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The effects of bisphenol A (BPA) on asthma have been reported in various in vitro, animal, and human epidemiologic studies. However, epidemiological studies on the effects of bisphenol S (BPS) and bisphenol F (BPF), which are substitutes of BPA, on asthma are lacking. The purpose of this study was to identify the association between BPA, BPS, and BPF and asthma. An asthma-related questionnaire; urinary BPA, BPS, BPF; and the possible confounders were analyzed among 922 adolescents aged 12-17 years who participated in the Korean National Environmental Health Survey 2016. In males, urinary BPA, BPS, and BPF did not show a significant relationship with the lifetime prevalence of asthma. In females, urinary BPS was higher in the asthma group ( p < 0.01). High urinary BPS showed a significant relationship with a high odds ratio (OR) of lifetime asthma prevalence in the model adjusted for possible confounders ( p < 0.05). High urinary BPS was particularly associated with an increase in the OR of asthma diagnosed after the age of 60 months ( p < 0.01). Urinary BPS was significantly associated with asthma diagnosis, especially after the age of 60 months, among Korean adolescent females.

Glycogen debranching enzyme (GDE) in mammals and yeast exhibits α-1,4-transferase and α-1,6-glucosidase activities within a single polypeptide chain and facilitates the breakdown of glycogen by a bi-functional mechanism. Each enzymatic activity of GDE is suggested to be associated with distinct domains; α-1,4-glycosyltransferase activity with the N-terminal domain and α-1,6-glucosidase activity with the C-terminal domain. Here, we present the biochemical features of the GDE from Saccharomyces cerevisiae using the substrate glucose(n)-β-cyclodextrin (Gn-β-CD). The bacterially expressed and purified GDE N-terminal domain (aa 1-644) showed α-1,4-transferase activity on maltotetraose (G4) and G4-β-CD, yielding various lengths of (G)n. Surprisingly, the N-terminal domain also exhibited α-1,6-glucosidase activity against G1-β-CD and G4-β-CD, producing G1 and β-CD. Mutational analysis showed that residues D535 and E564 in the N-terminal domain are essential for the transferase activity but not for the glucosidase activity. These results indicate that the N-terminal domain (1-644) alone has both α-1,4-transferase and the α-1,6-glucosidase activities and suggest that the bi-functional activity in the N-domain may occur via one active site, as observed in some archaeal debranching enzymes., (Copyright © 2014 Elsevier Inc. All rights reserved.)