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PubMed2004

Mixed antibody and T cell responses to peanut and the peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in an oral sensitization model.

BACKGROUND: Peanut allergy is known for its severity and persistence through life. Several peanut proteins have been identified as allergenic and are indicated as Ara h 1-7. Very little is known about the mechanisms that underlie sensitization to peanut proteins. OBJECTIVE: The purpose of the present study was to reveal the immune responses that are induced against peanut and the peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 during sensitization, including the very early responses. METHODS: Humoral and T cell responses against peanut and the peanut allergens were examined in an early and later stage of sensitization in an established murine model of peanut anaphylaxis. Therefore C3H/HeJ mice were orally exposed to two different doses of peanut extract plus cholera toxin. RESULTS: Oral sensitization to peanut was characterized by an antigen-induced mixed cytokine response in the spleen (IL-4, IL-5, IL-10 and IFN-gamma), which could already be observed 7 days after the onset of exposure. Additionally, polyisotypic humoral responses (IgE, IgG1 and IgG2a) against peanut were found in the serum. Moreover, we demonstrated that these T helper (Th)1/Th2 cytokine and antibody responses were also directed specifically against the major peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6. CONCLUSIONS: This study implicates that both Th1 and Th2 phenomena are involved in the development of peanut allergy in the C3H/HeJ murine model. Furthermore, we show that the present oral model is suitable to examine immune responses to food allergens during different stages of sensitization upon treatment with a whole food extract.

2S Albumins, Plant↗
PubMed1997

An evaluation of the sensitivity of subjects with peanut allergy to very low doses of peanut protein: a randomized, double-blind, placebo-controlled food challenge study.

BACKGROUND: The minimum dose of food protein to which subjects with food allergy have reacted in double-blind, placebo-controlled food challenges is between 50 and 100 mg. However, subjects with peanut allergy often report severe reactions after minimal contact with peanuts, even through intact skin. OBJECTIVE: We sought to determine whether adults previously proven by challenge to be allergic to peanut react to very low doses of peanut protein. METHODS: We used a randomized, double-blind, placebo-controlled food challenge of 14 subjects allergic to peanuts with doses of peanut ranging from 10 microg to 50 mg, administered in the form of a commercially available peanut flour. RESULTS: One subject had a systemic reaction to 5 mg of peanut protein, and two subjects had mild objective reactions to 2 mg and 50 mg of peanut protein, respectively. Five subjects had mild subjective reactions (1 to 5 mg and 4 to 50 mg). All subjects with convincing objective reactions had short-lived subjective reactions to preceding doses, as low as 100 microg in two cases. Five subjects did not react to any dose up to 50 mg. CONCLUSION: Even in a group of well-characterized, highly sensitive subjects with peanut allergy, the threshold dose of peanut protein varies. As little as 100 microg of peanut protein provokes symptoms in some subjects with peanut allergy.

Adult↗
PubMed2005

Double-blind placebo-controlled challenges for peanut allergy the efficiency of blinding procedures and the allergenic activity of peanut availability in the recipes.

BACKGROUND: A firm diagnosis of double-blind placebo-controlled food challenge (DBPCFC) would facilitate the diagnosis in patients with uncertain history of reaction. Guidelines are lacking for an upper provoking dose and how to hide high concentrations of peanuts. AIM: To develop and evaluate a double-blind recipe with minimum 10% of peanut. To compare the recipe with published recipes regarding blindness, taste, texture and immunoglobulin (Ig)E antibody binding to peanut. METHODS: A recipe (I) with 10% of peanut was developed evaluated and used in DBPCFC. The challenges were followed by development of a concentrated recipe (II) (15% peanut, 25% fat). Recipe II was compared with the only published recipe (III) (11% peanut, 7% fat) regarding taste, texture and availability of peanut. Recipe IV (12% peanut, 10% fat) was developed using the same methods. The binding of IgE in the recipes was measured using an inhibition method. RESULTS: During challenges, one patient reacted after 4 g, emphasizing the need for blinding recipes containing high doses of peanut. Evaluation between recipes II and III, only recipe II was regarded as blind by the taste panels. A tenfold lower availability of peanut protein in the recipe II was found at 50% of inhibition. Recipe IV had a better IgE binding that did not differ from the original peanut extract. CONCLUSION: The peanut taste and texture can be hidden in a challenge medium. The fat content was important for the availability of the allergenic protein in challenges. The availability of allergens must be taken into consideration when used for DBPCFC.

