Anti-Inflammatory Activity of Fucoidan Extracts In Vitro

Fucoidans are sulfated, complex, fucose-rich polymers found in brown seaweeds. Fucoidans have been shown to have multiple bioactivities, including anti-inflammatory effects, and are known to inhibit inflammatory processes via a number of pathways such as selectin blockade and enzyme inhibition, and have demonstrated inhibition of inflammatory pathologies in vivo. In this current investigation, fucoidan extracts from Undaria pinnatifida, Fucus vesiculosus, Macrocystis pyrifera, Ascophyllum nodosum, and Laminaria japonica were assessed for modulation of pro-inflammatory cytokine production (TNF-α, IL-1β, and IL-6) by human peripheral blood mononuclear cells (PBMCs) and in a human macrophage line (THP-1). Fucoidan extracts exhibited no signs of cytotoxicity in THP-1 cells after incubation of 48 h. Additionally, all fucoidan extracts reduced cytokine production in LPS stimulated PBMCs and human THP-1 cells in a dose-dependent fashion. Notably, the 5–30 kDa subfraction from Macrocystis pyrifera was a highly effective inhibitor at lower concentrations. Fucoidan extracts from all species had significant anti-inflammatory effects, but the lowest molecular weight subfractions had maximal effects at low concentrations. These observations on various fucoidan extracts offer insight into strategies that improve their efficacy against inflammation-related pathology. Further studies should be conducted to elucidate the mechanism of action of these extracts.     

Spatial Variations and Trends in Acid Deposition in Japan Within a 100 Km × 100 Km Region from 1989 to 1999

Water, Air, &; Soil Pollution - A monitoring network for acid deposition that consisted of five sites in Hyogo, Japan, and covered a region of about 100 km × 100 km revealed the spatial...     

R132 mutations in canine isocitrate dehydrogenase 1 (IDH1) lead to functional changes

Glioma is the second most common intracranial neoplasia in dogs, but the pathogenic mechanisms remain unclear. In humans, isocitrate dehydrogenase 1 (IDH1) is frequently mutated in gliomas. Although almost all human IDH1 mutations have been identified as involving the Arg132 codon, few studies have reported structural, functional, and mutational information for canine IDH1. Therefore, in this study, we cloned the canine IDH1 homologue and used PCR mutagenesis to substitute the wildtype (WT) Arg132 with His (R132H) or Ser (R132S). WT and mutated IDH1 were overexpressed in HeLa cells, and their presence was confirmed by immunoblotting and immunocytochemistry using mutation-specific antibodies. The IDH1 activity between WT, R132H, and R132S transfectants was compared by measuring the production of NADH and NADPH. NADPH production in R132H and R132S transfectants was lower than that in WT, but NADH levels were not significantly different. Finally, we detected increased expression of hypoxia inducible factor 1 alpha (HIF-1α) in the R132H and R132S transfectants. These results indicated that the canine IDH1 Arg132 mutation has the potential to induce carcinogenesis in canine somatic cells.     

Identification of food-derived elastin peptide, prolyl-glycine (Pro-Gly), in human blood after ingestion of elastin hydrolysate

Elastin hydrolysate has apparent beneficial effects, and the food-derived peptide prolyl-glycine (Pro-Gly) is present in human blood after oral ingestion. Following ingestion of elastin hydrolysate (10 g/60 kg body weight) by healthy human volunteers, peripheral blood was used to prepare plasma samples from which peptides were extracted by solid phase extraction and fractionated by size-exclusion chromatography (SEC). Peptides in the SEC fractions were derivatized with phenyl isothiocyanate (PITC) and resolved by reversed phase (RP)-HPLC. Pro-Gly was the major food-derived elastin peptide, reaching a maximum (18 μM) at 30 min after ingestion, and decreasing to approximately 20% at 4 h after ingestion. Finally, in cell culture, levels of Pro-Gly in the medium above 0.1 μg/mL significantly enhanced elastin synthesis of normal human dermal fibroblasts (NHDF) without affecting the rate of cell proliferation.     

Chemistry of Fog Water Collected in the Mt. Rokko Area (Kobe City, Japan) between April 1997 and March 2001

Fog chemistry was studied for four years (April 1997–March 2001) at Mt. Rokko (altitude 931 m) in Kobe, Japan. A collection of samples was obtained at a mountainous site close to a highly industrialized area. The samples were collected by an active string-fog collector. The summer fog was dense and frequent. The geography of Mt. Rokko is linked to the seasonality of the occurrence and the thickness of the fog. Among the meteorological parameters, the relative humidity was important for the occurrence of fog. The correlation of the concentrations of the components in fog water indicated that (NH₄)₂SO₄ and/or NH₄HSO₄ were involved in the process of the formation of fog drops in the atmosphere. The concentration of the components decreased with an increase in the liquid water content (LWC) of the fog, and the seasonal variation of the concentration of some components depended on the seasonal variation of the LWC. The equivalent ratio of NO₃ ^? to non-sea salt (nss?) SO₄ ^2? was considerably larger than that in precipitation. Ammonium ion accounted for the largest percentage of cations, which indicates that NH₄ ⁺ was an important counter cation for NO₃ ^? and nss-SO₄ ^2?. A unique fog event in which the air pollutants seemed to be scavenged stoichiometrically was sometimes observed. The methodology used for collecting fog water at 60 mL intervals provided detailed information.     

Purification and characterization of carbon monoxide dehydrogenase from the aerobic hyperthermophilic archaeon <Emphasis Type="Italic">Aeropyrum pernix</Emphasis>

The aerobic hyperthermophilic archaeon Aeropyrum pernix expresses carbon monoxide (CO) oxidation activity under heterotrophic growth conditions. Using activity stain gel analysis, CO oxidation activity was detected in a protein with a molecular mass of 210 kDa. The 210 kDa CODH protein was purified to homogeneity from A. pernix. Aeropyrum Mo-CODH catalyzed the oxidation of CO with a specific activity of 2.1 μmol CO min⁻¹ mg⁻¹ at 95°C, pH 8.0 using methyl viologen as the electron acceptor. The CODH protein showed high oxygen and thermo stability. The protein contains three subunits: L (86.6 kDa), M (34.5 kDa), and S (12.6 kDa), which form the LM₂S complex. The molecular mass of the complex was calculated by gel filtration and found to be 163.7 kDa. N-terminal amino acid sequencing and peptide mass fingerprinting analysis of the subunits indicated that they corresponded to NP_148462.1, NP_148464.2, and NP_148465.1, and their genes annotated the molybdo iron-sulfur flavoprotein carbon monoxide dehydrogenase S, L, and M subunits, respectively. Phylogenetic analysis revealed that CODH belongs to a novel clade of diverse CODHs.