Soybean isoflavones regulate dendritic cell function and suppress allergic sensitization to peanut

Masilamani, Madhan; Wei, John P.; Bhatt, Suresh; Paul, Megan; Yakir, Stefanie; Sampson, Hugh A.

doi:10.1016/j.jaci.2011.05.009

Cited by 83 publications

(73 citation statements)

References 73 publications

(88 reference statements)

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“…1b). In week 7, mice were orally challenged with 100 mg of CPE, their anaphylactic scores and the rectal temperatures were recorded followed by an intraperitoneal challenge with 9 mg defatted peanut protein, and anaphylactic scores and temperatures were recorded as described [10]. After oral challenge with peanut, 67% (14 out of 21) of soy-free mice showed symptoms of systemic anaphylaxis with severity varying from mild (score 1) to mild-moderate (score 2).…”

Section: Resultsmentioning

confidence: 99%

“…In weeks 6 and 7, mice were challenged orally twice in 30-min intervals with 100 mg CPE. The anaphylactic reactions were scored, and the rectal temperatures were recorded after 30 min [10]. In week 7, 30 min after the oral challenge, mice were then challenged intraperitoneally with 9 mg defatted peanut protein, and anaphylactic scores and temperatures were recorded 30 min later.…”

Section: Methodsmentioning

confidence: 99%

“…Yet, BALB/c mice do not show detectable anaphylaxis following oral challenge with the allergen and a minimal response when challenged via the intraperitoneal route [8,9]. Allergen-specific IgE levels in C3H/HeJ and C3H/HeOuJ mice are significantly lower compared to BALB/c, but these mice readily develop anaphylaxis upon challenge, closely mimicking human food allergy [8,10,11]. A number of studies in these mouse models have contributed towards developing new therapies for peanut allergy [12].…”

Section: Introductionmentioning

confidence: 99%

“…A number of studies in these mouse models have contributed towards developing new therapies for peanut allergy [12]. We have shown that dietary isoflavones suppress peanut allergic symptoms in C3H/HeJ mice [10] and upper airway hypersensitivity in BALB/c mice [13]. …”

Section: Introductionmentioning

confidence: 99%

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Dietary Elimination of Soybean Components Enhances Allergic Immune Response to Peanuts in BALB/c Mice

Chang¹,

Song²,

Li³

et al. 2015

Int Arch Allergy Immunol

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Background: Food allergy research is hampered by a lack of animal models that consistently mimic human food allergic responses. Laboratory mice are generally fed grain-based chow made with large amounts of soybeans rich in immunomodulatory isoflavones. We tested the role of dietary soy components in the induction of food allergic responses in the BALB/c mouse strain, which is known to be resistant to anaphylaxis when orally challenged by food allergens. Methods: Mice were fed a soy-free diet for 2 generations. After weaning, mice were maintained on the same diet or fed a diet containing soy isoflavones, i.e. genistein and daidzein, followed by weekly oral sensitizations with crude peanut extract plus cholera toxin and finally challenged at week 7. The anaphylactic symptoms, body temperature, peanut-specific antibodies and mast cell degranulation were assessed. Results: Soy-free diet mice showed significantly higher anaphylactic symptom scores and mast cell degranulation after challenge and higher peanut-specific antibody levels than mice fed regular chow. Introduction of a regular soy diet or an isoflavone diet to soy-free diet mice significantly suppressed the allergic reactions compared to the soy-free diet. Conclusion: Rodent diet is an important variable and needs to be taken into consideration when designing experiments involving animal models. Our results indicate that elimination of soy components from the diet enhances peanut sensitization in BALB/c mice. In addition to serving as a valuable tool to mimic human food allergy, the dietary influence on the immune response could have far-reaching consequences in research involving animal models.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Dietary Elimination of Soybean Components Enhances Allergic Immune Response to Peanuts in BALB/c Mice

Chang¹,

Song²,

Li³

et al. 2015

Int Arch Allergy Immunol

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“…Masilamani et al [67], showed that the dietary isoflavones genistein and daidzein suppressed allergic reactions to peanut in mice and regulated CTactivated human monocyte-derived DCs function in vitro. Recently, they extended this study by determining the effects of isoflavones on murine Th1 immune responses in vitro and in vivo [68], and found that they suppressed the expression of LPS-induced DC maturation markers, B7 costimulatory molecules and MHC molecules and selectively suppressed cytokine secretion (TNFα, IL-10, IL-6, IL-12) from LPS-activated DCs.…”