Allergens↗
PubMed1997

Systemic allergic reaction following ingestion of undeclared peanut flour in a peanut-sensitive woman.

BACKGROUND: Although peanuts and peanut butter are well recognized as food allergens, few reports describe allergic reactions associated with eating peanut flour. OBJECTIVE: To describe an allergic reaction that occurred in a peanut-sensitive woman who ate undeclared peanut flour that was part of a flavor ingredient contained in a dry soup mixture, and to estimate the amount of peanut protein the patient ingested. METHODS: The patient was interviewed, medical records from her emergency room visit were reviewed, and the manufacturer of the soup mix was investigated to ascertain the proportion of the soup mix constituted by the undeclared peanut flour. RESULTS: Minutes after ingesting the soup, a 33-year-old woman experienced a systemic allergic reaction. She was treated successfully in the emergency room with intravenous fluids, corticosteroids, and diphenhydramine. Investigation of the soup manufacturer revealed that undeclared peanut flour was a component of a flavoring ingredient in the soup. Based on the concentration of peanut flour in the flavoring, we estimated the patient ate approximately 45 mg of peanut protein. CONCLUSIONS: Inadvertent ingestion of peanut flour by peanut-sensitive individuals may lead to systemic allergic reactions.

Adult↗
PubMed2004

Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen.

BACKGROUND: A number of allergenic proteins in peanut has been described and the relative importance of these allergens is yet to be determined. OBJECTIVES: We have investigated the relevance of previously identified peanut allergens in well-characterized peanut-allergic patients by in vitro, ex vivo and in vivo assays. METHODS: Thirty-two adult peanut-allergic patients were included based on careful and standardized patient history and the presence of peanut-specific IgE. The diagnosis peanut allergy was confirmed using double-blind placebo-controlled food challenges in 23 patients. Major peanut allergens Ara h1, Ara h2 and Ara h3 were purified from peanuts using ion-exchange chromatography. IgE immunoblotting was performed and IgE-cross-linking capacity was examined by measuring histamine release (HR) after incubating patient basophils as well as passively sensitized basophils with several dilutions of the allergens. Intracutaneous tests (ICTs) using 10-fold dilution steps of the purified allergens and crude peanut extract were performed. RESULTS: Ara h2 was recognized most frequently (26 out of 32) in all tests and induced both positive skin tests and basophil degranulation at low concentrations, whereas Ara h1 and Ara h3 were recognized less frequently and reacted only at 100-fold higher concentrations as analysed with HR and intracutaneous testing (ICT). Next to the three tested allergens, proteins with molecular weights of somewhat smaller than 15 kDa were identified as a IgE-binding proteins on immunoblot in the majority of the patients (20 out of 32). CONCLUSION: We conclude that Ara h2 is, for our patient group, the most important peanut allergen, and that previously unidentified peanut proteins with molecular weights of somewhat smaller than 15 kDa may be important allergens as well. ICT in combination with basophil-HR and IgE immunoblotting provides insight in the patient specificity towards the individual peanut allergens.

2S Albumins, Plant↗
PubMed2004

Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy.

BACKGROUND: We recently described patients with soybean allergy mainly mediated by cross-reactivity to birch pollen allergens. A majority of those patients were reported to have peanut allergy. OBJECTIVE: We sought to study the occurrence of peanut allergy in patients allergic to birch pollen and characterized the Bet v 1-homologous peanut allergen Ara h 8. METHODS: Recombinant Ara h 8 was cloned with degenerated primers and expressed in Escherichia coli. Nine Swiss and 11 Dutch patients with peanut and birch pollen allergy and a positive double-blind, placebo-controlled food challenge result to peanut were investigated for IgE reactivity to birch pollen and purified peanut allergens and cross-reactivity between birch and peanut. Ara h 8 stability against digestion and roasting was assessed by means of RAST inhibition. The IgE cross-linking potency of Ara h 8 was tested on the basis of basophil histamine release. RESULTS: During double-blind, placebo-controlled food challenge, all patients experienced symptoms in the oral cavity, progressing to more severe symptoms in 40% of patients. CAP-FEIA detected recombinant (r) Ara h 8-specific IgE in 85%. IgE binding to Ara h 8 was inhibited by Bet v 1 in peanut extract immunoblotting and in RAST inhibition. In EAST inhibition recombinant rAra h 8 inhibited IgE binding to peanut in 4 of 7 tested patient sera. Antipeanut response was dominated by Ara h 8 in 12 of 17 tested patients. Furthermore, our results demonstrate a low stability of Ara h 8 to roasting and no stability to gastric digestion. Basophil histamine release with rAra h 8 was more than 20% in 5 of 7 tested sera. CONCLUSIONS: Peanut allergy might be mediated in a subgroup of our patients by means of cross-reaction of Bet v 1 with the homologous peanut allergen Ara h 8.

