Search

Your search keyword '"Lindner, Herbert H."' showing total 225 results
Start Over Author "Lindner, Herbert H."
225 results on '"Lindner, Herbert H."'

1. Author Correction: Feedback inhibition of cAMP effector signaling by a chaperone-assisted ubiquitin system

Author

Rinaldi, Laura, Donne, Rossella Delle, Catalanotti, Bruno, Torres-Quesada, Omar, Enzler, Florian, Moraca, Federica, Nisticò, Robert, Chiuso, Francesco, Piccinin, Sonia, Bachmann, Verena, Lindner, Herbert H., Garbi, Corrado, Scorziello, Antonella, Russo, Nicola Antonino, Synofzik, Matthis, Stelzl, Ulrich, Annunziato, Lucio, Stefan, Eduard, and Feliciello, Antonio

Published
2024
Full Text
View/download PDF

10. Feedback inhibition of cAMP effector signaling by a chaperone-assisted ubiquitin system

Author

Rinaldi, Laura, Delle Donne, Rossella, Catalanotti, Bruno, Torres-Quesada, Omar, Enzler, Florian, Moraca, Federica, Nisticò, Robert, Chiuso, Francesco, Piccinin, Sonia, Bachmann, Verena, Lindner, Herbert H, Garbi, Corrado, Scorziello, Antonella, Russo, Nicola Antonino, Synofzik, Matthis, Stelzl, Ulrich, Annunziato, Lucio, Stefan, Eduard, and Feliciello, Antonio

Published
2019
Full Text
View/download PDF

16. LAMTOR/Ragulator regulates lipid metabolism in macrophages and foam cell differentiation

Author

Lamberti, Giorgia, De Smet, Cedric H., Angelova, Mihaela, Kremser, Leopold, Taub, Nicole, Herrmann, Caroline, Hess, Michael W., Rainer, Johannes, Tancevski, Ivan, Schweigreiter, Rüdiger, Kofler, Reinhard, Schmiedinger, Thomas, Vietor, Ilja, Trajanoski, Zlatko, Ejsing, Christer S., Lindner, Herbert H., Huber, Lukas A., and Stasyk, Taras

Subjects
Macrophages, organelle proteomics, Proteins, Cell Differentiation, Lipid Droplets, Lipid Metabolism, Cell Fate Determination, Research Letters, foam cells, macrophages, transcriptomics, Mice, Research Letter, LAMTOR, Animals, Cholesterol Esters, ragulator, Transcriptome, Cells, Cultured
Abstract

Late endosomal/lysosomal adaptor and MAPK and mTOR activator (LAMTOR/Ragulator) is a scaffold protein complex that anchors and regulates multiprotein signaling units on late endosomes/lysosomes. To identify LAMTOR-modulated endolysosomal proteins, primary macrophages were derived from bone marrow of conditional knockout mice carrying a specific deletion of LAMTOR2 in the monocyte/macrophage cell lineage. Affymetrix-based transcriptomic analysis and quantitative iTRAQ-based organelle proteomic analysis of endosomes derived from macrophages were performed. Further analyses showed that LAMTOR could be a novel regulator of foam cell differentiation. The lipid droplet formation phenotype observed in macrophages was additionally confirmed in MEFs, where lipidomic analysis identified cholesterol esters as specifically downregulated in LAMTOR2 knockout cells. The data obtained indicate a function of LAMTOR2 in lipid metabolism.

Published
2019
Full Text
View/download PDF

19. Intracerebral Iron Accumulation may be Associated with Secondary Brain Injury in Patients with Poor Grade Subarachnoid Hemorrhage

Author

Helbok, Raimund, primary, Rass, Verena, additional, Kofler, Mario, additional, Talasz, Heribert, additional, Schiefecker, Alois, additional, Gaasch, Max, additional, Scherfler, Christoph, additional, Pfausler, Bettina, additional, Thomé, Claudius, additional, Beer, Ronny, additional, Lindner, Herbert H., additional, and Schmutzhard, Erich, additional

Published
2021
Full Text
View/download PDF

21. Analyses of linker histone--chromatin interactions in situ (1)

Author

Rundquist, Ingemar and Lindner, Herbert H.

Subjects
Chromatin -- Research, Histones -- Research, In situ hybridization -- Research, Biological sciences, Research
Abstract

Abstract: Recent studies, using cytometric techniques based on fluorescence microscopy, have provided new information on how linker histones interact with chromatin in vivo or in situ. In particular, the use [...]

