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At least 19 recordsLinked to original sources
PubMed2001

Vitrification of mouse oocytes in ethylene glycol-raffinose solution: effects of preexposure to ethylene glycol or raffinose on oocyte viability.

We investigated the effects of preexposure to ethylene glycol (EG) or raffinose on the viability of vitrified mouse oocytes. Ovulated oocytes at the metaphase II stage were preexposed either to 2 M EG for 0, 2, or 5 min or to ascending concentrations (0.15 followed by 0.3 M ) of raffinose solution for 2, 5, or 10 min each (here referred to as 2-2, 5-5, and 10-10 min, respectively). The oocytes were then exposed to a vitrification solution (VS), 6 M EG + 0.3 M raffinose, for 0.5, 1, 2, or 5 min and then vitrified or immediately diluted. After warming, the developmental capacity of oocytes was determined after in vitro fertilization. Volume changes in oocytes during preexposures and exposure to the VS were also investigated. The results demonstrated that preexposure to 2 M EG allowed shorter exposure times of oocytes to the VS and that predehydration in raffinose solutions for 5-5, but not 2-2 or 10-10 min, allowed a wider range of exposure times to the VS. Experiments on volume change suggested that the optimum time of exposure to the VS depends on the amount of EG permeation after preexposure to 2 M EG or to raffinose solutions. Preexposures to 2 M EG or raffinose under optimized conditions increased the viability of vitrified-warmed oocytes compared to direct exposure to VS without preexposures.

Animals↗
PubMed2002

Functional expression of a cDNA encoding pea (Pisum sativum L.) raffinose synthase, partial purification of the enzyme from maturing seeds, and steady-state kinetic analysis of raffinose synthesis.

Raffinose (O-alpha- D-galactopyranosyl-(1-->6)- O-alpha- D-glucopyranosyl-(1<-->2)- O-beta- D-fructofuranoside) is a widespread oligosaccharide in plant seeds and other tissues. Raffinose synthase (EC 2.4.1.82) is the key enzyme that channels sucrose into the raffinose oligosaccharide pathway. We here report on the isolation of a cDNA encoding for raffinose synthase from maturing pea ( Pisum sativum L.) seeds. The coding region of the cDNA was expressed in Spodoptera frugiperda Sf21 insect cells. The recombinant enzyme, a protein of glycoside hydrolase family 36, displayed similar kinetic properties to raffinose synthase partially purified from maturing seeds by anion-exchange and size-exclusion chromatography. Apart from the natural galactosyl donor galactinol ( O-alpha- D-galactopyranosyl-(1-->1)- L- myo-inositol), p-nitrophenyl alpha- D-galactopyranoside, an artificial substrate, was utilized as a galactosyl donor. An equilibrium constant of 4.1 was determined for the galactosyl transfer reaction from galactinol to sucrose. Steady-state kinetic analysis suggested that raffinose synthase is a transglycosidase operating by a ping-pong reaction mechanism and may also act as a glycoside hydrolase. The enzyme was strongly inhibited by 1-deoxygalactonojirimycin, a potent inhibitor for alpha-galactosidases (EC 3.2.1.22). The physiological implications of these observations are discussed.

Algorithms↗
PubMed2006

Different utilization of glucose and raffinose in Bifidobacterium breve and Bifidobacterium animalis.

Growth of 2 strains of Bifidobacterium breve and 4 strains of Bifidobacterium animalis was evaluated with glucose, raffinose or a mixture of glucose and raffinose as substrates. All strains of B. animalis and one strain of B. breve grew more slowly on glucose than on raffinose or the mixture of glucose and raffinose; one strain of B. breve grew more rapidly on the mixture of glucose and raffinose than on raffinose while 2 strains of B. animalis grew faster on raffinose than on the mixture of raffinose and glucose. Both strains of B. breve utilized glucose and raffinose simultaneously. In contrast, all strains of B. animalis strains displayed atypical growth with rapid utilization of raffinose followed by slow utilization of glucose. The cell morphology of all strains of B. animalis was affected by the sugar used for cultivation: tiny and rather spherical cells were observed on glucose while on media with raffinose the cells were large and had the species-specific shape. Description of preferential utilization of various saccharides by bifidobacteria can contribute to the development of new synbiotic preparations and new cultivation media for bifidobacteria.

Animals↗
PubMed2004

Reduction of allergic airway eosinophilia by dietary raffinose in Brown Norway rats.

