Evaluation of iodine levels in daily dietary intake and urine of persons participating in epidemiological studies in the Krakow macro-region after the disaster in Czernobyl and level of iodine in drinking water of that region]

Following the Czernobyl accident, an epidemiologic study was undertaken in which the daily iodine intake was estimated in 15% of the population studied. Iodine excretion was measured in single morning urine specimens. The iodine content was also assessed in the water form wells and in cow-milk at farms in randomly chosen villages in the region of Krynica and Nowy Sacz. On the basis of a 24-hour diet recall, the mass of each food product consumed daily was estimated for 483 persons in the Kraków voivodship (14.4% of the total population) and for 397 persons in the Nowy Sacz voivodship (15.8% of the total population). Using this data, the nutrient content of the daily diet was calculated for each studied individual. Measurements of iodine content in water and cow-milk show relatively lower iodine levels in the Nowy Sacz voivodship. The estimated value of the iodine content in milk (5.5 micrograms/100 g of milk) was considered in the estimates of the chemical composition of the daily diet of the inhabitants of this region. The mean values of the daily energy as well as the protein and calcium consumption in all subpopulations grouped with respect to domicile, age and sex, fell within the recommended daily allowances for these groups. The iodine content, while widely scattered, concentrated around low values. The median values of the iodine content in children of age 3-10 years, age 10-16 years and in adults, were 66%, 48% and 25-40% of the recommended daily allowances, respectively. No particular differences in the food intakes were observed between inhabitants of Kraków and Nowy Sacz voivodships. Nor were significant differences found in the urine iodine excretion in groups of these regions. The low iodine content in the daily food intake may be an essential factor in the ethiology of the increasing number of thyroid goiter.     

Ceramide inhibits the outward potassium current in rat pinealocytes

CD1 mice lacking the CB1 receptors (knockout, KO) were compared with wild-type littermates for their ability to degrade N-arachidonoylethanolamine (anandamide, AEA) through a membrane transporter (AMT) and a fatty acid amide hydrolase (FAAH). The regional distribution and age-dependence of AMT and FAAH activity were investigated. Anandamide membrane transporter and FAAH increased with age in knockout mice, whereas they showed minor changes in wild-type animals. Remarkably, they were higher in all brain areas of 6-month-old knockout versus wild-type mice, and even higher in 12-month-old animals. The molecular mass (approximately 67 kDa) and isoelectric point (approximately 7.6) of mouse brain FAAH were determined and the FAAH protein content was shown to parallel the enzyme activity. The kinetic constants of AMT and FAAH in the cortex of wild-type and knockout mice at different ages suggested that different amounts of the same proteins were expressed. The cortex and hippocampus of wild-type and knockout mice contained the following N-acylethanolamines: AEA (8% of total), 2-arachidonoylglycerol (5%), N-oleoylethanolamine (20%), N-palmitoylethanolamine (53%) and N-stearoylethanolamine (14%). These compounds were twice as abundant in the hippocampus as in the cortex. Minor differences were observed in AEA or 2-arachidonoylglycerol content in knockout versus wild-type mice, whereas the other compounds were lower in the hippocampus of knockout versus wild-type animals.     

The 20S proteasome processes NF-kappaB1 p105 into p50 in a translation-independent manner

The NF-kappaB p50 is the N-terminal processed product of the precursor, p105. It has been suggested that p50 is generated not from full-length p105 but cotranslationally from incompletely synthesized molecules by the proteasome. We show that the 20S proteasome endoproteolytically cleaves the fully synthesized p105 and selectively degrades the C-terminus of p105, leading to p50 generation in a ubiquitin-independent manner. As small as 25 residues C-terminus to the site of processing are sufficient to promote processing in vivo. However, any p105 mutant that lacks complete ankyrin repeat domain (ARD) is processed aberrantly, suggesting that native processing must occur from a precursor, which extends beyond the ARD. Remarkably, the mutant p105 that lacks the internal region including the glycine-rich region (GRR) is completely degraded by 20S proteasome in vitro. This suggests that the GRR impedes the complete degradation of the p105 precursor, thus contributing to p50 generation.     

