Removal of Pb(II) from water using keratin colloidal solution obtained from wool

The aim of this study is to investigate the use of keratin colloidal solution, which was obtained from wool, for the removal of Pb(II) from water. The addition of keratin colloidal solution (15 g L-1, 0.30 mL) to a Pb(II) solution (1.0 mM, 0.90 mL, pH 5.0) resulted in the formation and precipitation of a Pb-keratin aggregate. Measurement of the Pb(II) and protein concentrations in the supernatant solution revealed that 88 and 99 % of the Pb(II) and keratin protein were removed from the solution, respectively. The maximum Pb(II) uptake capacity of keratin in the colloidal solution was 43.3 mg g(-1). In addition, the Pb-keratin aggregate was easily decomposed via the addition of nitric acid, which enabled the recovery of Pb(II). However, aggregation did not occur in solutions with Pb(II) concentrations below 0.10 mM. Therefore, we used a keratin colloidal solution encapsulated in a dialysis cellulose tube to remove Pb(II) from 0.10 mM solutions, which enabled the removal of 95 % of the Pb(II). From these results, we conclude that keratin colloidal solution is useful for the treatment of water polluted with Pb(II).ArticleENVIRONMENTAL SCIENCE AND POLLUTION RESEARCH. 20(9):6531-6538 (2013)journal articl

ドウジキ ニ 1ガタ トウニョウビョウ オ ハッショウシ タセンセイ ジコ メンエキ ショウコウグン IIIガタ ト シンダンシ エタ コウキ コウレイシャ ノ ドウホウ ショウレイ

We herein presented a case of a ７９-year-old woman who was referred to our hospital with dry mouth and polyuria that had persisted for three months prior to her admission. She developed Hashimoto disease at ７３ years old and pernicious anemia at ７８ years old. Her blood glucose level was ６８２ mg/dl, HbA１c １４．６％, and urinary ketone was positive ; therefore, she was diagnosed with diabetic ketosis. Acute-onset autoimmune type １ diabetes mellitus was diagnosed based on the diagnostic criteria for acute-onset type １ diabetes mellitus （２０１２） by the committee of the Japan Diabetes Society. Autoimmune polyglandular syndrome was subsequently diagnosed based on the complications of type １ diabetes and Hashimoto’s thyroiditis. Her ８７-year-old brother had developed acute-onset autoimmune type １ diabetes ２ months before his sister was hospitalized. Autoimmune polyglandular syndrome type III was also diagnosed because he had autoimmune thyroid disease. No epidemiological data are currently available for late elderly with acute-onset type １ diabetes in Japan. To the best of our knowledge, this is the first case of acute-onset autoimmune type １ diabetes mellitus that developed around the same time period in an elderly brother and sister who were diagnosed with autoimmune polyglandular syndrome type III. Common genetic and environmental factors were etiologically implicated in the almost simultaneous onset between these siblings

14-3-3 suppresses the nuclear localization of threonine 157-phosphorylated p27(Kip1)

p27(Kip1) (p27), a CDK inhibitor, migrates into the nucleus, where it controls cyclin–CDK complex activity for proper cell cycle progression. We report here that the classical bipartite-type basic amino-acid cluster and the two downstream amino acids of the C-terminal region of p27 function as a nuclear localization signal (NLS) for its full nuclear import activity. Importin α3 and α5, but not α1, transported p27 into the nucleus in conjunction with importin β, as evidenced by an in vitro transport assay. It is known that Akt phosphorylates Thr 157 of p27 and this reduces the nuclear import activity of p27. Using a pull-down experiment, 14-3-3 was identified as the Thr157-phosphorylated p27NLS-binding protein. Although importin α5 bound to Thr157-phosphorylated p27NLS, 14-3-3 competed with importin α5 for binding to it. Thus, 14-3-3 sequestered phosphorylated p27NLS from importin α binding, resulting in cytoplasmic localization of NLS-phosphorylated p27. These findings indicate that 14-3-3 suppresses importin α/β-dependent nuclear localization of Thr157-phosphorylated p27, suggesting implications for cell cycle disorder in Akt-activated cancer cells

Nuclear Import of Epstein-Barr Virus Nuclear Antigen 1 Mediated by NPI-1 (Importin α5) Is Up- and Down-Regulated by Phosphorylation of the Nuclear Localization Signal for Which Lys379 and Arg380 Are Essential

Epstein-Barr virus (EBV) nuclear antigen 1 (EBNA-1) is essential for replication of episomal EBV DNAs and maintenance of latency. Multifunctional EBNA-1 is phosphorylated, but the significance of EBNA-1 phosphorylation is not known. Here, we examined the effects on nuclear translocation of Ser phosphorylation of the EBNA-1 nuclear localization signal (NLS) sequence, 379Lys-Arg-Pro-Arg-Ser-Pro-Ser-Ser386. We found that Lys379Ala and Arg380Ala substitutions greatly reduced nuclear transport and steady-state levels of green fluorescent protein (GFP)-EBNA1, whereas Pro381Ala, Arg382Ala, Pro384Ala, and Glu378Ala substitutions did not. Microinjection of modified EBNA-1 NLS peptide-inserted proteins and NLS peptides cross-linked to bovine serum albumin (BSA) showed that Ala substitution for three NLS Ser residues reduced the efficiency of nuclear import. Similar microinjection analyses demonstrated that phosphorylation of Ser385 accelerated the rate of nuclear import, but phosphorylation of Ser383 and Ser386 reduced it. However, transfection analyses of GFP-EBNA1 mutants with the Ser-to-Ala substitution causing reduced nuclear import efficiency did not result in a decrease in the nuclear accumulation level of EBNA-1. The results suggest dynamic nuclear transport control of phosphorylated EBNA-1 proteins, although the nuclear localization level of EBNA-1 that binds to cellular chromosomes and chromatin seems unchanged. The karyopherin α NPI-1 (importin α5), a nuclear import adaptor, bound more strongly to Ser385-phosphorylated NLS than to any other phosphorylated or nonphosphorylated forms. Rch1 (importin α1) bound only weakly and Qip1 (importin α3) did not bind to the Ser385-phosphorylated NLS. These findings suggest that the amino-terminal 379Lys-Arg380 is essential for the EBNA-1 NLS and that Ser385 phosphorylation up-regulates nuclear transport efficiency of EBNA-1 by increasing its binding affinity to NPI-1, while phosphorylation of Ser386 and Ser383 down-regulates it