Oral administration of raffinose, a naturally occurring indigestible oligosaccharide, has reportedly ameliorated atopic dermatitis in human subjects although the mechanism is unknown. The present study investigated the effect of dietary raffinose on allergen-induced airway eosinophilia in ovalbumin-sensitised Brown Norway rats as an atopic disease model. Brown Norway rats were immunised by subcutaneous injection with ovalbumin on day 0 and fed either a control diet or the diet supplemented with raffinose (50 g/kg diet). The rats were exposed to aerosolised ovalbumin on day 20, and broncho-alveolar lavage fluid was obtained on the next day. The number of eosinophils in the fluid was significantly lower in the rats fed the raffinose diet than in those fed the control diet. Dietary raffinose significantly reduced IL-4 and IL-5 mRNA levels in lung tissue and tended to lower ovalbumin-specific Ig E levels. Suppression of eosinophilia by dietary raffinose was still observed in caecectomised and neomycin-administered rats, suggesting little contribution by the colonic bacteria to the effect of raffinose. Intraperitoneal administration of raffinose also suppressed eosinophilia. Significant concentrations of raffinose were detected in portal venous and abdominal arterial plasma after the intragastric administration of raffinose. Overall, the findings suggest that dietary raffinose ameliorates allergic airway eosinophilia at least partly via post-absorptive mechanisms in Brown Norway rats.

Allergens↗
PubMed2005

Raffinose crystallization during freeze-drying and its impact on recovery of protein activity.

PURPOSE: To study i) phase transitions in raffinose solution in the frozen state and during freeze-drying and ii) evaluate the impact of raffinose crystallization on the recovery of protein activity in reconstituted lyophiles. METHODS: X-ray powder diffractometry (XRD) and differential scanning calorimetry (DSC) were used to study the frozen aqueous solutions of raffinose pentahydrate. Phase transitions during primary and secondary drying were monitored by simulating the entire freeze-drying process, in situ, in the sample chamber of the diffractometer. The activity of lactate dehydrogenase (LDH) in reconstituted lyophiles was determined spectrophotometrically. RESULTS: Raffinose formed a kinetically stable amorphous freeze-concentrated phase when aqueous solutions were frozen at different cooling rates. When these solutions were subjected to primary drying without annealing, raffinose remained amorphous. Raffinose crystallized as the pentahydrate when the solutions were annealed at a shelf temperature of -10 degrees C. Primary drying of these annealed systems resulted in the dehydration of raffinose pentahydrate to an amorphous phase. The phase separation of the protein from the amorphous raffinose in these two systems during freeze-drying resulted in a significant reduction in the recovery of LDH activity, even though the lyophile was amorphous. CONCLUSIONS: Annealing of frozen aqueous raffinose solutions can result in solute crystallization, possibly as the pentahydrate. The crystalline pentahydrate dehydrates during primary drying to yield an amorphous lyophile. Raffinose crystallization during freeze-drying is accompanied by a significant loss of protein activity.

Calorimetry, Differential Scanning↗
PubMed2001

Raffinose improves 24-hour lung preservation in low potassium dextran glucose solution: a histologic and ultrastructural analysis.

BACKGROUND: We have previously shown that the addition of raffinose to low potassium dextran (LPD) preservation solution improves transplanted rat lung function after 24 hours of storage. The mechanisms by which raffinose acts are unclear. The aim of this study was to examine the histologic and ultrastructural correlates of this enhanced pulmonary function after preservation with raffinose. METHODS: In a randomized, blinded study, rat lungs were flushed with LPD, or LPD containing 30 mmol/L of raffinose, and stored for 24 hours at 4 degrees C. Control lungs were flushed with LPD but not stored (n = 5 each group). Changes in postpreservation edema were determined. In addition, lungs were flushed with a trypan blue solution to quantify cell death, and examined using both light and electron microscopy. RESULTS: The LPD lungs gained significantly more weight (25.5%+/-5.5%) compared with raffinose-LPD lungs (5.2%+/-5.3%; p < 0.0001). There were higher percentages of dead cells in the LPD lungs (29%+/-0.3% of total cells) compared with raffinose-LPD lungs (14%+/-1.4%; p < 0.001) and control lungs (0.2%+/-5%; p < 0.001). Control lungs maintained normal ultrastructure, whereas LPD lungs showed a decreased number of intact type II pneumocytes and significant cellular necrosis. Interstitial and alveolar edema with interstitial macrophage infiltration was also observed. Alveolar capillaries were collapsed. In contrast, raffinose-LPD lungs showed only mild alterations such as minimal interstitial edematous expansion, fewer damaged cells, and minimal capillary injury. CONCLUSIONS: Raffinose exerts a cytoprotective effect on pulmonary grafts during preservation, which explains the previously documented improved function. This simple modification of LPD with raffinose may provide clinical benefit in extended pulmonary preservation.

