Transdermal exposure to HWP1 is sufficient to activate key immune pathways necessary for sensitizing mice for immediate hypersensitivity reactions. This study shows that HWP has a sensitizing potential as well as gluten, whereas its allergenicity may be different from that of gluten.

No abstract

Phagocytes play a central role in the host defense system, and the relationship between the mechanism of their activation and cytoskeletal reorganization has been studied. We have previously reported a possible involvement of cofilin, an actin-binding protein, in phagocyte functions through its phosphorylation/dephosphorylation and translocation to the plasma membrane regions. In this work, we have obtained a new line of evidence showing an important role of cofilin in phagocyte functions using the mouse macrophage cell line J774.1 and an antisense oligonucleotide to cofilin. Upon stimulation with opsonized zymosan (OZ), cofilin was phosphorylated, and it accumulated around phagocytic vesicles. As the antisense oligonucleotide to cofilin, a 20-mer S-oligo corresponding to the sequence including the AUG translational initiation site was found to be effective. In the cells treated with the antisense oligonucleotide, the amount of cofilin was less than 30% of that in the control cells, and the level of F-actin was two or three times higher than that in the control cells before and throughout the cell activation. In the antisense oligonucleotide-treated cells, OZ-triggered superoxide production was three times faster than that in the control cells. Furthermore, phagocytosis of OZ was enhanced by the antisense. These results show that cofilin plays an essential role in the control of phagocyte function through regulation of actin filament dynamics.Phagocytes, including neutrophils and macrophages, are at rest in the absence of any stimulant; but, when activated by invading microorganisms or harmful substances, they play a central role in host defense systems through chemotaxis, adhesion, phagocytosis, superoxide production, degranulation, and the release of cytokines or lipid mediators. The mechanism of phagocyte activation has been studied in terms of protein phosphorylation and cytoskeletal reorganization (1). Originally we found that cofilin, an actin-and phosphatidylinositol 4,5-bisphosphate-binding protein, is rapidly dephosphorylated upon cell activation and translocated to plasma membrane regions in neutrophil-like HL-60 cells (2). These findings have been confirmed by other groups (3-5). Cofilin is a widely distributed protein highly conserved among various species and plays an essential role in the control of actin filament dynamics (6 -8). It has been well investigated in, for example, Dictyostelium (9 -11), yeast (12-14), Xenopus egg (15-17), mammalian neural cells (18 -20), and immune cells (21-23). Cofilin can be phosphorylated at Ser-3, and only the unphosphorylated form of cofilin can bind actin and depolymerize or sever the actin filament. It is also proposed that cofilin is involved in the turnover of actin filament.To date we have studied the relation between cofilin and phagocyte functions. We used opsonized zymosan (OZ) 1 as a cell stimulant, a complement C3bi-coated insoluble polysaccharide, the receptor for which is a member of the ␤ 2 integrin family (CR3, CD11b/CD18), and have reported that co...

The Japanese food allergen labeling regulation was designed to match real Japanese food allergy circumstances and also to be enforced effectively; thus, (1) regulated food allergens were selected by prevalence and seriousness according to food allergy surveys in Japan; (2) the detection criterion for ELISA monitoring, 10 μg food allergen protein/g (or mL) food, was set up as the threshold value to regulate commercial prepackaged foods; and (3) official food allergen analytical methods, which can determine the threshold value accurately, were developed. These three points are distinctive from other countries. Furthermore, as an on-going project, the regulation has been amended according to food allergy circumstances and requirements of society. This paper presents recent changes regarding the Japanese food allergen labeling regulation. To date, the Japanese food allergen labeling regulation has been enforced for more than 15 years and seems to be working effectively. Now would be an opportune time to review the regulation for its next level of development.

The labeling of foods containing material derived from crustaceans such as shrimp and crab is to become mandatory in Japan because of increases in the number of allergy patients. To ensure proper labeling, 2 novel sandwich enzyme-linked immunosorbent assay (ELISA) kits for the determination of crustacean protein in processed foods, the N kit (Nissui Pharmaceutical Co., Ltd, Ibaraki, Japan) and the M kit (Maruha Nichiro Holdings, Inc., Ibaraki, Japan), have been developed. Five types of model processed foods containing 10 and/or 11.9 g/g crustacean soluble protein were prepared for interlaboratory evaluation of the performance of these kits. The N kit displayed a relatively high level of reproducibility relative standard deviation (interlaboratory precision; 4.08.4 RSDR) and sufficient recovery (6586) for all the model processed foods. The M kit displayed sufficient reproducibility (17.620.5 RSDR) and a reasonably high level of recovery (82103). The repeatability relative standard deviation (RSDr) values regarding the detection of crustacean proteins in the 5 model foods were mostly <5.1 RSDr for the N kit and 9.9 RSDr for the M kit. In conclusion, the results of this interlaboratory evaluation suggest that both these ELISA kits would be very useful for detecting crustacean protein in processed foods.