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414 results on '"Huber, Otmar"'

1. Epigenetic control over the cell-intrinsic immune response antagonizes self-renewal in acute myeloid leukemia

Author

Felipe Fumero, Eloísa, Walter, Carolin, Frenz, Joris Maximillian, Seifert, Franca, Alla, Vijay, Hennig, Thorben, Angenendt, Linus, Hartmann, Wolfgang, Wolf, Sebastian, Serve, Hubert, Oellerich, Thomas, Lenz, Georg, Müller-Tidow, Carsten, Schliemann, Christoph, Huber, Otmar, Dugas, Martin, Mann, Matthias, Jayavelu, Ashok Kumar, Mikesch, Jan-Henrik, and Arteaga, Maria Francisca

Published
2024
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2. Identification of Novel Nexilin Splice Variants in Mouse and Human Tissues.

Author

Jung, Paul, Fiedelak, André, Dreeßen, Celina, Huber, Otmar, and Reiche, Juliane

Subjects
ALTERNATIVE RNA splicing, HEART development, RECOMBINANT proteins, PROTEIN-protein interactions, ENDOTHELIAL cells
Abstract

There is no doubt that the proper development of the heart is important for its correct function, in addition, maturation processes of the heart are crucial as well. The actin-binding protein nexilin seems to take over central roles in the latter processes, as nexilin-deficient mice are phenotypically inconspicuous at birth but die within short time thereafter. Recently, it has been proposed that nexilin plays a role in the formation and function of transverse tubules (T-tubules), which are essential for excitation-contraction coupling in the hearts of mature animals. Although it has long been known that nexilin is subjected to alternative splicing, a molecular characterization of the respective isoforms is not yet available. Here, we describe novel nexilin splice variants and analyze their expression in tissues of mice and humans. Interestingly, nexilin isoforms segregate to myocyte- and epithelial-specific isoforms. Moreover, heart-specific isoforms of nexilin localize differently between atria and ventricles and are also expressed in the endothelial cells of blood vessels. Further, we narrowed down the critical exons in the actin-binding domains 1 and 2 (ABD1/2), and observed different self-interaction properties by recombinant protein interaction studies. Our results emphasize the diverse tissue and subcellular distribution of the individual nexilin isoforms and point to the importance of taking a closer look at the particular nexilin isoforms investigated. [ABSTRACT FROM AUTHOR]

Published
2024
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7. Ubiquitination contributes to the regulation of GDP-mannose pyrophosphorylase B activity.

Author

Franzka, Patricia, Mittag, Sonnhild, Chakraborty, Abhijnan, Huber, Otmar, and Hübner, Christian A.

Subjects
UBIQUITINATION, HUMAN genetics, PHOSPHORYLASES
Abstract

The article titled "Ubiquitination contributes to the regulation of GDP-mannose pyrophosphorylase B activity" discusses the role of ubiquitination in regulating the activity of GDP-mannose pyrophosphorylase B (GMPPB). The study found that autophagy and lysosomal degradation affect the protein levels of GMPPB. Additionally, the researchers discovered that ubiquitination is not necessary for the degradation of GMPPB but is important for its activity. The article provides experimental evidence and includes supplementary figures and data to support the findings. [Extracted from the article]

Published
2024

16. GMPPA defects cause a neuromuscular disorder with [alpha]-dystroglycan hyperglycosylation

Author

Franzka, Patricia, Henze, Henriette, Jung, M. Juliane, Schuler, Svenja Caren, Mittag, Sonnhild, Biskup, Karina, Liebmann, Lutz, Kentache, Takfarinas, Morales, Jose, Martinez, Braulio, Katona, Istvan, Herrmann, Tanja, Huebner, Antje-Kathrin, Hennings, J. Christopher, Groth, Susann, Gresing, Lennart, Horstkorte, Rudiger, Marquardt, Thorsten, Weis, Joachim, Kaether, Christoph, Mutchinick, Osvaldo M., Ori, Alessandro, Huber, Otmar, Blanchard, Veronique, von Maltzahn, Julia, and Hubner, Christian A.

Subjects
Medical research, Medicine, Experimental, Neuromuscular diseases -- Causes of -- Genetic aspects, Gene expression -- Research, Glycosylation -- Research, Protein metabolism -- Research, Membrane proteins -- Genetic aspects -- Health aspects, Metabolism, Inborn errors of -- Complications and side effects -- Genetic aspects, Health care industry
Abstract

