Mergers and acquisitions in Ukraine's banking: recent trends

У статті розглянуто особливості розвитку ринку M&A в банківському секторі України. Виокремлено та обґрунтовано сучасні тенденції на ринку, задля отримання більш повної його характеристики.The article is contained the features of market in the banking sector of Ukraine. Outlined and justified the current trends in the market, in order to obtain more of its characteristics

Loss of SORLA impairs vesicular trafficking of TrkB.

<p>(<b>A</b>) Movement of TrkB-EGFP in neurites of cultured hippocampal neurons. Arrows indicate anterograde (red) and retrograde movement (yellow), or no movement (blue) of vesicles. Images were captured every 2 sec. (<b>B</b>) The cumulative distance travelled by TrkB-EGFP fusion proteins either anterogradely or retrogradely is significantly reduced in <i>Sorl1^−/−</i> neurons as compared to controls (n = 14–16, Student’s <i>t</i>-test). (<b>C</b>) The cumulative anterograde or retrograde speed of the TrkB-EGFP fusion protein is significantly reduced in <i>Sorl1^−/−</i> neurons as compared to <i>Sorl1^+/+</i> cells (n = 14–16, Student’s <i>t</i>-test).</p

The global BDNF-dependent proteome response is altered in SORLA-deficient neurons.

<p>(<b>A</b>) A prototypic two-dimensional polyacrylamid gel of proteins from <i>Sorl1^−/−</i> primary cortical neurons stained with silver nitrate. Significant protein spot alterations in response to BDNF treatment (150 ng/ml for 2 days) in wild type neurons (red circles), in SORLA-deficient neurons (blue circles) or in both genotypes (green circles) as compared to untreated samples are indicated. (n = 6 biological replicates per genotype; Student’s <i>t</i>-test p<0.05). (<b>B</b>) Total number of protein spots altered in primary cortical neurons of the indicated genotypes in response to BNDF treatment as exemplified in panel A. (n = 6 biological replicates per genotype; Student’s <i>t</i>-test p<0.05).</p

Loss of SORLA aggravates neuromotoric deficits in Huntington’s disease mice.

<p>(<b>A</b>) At 10 weeks of age, Huntington’s disease mice deficient for SORLA (HD82x<i>Sorl1^−/−</i>) display aggravated hind limb clasping compared with HD82 control littermates (HD82x<i>Sorl1^+/+</i>). (<b>B, C</b>) Worsening of neuromotoric deficits due to loss of SORLA is also seen when comparing (HD82x<i>Sorl1^−/−</i>) animals with (HD82, <i>Sorl1^+/+</i>) controls of either sex at 10 (B) and 18 weeks of age (C) during consecutive days of rotarod performance test (n = 8–9, Mann-Whitney-U). (<b>D</b>) No difference in rotarod performance is seen comparing 10 weeks-old <i>Sorl1^+/+</i> and <i>Sorl1^−/−</i> mice matched for age and sex (n = 10, Mann-Whitney-U).</p

Selected list of proteins differentially regulated in SORLA-deficient versus wild type neurons following chronic BDNF application.

<p>The values indicate ratio of protein spot volume changes (increase ↑ or decrease ↓; ANOVA, p<0.05). Where applicable, data for different iso-spots of the same protein are given. n.a., not altered.</p

Reduced BDNF-dependent activation of TrkB in SORLA-deficient neurons.

<p>(<b>A, B</b>) Quantification of phosphorylated (p) forms of TrkB, Akt, and ERK in primary cortical neurons either non-treated (−) or treated with 150 ng/ml BDNF for 20 min (+) using Western blotting (A) and densitometric scanning of replicate blots (B). <i>Sorl1^−/−</i> neurons show reduced levels of pTrkB, pAKT, and pERK compared with <i>Sorl1^+/+</i> cells (n = 6–12, Mann-Whitney U test). (<b>C, D</b>) Quantification of total levels of TrkB, Akt, and ERK in primary neurons either non-treated (−) or treated with 150 ng/ml BDNF (+) for 20 min using Western blot (C) and densitometric scanning of replicate blots (D). Detection of tubulin (tub.) served as loading controls in A and C.</p

Production of Glycosylated Soluble Amyloid Precursor Protein Alpha (sAPPalpha) in <i>Leishmania tarentolae</i>