Published
2006

24. Capillary Electrophoresis-Mass Spectrometry at Trial by Metabo-Ring: Effective Electrophoretic Mobility for Reproducible and Robust Compound Annotation

Author

Drouin, Nicolas, primary, van Mever, Marlien, additional, Zhang, Wei, additional, Tobolkina, Elena, additional, Ferre, Sabrina, additional, Servais, Anne-Catherine, additional, Gou, Marie-Jia, additional, Nyssen, Laurent, additional, Fillet, Marianne, additional, Lageveen-Kammeijer, Guinevere S.M., additional, Nouta, Jan, additional, Chetwynd, Andrew J., additional, Lynch, Iseult, additional, Thorn, James A., additional, Meixner, Jens, additional, Lößner, Christopher, additional, Taverna, Myriam, additional, Liu, Sylvie, additional, Tran, N. Thuy, additional, Francois, Yannis, additional, Lechner, Antony, additional, Nehmé, Reine, additional, Al Hamoui Dit Banni, Ghassan, additional, Nasreddine, Rouba, additional, Colas, Cyril, additional, Lindner, Herbert H., additional, Faserl, Klaus, additional, Neusüß, Christian, additional, Nelke, Manuel, additional, Lämmerer, Stefan, additional, Perrin, Catherine, additional, Bich-Muracciole, Claudia, additional, Barbas, Coral, additional, Gonzálvez, Ángeles López, additional, Guttman, Andras, additional, Szigeti, Marton, additional, Britz-McKibbin, Philip, additional, Kroezen, Zachary, additional, Shanmuganathan, Meera, additional, Nemes, Peter, additional, Portero, Erika P., additional, Hankemeier, Thomas, additional, Codesido, Santiago, additional, González-Ruiz, Víctor, additional, Rudaz, Serge, additional, and Ramautar, Rawi, additional

Published
2020
Full Text
View/download PDF

32. Histone H1 interphase phosphorylation becomes largely established in G1 or early S phase and differs in G1 between T-lymphoblastoid cells and normal T cells

Author

Gréen Anna, Sarg Bettina, Gréen Henrik, Lönn Anita, Lindner Herbert H, and Rundquist Ingemar

Subjects
Genetics, QH426-470
Abstract

Abstract Background Histone H1 is an important constituent of chromatin, and is involved in regulation of its structure. During the cell cycle, chromatin becomes locally decondensed in S phase, highly condensed during metaphase, and again decondensed before re-entry into G1. This has been connected to increasing phosphorylation of H1 histones through the cell cycle. However, many of these experiments have been performed using cell-synchronization techniques and cell cycle-arresting drugs. In this study, we investigated the H1 subtype composition and phosphorylation pattern in the cell cycle of normal human activated T cells and Jurkat T-lymphoblastoid cells by capillary electrophoresis after sorting of exponentially growing cells into G1, S and G2/M populations. Results We found that the relative amount of H1.5 protein increased significantly after T-cell activation. Serine phosphorylation of H1 subtypes occurred to a large extent in late G1 or early S phase in both activated T cells and Jurkat cells. Furthermore, our data confirm that the H1 molecules newly synthesized during S phase achieve a similar phosphorylation pattern to the previous ones. Jurkat cells had more extended H1.5 phosphorylation in G1 compared with T cells, a difference that can be explained by faster cell growth and/or the presence of enhanced H1 kinase activity in G1 in Jurkat cells. Conclusion Our data are consistent with a model in which a major part of interphase H1 phosphorylation takes place in G1 or early S phase. This implies that H1 serine phosphorylation may be coupled to changes in chromatin structure necessary for DNA replication. In addition, the increased H1 phosphorylation of malignant cells in G1 may be affecting the G1/S transition control and enabling facilitated S-phase entry as a result of relaxed chromatin condensation. Furthermore, increased H1.5 expression may be coupled to the proliferative capacity of growth-stimulated T cells.

Published
2011
Full Text
View/download PDF

35. Quantitative Proteomics Using Ultralow Flow Capillary Electrophoresis–Mass Spectrometry

Author

Faserl, Klaus, Kremser, Leopold, Müller, Martin, Teis, David, and Lindner, Herbert H.

