Типологія синтаксичних конструкцій в німецькій та українській мовах

Німецька та українська мови є односистемними мовами: обидві належать до індоєвропейської мовної сім’ї. Спільні корені та тривалий період ізольованого розвитку, вказують на те, що вказані мови мають характеристики подібності та відмінності в своій внутрішній будові. Німецька та українська належать до синтетичного типу флективних мов. Це означає, що граматичне значення слів у них виражається, здебільшого, за допомогою системи флексій і реалізується в межах одного графічного слова. Але флективна система німецької мови бідніша, ніж у слов’янських мовах.Немецкий и украинский языки являются односистемными языками: оба принадлежат к индоевропейской языковой семье. Общие корни и длительный период изолированного развития, указывают на то, что указанные языки имеют характеристики сходства и различия в своем внутреннем строении. Немецкий и украинский принадлежат к синтетическому типу флективных языков. Это означает, что грамматическое значение слов в них выражается, в основном, с помощью системы флексий и реализуется в пределах одного графического слова. Но флективная система немецкого языка беднее, чем в славянских языках.German and Ukrainian are single-system languages: both belong to the Indo-European language family. Common roots and a long period of isolated development, indicate that these languages ​​have characteristics of similarity and differences in their internal structure. German and Ukrainian belong to the synthetic type of inflectional languages. This means that the grammatical meaning of words in them is expressed, mainly, with the help of a system of inflexions and is realized within a single graphic word. But the inflectional system of the German language is poorer than in the Slavic languages

Comparative Proteomic Expression Profile in All-<i>trans</i> Retinoic Acid Differentiated Neuroblastoma Cell Line

Neuroblastoma (NB) is an infant tumor which frequently differentiates into neurons. We used two-dimensional differential in-gel electrophoresis (2D-DIGE) to analyze the cytosolic and nuclear protein expression patterns of LAN-5 cells following neuronal differentiating agent all-trans-retinoic acid treatment. We identified several candidate proteins, from which Gβ2 and Prefoldin 3 may have a role on NB development. These results strength the use of proteomics to discover new putative protein targets in cancer. Keywords: neuroblastoma • all-trans-retinoic acid • 2D-DIGE • LAN-5 human neuroblastoma cell lin

Changes of the Hepatic Proteome in Hepatitis B-Infected Mouse Model at Early Stages of Fibrosis

Liver fibrosis (LF) is the accumulation of extracellular matrix (ECM) proteins due to chronic liver injury. We used two-dimensional differential in-gel electrophoresis (2D-DIGE) to perform a comparative analysis of cytosolic and nuclear protein patterns of nontransgenic (NTg) and HBV transgenic (Tg) mice livers at early stages of fibrosis. We identified several candidate proteins, involved in a variety of pathways, which could be used as putative biomarkers for LF early detection

Proteomic Signatures in Thapsigargin-Treated Hepatoma Cells

Thapsigargin, an inhibitor of the endoplasmic reticulum (ER) calcium transporters, generates Ca2+-store depletion within the ER and simultaneously increases Ca2+ level in the cytosol. Perturbation of Ca2+ homeostasis leads cells to cope with stressful conditions, including ER stress, which affect the folding of newly synthesized proteins and induce the accumulation of unfolded polypeptides and eventually apoptosis, via activation of the unfolded protein response pathway. In the present work, we analyzed the proteome changes in human hepatoma cells following acute treatment with thapsigargin. We highlighted a peculiar pattern of protein expression, marked by altered expression of calcium-dependent proteins, and of proteins involved in secretory pathways or in cell survival. For specific deregulated proteins, the thapsigargin-induced proteomic signature was compared by Western blotting to that resulting from the treatment of hepatoma cells with reducing agents or with proteasome inhibitors, to elicit endoplasmic reticulum stress by additional means and to reveal novel, potential targets of the unfolded protein response pathway

