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Pietuch, Anna
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Pietuch, Anna
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Pietuch, Anna
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Pietuch, A.
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2011Conference Abstract [["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Rother, Jan"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T08:53:37Z"],["dc.date.available","2018-11-07T08:53:37Z"],["dc.date.issued","2011"],["dc.format.extent","231"],["dc.identifier.isi","000293637300661"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22462"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Budapest, HUNGARY"],["dc.relation.issn","0175-7571"],["dc.title","Enhanced stimulation of Toll-like receptor 9 via immunostimulatory nanoparticles"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details WOS2010Journal Article Research Paper [["dc.bibliographiccitation.firstpage","2287"],["dc.bibliographiccitation.issue","13-14"],["dc.bibliographiccitation.journal","Journal of Adhesion Science and Technology"],["dc.bibliographiccitation.lastpage","2300"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Lorenz, Bärbel"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Fine, Tamir"],["dc.contributor.author","Tarantola, Marco"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Wegener, Joachim"],["dc.date.accessioned","2017-09-07T11:46:42Z"],["dc.date.available","2017-09-07T11:46:42Z"],["dc.date.issued","2010"],["dc.description.abstract","The adhesion of MDCK II cells to porous and non-porous silicon substrates has been investigated by means of fluorescence and atomic force microscopy. The MDCK II cell density and the average height of the cells were increased on porous silicon substrates with regular 1.2 mu m pores as compared to flat, non-porous surfaces. In addition, we found a substantially reduced actin cytoskeleton within confluent cells cultured on the macroporous substrate compared to flat surfaces. The perturbation of the cytoskeleton relates to a significantly reduced expression of integrins on the porous area. The loss of stress fibers and cortical actin is accompanied by a dramatically reduced Young's modulus of 0.15 kPa compared to 6 kPa on flat surfaces as revealed by site-specific force-indentation experiments. (C) Koninklijke Brill NV, Leiden, 2010"],["dc.identifier.doi","10.1163/016942410X508028"],["dc.identifier.gro","3142996"],["dc.identifier.isi","000284152300013"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/462"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0169-4243"],["dc.title","Cell Adhesion to Ordered Pores: Consequences for Cellular Elasticity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI WOS2013Journal Article [["dc.bibliographiccitation.firstpage","712"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","722"],["dc.bibliographiccitation.volume","1833"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Brueckner, Bastian Rouven"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T09:27:47Z"],["dc.date.available","2018-11-07T09:27:47Z"],["dc.date.issued","2013"],["dc.description.abstract","Osmotic stress poses one of the most fundamental challenges to living cells. Particularly, the largely inextensible plasma membrane of eukaryotic cells easily ruptures under in-plane tension calling for sophisticated strategies to readily respond to osmotic stress. We describe how epithelial cells react and adapt mechanically to the exposure to hypotonic and hypertonic solutions in the context of a confluent monolayer. Site-specific indentation experiments in conjunction with tether pulling on individual cells have been carried out with an atomic force microscope to reveal spatio-temporal changes in membrane tension and surface area. We found that cells compensate for an increase in lateral tension due to hypoosmotic stress by sacrificing excess of membrane area stored in protrusions and invaginations such as microvilli and caveolae. At mild hypotonic conditions lateral tension increases partly compensated by surface are regulation, i.e. the cell sacrifices some of its membrane reservoirs. A loss of membrane-actin contacts occurs upon exposure to stronger hypotonic solutions giving rise to a drop in lateral tension. Tension release recovers on longer time scales by an increasing endocytosis, which efficiently removes excess membrane from the apical side to restore the initial pre-stress. Hypertonic solutions lead to shrinkage of cells and collapse of the apical membrane onto the cortex. Exposure to distilled water leads to stiffening of cells due to removal of excess surface area and tension increase due to elevated osmotic pressure across the plasma membrane. (c) 2012 Elsevier B.V. All rights reserved."],["dc.description.sponsorship","DFG [SFB 937]; Dorothea Schlozer Foundation of Georg-August-University"],["dc.identifier.doi","10.1016/j.bbamcr.2012.11.006"],["dc.identifier.isi","000315308100029"],["dc.identifier.pmid","23178740"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30619"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0167-4889"],["dc.title","Membrane tension homeostasis of epithelial cells through surface area regulation in response to osmotic stress"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2015Journal Article [["dc.bibliographiccitation.firstpage","281"],["dc.bibliographiccitation.journal","Beilstein Journal of