Animals↗
PubMed1999

O-raffinose cross-linking markedly reduces systemic and renal vasoconstrictor effects of unmodified human hemoglobin.

The hemodynamic effects of a 20% exchange-transfusion with different solutions of highly purified human hemoglobin A-zero (A0) were evaluated. We compared unmodified hemoglobin with hemoglobin cross-linked with O-raffinose. Unmodified hemoglobin increased systemic vascular resistance and mean arterial pressure more than the O-raffinose cross-linked hemoglobin solution (by approximately 45% and approximately 14%, respectively). Unmodified hemoglobin markedly reduced cardiac output (CO) by approximately 21%, whereas CO was unaffected by the O-raffinose cross-linked hemoglobin solution. Unmodified and O-raffinose cross-linked hemoglobin solutions increased mean arterial pressure to comparable extents ( approximately 14% and approximately 9%, respectively). Unmodified hemoglobin increased renal vascular resistance 2-fold and reduced the glomerular filtration rate by 58%. In marked contrast, the O-raffinose cross-linked hemoglobin had no deleterious effect on the glomerular filtration rate, renal blood flow, or renal vascular resistance. The extents to which unmodified and O-raffinose cross-linked hemoglobin solutions inactivated nitric oxide also were compared using three separate in vitro assays: platelet nitric oxide release, nitric oxide-stimulated platelet cGMP production, and endothelium-derived relaxing factor-mediated inhibition of platelet aggregation. Unmodified hemoglobin inactivated or oxidized nitric oxide to a greater extent than the O-raffinose cross-linked hemoglobin solutions in all three assays. In summary, O-raffinose cross-linking substantially reduced the systemic vasoconstriction and the decrease in CO induced by unmodified hemoglobin and eliminated the deleterious effects of unmodified hemoglobin on renal hemodynamics and function. We hypothesize that O-raffinose cross-linking reduces the degree of oxidation of nitric oxide and that this contributes to the reduced vasoactivity of this modified hemoglobin.

Animals↗
PubMed2005

Molecular mobility in raffinose in the crystalline pentahydrate form and in the amorphous anhydrous form.

PURPOSE: The aims of the study are to characterize the slow molecular mobility in solid raffinose in the crystalline pentahydrate form, as well as in the anhydrous amorphous form (Tg = 109 degrees C at 5 degrees C/min), and to analyze the differences and the similarities of the molecular motions in both forms. METHODS: Thermally stimulated depolarization current (TSDC) is used to isolate the individual modes of motion present in raffinose, in the temperature range between -165 and +60 degrees C. From the experimental output of the TSDC experiments, the kinetic parameters associated with the different relaxational modes of motion were obtained, which allowed a detailed characterization of the distribution of relaxation times of the complex relaxations observed in raffinose. The features of the glass transition relaxation in raffinose were characterized by differential scanning calorimetry (DSC). RESULTS: A complex mobility was found in the crystalline form of raffinose. From the analysis of the TSDC data, we conclude that these molecular motions are local and noncooperative. A sub-Tg relaxation, or secondary process, was also detected and analyzed by TSDC in the amorphous phase. It has low activation energy and low degree of cooperativity. The glass transition was studied by DSC. The fragility index (Angell's scale) of raffinose obtained from DSC data is m = 148. CONCLUSIONS: TSDC proved to be an adequate technique to study the molecular mobility in the crystalline pentahydrate form of raffinose. In the amorphous form, on the other hand, the secondary relaxation was analyzed by TSDC, but the study of the glass transition relaxation was not possible by this experimental technique as a consequence of conductivity problems. The DSC study of the glass transition indicates that raffinose is an extremely fragile glass former.

Calorimetry, Differential Scanning↗
PubMed2004

The role of raffinose in the cold acclimation response of Arabidopsis thaliana.