GDP-mannose-pyrophosphorylase-B (GMPPB) facilitates the generation of GDP-mannose, a sugar donor required for glycosylation. GMPPB defects cause muscle disease due to hypoglycosylation of [alpha]-dystroglycan ([alpha]-DG). AlphaDG is part of a protein complex, which links the extracellular matrix with the cytoskeleton, thus stabilizing myofibers. Mutations of the catalytically inactive homolog GMPPA cause alacrima, achalasia, and mental retardation syndrome (AAMR syndrome), which also involves muscle weakness. Here, we showed that Gmppa-KO mice recapitulated cognitive and motor deficits. As structural correlates, we found cortical layering defects, progressive neuron loss, and myopathic alterations. Increased GDP-mannose levels in skeletal muscle and in vitro assays identified GMPPA as an allosteric feedback inhibitor of GMPPB. Thus, its disruption enhanced mannose incorporation into glycoproteins, including [alpha]-DG in mice and humans. This increased [alpha]-DG turnover and thereby lowered [alpha]-DG abundance. In mice, dietary mannose restriction beginning after weaning corrected [alpha]-DG hyperglycosylation and abundance, normalized skeletal muscle morphology, and prevented neuron degeneration and the development of motor deficits. Cortical layering and cognitive performance, however, were not improved. We thus identified GMPPA defects as the first congenital disorder of glycosylation characterized by [alpha]-DG hyperglycosylation, to our knowledge, and we have unraveled underlying disease mechanisms and identified potential dietary treatment options., Introduction Cell surface proteins are important for the attachment of a cell to the extracellular matrix (ECM). They are modified by post-translational covalent attachment of branched carbohydrate oligomers. N-linked oligosaccharides [...]

Published
2021
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17. A microfluidically perfused three dimensional human liver model

Author

Rennert, Knut, Steinborn, Sandra, Gröger, Marko, Ungerböck, Birgit, Jank, Anne-Marie, Ehgartner, Josef, Nietzsche, Sandor, Dinger, Julia, Kiehntopf, Michael, Funke, Harald, Peters, Frank T., Lupp, Amelie, Gärtner, Claudia, Mayr, Torsten, Bauer, Michael, Huber, Otmar, and Mosig, Alexander S.

Published
2015
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29. Transient opening of the perineurial barrier for analgesic drug delivery

Author

Hackel, Dagmar, Krug, Susanne M., Sauer, Reine-Solange, Mousa, Shaaban A., Böcker, Alexander, Pflücke, Diana, Wrede, Esther-Johanna, Kistner, Katrin, Hoffmann, Tali, Niedermirtl, Benedikt, Sommer, Claudia, Bloch, Laura, Huber, Otmar, Blasig, Ingolf E., Amasheh, Salah, Reeh, Peter W., Fromm, Michael, Brack, Alexander, and Rittner, Heike L.

Published
2012

39. The tumor suppressor Fhit acts as a repressor of [beta]-catenin transcriptional activity

Author

Weiske,Jorg, Albring, Kai Frederik, and Huber, Otmar

Subjects
Tumor suppressor genes -- Properties, Cell adhesion -- Genetic aspects, Genetic transcription -- Research, Lymphoid tissue -- Genetic aspects, T cells -- Genetic aspects, Histidine -- Properties, Science and technology
Abstract

The Fra3B locus on chromosome 3p14.2 targeting the fragile histidine triad (Fhit) gene represents one of the most common fragile sites of the human genome and is associated with early preneoplastic and malignant disorders in multiple human tumors. Fhit was classified as a tumor suppressor; however, the molecular mechanisms of its function are not well established. Here, we report that Fhit associates with the lymphoid enhancer-binding factor 1/T cell factor/[beta]-catenin complex by directly binding to [beta]-catenin, a major player in the canonical Wnt pathway that is deregulated in numerous forms of human cancer. In binding to the [beta]-catenin C-terminal domain, Fhit represses transcription of target genes such as cyclin D1, axin2, MMP-14, and survivin. Knockdown of Fhit reversed this effect, whereas this reversal was not detectable when [beta]-catenin was knocked down simultaneously. The Fhit enzymatic activity as a diadenosine-polyphosphate hydrolase is not required for the down-regulation of [beta]-catenin-mediated transcription as examined with an enzymatic inactive Fhit-H96N protein. ChIPs revealed recruitment of Fhit/[beta]-catenin complexes to target gene promoters. In soft agar assays Fhit and [beta]-catenin are involved in regulation of anchorage-independent growth. These observations assign to the tumor suppressor Fhit an unexpected role in the regulation of [beta]-catenin-mediated gene transcription. histidine triad | T cell factor | lymphoid enhancer-binding factor 1

Published
2007

42. GMPPA defects cause a neuromuscular disorder with α-dystroglycan hyperglycosylation

Author

Franzka, Patricia, primary, Henze, Henriette, additional, Jung, M. Juliane, additional, Schüler, Svenja Caren, additional, Mittag, Sonnhild, additional, Biskup, Karina, additional, Liebmann, Lutz, additional, Kentache, Takfarinas, additional, Morales, José, additional, Martínez, Braulio, additional, Katona, Istvan, additional, Herrmann, Tanja, additional, Huebner, Antje-Kathrin, additional, Hennings, J. Christopher, additional, Groth, Susann, additional, Gresing, Lennart, additional, Horstkorte, Rüdiger, additional, Marquardt, Thorsten, additional, Weis, Joachim, additional, Kaether, Christoph, additional, Mutchinick, Osvaldo M., additional, Ori, Alessandro, additional, Huber, Otmar, additional, Blanchard, Véronique, additional, von Maltzahn, Julia, additional, and Hübner, Christian A., additional

Published
2021
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