Our results suggest that supplementation with probiotic L. plantarum CJLP133 is beneficial in the treatment of pediatric AD.

loss-of-function mutations in FLG leading to near-complete absence of profilaggrin in the homozygous or compound heterozygous state. Therefore it can be hypothesized that filaggrin deficiency contributes to the observed photosensitivity and/or reduced threshold to UVB-induced erythema in patients with AD. We have performed a detailed analysis of cutaneous photoresponse in clinically normal skin to avoid the confounding effects of atopic inflammation. Our findings have excluded a large effect of FLG genotype on photosensitivity (> _1.8-fold difference in MED) at any of the wavebands tested. In addition, the results of our monochromator phototesting did not indicate a differential erythemal sensitivity within the wavelengths representing UVB, as would be predicted from the known absorption spectrum of UCA. One limitation of our study is that the healthy volunteers did not include any subjects with ichthyosis vulgaris, and therefore we have not excluded the possibility that FLG homozygous (or compound heterozygous) subjects might show greater erythemal sensitivity than wild-type subjects. However, FLG-null heterozygosity has a significant effect on filaggrin expression in vivo, 9,10 and therefore we would expect an effect to be observed in FLG heterozygotes if this was substantial. The fact that observations of UVB-induced damage in murine and in vitro models have not been supported by clinical data suggest that different mechanisms lead to cutaneous erythema in vivo than the markers of UV damage studied in vitro and in mice. For example, apoptosis is known to occur within areas of skin damaged by UVexposure, and this is associated with cutaneous erythema, but the relationship is nonlinear. Furthermore, the photoprotective effect of the FLG wild-type genotype might be attributable to a mechanical filtering of UV radiation by the stratum corneum rather than by chemical photoimmunosuppression. In conclusion, our FLG genotype-stratified analysis of responses to UV and visible radiation in clinically normal skin does not support the hypothesis that the breakdown products of filaggrin play a major role in the sensitivity of human skin to UV-induced erythema. This has relevance to the ongoing search for predictors of patient response in phototherapy for AD and for the development of personalized medicine. We thank the patients and volunteers who participated in this study and Lynn Fullerton, who provided technical support in the photobiology investigations. We are very grateful to Professors

PurposeIt is known that ovomucoid, an egg allergen, is heat resistant and remains soluble after heating. However, a recent study showed that the antigenic activity of ovomucoid could be reduced by heating when egg white (EW) was mixed with wheat flour. This study was performed to determine the influence of wheat flour on the antigenic activities of EW proteins when EW is heated, and the influence of the duration of heat treatment.MethodsA mixture of EW and wheat flour was kneaded for 10 minutes and then baked at 180℃ for 10 minutes and 30 minutes. The EW without wheat flour was also heated at 180℃ for 10 minutes and 30 minutes. The proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and IgE immunoblotting was performed with the pooled sera of 5 egg-allergic patients. The antigenic activities of ovomucoid in different EW samples were measured by inhibition enzyme-linked immunosorbent assay (ELISA).Results1) SDS-PAGE: the intensity of the 37-50 kD bands (overlapped bands of ovomucoid and ovalbumin) decreased significantly in the mixture of EW and wheat flour baked for 30 minutes, compared with the mixture baked for 10 minutes, heated EW and raw EW. 2) IgE immunoblot: in the mixture of EW and wheat, a remarkable decrease of IgE reactivity to 37-50 kD was observed when baked for 30 minutes. 3) Inhibition ELISA: the antigenic activity of ovomucoid decreased significantly in the mixture of EW and wheat baked for 30 minutes, but not in the heated pure EW.ConclusionsThis study showed that the antigenic activity of ovomucoid can be reduced by baking EW with wheat flour. The decrease in ovomucoid antigenicity in the baked mixture of EW and wheat flour was dependent on the time of heat treatment, indicating that heating should be prolonged to achieve a reduction in ovomucoid antigenic activity.

BACKGROUND/OBJECTIVESDue to its beneficial health effects, use of buckwheat has shown a continuous increase, and concerns regarding the allergic property of buckwheat have also increased. This study was conducted for evaluation of the hydrolytic effects of seven commercial proteases on buckwheat allergens and its allergenicity.MATERIALS/METHODSExtracted buckwheat protein was hydrolyzed by seven proteolytic enzymes at individual optimum temperature and pH for four hours. Analysis was then performed using SDS-PAGE, immunoblotting, and competitive inhibition ELISA (ciELISA) with rabbit antiserum to buckwheat protein, and direct ELISA with pooled serum of 21 buckwheat-sensitive patients.RESULTSAlkaline protease, classified as serine peptidase, was most effective in reducing allergenicity of buckwheat protein. It caused decomposition of the whole buckwheat protein, as shown on SDS-PAGE, and results of immunoblotting showed that the rabbit antiserum to buckwheat protein no longer recognized it as an antigen. Allergenicity showed a decrease of more than 50% when pooled serum of patients was used in ELISA. Two proteolytic enzymes from Aspergillus sp. could not hydrolyze buckwheat allergens effectively, and the allergenicity even appeared to increase.CONCLUSIONSSerine-type peptidases appeared to show a relatively effective reduction of buckwheat allergenicity. However, the antigenicity measured using rabbit antiserum did not correspond to the allergenicity measured using sera from human patients. Production of less allergenic buckwheat protein may be possible using enzymatic hydrolysis.