In many plants raffinose family oligosaccharides are accumulated during cold acclimation. The contribution of raffinose accumulation to freezing tolerance is not clear. Here, we investigated whether synthesis of raffinose is an essential component for acquiring frost tolerance. We created transgenic lines of Arabidopsis thaliana accessions Columbia-0 and Cape Verde Islands constitutively overexpressing a galactinol synthase (GS) gene from cucumber. GS overexpressing lines contained up to 20 times as much raffinose as the respective wild-type under non-acclimated conditions and up to 2.3 times more after 14 days of cold acclimation at 4 degrees C. Furthermore, we used a mutant carrying a knockout of the endogenous raffinose synthase (RS) gene. Raffinose was completely absent in this mutant. However, neither the freezing tolerance of non-acclimated leaves, nor their ability to cold acclimate were influenced in the RS mutant or in the GS overexpressing lines. We conclude that raffinose is not essential for basic freezing tolerance or for cold acclimation of A. thaliana.

Acclimatization↗
PubMed1998

Experimental use of raffinose as an osmotic agent for peritoneal dialysis.

Conventional glucose-based solutions for peritoneal dialysis fluids have been shown to raise problems of biocompatibility. We therefore evaluated the ultrafiltration capabilities of raffinose as an alternative osmotic agent in a non-uremic rat model. Animals were divided into four groups and injected intraperitoneally with solutions containing raffinose (4.5%, 345 mOsm/kg; 16.7%, 518 mOsm/kg) or glucose (1.5%, 346 mOsm/kg; 4.25%, 489 mOsm/kg). Data obtained from animals exposed to 16.7% raffinose were excluded because of precipitation of the osmotic agent. Low-osmolality raffinose solution induced higher ultrafiltered volume than the low-osmolality glucose-enriched fluid at 120 minutes of dwelling time. No significant differences were observed in effluent sodium and potassium concentration and protein dialysate-to-plasma (D/P) ratio. The D/P ratio of phosphate was higher in the low-osmolality raffinose-based fluid than in the low-osmolality glucose solution. The osmolality of the solutions was significantly decreased after a dwelling time of 120 minutes. We conclude that 4.5% raffinose is an effective osmotic agent. Total or partial replacement of glucose by raffinose for clinical peritoneal dialysis could be eventually considered after appropriate evaluation of its biocompatibility and general side effects.

Animals↗
PubMed1999

Structural and dynamic properties of crystalline and amorphous phases in raffinose-water mixtures.

PURPOSE: To obtain an improved characterisation of the raffinose-water solid-solid and solid-liquid state diagram, and to study the thermophysical behaviour of the solid amorphous phase. This information is expected to shed light on the potential of raffinose as a pharmaceutical excipient, for stabilising labile preparations at high temperatures. METHODS: X-ray diffraction, scanning electron microscopy, polarised-light microscopy, differential scanning calorimetry (DSC) and thermogravimetric analysis (TGA) were applied to study raffinose pentahydrate and its behaviour during progressive dehydration. RESULTS: Isothermal dehydration of raffinose pentahydrate led to its gradual amorphisation, but also to minor changes in the diffractograms, suggesting the probability of lower stable hydrates. Their existence was confirmed by DSC. Anhydrous raffinose was found to be completely amorphous, and this was supported by the gradual disappearance of birefringence during dehydration. In contrast, electron micrographs, taken during the dehydration process, exhibited no changes in the original ultrastructural crystal morphology. The widths of the glass-to-fluid transitions and the absolute specific heats of crystalline and amorphous phases in the vitreous and fluid states were used to estimate some structural and relaxation characteristics of amorphous raffinose-water mixtures. CONCLUSIONS: Raffinose forms the most "fragile" glass of those pharmaceutical excipients for which data are available. In its thermomechanical properties, it is superior to trehalose and should therefore be effective as a long-term stabiliser for dried biopharmaceutical preparations at temperatures up to 65 degrees C.

Calorimetry, Differential Scanning↗
PubMed1981

Hypo- and hyperosmolal saline and raffinose on kidney cortical cell volume at 37 degrees C.

