Physical Activity Participation by Parental Language Use in 4th, 8th,and 11th Grade Students in Texas,USA

Research on physical activity (PA) by level of acculturation in Hispanic children is limited and findings have been mixed. We examined PA participation by primary language used with parents in a representative sample of 4th, 8th, and 11th grade Texas public school students. Mixed-effects regression models were conducted using cross-sectional data from the 2004–2005 School Physical Activity and Nutrition Study (n = 22,049). Self-reported PA was compared among three language-ethnic groups: Spanish-Hispanic (SH) (referent); English-Hispanic (EH); and English-Other (EO). EH and/or EO girls were generally between 1.25 and 2.58 [OR] times more likely to participate in PA across grade levels, with the largest differences found for school sports in 8th grade girls. EH and EO 8th grade boys were 1.71 (CI: 1.40, 2.10) and 2.06 (CI: 1.68, 2.51) times, respectively, more likely to participate in school sports. Findings indicate important disparities in Spanish-speaking Hispanic children’s PA participation.     

Raw soya-bean flour increases cholecystokinin release in man

1. The aim of the present study was to determine whether oral ingestion of raw soya-bean flour, which contains trypsin inhibitors, alters the release of cholecystokinin (CCK) in man. 2. Eleven healthy volunteers ate two mixed meals: one with raw soya-bean flour and the other with soya-bean flour that had been heat-treated. The two flours inhibited 34 and 3 mg trypsin/g flour respectively. 3. CCK was measured in plasma using a bioassay based on the release of amylase (EC 3.2.1.1) from dispersed rat pancreatic acini. 4. The peak CCK response was 16.8 (SE 8.1) pmol/l with raw soya-bean flour but 4.9 (SE 2.8) pmol/l with heat-treated flour (P less than 0.05). 5. We conclude that ingestion of raw soya-bean flour increases CCK release in man and that heat treatment which reduces the trypsin inhibitor content of the flour also diminishes its CCK-releasing effect.     

Folding of the conserved domain but not of flanking regions in the integrin β2 subunit requires association with the α subunit

We have used immunoprecipitation with mAbs to probe folding during biosynthesis of the β₂ integrin subunit of lymphocyte function-associated antigen 1 (LFA-1; CD11a/CD18) before and after association with the α_L subunit. An evolutionarily conserved region is present in the β₂ subunit between amino acid residues 102 and 344. mAbs to one subregion before the conserved region, and two subregions after the conserved domain, immunoprecipitated both the unassociated β′₂ precursor and mature α_L/β₂ complex, suggesting portions of these subregions are folded before association with α_L. An activating mAb to the C-terminal cysteine-rich region, KIM127, preferentially bound to the unassociated β subunit, suggesting that it may bind to an epitope that is in an αβ interface in unactivated LFA-1. By contrast, mAbs to five different epitopes in the conserved region did not react with unassociated β′₂ precursor, suggesting that this region folds after α_L association and is intimately associated with the α_L subunit in the α_L/β₂ complex. mAbs to two different epitopes that involve the border between the conserved region and the C-terminal segment, were fully or partially reactive with the β′₂ precursor, suggesting that this region is partially folded before association with α_L. The findings suggest that the conserved region is a distinct folding and hence structural unit, and is intimately associated with the α subunit.