Soft roll linings - better conduits: First press of the PS 2, paper machine, Belisce, Croatia

Paper with demanding technical properties is formed in the press of the paper machine when the paper pulp is passed between the rolls. In order to form paper in the appropriate manner, an elastic lining with particular stiffness is spread over the rolls. In this study a practical example of how softer linings generally give better results concerning the percentage of the dry part and the paper structure is presented. From the rubber roll manufacturers' point of view, the weak side of soft linings lies in greater deformations, which present difficulties in obtaining good adhesion between the lining and metal core of the roll. Only the best manufacturers in the industry can match such high demands

Decelerated degradation of short peptides by the 20S proteasome

AbstractBased on a twelve residue master peptide comprising all five specific cleavage sites defined for the proteasome, a set of variant peptides was generated in order to probe specificity and to elucidate the mechanism which determines product size. It is shown that the rate of degradation by the 20S proteasome from Thermoplasma acidophilum depends critically on the length of the peptide substrate. Peptides of 14 residues and longer are degraded much faster than shorter peptides although the sites of cleavage remain unchanged. The decelerated degradation of peptides shorter than 14 residues explains the accumulation of products with an average length of seven to nine residues

Glucosamine (GlcN) Decreases Phosphorylation of FOXO1 and Paxillin in NK-92 Cells.

<p>(A) Representative immunoblots show the immunoprecipitation of whole-cell lysates, using anti-FOXO1 antibodies, followed by immunoblotting with anti-phospho-Ser antibodies (upper), and reblotting with anti-<i>O</i>-GlcNAc (middle) antibodies, of the NK-92 cells untreated or treated with GlcN. (B) Whole-cell lysates were subjected to immunoprecipitation with anti-paxillin antibodies. Immunoprecipitates were analyzed by immunoblotting with anti-phospho-Thr antibodies (upper), and anti- <i>O</i>-GlcNAc (middle). Total paxillin levels were analyzed using the anti-paxillin antibodies (lower).</p

Glucosamine (GlcN) Prolongs ERK Phosphorylation in NK-92 cells.

<p>(A) Representative western blots showing the expression of phosphorylated P38, JNK, and ERK, and total MAPK protein levels in NK-92 cells treated with IL2 alone or in combination with GlcN. (B) Quantification of phosphorylated P38, JNK, and ERK levels in cells treated with IL2 alone or in combination with GlcN, normalized to the total protein levels. Error bars represent standard deviations.</p

Glucosamine (GlcN) Prevents Lytic Granule Polarization in NK Cells.

<p>(A) Polarization of granules expressing perforin (green) in the NK-92 and K562 cell conjugates, in presence or absence of GlcN (upper panels). Representative images of at least 60 NK-92/K562 conjugates are shown. Polarization of granules expressing perforin (green) in the mouse primary NK cell and 4T1 cell conjugates, in presence or absence of GlcN (lower panels). Representative images of at least 20 NK/4T1 conjugates are presented. Conjugates were considered polarized when the perforin signal was located in the quarter of the NK cell nearest to the target cell (merged image). Right, bright-filter images, for detection of the conjugates. (B) Distribution analysis, showing the percentage of NK-92 and K562 conjugates with polarized lytic granules in the untreated and GlcN-treated cells. (C) Western blots of NK-92 cell lysates untreated and treated with GlcN, showing the amount of perforin.</p

Glucosamine (GlcN) Treatment Affects Cathepsin C and E Intracellular Levels and Localization in NK-92 cells.

<p>(A) Activities of specific cysteine cathepsins (substrate, Z-Phe-Arg-AMC), cathepsin E (KYS-1), and cathepsin C (H-Gly-Phe-AMC) determined in NK-92 cells treated with or without GlcN. Enzyme activities are presented as fold changes relative to the activity of these enzymes in the untreated cells. (B) Secreted cathepsin C activity following GlcN treatment. Results are presented as fold changes relative to the values obtained for the controls samples. Error bars represent standard deviations of the results obtained from five independent experiments. (C) Cathepsin E and C levels in the lysate of the untreated and GlcN-treated NK-92 cells. β-actin levels were used for normalization. (D) Cathepsin C <i>N</i>-glycosylation type in the GlcN-treated and untreated cells determined using EndoH (EH) and PNGaseF (P). (E) Subcellular localization of cathepsins C (white) and E (green) in NK-92 cells cultured with K562 cells, untreated or treated with GlcN. Cell nuclei were stained with DAPI, the right panel represent bright- filter (BF). Merged images show the overlapping signals. (F) Cathepsin C (green) and perforin (red) colocalization in GlcN-treated and untreated cells. The colocalized area panel shows colocalized area calculated by the LAS AF software.</p

Glucosamine (GlcN) Triggers Nuclear Translocation of Phosphorylated ERK.

<p>(A) Representative images of phospho-ERK (green) expression in NK-92 cells treated with either GlcN and IL2 or IL2 alone. DAPI was used to stain the NK-92 cell nuclei. The merged image shows the overlapping DAPI and phospho-ERK signals. (B) Ratios of the nuclear and cytoplasmic concentrations of p-ERK in the GlcN-treated and untreated NK-92 cells. Sixty individual cells were analyzed in three independent microscopic slides. (C) Imunoblot shows the amount of p-ERK in the nuclei and cytoplasm of control and IL-2 activated (for 60 minutes) cells, treated with GlcN or left untreated. Histone H3 and GAPDH are showing that nuclear and cytosolic fractions were clear.</p

Glucosamine (GlcN) Suppresses the Cytotoxic Activity of NK-92 Cells Against K562 Cells.

<p>(A) Cytotoxicity of NK-92 cells against K562 cells, following treatment of the cultures overnight (ON) with different concentrations of GlcN or <i>N</i>-acetyl GlcN (GlcNAc). (B) Cytotoxicity of NK-92 cells against K562 cells after ON pretreatment with GlcN, followed by 5-mM GlcN supplementation during the assay. All experiments were performed independently five times. Error bars represent standard deviations.</p