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336 results on '"Sarg, Bettina"'

53. Nogo-A couples with Apg-1 through interaction and co-ordinate expression under hypoxic and oxidative stress

Author

Kern, Florian, Stanika, Ruslan I., Sarg, Bettina, Offterdinger, Martin, Hess, Daniel, Obermair, Gerald J., Lindner, Herbert, Bandtlow, Christine E., Hengst, Ludger, and Schweigreiter, Rüdiger

Subjects
Nogo Proteins, RHD, reticulon homology domain, interaction, Down-Regulation, Mice, Inbred Strains, CHO Cells, RTN, reticulon, CNS, central nervous system, TCA, trichloroacetic acid, Hippocampus, Hsp, heat-shock protein, ER, endoplasmic reticulum, Mice, ROS, reactive oxygen species, Cricetulus, mental disorders, oxidative stress, Animals, HSP70 Heat-Shock Proteins, Myelin Sheath, EBFP2, enhanced blue fluorescent protein 2, Neurons, Prdx2, peroxiredoxin 2, BiP, immunoglobulin heavy-chain-binding protein, hypoxia, PLA, proximity ligation assay, Nogo, heat-shock protein, neuron, Cell Hypoxia, CHO, Chinese-hamster ovary, PFA, paraformaldehyde, psychological phenomena and processes, Myelin Proteins, Research Article
Abstract

Nogo-A is the largest isoform of the Nogo/RTN4 (reticulon 4) proteins and has been characterized as a major myelin-associated inhibitor of regenerative nerve growth in the adult CNS (central nervous system). Apart from the myelin sheath, Nogo-A is expressed at high levels in principal neurons of the CNS. The specificity of Nogo-A resides in its central domain, NiG. We identified Apg-1, a member of the stress-induced Hsp110 (heat-shock protein of 110 kDa) family, as a novel interactor of NiG/Nogo-A. The interaction is selective because Apg-1 interacts with Nogo-A/RTN4-A, but not with RTN1-A, the closest paralogue of Nogo-A. Conversely, Nogo-A binds to Apg-1, but not to Apg-2 or Hsp105, two other members of the Hsp110 family. We characterized the Nogo-A–Apg-1 interaction by affinity precipitation, co-immunoprecipitation and proximity ligation assay, using primary hippocampal neurons derived from Nogo-deficient mice. Under conditions of hypoxic and oxidative stress we found that Nogo-A and Apg-1 were tightly co-regulated in hippocampal neurons. Although both proteins were up-regulated under hypoxic conditions, their expression levels were reduced upon the addition of hydrogen peroxide. Taken together, we suggest that Nogo-A is closely involved in the neuronal response to hypoxic and oxidative stress, an observation that may be of relevance not only in stroke-induced ischaemia, but also in neuroblastoma formation., The nerve growth inhibitor Nogo-A selectively binds to the heat-shock protein Apg-1 and the expression levels of these two interactors are co-regulated under different forms of stress in neurons.

Published
2013

54. Direct association of the reticulon protein RTN1A with the ryanodine receptor 2 in neurons

Author

Kaya, Levent, Meissner, Barbara, Riedl, Maria Christine, Muik, Martin, Schwarzer, Christoph, Ferraguti, Francesco, Sarg, Bettina, Lindner, Herbert, Schweigreiter, Rüdiger, Knaus, Hans-Günther, Romanin, Christoph, and Bandtlow, Christine E.