Nanotechnology"],["dc.bibliographiccitation.lastpage","292"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Breus, Vladimir V."],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Tarantola, Marco"],["dc.contributor.author","Basche, Thomas"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T10:01:58Z"],["dc.date.available","2018-11-07T10:01:58Z"],["dc.date.issued","2015"],["dc.description.abstract","In this work, cytotoxicity and cellular impedance response was compared for CdSe/ZnS core/shell quantum dots (QDs) with positively charged cysteamine-QDs, negatively charged dihydrolipoic acid-QDs and zwitterionic D-penicillamine-QDs exposed to canine kidney MDCKII cells. Pretreatment of cells with pharmacological inhibitors suggested that the uptake of nanoparticles was largely due to receptor-independent pathways or spontaneous entry for carboxylated and zwitterionic QDs, while for amine-functionalized particles involvement of cholesterol-enriched membrane domains is conceivable. Cysteamine-QDs were found to be the least cytotoxic, while D-penicillamine-QDs reduced the mitochondrial activity of MDCKII by 20-25%. Although the cell vitality appeared unaffected (assessed from the changes in mitochondrial activity using a classical MTS assay after 24 h of exposure), the binding of QDs to the cellular interior and their movement across cytoskeletal filaments (captured and characterized by single-particle tracking), was shown to compromise the integrity of the cytoskeletal and plasma membrane dynamics, as evidenced by electric cell-substrate impedance sensing."],["dc.description.sponsorship","DFG"],["dc.identifier.doi","10.3762/bjnano.6.26"],["dc.identifier.isi","000348940700001"],["dc.identifier.pmid","25821666"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38141"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Beilstein-institut"],["dc.relation.issn","2190-4286"],["dc.title","The effect of surface charge on nonspecific uptake and cytotoxicity of CdSe/ZnS core/shell quantum dots"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2011Journal Article [["dc.bibliographiccitation.firstpage","254"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Nanotoxicology"],["dc.bibliographiccitation.lastpage","268"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Tarantola, Marco"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Schneider, David"],["dc.contributor.author","Rother, Jan"],["dc.contributor.author","Sunnick, Eva"],["dc.contributor.author","Rosman, Christina"],["dc.contributor.author","Pierrat, Sebastien"],["dc.contributor.author","Soennichsen, Carsten"],["dc.contributor.author","Wegener, Joachim"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T08:55:39Z"],["dc.date.available","2018-11-07T08:55:39Z"],["dc.date.issued","2011"],["dc.description.abstract","Nanoparticle exposure is monitored by a combination of two label-free and non-invasive biosensor devices which detect cellular shape and viscoelasticity (quartz crystal microbalance), cell motility and the dynamics of epithelial cell-cell contacts (electric cell-substrate impedance sensing). With these tools we have studied the impact of nanoparticle shape on cellular physiology. Gold (Au) nanoparticles coated with CTAB were synthesized and studied in two distinct shapes: Spheres with a diameter of (43 +/-+/- 4) nm and rods with a size of (38 +/-+/- 7) nm xx (17 +/-+/- 3) nm. Dose-response experiments were accompanied by conventional cytotoxicity tests as well as fluorescence and dark-field microscopy to visualize the intracellular particle distribution. We found that spherical gold nanoparticles with identical surface functionalization are generally more toxic and more efficiently ingested than rod-shaped particles. We largely attribute the higher toxicity of CTAB-coated spheres as compared to rod-shaped particles to a higher release of toxic CTAB upon intracellular aggregation."],["dc.description.sponsorship","German Science Foundation (DFG) [JA 963/10-1]"],["dc.identifier.doi","10.3109/17435390.2010.528847"],["dc.identifier.isi","000290936000013"],["dc.identifier.pmid","21050076"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22954"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Ltd"],["dc.relation.issn","1743-5404"],["dc.relation.issn","1743-5390"],["dc.title","Toxicity of gold-nanoparticles: Synergistic effects of shape and surface functionalization on micromotility of epithelial cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2015Journal Article [["dc.bibliographiccitation.firstpage","223"],["dc.bibliographiccitation.journal","Beilstein Journal of Nanotechnology"],["dc.bibliographiccitation.lastpage","231"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Brueckner, Bastian Rouven"],["dc.contributor.author","Schneider, David"],["dc.contributor.author","Tarantola, Marco"],["dc.contributor.author","Rosman, Christina"],["dc.contributor.author","Soennichsen, Carsten"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T10:02:05Z"],["dc.date.available","2018-11-07T10:02:05Z"],["dc.date.issued","2015"],["dc.description.abstract","Background: The impact of gold nanoparticles on cell viability has been extensively studied in the past. Size, shape and surface functionalization including opsonization of gold particles ranging from a few nanometers to hundreds of nanometers are among the most crucial parameters that have been focussed on. Cytoxicity of nanomaterial has been assessed by common cytotoxicity assays targeting enzymatic activity such as LDH, MTT and ECIS. So far, however, less attention has been paid to the mechanical