Proteomic Signatures in Thapsigargin-Treated Hepatoma Cells

Thapsigargin, an inhibitor of the endoplasmic reticulum (ER) calcium transporters, generates Ca2+-store depletion within the ER and simultaneously increases Ca2+ level in the cytosol. Perturbation of Ca2+ homeostasis leads cells to cope with stressful conditions, including ER stress, which affect the folding of newly synthesized proteins and induce the accumulation of unfolded polypeptides and eventually apoptosis, via activation of the unfolded protein response pathway. In the present work, we analyzed the proteome changes in human hepatoma cells following acute treatment with thapsigargin. We highlighted a peculiar pattern of protein expression, marked by altered expression of calcium-dependent proteins, and of proteins involved in secretory pathways or in cell survival. For specific deregulated proteins, the thapsigargin-induced proteomic signature was compared by Western blotting to that resulting from the treatment of hepatoma cells with reducing agents or with proteasome inhibitors, to elicit endoplasmic reticulum stress by additional means and to reveal novel, potential targets of the unfolded protein response pathway

Proteomic Signatures in Thapsigargin-Treated Hepatoma Cells

Thapsigargin, an inhibitor of the endoplasmic reticulum (ER) calcium transporters, generates Ca2+-store depletion within the ER and simultaneously increases Ca2+ level in the cytosol. Perturbation of Ca2+ homeostasis leads cells to cope with stressful conditions, including ER stress, which affect the folding of newly synthesized proteins and induce the accumulation of unfolded polypeptides and eventually apoptosis, via activation of the unfolded protein response pathway. In the present work, we analyzed the proteome changes in human hepatoma cells following acute treatment with thapsigargin. We highlighted a peculiar pattern of protein expression, marked by altered expression of calcium-dependent proteins, and of proteins involved in secretory pathways or in cell survival. For specific deregulated proteins, the thapsigargin-induced proteomic signature was compared by Western blotting to that resulting from the treatment of hepatoma cells with reducing agents or with proteasome inhibitors, to elicit endoplasmic reticulum stress by additional means and to reveal novel, potential targets of the unfolded protein response pathway

Selected spots for MS analysis.

<p>(<b>A</b>) Coloured circles indicate the position on Pro-Q Diamond-stained gels of the 13 protein spots picked for MS analysis. Red circles are associated to hyperphosphorylated proteins; blue circles are associated to hypophosphorylated proteins. Boxes show an enlargement of picked spots. (<b>B</b>) Fold change values for the 13 selected spots. All the spots were differentially stained in anti-TG2-treated cells with respect to control IgG-treated cells. <i>P<0.05</i> (Student’s t-test).</p

MS analysis and database searching of the 13 spots with differential phosphorylation level in samples from anti-TG2 treated cells and from control-IgG treated cells.

<p>Spot number, UniProt protein ID and accession code, protein name, Mascot score, theoretical protein mass and pI values, number of peptide matches, sequence coverage and emPAI values are listed for each protein.</p

Representative 2-D-maps of phosphorylated and total proteins from Caco-2 cells treated with anti-TG2/control antibodies.

<p>Total protein extracts (150 µg) were separated on linear IPG strips 7 cm, pH 4.0–7.0, followed by 10%-sodium dodecyl sulphate polyacrylamide gel electrophoresis. 2-D gels were stained with the phosphoprotein-specific reagent Pro-Q Diamond (<b>A</b>) and with the SyproRuby dye to detect total proteins (<b>B</b>). 2-D-maps are representative of three biological independent replicates.</p

Validation of differential phosphorylation levels by western blot analysis.

<p>Total protein extracts (150 µg) from Caco-2 cells treated with anti-TG2 antibodies or with control IgG were separated by 2-DE using linear IPG strips, pH 5.5–6.7 for EF1γ (<b>A</b>), pH 4.7–5.9 for HSP60 (<b>B</b>), pH 3.9–5.1 for TCTP (<b>C</b>). Specific proteins were identified by immunoblot analysis.</p