Subjects
DAB, 3,3′-diaminobenzidine tetrahydrochloride dihydrate, Male, Recombinant Fusion Proteins, RHD, reticulon homology domain, Blotting, Western, PB, phosphate buffer, Nerve Tissue Proteins, RTN, reticulon protein, IPTG, isopropyl-β-d-thiogalactopyranoside, Hippocampus, Article, ER, endoplasmic reticulum, Immunoenzyme Techniques, Rats, Sprague-Dawley, Mice, Cytosol, Tandem Mass Spectrometry, Calcium homeostasis, Animals, Humans, Immunoprecipitation, Molecular Biology, Cells, Cultured, Neurons, Binding Sites, Ryanodine, Brain, Ryanodine Receptor Calcium Release Channel, Cell Biology, RyR, ryanodine receptor, CICR, calcium induced calcium release, CA, cornu ammonis, Rats, Protein–protein interaction, cardiovascular system, Reticulon, Calcium, Protein Binding
Abstract

RTN1A is a reticulon protein with predominant localization in the endoplasmic reticulum (ER). It was previously shown that RTN1A is expressed in neurons of the mammalian central nervous system but functional information remains sparse. To elucidate the neuronal function of RTN1A, we chose to focus our investigation on identifying possible novel binding partners specifically interacting with the unique N-terminus of RTN1A. Using a nonbiased approach involving GST pull-downs and MS analysis, we identified the intracellular calcium release channel ryanodine receptor 2 (RyR2) as a direct binding partner of RTN1A. The RyR2 binding site was localized to a highly conserved 150-amino acid residue region. RTN1A displays high preference for RyR2 binding in vitro and in vivo and both proteins colocalize in hippocampal neurons and Purkinje cells. Moreover, we demonstrate the precise subcellular localization of RTN1A in Purkinje cells and show that RTN1A inhibits RyR channels in [3H]ryanodine binding studies on brain synaptosomes. In a functional assay, RTN1A significantly reduced RyR2-mediated Ca2 + oscillations. Thus, RTN1A and RyR2 might act as functional partners in the regulation of cytosolic Ca2 + dynamics the in neurons., Highlights • The reticulon protein RTN1A is an ER-resident protein of unknown function. • We identified the intracellular calcium release channel ryanodine receptor RyR2 as a specific binding partner of RTN1A. • RNT1A co-immunoprecipitates and colocalizes with the ryanodine receptor RyR2 in neurons via its N-terminal domain. • Binding of RTN1A modulates the activity of RyR2. • RTN1A and RyR2 might act as functional partners in the regulation of cytosolic Ca2 + dynamics

Published
2013

55. Myosin kinase of molluscan smooth muscle: regulation by binding of calcium to the substrate and inhibition of myorod and twitchin phosphorylation by myosin

Author

Sobieszek, Apolinary, Sarg, Bettina, Lindner, Herbert, Matusovsky, Oleg S., and Zukowska, Magdalena

Subjects
Ammonium sulphate -- Chemical properties, Mollusks -- Physiological aspects, Mollusks -- Genetic aspects, Phosphorylation -- Analysis, Phosphotransferases -- Chemical properties, Phosphotransferases -- Structure, Biological sciences, Chemistry
Abstract

Ammonium sulfate fractionation and divalent cation precipitation were applied to purify major contractile proteins from relaxed actomyosin extracted from molluscan catch muscle myofibrils, as a supramolecular complex composed of twitchin (TW), myosin (MY), and myorod (MR). The phosphorylation of twitchin by PKA-like kinase and the phosphorylation of myosin and myorod by myosin-associated kinase were found to play crucial role in the development of the catch state.

Published
2010

56. Ferricrocin, a siderophore involved in intra- and transcellular iron distribution in Aspergillus fumigatus

Author

Wallner, Anja, Blatzer, Michael, Schrettl, Markus, Sarg, Bettina, Lindner, Herbert, and Haas, Hubertus

Subjects
Aspergillus -- Genetic aspects, Aspergillus -- Physiological aspects, Iron proteins -- Research, Siderophores (Microbiology) -- Research, Biological sciences
Abstract

The deficiency in the intracellular siderophore ferricrocin has caused iron starvation in conidia of Aspergillus fumigatus, which has shown that ferricrocin is involved in intra- and transcellular iron distribution. The studies have shown that ferricrocin has represented the first intracellular iron transporter identified in any organism.