Adolescent↗
PubMed1981

Peanut oil is not allergenic to peanut-sensitive individuals.

Ten peanut-sensitive patients were enrolled in a double-blind crossover trial to determine whether ingestion of peanut oil can induce adverse reactions in such individuals. All patients had experienced prior allergic reactions to peanut ingestion, including any of the following: generalized urticaria, angioedema, abdominal cramps, vomiting, diarrhea, bronchospasm, or shock. All patients had elevated levels of serum IgE antibodies to both crude peanut extract and the purified peanut allergen, Peanut-I, by RAST assay; binding values ranged from 2 to 26 times that of negative control serum. All patients demonstrated negative puncture skin tests to both peanut oil and olive oil (control). At 30-min intervals, patients ingested 1, 2, and 5 ml of either oil contained in 1 ml capsules while under constant observation. These quantities exceed the maximum estimated dose of peanut oil that would occur in single meals. Patients returned 2 wk later for ingestion challenge with the remaining oil. No untoward reactions were observed with either peanut oil or olive oil. Peanut oil ingestion does not pose a risk to peanut-sensitive individuals.

Adolescent↗
PubMed2004

[Effects of peanut mixed cropping with different gramineous plants on apoplast iron accumulation and reducing capacity of peanut].

The effects of peanut mixed cropping with five different gramineous plants on apoplast iron accumulation and reducing capacity of peanut were investigated by soil culture experiment. The results showed that mixed cropping of maize, barley, oats, wheat, and sorghum with peanut could improve iron nutrition of peanut respectively. The phytosiderophores excretion rate of barley, oats and wheat were much higher than that of maize, and the phytosiderophores excretion rate of sorghum was lower than that of maize. In comparison with peanut in monocropping the iron content in different organs of peanut mixed with maize, barley, oats, wheat and sorghum were increased. The Fe content in root apoplast of peanut mixed with five different gramineous was gradually increased and higher than that of peanut in monocropping at different growth days. At the same time, the mixed cropping systems remarkably improved the soil Fe availability in the rhizosphere and root Fe reducing capacity of peanut. The higher root Fe (III) reducing capacity and much more available Fe in the rhizospe (III) of peanut in mixed cropping played an important role in improving iron nutrition of peanut.

Arachis↗
PubMed1980

Interaction of lectins from soybean and peanut with rhizobia that nodulate soybean, peanut, or both plants.

Four of 14 strains of Rhizobium japonicum from soybean nodulated peanut (Arachis hypogaea L. cultivar Jumbo Virginia), and 3 of 8 Rhizobium sp. strains from peanut nodulate soybean (Glycine max (L.) Merr. cultivar Harosoy 63). Cells of three peanut rhizobia bound fluorescent- and radioisotope-labeled soybean lectin. Two of these strains failed to nodulate soybean, and conversely, two peanut strains that nodulated soybean did not bind to soybean lectin. Both culture medium and age had pronounced effects of the number of peanut rhizobia cells that bound fluorescent-labeled soybean lectin. Harosoy 63 soybean root exudates stimulated the growth of peanut rhizobia, but had no consistent influence on the number of cells that bound soybean lectin. Although extracellular soybean lectin receptors were present in culture fluids from each of the peanut rhizobia whose cells bound the lectin, the titer of receptors was greatest for strains 3G4b5. The affinity constants for the adherence of soybean lectin to Rhizobium sp. 3G4b5 cells from cultures of various ages ranged from 4.2 X 10(6) to 4.9 X 10(6) M-1, and the number of lectin binding sites per cell decreased as cells aged. Cells of the soybean and peanut rhizobia did not bind fluorescent- or radioisotope-labeled peanut lectin. The results indicate that there is no relationship between the ability of peanut and soybean rhizobia to nodulate the reciprocal host plant and their ability to bind to the lectin of that plant.