parameters of cells exposed to gold particles, which is an important reporter on the cellular response to external stimuli. Results: Mechanical properties of confluent MDCK II cells exposed to gold nanorods as a function of surface functionalization and concentration have been explored by atomic force microscopy and quartz crystal microbalance measurements in combination with fluorescence and dark-field microscopy. Conclusion: We found that cells exposed to CTAB coated gold nanorods display a concentration-dependent stiffening that cannot be explained by the presence of CTAB alone. The stiffening results presumably from endocytosis of particles removing excess membrane area from the cell's surface. Another aspect could be the collapse of the plasma membrane on the actin cortex. Particles coated with PEG do not show a significant change in elastic properties. This observation is consistent with QCM measurements that show a considerable drop in frequency upon administration of CTAB coated rods suggesting an increase in acoustic load corresponding to a larger stiffness (storage modulus)."],["dc.description.sponsorship","DFG"],["dc.identifier.doi","10.3762/bjnano.6.21"],["dc.identifier.isi","000348943900001"],["dc.identifier.pmid","25671166"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38155"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Beilstein-institut"],["dc.relation.issn","2190-4286"],["dc.title","Mechanical properties of MDCK II cells exposed to gold nanorods"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2014Journal Article Research Paper [["dc.bibliographiccitation.firstpage","9833"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","9843"],["dc.bibliographiccitation.volume","289"],["dc.contributor.author","Braunger, Julia A."],["dc.contributor.author","Brückner, Bastian R."],["dc.contributor.author","Nehls, Stefan"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Gerke, Volker"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:46:19Z"],["dc.date.available","2017-09-07T11:46:19Z"],["dc.date.issued","2014"],["dc.description.abstract","Background: Ezrin can establish a dynamic linkage between plasma membrane and cytoskeleton. Results: The individual bond strength between ezrin and F-actin is small, but the number of attachment sites is significantly altered by phosphatidylinositol 4,5-bisphosphate (PIP2). Conclusion: PIP2 activates ezrin to establish multiple weak ezrin/F-actin interactions. Significance: Plasma membrane tension is maintained by ezrin/F-actin interactions. Direct linkage between the plasma membrane and the actin cytoskeleton is controlled by the protein ezrin, a member of the ezrin-radixin-moesin protein family. To function as a membrane-cytoskeleton linker, ezrin needs to be activated in a process that involves binding of ezrin to phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphorylation of a conserved threonine residue. Here, we used colloidal probe microscopy to quantitatively analyze the interaction between ezrin and F-actin as a function of these activating factors. We show that the measured individual unbinding forces between ezrin and F-actin are independent of the activating parameters, in the range of approximately 50 piconewtons. However, the cumulative adhesion energy greatly increases in the presence of PIP2 demonstrating that a larger number of bonds between ezrin and F-actin has formed. In contrast, the phosphorylation state, represented by phosphor-mimetic mutants of ezrin, only plays a minor role in the activation process. These results are in line with in vivo experiments demonstrating that an increase in PIP2 concentration recruits more ezrin to the apical plasma membrane of polarized cells and significantly increases the membrane tension serving as a measure of the adhesion sites between the plasma membrane and the F-actin network."],["dc.identifier.doi","10.1074/jbc.M113.530659"],["dc.identifier.gro","3142143"],["dc.identifier.isi","000333807000033"],["dc.identifier.pmid","24500715"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5022"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [STE 884/11-1, GE 514/8-1, GE 514/9-1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Phosphatidylinositol 4,5-Bisphosphate Alters the Number of Attachment Sites between Ezrin and Actin Filaments A COLLOIDAL PROBE STUDY "],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2013Conference Abstract [["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Brueckner, B. R."],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T09:22:32Z"],["dc.date.available","2018-11-07T09:22:32Z"],["dc.date.issued","2013"],["dc.format.extent","S46"],["dc.identifier.isi","000330215300043"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29361"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Lisbon, PORTUGAL"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.title","Challenging cellular mechanics - tension homeostasis by surface area regulation"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details WOS2011Conference Abstract [["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T08:53:36Z"],["dc.date.available","2018-11-07T08:53:36Z"],["dc.date.issued","2011"],["dc.format.extent","162"],["dc.identifier.isi","000293637300421"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22453"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Budapest, HUNGARY"],["dc.relation.issn","0175-7571"],["dc.title","Manipulation of cellular mechanics"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details WOS