogenous immune complexes that may be present in the blood of such patients; immune complexes may stimulate monocytes and possibly other mononuclear phagocytes to increase their capacity to bind and catabolize soluble immune complexes.
We studied the binding and degradation of stable, soluble heat aggregates of 125I-IgG (A-IgG) by monocytes from 30 patients with systemic lupus erythematosus (SLE) and 30 normals. Relative avidities (KE) for Fc receptor (FcR) binding of A-IgG and maximal binding of A-IgG by monocytes were determined from Scatchard plots of binding data obtained at 4 degrees C. Rates of degradation (Vmax) of A-IgG at 37 degrees C were calculated from Lineweaver-Burke plots of the Michaelis-Menton equation. KE were decreased in SLE monocytes (15.5 X 10(-9) L/M) as compared with normals (20.1 X 10(-9) L/M, p less than 0.005) and Vmax were decreased for SLE (0.89 ng/hr) as compared with normals (1.11 ng/hr, p less than 0.005). The maximal FcR binding by SLE monocytes was not statistically different in SLE patients and normals, but monocytes from SLE patients with active disease showed a lower maximal binding capacity for A-IgG (4.9 ng/10(5) cells) than normals (5.4 ng/10(5) cells, p less than 0.05). KE and Vmax in SLE were also lower for patients with active disease than for normal subjects. KE in patients whose anti-ssDNA binding was greater than 20% were lower than for those with DNA binding of less than 20% (p less than 0.005). These data suggest that patients with active SLE have diminished numbers of available FcR on their circulating monocytes, possibly due to interiorization of FcR during endocytosis of endogenous circulating immune complexes.
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