Search

In high‐income nations, multiple micronutrient (MMN) supplementation during pregnancy is a common practice. We aimed to describe maternal characteristics associated with supplement use and daily dose of supplemental nutrients consumed in pregnancy, and whether guideline alignment and nutrient status are related to supplement use. The Queensland Family Cohort is a prospective, Australian observational longitudinal study. Maternal characteristics, nutrient intake from food and supplements, and biochemical nutrient status were assessed in the second trimester (n = 127). Supplement use was reported by 89% of participants, of whom 91% reported taking an MMN supplement. Participants who received private obstetric care, had private health insurance and had greater alignment to meat/vegetarian alternatives recommendations were more likely to report MMN supplement use. Private obstetric care and general practitioner shared care were associated with higher daily dose of supplemental nutrients consumed compared with midwifery group practice. There was high reliance on supplements to meet nutrient reference values for folate, iodine and iron, but only plasma folate concentrations were higher in MMN supplement versus nonsupplement users. Exceeding the upper level of intake for folic acid and iron was more likely among combined MMN and individual supplement/s users, and associated with higher plasma concentrations of the respective nutrients. Given the low alignment with food group recommendations and potential risks associated with high MMN supplement use, whole food diets should be emphasized. This study confirms the need to define effective strategies for optimizing nutrient intake in pregnancy, especially among those most vulnerable where MMN supplement use may be appropriate. Key messages: Multiple micronutrient (MMN) supplementation during pregnancy is a common practice in high‐income countries.Participants who received private obstetric care, had private health insurance and had greater alignment to meat/vegetarian alternatives recommendations were more likely to report MMN supplement use.There was high reliance on supplements to meet intake guidelines for folate, iodine and iron, which also raised concern for excess nutrient intake.This study confirms the need to define effective strategies for optimizing nutrient intake in pregnancy, including the promotion of whole food diets and appropriate use of MMN supplements. [ABSTRACT FROM AUTHOR]

Inorganic sulfate is essential for numerous functions in mammalian physiology. In the present study, we characterized the functional properties of the rat Na+–sulfate cotransporter NaS2 (rNaS2), determined its tissue distribution, and identified its gene ( slc13a4) structure. Expression of rNaS2 protein in Xenopus oocytes led to a Na+-dependent transport of sulfate that was inhibited by phosphate, thiosulfate, tungstate, selenate, oxalate, and molybdate, but not by citrate, succinate, or DIDS. Transport kinetics of rNaS2 determined a KM for sulfate of 1.26 mM. Na+ kinetics determined a Hill coefficient of n=3.0±0.7, suggesting a Na+:SO stoichiometry of 3:1. rNaS2 mRNA was highly expressed in placenta, with lower levels found in the brain and liver. slc13a4 maps to rat chromosome 4 and contains 17 exons, spanning over 46 kb in length. This gene produces two alternatively spliced transcripts, of which the transcript lacking exon 2 is the most abundant form. Its 5′ flanking region contains CAAT- and GC-box motifs and a number of putative transcription factor binding sites, including GATA-1, SP1, and AP-2 consensus sequences. This is the first study to characterize rNaS2 transport kinetics, define its tissue distribution, and resolve its gene ( slc13a4) structure and 5′ flanking region. [ABSTRACT FROM AUTHOR]

The transmissible spongiform encephalopathies are characterized by conversion of a host protein, PrPC (cellular prion protein), to a protease‐resistant isoform, PrPSc (prion protein scrapie isoform). The importance of the highly flexible, N‐terminal region of PrP has recently become more widely appreciated, particularly the biological activities associated with its metal ion‐binding domain and its potential to form a poly(L‐proline) II (PPII) helix. Circular dichroism spectroscopy of an N‐terminal peptide, PrP37–53, showed that the PPII helix is formed in aqueous buffer; as it also contains an Xaa–Pro–Gly consensus sequence, it may act as a substrate for the collagen‐modifying enzyme prolyl 4‐hydroxylase. Direct evidence for this modification was obtained by mass spectrometry and Edman sequencing in recombinant mouse PrP secreted from stably transfected Chinese hamster ovary cells. Almost complete conversion of proline to 4‐hydroxyproline occurs specifically at residue Pro44 of this murine protein; the same hydroxylated residue was detected, at lower levels, in PrPSc from the brains of scrapie‐infected mice. Cation binding and/or post‐translational hydroxylation of this region of PrP may regulate its role in the physiology and pathobiology of the cell. [ABSTRACT FROM AUTHOR]