@article{KurulganDemirciDemirciLinderetal.2012, author = {Kurulgan Demirci, Eylem and Demirci, Taylan and Linder, Peter and Trzewik, J{\"u}rgen and Gierkowski, Jessica Ricarda and Gossmann, Matthias and Kayser, Peter and Porst, Dariusz and Digel, Ilya and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l}, title = {rhAPC reduces the endothelial cell permeability via a decrease of contractile tensions induced by endothelial cells}, series = {Journal of Bioscience and Bioengineering}, volume = {113}, journal = {Journal of Bioscience and Bioengineering}, number = {2}, publisher = {Elsevier}, address = {Amsterdam}, issn = {1347-4421}, doi = {10.1016/j.jbiosc.2012.03.019}, pages = {212 -- 219}, year = {2012}, abstract = {All cells generate contractile tension. This strain is crucial for mechanically controlling the cell shape, function and survival. In this study, the CellDrum technology quantifying cell's (the cellular) mechanical tension on a pico-scale was used to investigate the effect of lipopolysaccharide (LPS) on human aortic endothelial cell (HAoEC) tension. The LPS effect during gram-negative sepsis on endothelial cells is cell contraction causing endothelium permeability increase. The aim was to finding out whether recombinant activated protein C (rhAPC) would reverse the endothelial cell response in an in-vitro sepsis model. In this study, the established in-vitro sepsis model was confirmed by interleukin 6 (IL-6) levels at the proteomic and genomic levels by ELISA, real time-PCR and reactive oxygen species (ROS) activation by florescence staining. The thrombin cellular contraction effect on endothelial cells was used as a positive control when the CellDrum technology was applied. Additionally, the Ras homolog gene family, member A (RhoA) mRNA expression level was checked by real time-PCR to support contractile tension results. According to contractile tension results, the mechanical predominance of actin stress fibers was a reason of the increased endothelial contractile tension leading to enhanced endothelium contractility and thus permeability enhancement. The originality of this data supports firstly the basic measurement principles of the CellDrum technology and secondly that rhAPC has a beneficial effect on sepsis influenced cellular tension. The technology presented here is promising for future high-throughput cellular tension analysis that will help identify pathological contractile tension responses of cells and prove further cell in-vitro models.}, language = {en} } @article{BassamHeschelerTemizArtmannetal.2012, author = {Bassam, Rasha and Hescheler, J{\"u}rgen and Temiz Artmann, Ayseg{\"u}l and Artmann, Gerhard and Digel, Ilya}, title = {Effects of spermine NONOate and ATP on the thermal stability of hemoglobin}, series = {BMC Biophysics}, volume = {5}, journal = {BMC Biophysics}, publisher = {BioMed Central}, address = {London}, issn = {2046-1682}, doi = {10.1186/2046-1682-5-16}, pages = {Art. 16}, year = {2012}, abstract = {Background Minor changes in protein structure induced by small organic and inorganic molecules can result in significant metabolic effects. The effects can be even more profound if the molecular players are chemically active and present in the cell in considerable amounts. The aim of our study was to investigate effects of a nitric oxide donor (spermine NONOate), ATP and sodium/potassium environment on the dynamics of thermal unfolding of human hemoglobin (Hb). The effect of these molecules was examined by means of circular dichroism spectrometry (CD) in the temperature range between 25°C and 70°C. The alpha-helical content of buffered hemoglobin samples (0.1 mg/ml) was estimated via ellipticity change measurements at a heating rate of 1°C/min. Results Major results were: 1) spermine NONOate persistently decreased the hemoglobin unfolding temperature T u irrespectively of the Na + /K + environment, 2) ATP instead increased the unfolding temperature by 3°C in both sodium-based and potassium-based buffers and 3) mutual effects of ATP and NO were strongly influenced by particular buffer ionic compositions. Moreover, the presence of potassium facilitated a partial unfolding of alpha-helical structures even at room temperature. Conclusion The obtained data might shed more light on molecular mechanisms and biophysics involved in the regulation of protein activity by small solutes in the cell.