Subjects
Proteomics, Proteome, Electrophoresis, Capillary, Proteins, Peptides, Article, Mass Spectrometry, Chromatography, Liquid
Abstract

In this work, we evaluate the incorporation of an ultralow flow interface for coupling capillary electrophoresis (CE) and mass spectrometry (MS), in combination with reversed-phase high-pressure liquid chromatography (HPLC) fractionation as an alternate workflow for quantitative proteomics. Proteins, extracted from a SILAC (stable isotope labeling by amino acids in cell culture) labeled and an unlabeled yeast strain were mixed and digested enzymatically in solution. The resulting peptides were fractionated using RP-HPLC and analyzed by CE–MS yielding a total of 28 538 quantified peptides that correspond to 3 272 quantified proteins. CE–MS analysis was performed using a neutral capillary coating, providing the highest separation efficiency at ultralow flow conditions (

Published
2015

36. LAMTOR/Ragulator is a negative regulator of Arl8b- and BORC-dependent late endosomal positioning

Author

Filipek, Przemyslaw A., de Araujo, Mariana E.G., Vogel, Georg F., De Smet, Cedric H., Eberharter, Daniela, Rebsamen, Manuele, Rudashevskaya, Elena L., Kremser, Leopold, Yordanov, Teodor, Tschaikner, Philipp, Fürnrohr, Barbara G., Lechner, Stefan, Dunzendorfer-Matt, Theresia, Scheffzek, Klaus, Bennett, Keiryn L., Superti-Furga, Giulio, Lindner, Herbert H., Stasyk, Taras, and Huber, Lukas A.

Subjects
Epidermal Growth Factor, ADP-Ribosylation Factors, Movement, Intracellular Signaling Peptides and Proteins, Nerve Tissue Proteins, Endosomes, Microtubules, Article, Protein Transport, HEK293 Cells, Gene Expression Regulation, Multiprotein Complexes, Commentary, Humans, Protein Isoforms, Spotlight, Carrier Proteins, Lysosomes, Research Articles, HeLa Cells, Signal Transduction
Abstract

Functions of lysosomes are tightly associated with their position within the cell. Filipek et al. identify the EGF-dependent LAMTOR/Ragulator-BORC interaction as a negative regulator of Arl8b lysosomal recruitment that triggers plus-end directed lysosome movement., Signaling from lysosomes controls cellular clearance and energy metabolism. Lysosomal malfunction has been implicated in several pathologies, including neurodegeneration, cancer, infection, immunodeficiency, and obesity. Interestingly, many functions are dependent on the organelle position. Lysosomal motility requires the integration of extracellular and intracellular signals that converge on a competition between motor proteins that ultimately control lysosomal movement on microtubules. Here, we identify a novel upstream control mechanism of Arl8b-dependent lysosomal movement toward the periphery of the cell. We show that the C-terminal domain of lyspersin, a subunit of BLOC-1–related complex (BORC), is essential and sufficient for BORC-dependent recruitment of Arl8b to lysosomes. In addition, we establish lyspersin as the linker between BORC and late endosomal/lysosomal adaptor and mitogen activated protein kinase and mechanistic target of rapamycin activator (LAMTOR) complexes and show that epidermal growth factor stimulation decreases LAMTOR/BORC association, thereby promoting BORC- and Arl8b-dependent lysosomal centrifugal transport.

Published
2017

37. The structure of the Shiga toxin 2a A‐subunit dictates the interactions of the toxin with blood components

Author

Brigotti, Maurizio, primary, Orth‐Höller, Dorothea, additional, Carnicelli, Domenica, additional, Porcellini, Elisa, additional, Galassi, Elisabetta, additional, Tazzari, Pier Luigi, additional, Ricci, Francesca, additional, Manoli, Francesco, additional, Manet, Ilse, additional, Talasz, Heribert, additional, Lindner, Herbert H., additional, Speth, Cornelia, additional, Erbeznik, Thomas, additional, Fuchs, Stefan, additional, Posch, Wilfried, additional, Chatterjee, Sneha, additional, and Würzner, Reinhard, additional

Published
2019
Full Text
View/download PDF

38. Multimerization results in formation of re-bindable metabolites: A proof of concept study with FSC-based minigastrin imaging probes targeting CCK2R expression

Author

Summer, Dominik, primary, Kroess, Andrea, additional, Woerndle, Rudolf, additional, Rangger, Christine, additional, Klingler, Maximilian, additional, Haas, Hubertus, additional, Kremser, Leopold, additional, Lindner, Herbert H., additional, von Guggenberg, Elisabeth, additional, and Decristoforo, Clemens, additional

Published
2018
Full Text
View/download PDF

40. Counterregulation of cAMP-directed kinase activities controls ciliogenesis

Author

Porpora, Monia, primary, Sauchella, Simona, additional, Rinaldi, Laura, additional, Delle Donne, Rossella, additional, Sepe, Maria, additional, Torres-Quesada, Omar, additional, Intartaglia, Daniela, additional, Garbi, Corrado, additional, Insabato, Luigi, additional, Santoriello, Margherita, additional, Bachmann, Verena A., additional, Synofzik, Matthis, additional, Lindner, Herbert H., additional, Conte, Ivan, additional, Stefan, Eduard, additional, and Feliciello, Antonio, additional

