9 results on '"Sarg, Bettina"'
Search Results
2. Additional file 3 of Expression of transport proteins in the rete mirabile of european silver and yellow eel
- Author
-
Schneebauer, Gabriel, Drechsel, Victoria, Dirks, Ron, Faserl, Klaus, Sarg, Bettina, and Pelster, Bernd
- Subjects
Data_FILES - Abstract
Additional file 3.
- Published
- 2021
- Full Text
- View/download PDF
3. Additional file 5 of Expression of transport proteins in the rete mirabile of european silver and yellow eel
- Author
-
Schneebauer, Gabriel, Drechsel, Victoria, Dirks, Ron, Faserl, Klaus, Sarg, Bettina, and Pelster, Bernd
- Subjects
Data_FILES - Abstract
Additional file 5.
- Published
- 2021
- Full Text
- View/download PDF
4. Additional file 1 of Expression of transport proteins in the rete mirabile of european silver and yellow eel
- Author
-
Schneebauer, Gabriel, Drechsel, Victoria, Dirks, Ron, Faserl, Klaus, Sarg, Bettina, and Pelster, Bernd
- Subjects
Data_FILES - Abstract
Additional file 1.
- Published
- 2021
- Full Text
- View/download PDF
5. A+-Helix of Protein C Inhibitor (PCI) Is a Cell-penetrating Peptide That Mediates Cell Membrane Permeation of PCI*
- Author
-
Yang, Hanjiang, Wahlmüller, Felix Christof, Sarg, Bettina, Furtmüller, Margareta, and Geiger, Margarethe
- Subjects
Serpin ,Cell Membrane Permeability ,Nuclear Translocation ,Serine Endopeptidases ,Cell Biology ,Cell-Penetrating Peptides ,U937 Cells ,GPI-Linked Proteins ,Cell-penetrating Peptide (CPP) ,Testisin ,Mice ,surgical procedures, operative ,Cell Line, Tumor ,Animals ,Humans ,cardiovascular diseases ,Cell Permeabilization ,Peptides ,therapeutics ,Protein C Inhibitor - Abstract
Background: Extracellular protein C inhibitor (PCI) can cross the cellular plasma membrane. Results: Testisin (fluid-phase and cell membrane-anchored) cleaves PCI close to its N terminus. N-terminally truncated PCI can no longer be internalized by cells. Conclusion: Testisin removes helix A+, a cell-penetrating peptide, which mediates cell membrane permeation of PCI. Significance: Testisin or other proteases could regulate PCI internalization by removing its N terminus., Protein C inhibitor (PCI) is a serpin with broad protease reactivity. It binds glycosaminoglycans and certain phospholipids that can modulate its inhibitory activity. PCI can penetrate through cellular membranes via binding to phosphatidylethanolamine. The exact mechanism of PCI internalization and the intracellular role of the serpin are not well understood. Here we showed that testisin, a glycosylphosphatidylinositol-anchored serine protease, cleaved human PCI and mouse PCI (mPCI) at their reactive sites as well as at sites close to their N terminus. This cleavage was observed not only with testisin in solution but also with cell membrane-anchored testisin on U937 cells. The cleavage close to the N terminus released peptides rich in basic amino acids. Synthetic peptides corresponding to the released peptides of human PCI (His1–Arg11) and mPCI (Arg1–Ala18) functioned as cell-penetrating peptides. Because intact mPCI but not testisin-cleaved mPCI was internalized by Jurkat T cells, a truncated mPCI mimicking testisin-cleaved mPCI was created. The truncated mPCI lacking 18 amino acids at the N terminus was not taken up by Jurkat T cells. Therefore our model suggests that testisin or other proteases could regulate the internalization of PCI by removing its N terminus. This may represent one of the mechanisms regulating the intracellular functions of PCI.
- Published
- 2014
6. 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
7. 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
8. Methylation of H2AR29 is a novel repressive PRMT6 target
- Author
-
Waldmann, Tanja, Izzo, Annalisa, Kamieniarz, Kinga, Richter, Florian, Vogler, Christine, Sarg, Bettina, Lindner, Herbert, Young, Nicolas L, Mittler, Gerhard, Garcia, Benjamin A, and Schneider, Robert
- Subjects
lcsh:Genetics ,lcsh:QH426-470 ,ddc:570 ,Research ,Genetics ,Molecular Biology - Abstract
Background Covalent histone modifications are central to all DNA-dependent processes. Modifications of histones H3 and H4 are becoming well characterised, but knowledge of how H2A modifications regulate chromatin dynamics and gene expression is still very limited. Results To understand the function of H2A modifications, we performed a systematic analysis of the histone H2A methylation status. We identified and functionally characterised two new methylation sites in H2A: R11 (H2AR11) and R29 (H2AR29). Using an unbiased biochemical approach in combination with candidate assays we showed that protein arginine methyltransferase (PRMT) 1 and PRMT6 are unique in their ability to catalyse these modifications. Importantly we found that H2AR29me2 is specifically enriched at genes repressed by PRMT6, implicating H2AR29me2 in transcriptional repression. Conclusions Our data establishes R11 and R29 as new arginine methylation sites in H2A. We identified the specific modifying enzymes involved, and uncovered a novel functional role of H2AR29me2 in gene silencing in vivo. Thus this work reveals novel insights into the function of H2A methylation and in the mechanisms of PRMT6-mediated transcriptional repression.
- Published
- 2011
- Full Text
- View/download PDF
9. 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
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.