[TWO SCHOOL-AGED CASES OF FRUIT GIBBERELLIN-REGULATED PROTEIN ALLERGY WHICH NEED INDIVIDUAL REMOVAL STRATEGY IN SCHOOL LUNCH].

Gibberellin-regulated protein (GRP) is a newly discovered allergen in systemic fruit allergies. The kind of fruits which cause allergy is extensive as GRP is universally included in plants. Two children with GRP allergy were reported. Case 1: A 6-year-old boy experienced anaphylaxis while running after school lunch, which included canned peaches. A skin prick test (SPT) and blood examination suggested that he had peach GRP allergy. Six months and three years later, he experienced a similar episode after eating apple and citrus flesh, respectively. Case 2: An 11-year-old boy experienced anaphylaxis while running after consuming canned peaches during school lunch. A SPT implied that he had peach GRP allergy. However, a similar episode occurred after eating strawberry flesh 18 months later.Patients with GRP allergy often have one or more allergies to fruits other than peaches, as in these cases, and relevant fruits differ depending on the case. Particularly, clinicians should recognize that apple and citrus fruits are frequently included in school lunches as fruit flesh and as flavoring or seasoning in ready-made sauces or dressings. Therefore, an appropriate removal strategy should be considered in school lunches depending on each case of GRP allergy.

Enhanced ATPase activities as a primary defect of mutant valosin-containing proteins that cause inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia.

Valosin-containing protein (VCP) has been shown to colocalize with abnormal protein aggregates, such as nuclear inclusions of Huntington disease and Machado-Joseph disease, Lewy bodies in Parkinson disease. Several mis-sense mutations in the human VCP gene have been identified in patients suffering inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia (IBMPFD). Recently, we have shown that VCP possesses both aggregate-forming and aggregate-clearing activities. Here, we showed that in cells treated with proteasome inhibitors VCP first appeared as several small aggregates throughout the cells; and then, these small aggregates gathered together into a single big aggregate. Subcellular localization and ATPase activity of VCP clearly influenced the localization of the aggregates. Furthermore, all tested IBMPFD-causing mutant VCPs, possessed elevated ATPase activities and enhanced aggregate-forming activities in cultured cells. In Drosophila, these mutants and VCP(T761E), a super active VCP, did not appear to spontaneously induce eye degeneration, but worsened the phenotype when co-expressed with polyglutamines. Unexpectedly, these VCPs did not apparently change sizes and the amounts of polyglutamine aggregates in Drosophila eyes. Elevated ATPase activities, thus, may be a hidden primary defect causing IBMPFD pathological phenotypes, which would be revealed when abnormal proteins are accumulated, as typically observed in aging.