Published
2018
Full Text
View/download PDF

42. Counterregulation of cAMP-directed kinase activities controls ciliogenesis

Author

Porpora, Monia, Sauchella, Simona, Bachmann, Verena A, Synofzik, Matthis, Lindner, Herbert H, Conte, Ivan, Stefan, Eduard, Feliciello, Antonio, Rinaldi, Laura, Delle Donne, Rossella, Sepe, Maria, Torres-Quesada, Omar, Intartaglia, Daniela, Garbi, Corrado, Insabato, Luigi, and Santoriello, Margherita

Subjects
animal structures, Science, Ubiquitin-Protein Ligases, PCM1 protein, human, Oryzias, genetics [Hypogonadism], Cell Cycle Proteins, genetics [NIMA-Related Kinases], metabolism [Cyclic AMP-Dependent Protein Kinases], Autoantigens, Article, metabolism [Cell Cycle Proteins], metabolism [Autoantigens], metabolism [Ubiquitin-Protein Ligases], metabolism [NIMA-Related Kinases], Nek10 protein, human, Animals, Humans, NIMA-Related Kinases, Spinocerebellar Ataxias, genetics [Spinocerebellar Ataxias], Cilia, Phosphorylation, lcsh:Science, Cells, Cultured, STUB1 protein, human, Centrioles, genetics [Ubiquitin-Protein Ligases], embryology [Oryzias], Hypogonadism, Ubiquitination, metabolism [Centrioles], physiology [NIMA-Related Kinases], Cyclic AMP-Dependent Protein Kinases, HEK293 Cells, Proteolysis, metabolism [Cilia], lcsh:Q, ddc:500
Abstract

The primary cilium emanates from the cell surface of growth-arrested cells and plays a central role in vertebrate development and tissue homeostasis. The mechanisms that control ciliogenesis have been extensively explored. However, the intersection between GPCR signaling and the ubiquitin pathway in the control of cilium stability are unknown. Here we observe that cAMP elevation promotes cilia resorption. At centriolar satellites, we identify a multimeric complex nucleated by PCM1 that includes two kinases, NEK10 and PKA, and the E3 ubiquitin ligase CHIP. We show that NEK10 is essential for ciliogenesis in mammals and for the development of medaka fish. PKA phosphorylation primes NEK10 for CHIP-mediated ubiquitination and proteolysis resulting in cilia resorption. Disarrangement of this control mechanism occurs in proliferative and genetic disorders. These findings unveil a pericentriolar kinase signalosome that efficiently links the cAMP cascade with the ubiquitin-proteasome system, thereby controlling essential aspects of ciliogenesis., The mechanisms that control ciliogenesis have been extensively explored however the signaling mechanisms that control cilium stability remain unclear. Here the authors show that GPCR signaling regulates cilia resorption via the ubiquitin-proteasome system.

Published
2016
Full Text
View/download PDF

43. 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

47. LAMTOR/Ragulator regulates lipid metabolism in macrophages and foam cell differentiation.

Author

Lamberti, Giorgia, De Smet, Cedric H., Angelova, Mihaela, Kremser, Leopold, Taub, Nicole, Herrmann, Caroline, Hess, Michael W., Rainer, Johannes, Tancevski, Ivan, Schweigreiter, Rüdiger, Kofler, Reinhard, Schmiedinger, Thomas, Vietor, Ilja, Trajanoski, Zlatko, Ejsing, Christer S., Lindner, Herbert H., Huber, Lukas A., and Stasyk, Taras

Subjects
LIPID metabolism, CELL differentiation, LYSOSOMES, FOAM cells, BONE marrow, SCAFFOLD proteins
Abstract

Late endosomal/lysosomal adaptor and MAPK and mTOR activator (LAMTOR/Ragulator) is a scaffold protein complex that anchors and regulates multiprotein signaling units on late endosomes/lysosomes. To identify LAMTOR‐modulated endolysosomal proteins, primary macrophages were derived from bone marrow of conditional knockout mice carrying a specific deletion of LAMTOR2 in the monocyte/macrophage cell lineage. Affymetrix‐based transcriptomic analysis and quantitative iTRAQ‐based organelle proteomic analysis of endosomes derived from macrophages were performed. Further analyses showed that LAMTOR could be a novel regulator of foam cell differentiation. The lipid droplet formation phenotype observed in macrophages was additionally confirmed in MEFs, where lipidomic analysis identified cholesterol esters as specifically downregulated in LAMTOR2 knockout cells. The data obtained indicate a function of LAMTOR2 in lipid metabolism. [ABSTRACT FROM AUTHOR]