Microbial flocculant from Arcuadendron sp. TS-49

Summary A flocculant was purified from the culture broth of Archuadendron sp. TS-49 by a series of precipitations with acetone, 60% ammonium sulfate-butanol, salting-out by dialysis, and cetylpyridinium chloride. The flocculating activity was observed most highly at pH 3.0 and markedly enhanced by the addition of salts, especially in the case of FeCl₃ or FeSO₄. This bioflocculant efficiently flocculated all tested solids, including various microorganisms and organic/ inorganic materials. Qualitative analyses of the bioflocculant showed that it might contain hexosamine, uronic acid, neutral sugar, and protein.     

Induction of base damages representing a high risk site for double-strand DNA break formation in genomic DNA by exposure of cells to DNA damaging agents

DNA repair is known as a defense mechanism against genotoxic insults. However, the most lethal type of DNA damages, double-strand DNA breaks (DSBs), can be produced by DNA repair. We have previously demonstrated that when long patch base excision repair attempts to repair a synthetic substrate containing two uracils, the repair produces DSBs (Vispe, S. and Satoh, M. S. (2000) J. Biol. Chem. 275, 27386-27392 and Vispe, S., Ho, E. L., Yung, T. M., and Satoh, M. S. (2003) J. Biol. Chem. 278, 35279-35285). In this synthetic substrate, the two uracils are located on the opposite DNA strands (separated by an intervening sequence stable at 37 degrees C) and represent a high risk site for DSB formation. It is not clear, however, whether similar high risk sites are also induced in genomic DNA by exposure to DNA damaging agents. Thus, to investigate the mechanisms of DSB formation, we have modified the DSB formation assay developed previously and demonstrated that high risk sites for DSB formation are indeed generated in genomic DNA by exposure of cells to alkylating agents. In fact, genomic DNA containing alkylated base damages, which could represent high risk sites, are converted into DSBs by enzymes present in extracts prepared from cells derived from clinically normal individuals. Furthermore, DSBs are also produced by extracts from cells derived from ataxia-telangiectasia patients who show cancer proneness due to an impaired response to DSBs. These results suggest the presence of a novel link between base damage formation and DSBs and between long patch base excision repair and human diseases that occur due to an impaired response to DSB.     

Characterization of Fibrinogen Binding by Glycoproteins Srr1 and Srr2 of Streptococcus agalactiae

The serine-rich repeat glycoproteins of Gram-positive bacteria comprise a large family of cell wall proteins. Streptococcus agalactiae (group B streptococcus, GBS) expresses either Srr1 or Srr2 on its surface, depending on the strain. Srr1 has recently been shown to bind fibrinogen, and this interaction contributes to the pathogenesis of GBS meningitis. Although strains expressing Srr2 appear to be hypervirulent, no ligand for this adhesin has been described. We now demonstrate that Srr2 also binds human fibrinogen and that this interaction promotes GBS attachment to endothelial cells. Recombinant Srr1 and Srr2 bound fibrinogen in vitro, with affinities of K_D = 2.1 × 10⁻⁵ and 3.7 × 10⁻⁶ m, respectively, as measured by surface plasmon resonance spectroscopy. The binding site for Srr1 and Srr2 was localized to tandem repeats 6–8 of the fibrinogen Aα chain. The structures of both the Srr1 and Srr2 binding regions were determined and, in combination with mutagenesis studies, suggest that both Srr1 and Srr2 interact with a segment of these repeats via a “dock, lock, and latch” mechanism. Moreover, properties of the latch region may account for the increased affinity between Srr2 and fibrinogen. Together, these studies identify how greater affinity of Srr2 for fibrinogen may contribute to the increased virulence associated with Srr2-expressing strains.