Arachis↗
PubMed2004

cDNA clone of a putative peanut (Arachis hypogaea L.) trypsin inhibitor has homology with peanut allergens Ara h 3 and Ara h 4.

Trypsin inhibitors are pathogenesis-related (PR) proteins, which play an important role in the plant defense mechanism against insects and pathogens. Peanut trypsin inhibitors are low molecular mass seed storage proteins. Like peanut allergens, they are stable to acid and heat, resistant to digestion, and can have a negative impact on human health. In peanut, five Bowman-Birk trypsin inhibitors (BBTI) have been isolated and amino acid sequences published. However, to date, no peanut BBTI sequence is available at both the cDNA and the genomic levels. The objectives of this investigation were (i) to synthesize degenerate oligonucleotides based on conserved regions of published amino acid sequences of BBTI, BII, and BIII; (ii) to isolate, sequence, and analyze at least one positive peanut trypsin inhibitor cDNA clone using the synthesized (32)P-labeled oligonucleotides as probes; and (iii) to determine its trypsin inhibitory activity. Thirty-two degenerate oligonucleotides DNA primers of 24 nucleotides each were synthesized based on the published amino acid sequences of peanut BBTI, and two were selected as probes to screen a peanut Lambda gt 11 cDNA library. Three putative positive clones were isolated, purified, and subcloned, and one was sequenced. Sequence analysis revealed a partial cDNA clone of 643 bp with a start codon. This clone shares 93 and 96% nucleotide sequence homology with peanut allergens Ara h 3 and Ara h 4 cDNA clones, respectively. A trypsin inhibitor assay revealed that peanut allergen Ara h 3 has a trypsin inhibitory activity of 11 238 TIA/mg protein. We concluded that peanut allergen Ara h 3 may also function as a trypsin inhibitor.

Allergens↗
PubMed1997

Randomised, double blind, crossover challenge study of allergenicity of peanut oils in subjects allergic to peanuts.

OBJECTIVE: To determine the in vivo allergenicity of two grades of peanut oil for a large group of subjects with proved allergy to peanuts. DESIGN: Double blind, crossover food challenge with crude peanut oil and refined peanut oil. SETTING: Dedicated clinical investigation unit in a university hospital. SUBJECTS: 60 subjects allergic to peanuts; allergy was confirmed by challenge tests. OUTCOME MEASURES: Allergic reaction to the tested peanut oils. RESULTS: None of the 60 subjects reacted to the refined oil; six (10%) reacted to the crude oil. Supervised peanut challenge caused considerably less severe reactions than subjects had reported previously. CONCLUSIONS: Crude peanut oil caused allergic reactions in 10% of allergic subjects studied and should continue to be avoided. Refined peanut oil did not pose a risk to any of the subjects. It would be reasonable to recommend a change in labelling to distinguish refined from crude peanut oil.

Adolescent↗
PubMed1999

trans-resveratrol content in commercial peanuts and peanut products.

A modified high-performance liquid chromatographic (HPLC) method for determination of trans-resveratrol (resveratrol) in peanuts and peanut products has been developed. Resveratrol was extracted with acetonitrile-water (90/10, v/v) by blending with diatomaceous earth at high speed followed by purification of an aliquot of the extract on a minicolumn packed with Al(2)O(3)-ODS (C(18)) mixture. The column was eluted with acetonitrile-water (90/10, v/v), eluate was evaporated under nitrogen, and residue was dissolved in HPLC mobile phase. Resveratrol in an aliquot of purified extract was quantitated by HPLC on silica gel with n-hexane-2-propanol-water-acetonitrile-acetic acid (1050/270/17/5/1, v/v) as a mobile phase. The recovery of resveratrol added to diatomaceous earth at 0.05 microg/g was 98.95 +/- 17.79%; the recovery of the standard added to fresh peanuts (with 0.070 microg/g natural level of resveratrol) at 0.50, 5.00, and 10.00 microg/g was 117.23 +/- 8.87, 100.10 +/- 2.49, and 100.45 +/- 1.51%, respectively. The quantitation limit of resveratrol in fresh peanuts was about 0. 01 microg/g. Roasted peanuts had the lowest content of resveratrol of 0.055 +/- 0.023 microg/g (n = 21), while in peanut butter its concentration was significantly higher, 0.324 +/- 0.129 microg/g (n = 46), and boiled peanuts had the highest level of 5.138 +/- 2.849 microg/g (n = 12). Resveratrol content in commercial peanut products was similar to the resveratrol content of the raw peanut fractions routinely used for making them.