Published
2009

57. Histone H1 dephosphorylation is not a general feature in early apoptosis

Author

Green, Anna, Sarg, Bettina, Koutazamani, Elisavet, Genheden, Ulrika, Lindner, Herbert H., and Rundquist, Ingemar

Subjects
Apoptosis -- Analysis, Histones -- Chemical properties, Phosphorylation -- Analysis, Biological sciences, Chemistry
Abstract

The intrinsic, as well as the extrinsic pathways are studied to explain the relation existing between apoptosis and histone H1 phosphorylation in Jurkat cells after the induction of apoptosis. The H1 subtypes are shown to get dephosphorylated on the addition of apoptosis.

Published
2008

60. In vitro acetylation of HMGB-1 and -2 proteins by CBP: the role of the acidic tail

Author

Pasheva, Evdokia, Sarov, Mihail, Bidjekov, Kiril, Ugrinova, Iva, Sarg, Bettina, Lindner, Herbert, and Pashev, Iliya G.

Subjects
Acetylene -- Analysis, Protein binding -- Analysis, Biological sciences, Chemistry
Abstract

Histone acetyltransferases CREB-binding protein (CBP), p300/CBP-associated factor (PCAF), and Tat-interactive protein, 60 kDa (Tip60) is experimented for their ability to in vitro acetylate high-mobility group box-containing proteins 1 and 2(HMGB-1 and -2) and the role of C-terminal domain on the pattern of acetylation as well as some properties of the modified truncated protein. It is found that the modifications in the acetylation pattern of HMGB-1 and -2 upon removal of the C-terminal tail are regarded as a means by which the acidic domain modulates some properties of these proteins.

Published
2004

61. Hyperosmotic stress: in situchromatin phase separation

Author

Olins, Ada L., Gould, Travis J., Boyd, Logan, Sarg, Bettina, and Olins, Donald E.

Abstract

ABSTRACTDehydration of cells by acute hyperosmotic stress has profound effects upon cell structure and function. Interphase chromatin and mitotic chromosomes collapse (“congelation”). HL-60/S4 cells remain ~100% viable for, at least, 1 hour, exhibiting shrinkage to ~2/3 their original volume, when placed in 300mM sucrose in tissue culture medium. Fixed cells were imaged by immunostaining confocal and STED microscopy. At a “global” structural level (μm), mitotic chromosomes congeal into a residual gel with apparent (phase) separations of Ki67, CTCF, SMC2, RAD21, H1 histones and HMG proteins. At an “intermediate” level (sub-μm), radial distribution analysis of STED images revealed a most probable peak DNA density separation of ~0.16 μm, essentially unchanged by hyperosmotic stress. At a “local” structural level (~1-2 nm), in vivo crosslinking revealed essentially unchanged crosslinked products between H1, HMG and inner histones. Hyperosmotic cellular stress is discussed in terms of concepts of mitotic chromosome structure and liquid-liquid phase separation.

Published
2020
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63. Blocking Hsp70 Enhances the Efficiency of Amphotericin B Treatment against Resistant Aspergillus terreus Strains

Author

Blatzer, Michael, primary, Blum, Gerhard, additional, Jukic, Emina, additional, Posch, Wilfried, additional, Gruber, Peter, additional, Nagl, Markus, additional, Binder, Ulrike, additional, Maurer, Elisabeth, additional, Sarg, Bettina, additional, Lindner, Herbert, additional, Lass-Flörl, Cornelia, additional, and Wilflingseder, Doris, additional

Published
2015
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66. Identification of Hsc70 as target for AGE modification in senescent human fibroblasts

Author

Sarg, Bettina, Lindner, Herbert, Unterluggauer, Hermann, Micutkova, Lucia, Hernebring, Malin, Jansen-Dürr, Pidder, and Nystrom, Thomas

Subjects
Fibroblasts, Endothelial cells, Senescence, Protein carbonyls, Advanced glycation end products, Hsc 70
Abstract