Cell water content was measured in respiring rat renal cortical slices incubated in hypo- and hyperosmolal saline with and without raffinose and ouabain for 60 min at 37 degrees C. At 60 min, hyposmolal saline (228 mosmol/kg H2O) caused a 16% swelling of cells, whereas addition of 73 mM raffinose (299 mosmol/kg H2O) caused a 33% shrinkage. Physiological saline plus raffinose (364 mosmol/kg H2O) caused a 28% cell shrinkage, whereas addition of saline (385 mosmol/kg H2O) produced only a 10% decrease in cell volume. The effects of raffinose were reversible. At physiological Na concentrations, osmole for osmole raffinose was 4 times as effective in shrinking cells as saline, but only 2 times as effective at Na of 112 mM. Osmotic effectiveness of saline changed, that of raffinose did not. Ouabain caused no changes in cell volume and did not prevent the effect of raffinose. In conclusion, there is no volume regulation to nonelectrolyte solutes and only partial volume regulation to saline, and this is due to differential osmotic effects of these solutes, that of saline decreasing from low to high Na.

Animals↗
PubMed2004

Ingestion of raffinose promotes calcium absorption in the large intestine of rats.

We examined the effects of feeding raffinose on intestinal calcium absorption in ovariectomized rats by two separate experiments. In experiment 1, female Sprague-Dawley rats (6 wk old) were divided into two groups: sham operation and ovariectomy, and fed diets with or without raffinose (30 g/kg diet) for 4 wk. In experiment 2, ovariectomized rats with cecocolonectomy or transsection and reanastomosis (sham) were divided into two groups as in experiment 1 and fed the same diets for 3 wk. In experiment 1, calcium absorption was lower in the ovariectomized rats than in the sham rats but calcium absorption in rats fed the raffinose diet was higher than that in rats fed the raffinose-free diet. In experiment 2, increased calcium absorption in the raffinose group was abolished by cecocolonectomy. The impaired absorption in ovariectomized rats was restored by feeding raffinose. The large intestine is involved in the beneficial effects of raffinose.

Animals↗
PubMed2005

O-raffinose crosslinked hemoglobin lacks site-specific chemistry in the central cavity: structural and functional consequences of beta93Cys modification.

Reacting human deoxyHbA0 with oxidized raffinose (O-raffinose), a trisaccharide, results in a low oxygen affinity "blood substitute," stabilized in a noncooperative T-conformation and possesses readily oxidizable rhombic heme. In this study, we fractionated the O-raffinose-modified HbA0 heterogeneous polymer (O-R-PolyHbA0) into six distinct fractions with a molecular weight distribution ranging from 64 to approximately 600 kDa using size-exclusion chromatography (SEC). Oxygen equilibrium and kinetics binding parameters of all fractions were nearly identical, reflecting a lack of heterogeneity in ligand binding properties among O-R-PolyHbA0 species (Hill coefficient n equal to 1.0). Several mass spectrometry techniques were used to evaluate undigested and digested HbA0, O-R-PolyHbA0, and O-R-PolyHbA0 fractions. Proposed sites of intramolecular crosslinking (i.e., beta1Lys82, beta2Lys82, and beta1Val1) were not found to be the predominant site of crosslinking within the central cavity. Intermolecular crosslinking with O-raffinose results in no discernible site of amino acids modifications with the exception of beta93Cys and alpha104Cys. Based on accessible surface area (ASA) calculations in intact deoxyHbA0, slight conformational changes are required to allow for the S on alpha104Cys to be modified during the reaction with O-raffinose or its partially oxidized product(s). The stabilization of HbA0 in the T-conformation may not be a direct correlate of O-raffinose induced changes, but an indirect consequence of changing hydration in the water-filled central cavity and/or the distal heme pocket leading in the latter case to accelerated iron oxidation. Structural data presented here when taken together with the oxidative instability of O-R-PolyHbA0 may provide some basis for the reported toxicity of this oxygen carrier.

Amino Acid Sequence↗
PubMed1995

Leguminosae in the diet: the raffinose-stachyose question.

Adhering to a galactose-free diet by strictly avoiding dairy products and known hidden sources of galac-tose does not completely normalize galactose-1-phosphate (gal-1-P) in erythrocytes from patients with galactosemia. Major neurological complications, even in the best treated patients, are threatening a good clinical outcome and dictate a continuous search for leaks in the dietary regimen. Raffinose and stachyose, present in important amounts in various vegetables, contain alpha-1,4 linked galactose which is cleaved only by bacterial alpha-galactosidases, presumably in the lower part of the gut. In order to test the hypothesis whether galactose released from raffinose and stachyose could be a source of absorbed galactose and a cause of elevated gal-1-P six patients with galactosemia (aged 6-24 years), underwent a raffinose- and stachyose-poor dietary regimen for 2 weeks. Before, after, and during the test period, the daily intake of stachyose and raffinose as well of protein, carbohydrate, fat and minerals was calculated from food protocols obtained from the patients. Plasma galactose and erythrocyte gal-1-P were measured at the end of the three test phases. Stachyose and raffinose intake was reduced to 5%-10% during the experimental diet, which was well tolerated, except for constipation in some patients. In five of the six patients gal-1-P in erythrocytes was somewhat lower (statistically not significant) during the test phase than during regular diet while plasma galactose remained unchanged. Galactose released from raffinose and stachyose may be absorbed and contribute to elevated gal-1-P values in erythrocytes of galactosemic patients.