Arachis↗
PubMed2001

Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world.

BACKGROUND: The serology of peanut allergy seems to be different in various parts of the world. We analyzed the composition of 13 samples of three varieties of peanut in order to compare their allergenic nature. METHODS: Peanut cultivars that are commonly processed in the West were analyzed for protein content, protein composition, and Ara h 1 and Ara h 2 content by biochemical methods. IgE-binding properties were analyzed by ELISA using serum from patients with documented peanut allergy. RESULTS: Total protein contents were comparable for all tested samples (24-29%), and proteins were extractable to the same extent. SDS-PAGE patterns differed slightly, but all major bands were visible in all samples (molecular masses of approximately 14100 kDa under reducing conditions). Ara h 1 and Ara h 2 were quantified by SDS PAGE densitometry and were expressed as percentage of the total protein content. Ara h 1 was in the range 12-16%, whereas Ara h 2 was 5.9-9.3%. In view of the analytic uncertainty of this determination, the content of both Ara h 1 and Ara h 2 was not significantly different between the tested samples. In an IgE-binding inhibition ELISA, the affinities of the peanut proteins for peanut-specific IgE were measured. Minor differences were observed between the tested samples, with the most potent IgE-binding sample having a two times higher ability to bind IgE than the weakest IgE-binding sample. CONCLUSIONS: The results suggest that peanuts of different varieties and from different parts of the world contain similar proteins, including Ara h I and Ara h 2. Consequently, the IgE-binding properties are similar to a great extent. This indicates that differences in the serology of peanut allergy may not originate from differences in the allergen composition of the peanut.

2S Albumins, Plant↗
PubMed2000

Survival of Salmonella in peanut butter and peanut butter spread.

In 1996, the first documented outbreak of salmonellosis associated with the consumption of peanut butter was reported. This study was undertaken to determine survival characteristics of high (5.68 log10 cfu g(-1)) and low (1.51 log10 cfu g(-1)) inocula of a five-serotype mixture of Salmonella in five commercial peanut butters and two commercial peanut butter spreads. Populations in samples inoculated with 5.68 log10 cfu g(-1) and stored for 24 weeks at 21 or 5 degrees C decreased 4.14-4.50 log10 cfu g(-1) and 2.86-4.28 log10 cfu g(-1), respectively, depending on the formulation. The order of retention of viability was: peanut butter spreads > traditional (regular) and reduced sugar, low-sodium peanut butters > natural peanut butter. Differences in rates of inactivation are attributed to variation in product composition as well as size and stability of water droplets in the colloidal matrix, which may influence nutrient availability. With the exception of natural peanut butter, products initially inoculated with 1.51 log10 cfu of Salmonella g(-1) (32 cfu g(-1)) were positive for the pathogen after storage for 24 weeks at 5 degrees C. At 21 degrees C, however, with the exception of one peanut butter spread, all products were negative for Salmonella after storage for 24 weeks. Post-process contamination of peanut butter and spreads with Salmonella may to result in survival in these products for the duration of their shelf life at 5 degrees C and possibly 21 degrees C, depending on the formulation.

Arachis↗
PubMed1995

Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity.

Peanut allergy is a significant health problem because of the frequency, the potential severity, and the chronicity of the allergic sensitivity. Serum IgE from patients with documented peanut hypersensitivity reactions and a peanut cDNA expression library were used to identify clones that encode peanut allergens. One of the major peanut allergens, Ara h I, was selected from these clones using Ara h I specific oligonucleotides and polymerase chain reaction technology. The Ara h I clone identified a 2.3-kb mRNA species on a Northern blot containing peanut poly (A)+ RNA. DNA sequence analysis of the cloned inserts revealed that the Ara h I allergen has significant homology with the vicilin seed storage protein family found in most higher plants. The isolation of the Ara h I clones allowed the synthesis of this protein in E. coli cells and subsequent recognition of this recombinant protein in immunoblot analysis using serum IgE from patients with peanut hypersensitivity. With the production of the recombinant peanut protein it will now be possible to address the pathophysiologic and immunologic mechanisms regarding peanut hypersensitivity reactions specifically and food hypersensitivity in general

Adult↗
PubMed1984

The absorption and transport of dietary cholesterol in the presence of peanut oil or randomized peanut oil.