Soluble amyloid precursor protein alpha (sAPPalpha) is a cleavage product of the amyloid precursor protein (APP), the etiologic agent in Alzheimer’s disease (AD). Reduced expression of sAPPalpha was previously found in the brains of AD patients, and it was suggested that sAPPalpha might counteract neurotoxic effects of Abeta, another APP cleavage product with enhanced abundance in Alzheimer’s diseased brains. However, little is known about the biological functions of sAPPalpha. Thus, efficient production of this protein is a prerequisite for further studies. The unicellular eukaryotic parasite <i>Leishmania tarentolae</i> has recently emerged as a promising expression system for eukaryotic proteins due to its ability to posttranslationally modify proteins combined with easy cultivation and high protein yield. Interestingly, sAPPalpha produced in <i>L. tarentolae</i> was biologically active and glycosylated. In contrast to nonglycosylated sAPPalpha expressed in <i>Eschericha coli</i>, it also featured higher stability against enzymatic degradation. Detailed analysis of the glycosylation pattern of sAPPalpha produced in <i>L. tarentolae</i> by PGC–LC–ESI–MS/MS N-glycan analysis identified among eukaryotic species the highly conserved core pentasaccharide (Man3GlcNAc2) as being attached to Asn467 of sAPPalpha. Using oxonium ion scanning of CID–MS/MS spectra in combination with ETD fragmentation, we also identified two peptides (peptides 269–288 and 575–587) modified with <i>N</i>-acetyl hexosamine (HexNAc) residues. One of these O-glycosylation sites could be unambiguously assigned to Thr576 of sAPPalpha. This is the first time that O-glycosylation of a recombinant protein expressed in <i>L. tarentolae</i> has been demonstrated. Together, human sAPPalpha produced in <i>L. tarentolae</i> was N- and O-glycosylated on similar sites as described for mammalian-expressed sAPPalpha and showed similar biological activity. This demonstrates that <i>L. tarentolae</i> is a very suitable and simple to handle expression system for mammalian glycoproteins

Generation and Characterization of a <i>Leishmania tarentolae</i> Strain for Site-Directed <i>in Vivo</i> Biotinylation of Recombinant Proteins

<i>Leishmania tarentolae</i> is a non-human-pathogenic Leishmania species of growing interest in biotechnology, as it is well-suited for the expression of human recombinant proteins. For many applications it is desirable to express recombinant proteins with a tag allowing easy purification and detection. Hence, we adopted a scheme to express recombinant proteins with a His₆-tag and, additionally, to site-specifically <i>in vivo</i> biotinylate them for detection. Biotinylation is a relatively rare modification of endogenous proteins that allows easy detection with negligible cross-reactivity. Here, we established a genetically engineered <i>L. tarentolae</i> strain constitutively expressing the codon-optimized biotin-protein ligase from <i>Escherichia coli</i> (BirA). We thoroughly analyzed the strain for functionality using 2-D polyacrylamide-gel electrophoresis (PAGE), mass spectrometry, and transmission electron microscopy (TEM). We could demonstrate that neither metabolic changes (growth rate) nor structural abnormalities (TEM) occurred. To our knowledge, we show the first 2-D PAGE analyses of <i>L. tarentolae</i>. Our results demonstrate the great benefit of the established <i>L. tarentolae in vivo</i> biotinylation strain for production of dual-tagged recombinant proteins. Additionally, 2-D PAGE and TEM results give insights into the biology of <i>L. tarentolae</i>, helping to better understand Leishmania species. Finally, we envisage that the system is transferable to human-pathogenic species

CDK5 associated proteins significantly altered in expression after treatment of neurons with sAPPalpha (1 h, 48 h indicate duration of treatment; ↑ up-regulation, ↓ down-regulation, ratio treated/control).

<p>CDK5 associated proteins significantly altered in expression after treatment of neurons with sAPPalpha (1 h, 48 h indicate duration of treatment; ↑ up-regulation, ↓ down-regulation, ratio treated/control).</p

Reduced uptake of sAPPalpha in SORLA-deficient neurons.

<p>Quantification of human, recombinant sAPPalpha in primary cortical neurons either non-treated (control) or treated with 300 ng/ml sAPPalpha for 1 h using Western blotting (<b>A</b>) and densitometric scanning of replicate blots (<b>B</b>). <i>Sorl1^−/−</i> neurons show reduced levels sAPPalpha after one hour of treatment compared with wild-type cells (wt; n = 8, Mann-Whitney U test). Actin served as loading control.</p