Adult↗
PubMed2000

Raffinose improves the function of rat pulmonary grafts stored for twenty-four hours in low-potassium dextran solution.

OBJECTIVES: The perfect strategy for pulmonary graft preservation remains elusive. Experimental work supports the use of perfusates, such as Euro-Collins, University of Wisconsin, and low-potassium dextran solutions. We use low-potassium dextran solution in our clinical program, but we aim for continued improvement. The trisaccharide raffinose has been shown to be responsible for the efficacy of University of Wisconsin perfusate in lung preservation. Raffinose is superior to a variety of other saccharides for this purpose. We tested the hypothesis that the addition of raffinose to low-potassium dextran solution might further improve graft function. METHODS: In a randomized blinded study with a rat left lung transplant model, donor lungs were flushed with either standard low-potassium dextran solution or low-potassium dextran solution modified by the addition of 30 mmol/L raffinose (n = 5 for each group). Alprostadil (prostaglandin E(1), 500 microg/L) was added to the perfusates in accordance with our clinical practice. Grafts were stored inflated at 4 degrees C for 24 hours. After transplantation, recipients were ventilated with a fraction of inspired oxygen of 1 and a positive end-expiratory pressure of 2 cm H(2)O. Graft function was evaluated by measuring oxygenation at 2 hours after graft reperfusion, peak airway pressure throughout the reperfusion period, and the wet/dry lung weight ratio. RESULTS: The group receiving low-potassium dextran solution with raffinose demonstrated significantly higher oxygenation (oxygen tension, 370 +/- 45 mm Hg vs 150 +/- 64 mm Hg; P =.0025), lower peak airway pressures at 2 hours after lung reperfusion (11 +/- 2.7 mm Hg vs 16 +/- 2.4 mm Hg; P <.001), and a lower wet/dry weight ratio (4.7 +/- 1.26 vs 11 +/- 5. 0; P =.017). CONCLUSION: Modification of low-potassium dextran solution with the trisaccharide raffinose resulted in a significant improvement in graft function in this model and merits further evaluation with respect to the mechanisms involved.

Animals↗
PubMed2002

Suppressive effect of dietary raffinose on T-helper 2 cell-mediated immunity.

The effects of the dietary oligosaccharide raffinose on immune responses, with special reference to its anti-allergic functions, were examined in vivo. First, feeding a diet supplemented with 50 g raffinose/kg to BALB/c mice significantly (P<0.05) increased interleukin (IL) 12 secretion from isolated Peyer's patch (PP) cells in vitro compared with feeding control diet. When isolated PP cells were used as antigen-presenting cells (APC) for CD4+ T-splenocytes isolated from ovalbumin (OVA)-specific T-cell receptor transgenic (Tg) mice in the presence of OVA as antigen, significantly (P<0.05) higher levels of interferon-gamma were observed in the cultures using APC from raffinose-fed mice than those cultures using APC from control mice. Second, the diet containing 50 g raffinose/kg or control diet was fed to OVA Tg mice, and subsequently, OVA was added to each diet to prime T cells in vivo. CD4+ T-cells from the mesenteric lymph nodes of the raffinose-fed mice secreted significantly (P<0.05) higher levels of IL-2 and significantly (P<0.05) lower levels of IL-4 following in vitro antigenic stimulation compared with those of the control mice. These present results suggest that feeding raffinose may suppress differentiation of naïve T-helper (Th) cells into Th2 cells in the mesenteric lymphoid nodes. Last, feeding raffinose suppressed rises of serum immunoglobulin E levels in the Tg mice treated with long-term ingestion of OVA. In conclusion, it is suggested that dietary raffinose suppresses serum immunoglobulin E response through suppression of Th2-type immune response against oral antigen in the lymphoid organs located in or near the intestine.

Animals↗