Peanut oil has been shown to be unexpectedly atherogenic for cholesterol-fed rats, rabbits and rhesus monkeys. However, randomization (rearrangement of fatty acids to random distribution) of peanut oil significantly reduced its atherogenicity for rabbits and monkeys. This study was conducted to investigate whether the absorption and transport of dietary cholesterol was altered in the presence of peanut oil or randomized peanut oil, thereby accounting for the difference in the atherogenicity of the two diets. Intestinal lymph fistula rats were infused intraduodenally with a lipid emulsion at a rate of 3 ml/hr. The lipid emulsion contained either peanut oil (control) or randomized peanut oil (experimental) (10 mM), 14C-cholesterol (1.3 mM) and sodium taurocholate (19 mM) in phosphate-buffered saline, pH 6.4. Lymph triglyceride, cholesterol and phospholipid outputs were similar in both groups of rats during fasting and subsequently during lipid infusion. Comparable recovery of 14C-cholesterol from the intestinal lumen and the intestinal mucosa of the control and the experimental rats showed that the absorption and transport of dietary cholesterol were similar in both groups of rats. Analyses of the fatty acid of both lymph and intestinal mucosal lipid again failed to reveal a difference between the 2 groups of rats. It is concluded that the difference in the atherogenicity between the peanut oil and the randomized peanut oil is probably caused by events subsequent to the release of cholesterol containing chylomicrons and very low density lipoproteins by the small intestinal epithelial cells.

Animals↗
PubMed2001

Specific IgE antibodies to peanut in western Sweden--has the occurrence of peanut allergy increased without an increase in consumption?

BACKGROUND: Sensitization to peanut has seldom been investigated in Sweden. Therefore, all IgE-specific tests for peanut during a 5-year period were reviewed to study the relation between the levels of specific IgE antibody to peanut and age, sex, symptoms, and other atopic manifestations. METHODS: All serum samples were analyzed for IgE antibodies to peanut in relation to sex, age, clinical reactions, and other food allergens. A subgroup was asked to answer a questionnaire about symptoms and atopic manifestations in relation to IgE antibody levels. RESULTS: During the study period, 2417 tests were made for peanut. There was an increased prevalence of detectable IgE antibodies during the years studied. More than 80 individuals under 2 years of age were sensitized to peanut. In the subgroup, individuals with detectable IgE antibodies reported a shorter reaction time after eating peanuts than individuals with normal IgE antibody levels (P < 0.05). CONCLUSION: The reaction pattern to peanuts in Sweden is similar to that in many other countries despite a reported steady and low consumption. The severity of symptoms was connected to age and IgE antibody level. Patients with normal or low IgE antibody levels were not always free of symptoms even though their risk of allergic symptoms was reduced.

Adolescent↗
PubMed2003

Fluocinolone acetonide 0.01% in peanut oil: therapy for childhood atopic dermatitis, even in patients who are peanut sensitive.

BACKGROUND: Fluocinolone acetonide 0.01% in a blend of refined peanut and mineral oils has been used as treatment for scalp psoriasis for several years, but only more recently for atopic dermatitis. OBJECTIVE: We sought to study the effectiveness for atopic dermatitis, potential for adrenal axis suppression, and safety of the fluocinolone acetonide 0.01% in oil in children with atopic dermatitis, including children with atopic dermatitis and peanut allergic sensitivity. METHODS: Three separate studies were performed in children aged 2 to 12 years with atopic dermatitis: multicenter double-blind, randomized, and vehicle-controlled trial; cortisol stimulation testing; and prick testing, patch testing, and monitored medication use in children with peanut allergic sensitivity. RESULTS: Improvement of >/=50% was demonstrated within 2 weeks in 81% to 87% of 81 patients treated with active medication versus 39% of 45 children treated with vehicle oil alone. No adrenal suppression occurred after 4 weeks of therapy in 32 patients. None of 9 patients who were peanut sensitive reacted to either the full formulation or vehicle in prick or patch testing; 20 children who were peanut sensitive showed no allergic reactions after application of the medication. CONCLUSION: Fluocinolone 0.01% in peanut oil is an effective alternative to the use of topical corticosteroid agents in ointment, cream, and lotion forms in children. No evidence of adrenal suppression or adverse local effects were demonstrated in these studies. The medication was well tolerated in patients with peanut allergic sensitivity.

Administration, Topical↗