Validation of predictive equations for resting energy expenditure in Japanese pediatric Crohn's disease patients: preliminary study.

BACKGROUND: Predictive equations are often used to estimate resting energy expenditure (REE). Determining the appropriate equation for different patient types, however, remains inconclusive, as in the case of Japanese children with Crohn's disease (CD). The aim of this study was to identify an appropriate predictive equation for measuring REE in Japanese children with CD. METHODS: Twelve Japanese children with CD managed at the National Center for Child Health and Development in Tokyo, Japan, were studied. REE (kcal/day) was measured using indirect calorimetry. The predictive equations used were the Japanese Dietary Reference Intakes (2010), the Schofield equation, the Food and Agriculture Organization/World Health Organization/United Nations University (FAO/WHO/UNU) equation and the Cunningham equation. Difference between predicted and measured REE was analyzed on Bland-Altman plot. RESULTS: Japanese Dietary Reference Intakes (2010) had the smallest difference between predicted and measured REE. Weight was the primary predictor of REE on multiple regression analysis. As well, Japanese Dietary Reference Intakes (2010) had the highest ratio of weight to predicted REE (98.5%). CONCLUSIONS: Of the four equations, Japanese Dietary Reference Intakes (2010) appeared to be the most practical and accurate predictive equation for REE in Japanese children with CD.

Overexpression and functional characterization of a serine carboxypeptidase inhibitor (I(C)) from Saccharomyces cerevisiae.

Carboxypeptidase Y (CPY) inhibitor, I(C), a cytoplasmic inhibitor of vacuolar proteinases in yeast, Saccharomyces cerevisiae, was purified by means of a high-level expression system using a proteinase-deficient strain, BJ2168, and an expression vector with the promoter GAL1. The purified I(C) exists as a monomeric beta-protein in solution with a mole-cular weight of 24,398.4 as determined by gel filtration chromatography, MALDI-TOF mass spectrometry, and far-UV CD spectroscopy. The acetylated N-terminal methionine residue is the sole posttranslational modification. I(C) specifically inhibits both the peptidase and anilidase activities of CPY with inhibitor constants (K(i)) of approximately 1.0 x 10(-9) M. The chemical modification of I(C) with sulfhydryl reagents indicated that it lacks disulfide bonds and has two free SH groups, which are responsible, not for the inhibitory function, but, apparently, for the folding of the overall structure. The formation of a complex of I(C) with CPY was highly specific, as evidenced by no detectable interaction with pro-CPY. Chemical modification studies of the CPY-I(C) complex with specific reagents demonstrated that the catalytic Ser146 and S1 substrate-binding site of CPY are covered in the complex.