Cellular senescence is known as a potent mechanism of tumor suppression, and cellular senescence in vitro also reflects at least some features of aging in vivo. The Free Radical Theory of aging suggests that reactive oxygen species are important causative agents of aging and cellular senescence. Besides damage of nucleic acids and lipids, also oxidative modifications of proteins have been described as potential causative events in the senescence response. However, the identity of protein targets for post-translational modifications in senescent cells has remained unclear. In the present communication, we analyzed the occurrence of oxidative posttranslational modifications in senescent human endothelial cells and dermal fibroblasts. We found a significant increase in the level of protein carbonyls and AGE modification with senescence in both cell types. Using 2D-Gel electrophoresis and Western Blot we found that heat shock cognate protein 70 is a bona fide target for AGE modification in human fibroblasts.

Published
2008

67. Identification of voltage-gated K+ channel beta 2 (Kvβ2) subunit as a novel interaction partner of the pain transducer Transient Receptor Potential Vanilloid 1 channel (TRPV1)

Author

Bavassano, Carlo, primary, Marvaldi, Letizia, additional, Langeslag, Michiel, additional, Sarg, Bettina, additional, Lindner, Herbert, additional, Klimaschewski, Lars, additional, Kress, Michaela, additional, Ferrer-Montiel, Antonio, additional, and Knaus, Hans-Günther, additional

Published
2013
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80. Proteomic Profiling of Acute Cardiac Allograft Rejection

Author

Kienzl, Katrin, primary, Sarg, Bettina, additional, Golderer, Georg, additional, Obrist, Peter, additional, Werner, Ernst R., additional, Werner-Felmayer, Gabriele, additional, Lindner, Herbert, additional, Maglione, Manuel, additional, Schneeberger, Stefan, additional, Margreiter, Raimund, additional, and Brandacher, Gerald, additional

Published
2009
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81. Proteomic identification of aldo-keto reductase AKR1B10 induction after treatment of colorectal cancer cells with the proteasome inhibitor bortezomib

Author

Loeffler-Ragg, Judith, primary, Mueller, Doris, additional, Gamerith, Gabriele, additional, Auer, Thomas, additional, Skvortsov, Sergej, additional, Sarg, Bettina, additional, Skvortsova, Ira, additional, Schmitz, Klaus J., additional, Martin, Hans-Jörg, additional, Krugmann, Jens, additional, Alakus, Hakan, additional, Maser, Edmund, additional, Menzel, Jürgen, additional, Hilbe, Wolfgang, additional, Lindner, Herbert, additional, Schmid, Kurt W., additional, and Zwierzina, Heinz, additional

Published
2009
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83. Functional aspects of the solution structure and dynamics of PAF - a highly-stable antifungal protein fromPenicillium chrysogenum

Author

Batta, Gyula, primary, Barna, Teréz, additional, Gáspári, Zoltán, additional, Sándor, Szabolcs, additional, Kövér, Katalin E., additional, Binder, Ulrike, additional, Sarg, Bettina, additional, Kaiserer, Lydia, additional, Chhillar, Anil K., additional, Eigentler, Andrea, additional, Leiter, Éva, additional, Hegedüs, Nikoletta, additional, Pócsi, István, additional, Lindner, Herbert, additional, and Marx, Florentine, additional

Published
2009
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94. ICln159 Folds into a Pleckstrin Homology Domain-like Structure

Author

Fürst, Johannes, primary, Schedlbauer, Andreas, additional, Gandini, Rosaria, additional, Garavaglia, Maria Lisa, additional, Saino, Stefano, additional, Gschwentner, Martin, additional, Sarg, Bettina, additional, Lindner, Herbert, additional, Jakab, Martin, additional, Ritter, Markus, additional, Bazzini, Claudia, additional, Botta, Guido, additional, Meyer, Giuliano, additional, Kontaxis, Georg, additional, Tilly, Ben C., additional, Konrat, Robert, additional, and Paulmichl, Markus, additional

Published
2005
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