}, language = {en} } @incollection{DigelMansurovBiisenbaevetal.2012, author = {Digel, Ilya and Mansurov, Zulkhair and Biisenbaev, Makhmut and Savitskaya, Irina and Kistaubaeva, Aida and Akimbekov, Nuraly and Zhubanova, Azhar}, title = {Heterogeneous Composites on the Basis of Microbial Cells and Nanostructured Carbonized Sorbents}, series = {Composites and Their Applications}, booktitle = {Composites and Their Applications}, editor = {Hu, Ning}, publisher = {Intech}, address = {London}, isbn = {978-953-51-0706-4}, doi = {10.5772/47796}, pages = {249 -- 272}, year = {2012}, abstract = {The fact that microorganisms prefer to grow on liquid/solid phase surfaces rather than in the surrounding aqueous phase was noticed long time ago [1]. Virtually any surface - animal, mineral, or vegetable - is a subject for microbial colonization and subsequent biofilm formation. It would be adequate to name just a few notorious examples on microbial colonization of contact lenses, ship hulls, petroleum pipelines, rocks in streams and all kinds of biomedical implants. The propensity of microorganisms to become surface-bound is so profound and ubiquitous that it vindicates the advantages for attached forms over their free-ranging counterparts [2]. Indeed, from ecological and evolutionary standpoints, for many microorganisms the surface-bound state means dwelling in nutritionally favorable, non-hostile environments [3]. Therefore, in most of natural and artificial ecosystems surface-associated microorganisms vastly outnumber organisms in suspension and often organize into complex communities with features that differ dramatically from those of free cells [4].}, language = {en} } @article{MansurovDigelBiisenbaevetal.2012, author = {Mansurov, Z. and Digel, Ilya and Biisenbaev, M. and Savistkaya, I. and Kistaubaeva, A. and Akimbekov, N. and Zhubanova, A.}, title = {Bio-composite material on the basis of carbonized rice husk in biomedicine and environmental applications}, series = {Eurasian Chemico-Technological Journal}, volume = {14}, journal = {Eurasian Chemico-Technological Journal}, number = {2}, publisher = {Institute of Combustion Problems}, address = {Almaty}, issn = {2522-4867}, doi = {10.18321/ectj105}, pages = {115 -- 131}, year = {2012}, language = {en} } @article{BassamDigelHescheleretal.2013, author = {Bassam, Rasha and Digel, Ilya and Hescheler, J{\"u}rgen and Temiz Artmann, Ayseg{\"u}l and Artmann, Gerhard}, title = {Effects of spermine NONOate and ATP on protein aggregation: light scattering evidences}, series = {BMC Biophysics}, journal = {BMC Biophysics}, publisher = {BioMed Central}, address = {London}, isbn = {2046-1682}, url = {http://nbn-resolving.de/10.1186/2046-1682-6-1}, pages = {1 -- 14}, year = {2013}, language = {en} } @article{MiciliValterOflazetal.2013, author = {Micili, Serap C. and Valter, Markus and Oflaz, Hakan and Ozogul, Candan and Linder, Peter and F{\"o}ckler, Nicole and Artmann, Gerhard and Digel, Ilya and Temiz Artmann, Ayseg{\"u}l}, title = {Optical coherence tomography : a potential tool to predict premature rupture of fetal membranes}, series = {Proceedings of the Institution of Mechanical Engineers. Part H : Journal of engineering in medicine}, volume = {Vol. 227}, journal = {Proceedings of the Institution of Mechanical Engineers. Part H : Journal of engineering in medicine}, number = {No. 4}, publisher = {Sage}, address = {London}, issn = {0046-2039 (Print) ; 2041-3033 (E-Journal)}, pages = {393 -- 401}, year = {2013}, language = {en} } @article{AkimbekovDigelTastambeketal.2013, author = {Akimbekov, N. S. and Digel, Ilya and Tastambek, K. T. and Zhubanova, A. A.}, title = {Biocompatibility of carbonized rice husk with a rat heart cells line H9c2}, series = {Experimental Biology}, volume = {59}, journal = {Experimental Biology}, number = {3/1}, issn = {1563-0218}, pages = {23 -- 25}, year = {2013}, language = {en} } @article{AkimbekovDigelSavitkayaetal.2013, author = {Akimbekov, N.Sh. and Digel, Ilya and Savitkaya, I.S. and Zhubanova, A.A. and Tastambek, K.T.}, title = {Investigations of LPS endotoxin elimination in the flowing column conditions with the sorbent on the basis of carbonized rice husk}, series = {KazNU Bulletin. Biology series}, volume = {57}, journal = {KazNU Bulletin. Biology series}, number = {1}, issn = {1563-0218}, pages = {124 -- 127}, year = {2013}, language = {en} } @article{DigelAkimbekovTuralievaetal.2013, author = {Digel, Ilya and Akimbekov, N. and Turalieva, M. and Mansurov, Z. and Temiz Artmann, Ayseg{\"u}l and Eshibaev, A. and Zhubanova, A.}, title = {Usage of Carbonized Plant Wastes for Purification of Aqueous Solutions}, series = {Journal of Industrial Technology and Engineering}, volume = {2}, journal = {Journal of Industrial Technology and Engineering}, number = {07}, pages = {47 -- 54}, year = {2013}, language = {en} } @article{ZhubanovaMansurovDigeletal.2013, author = {Zhubanova, А. and Mansurov, Z.A. and Digel, Ilya and Saviskaya, I.S. and Akimbekov, N.Sh.}, title = {Designing of Heterogeneous Nanobiocomposites for Biotechnology}, series = {KazNU Bulletin. Biology series}, volume = {59}, journal = {KazNU Bulletin. Biology series}, number = {No 3/1}, isbn = {1563-0218}, pages = {89 -- 93}, year = {2013}, language = {ru} }