Published
2020
Full Text
View/download PDF

49. Histone H5chromatin interactions in situ are strongly modulated by H5 C-terminal phosphorylation

Author

Kostova-Koleva, Nora N., Srebreva, Ljuba, Markov, Dimiter V., Sarg, Bettina, Lindner, Herbert H., Rundquist, Ingemar, Kostova-Koleva, Nora N., Srebreva, Ljuba, Markov, Dimiter V., Sarg, Bettina, Lindner, Herbert H., and Rundquist, Ingemar

Abstract

We used linker histone-depleted normal human fibroblast nuclei as templates to study how phosphorylation affects histone H5 binding to chromatin in situ. Permeabilized cells were treated with 0.7 M NaCl to extract the native linker histones. Histone H5 was purified from chicken erythrocytes and phosphorylated in vitro by recombinant cdk5/p35 kinase. High performance capillary electrophoresis (HPCE) showed that the phosphorylated protein contained a mixture of multiply phosphorylated forms. Control experiments, using mass spectrometry, revealed that up to five SPXK motifs in the C terminus were phosphorylated, but also that about 10% of the protein contained one phosphoserine in the N-terminus. Reconstitution of H1-depleted fibroblast nuclei with nonphosphorylated or phosphorylated H5 was performed at physiological ionic strength. The bound H5 was then extracted using NaCl concentrations in the range of 0.15 to 0.7 M. The release of the H5 molecules was monitored by DAPI staining and image cytofluorometry. Our results show that H5 phosphorylation substantially reduced its affinity for chromatin in situ, which support previous observations indicating that C-terminal phosphorylation may be essential for the biological functions of linker histones., Funding Agencies|Bulgarian National Science Fund|K-906/1999|Swedish Research Council|349-2001-6688|European Science Foundation EUROCORES Programme EuroDYNA (Austrian Science Foundation)|I23-B03|EC Sixth Framework Programme|ERAS-CT-2003-980409

Published
2013
Full Text
View/download PDF

50. Histone H1 interphase phosphorylation becomes largely established in G(1) or early S phase and differs in G(1) between T-lymphoblastoid cells and normal T cells

Author

Gréen, Anna, Sarg, Bettina, Green, Henrik, Lönn, Anita, Lindner, Herbert H, Rundquist, Ingemar, Gréen, Anna, Sarg, Bettina, Green, Henrik, Lönn, Anita, Lindner, Herbert H, and Rundquist, Ingemar

Abstract

Background: Histone H1 is an important constituent of chromatin, and is involved in regulation of its structure. During the cell cycle, chromatin becomes locally decondensed in S phase, highly condensed during metaphase, and again decondensed before re-entry into G(1). This has been connected to increasing phosphorylation of H1 histones through the cell cycle. However, many of these experiments have been performed using cell-synchronization techniques and cell cycle-arresting drugs. In this study, we investigated the H1 subtype composition and phosphorylation pattern in the cell cycle of normal human activated T cells and Jurkat T-lymphoblastoid cells by capillary electrophoresis after sorting of exponentially growing cells into G(1), S and G(2)/M populations. less thanbrgreater than less thanbrgreater thanResults: We found that the relative amount of H1.5 protein increased significantly after T-cell activation. Serine phosphorylation of H1 subtypes occurred to a large extent in late G(1) or early S phase in both activated T cells and Jurkat cells. Furthermore, our data confirm that the H1 molecules newly synthesized during S phase achieve a similar phosphorylation pattern to the previous ones. Jurkat cells had more extended H1.5 phosphorylation in G(1) compared with T cells, a difference that can be explained by faster cell growth and/or the presence of enhanced H1 kinase activity in G(1) in Jurkat cells. less thanbrgreater than less thanbrgreater thanConclusion: Our data are consistent with a model in which a major part of interphase H1 phosphorylation takes place in G(1) or early S phase. This implies that H1 serine phosphorylation may be coupled to changes in chromatin structure necessary for DNA replication. In addition, the increased H1 phosphorylation of malignant cells in G(1) may be affecting the G(1)/S transition control and enabling facilitated S-phase entry as a result of relaxed chromatin condensation. Furthermore, increased H1.5 expression may be coupl, Funding Agencies|Austrian Science Foundation| I23-B03 |EC Sixth Framework Programme| ERAS-CT-2003-980409 |Swedish Cancer Society

Published
2011
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results