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We studied the prevalence of allergic disorders in an unselected group of 708 adolescents aged 15-17 years. All subjects were physically examined and interviewed by the authors. The prevalence of past or present asthma was 5.7% in boys and 3.1% in girls. The figures for hay fever were 14% and 8%, and for atopic dermatitis (including allergic urticaria) 25% and 30%, respectively. In 24% of all symptomatic subjects, the condition had not been active during the year preceding the study. The sex difference in the prevalence of hay fever was significant. It is associated with higher immediate skin test reactivity in boys. A progressive increase in the frequency of allergic disorders was observed with increasing number of positive skin reactions in both boys and girls. Respiratory allergy was closely related to a positive skin test: 87% of the asthmatics and 83% of all those with allergic rhinitis exhibited at least one positive skin reaction. For atopic dermatitis the association was less pronounced. Nineteen per cent of the population studied had a positive symptom history and a positive skin test to pollens, animal epithelia or dusts indicating a clinically significant relationship. However, 39% of the 346 subjects with a positive skin test, including some with a large number of positive reactions, were completely asymptomatic.

ODC (ornithine decarboxylase), the rate-limiting enzyme in polyamine biosynthesis, is regulated by specific inhibitors, AZs (antizymes), which in turn are inhibited by AZI (AZ inhibitor). We originally identified and cloned the cDNA for a novel human ODC-like protein called ODCp (ODC paralogue). Since ODCp was devoid of ODC catalytic activity, we proposed that ODCp is a novel form of AZI. ODCp has subsequently been suggested to function either as mammalian ADC (arginine decarboxylase) or as AZI in mice. Here, we report that human ODCp is a novel AZI (AZIN2). By using yeast two-hybrid screening and in vitro binding assay, we show that ODCp binds AZ1-3. Measurements of the ODC activity and ODC degradation assay reveal that ODCp inhibits AZ1 function as efficiently as AZI both in vitro and in vivo. We further demonstrate that the degradation of ODCp is ubiquitin-dependent and AZ1-independent similar to the degradation of AZI. We also show that human ODCp has no intrinsic ADC activity.