Section: Nwaru Et Al (2010) [38]mentioning

confidence: 99%

The Potential of Maternal Dietary Modification for Prevention of Food Allergy

Luengo¹,

Song²

2013

J Aller Ther

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Effective primary preventions strategies aimed at reducing the onset of IgE sensitization are urgently needed as the incidence of childhood food allergy keeps increasing.Studies eliminating food allergens during pregnancy have failed to show reduction in the prevalence of long-term IgE-mediated food allergy in children, and recent data provides direct evidence supporting early oral exposure as a means of preventing development of allergy. Since effects on early immune programming may be more significant in utero, there has been increasing interest in the potential protective role of maternal dietary modifications on the development of FA in offspring.In this article, we will review the current knowledge from animal and clinical studies on the role of maternal dietary modification, mainly through supplementation with vitamins, polyunsaturated fatty acids and probiotics, for the prevention of food allergy. Besides, the potential role of some promising FA treatments like Chinese herbal formula FAHF-2 for the primary prevention of FA in offspring will be reviewed. be due to uncontrolled environmental factors, timing of introduction to PN and different study protocols and populations, as well as undefined co-factors in maternal diet such as microbes [18][19][20]. In addition, retrospective maternal recall of dietary intake during pregnancy (and or lactation), sometimes months or years later, may contain recall bias. At present, the standard practice for PNA and other food allergies is strict allergen avoidance. There is no clinical study reporting whether peanut allergic mother consumption of controlled low doses of peanut that do not trigger clinical reactions would prevent offspring peanut or other food allergies. The Potential of Maternal Dietary Modification for Prevention of Food AllergyOlga Maternal allergenic food consumption for preventing food allergy in offspring: Animal studiesIn recent years several studies in animal models have provided direct evidence supporting early oral exposure as a means of preventing development of allergy.Melkild et al. [21] showed that intraperitoneal immunization of naïve mice with ovalbumin and adjuvant (Al(OH) 3 ) during pregnancy and lactation significantly reduced the specific IgE response and increased the IgG2a response in their offspring. Moreover, the IgE suppression was stronger if maternal allergen exposure was during early pregnancy (3 days into pregnancy) compared to a late pregnancy exposure (17 days into pregnancy). The same group reported that the protective effect of maternal immunization was affected by the type of adjuvant used: while offspring from mothers immunized with OVA and either pertussis toxin (PT) or Al(OH) 3 showed reduced levels of OVA-specific IgE and IgG1 and increased levels of OVA-specific IgG2a antibodies, maternal immunization with CpG and OVA did not affect antibody responses in offspring [22]. However, whether this effect is dependent on the specific adjuvant and/or the route of exposure employed has to be further investigated. Le...

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Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

Nan

Wang²,

Sun

et al. 2016

Luminescence

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The interaction of pepsin with daidzein (Dai) or genistein (Gen) was investigated using spectroscopic techniques under simulated physiological conditions. Dai and Gen can quench the fluorescence of pepsin and the quenching mechanism was a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ΔΗ, ΔG and ΔS were calculated. The results indicated that van der Waals forces and hydrogen bond formation played major roles in the interaction of Dai or Gen with pepsin. The binding distance between pepsin and Dai or Gen was calculated according to energy transfer theory. The results of synchronous fluorescence spectra showed that the microenvironment and conformation of pepsin were changed. UV absorption and 3D fluorescence spectra showed that the binding interaction disturbed the microenvironment of amino acid residues and induced conformational changes in pepsin. Molecular docking results showed that Dai and Gen entered into the hydrophobic cavity of pepsin and two hydrogen bonds formed between Dai or Gen and pepsin. The results demonstrated that the interaction behavior between Dai and Gen with pepsin was slightly different, which denoted that the 5-hydroxyl group of Gen, to a certain extent, had an effect on ligand binding to proteins. Copyright © 2016 John Wiley & Sons, Ltd.

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Soybean isoflavones regulate dendritic cell function and suppress allergic sensitization to peanut

Cited by 83 publications

References 73 publications

Dietary Elimination of Soybean Components Enhances Allergic Immune Response to Peanuts in BALB/c Mice

Dietary Elimination of Soybean Components Enhances Allergic Immune Response to Peanuts in BALB/c Mice

The Potential of Maternal Dietary Modification for Prevention of Food Allergy

Spectroscopy and molecular docking study on the interaction of daidzein and genistein with pepsin

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