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  1. Article ; Online: The Microenvironment of the Pathogenesis of Cardiac Hypertrophy

    Farhad Bazgir / Julia Nau / Saeideh Nakhaei-Rad / Ehsan Amin / Matthew J. Wolf / Jeffry J. Saucerman / Kristina Lorenz / Mohammad Reza Ahmadian

    Cells, Vol 12, Iss 1780, p

    2023  Volume 1780

    Abstract: Pathological cardiac hypertrophy is a key risk factor for the development of heart failure and predisposes individuals to cardiac arrhythmia and sudden death. While physiological cardiac hypertrophy is adaptive, hypertrophy resulting from conditions ... ...

    Abstract Pathological cardiac hypertrophy is a key risk factor for the development of heart failure and predisposes individuals to cardiac arrhythmia and sudden death. While physiological cardiac hypertrophy is adaptive, hypertrophy resulting from conditions comprising hypertension, aortic stenosis, or genetic mutations, such as hypertrophic cardiomyopathy, is maladaptive. Here, we highlight the essential role and reciprocal interactions involving both cardiomyocytes and non-myocardial cells in response to pathological conditions. Prolonged cardiovascular stress causes cardiomyocytes and non-myocardial cells to enter an activated state releasing numerous pro-hypertrophic, pro-fibrotic, and pro-inflammatory mediators such as vasoactive hormones, growth factors, and cytokines, i.e., commencing signaling events that collectively cause cardiac hypertrophy. Fibrotic remodeling is mediated by cardiac fibroblasts as the central players, but also endothelial cells and resident and infiltrating immune cells enhance these processes. Many of these hypertrophic mediators are now being integrated into computational models that provide system-level insights and will help to translate our knowledge into new pharmacological targets. This perspective article summarizes the last decades’ advances in cardiac hypertrophy research and discusses the herein-involved complex myocardial microenvironment and signaling components.
    Keywords cardiac hypertrophy ; cardiomyocytes ; heart failure ; myocardial microenvironment ; myofibroblasts ; pressure overload ; Biology (General) ; QH301-705.5
    Subject code 610
    Language English
    Publishing date 2023-07-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Inhibition Properties and Thermodynamic Changes of Binding of p-perazine-bis and p-peridine Dithiocarbamate Sodium Salts to Mushroom Tyrosinase

    Ehsan Amin / Ali Akbar Saboury / Hassan Mansouri-Torshizi / Samaneh Zolghadri

    Iranian Journal of Chemistry & Chemical Engineering, Vol 38, Iss 3, Pp 127-

    2019  Volume 136

    Abstract: A mono- and a bi-functional dithiocarbamates as sodium salts were obtained by treating p-peridine or p-perazine in aceton-water mixture with CS2 in the presence of NaOH. These anionic water soluble compounds have been characterized by elemental analysis, ...

    Abstract A mono- and a bi-functional dithiocarbamates as sodium salts were obtained by treating p-peridine or p-perazine in aceton-water mixture with CS2 in the presence of NaOH. These anionic water soluble compounds have been characterized by elemental analysis, IR and 1H NMR spectroscopic studies. Both compounds (p-peridine (I) and p-perazine-bis dithiocarbamate (II) sodium salts) were examined for inhibition of mushroom tyrosinase (MT) activity. The results showed that they inhibit MT competitively. KI values of two compounds at 27°C are 2 and 4 mM. Therefore, the compound (I) is more potent than (II). They chelate active site of tyrosinase via electrostatic interactions. These conclusions are proved by obtained thermodynamic parameters and fluorescence studies. Extrinsic fluorescence studies disprove any tertiary structure changes of MT. Major enthalpy changes in binding of compound (II) in comparison to (I) show that including two carbamate tails in such compounds disturb balancing of hydrophobic interactions with vicinity of active site of enzyme.
    Keywords inhibition ; thermodynamic changes ; dithiocarbamate sodium salts ; mushroom tyrosinase ; Chemical engineering ; TP155-156 ; Chemistry ; QD1-999
    Language English
    Publishing date 2019-06-01T00:00:00Z
    Publisher Iranian Institute of Research and Development in Chemical Industries (IRDCI)-ACECR
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Characterization of the HCN Interaction Partner TRIP8b/PEX5R in the Intracardiac Nervous System of TRIP8b-Deficient and Wild-Type Mice

    Katharina Scherschel / Hanna Bräuninger / Andrea Mölders / Nadine Erlenhardt / Ehsan Amin / Christiane Jungen / Ulrike Pape / Diana Lindner / Dane M. Chetkovich / Nikolaj Klöcker / Christian Meyer

    International Journal of Molecular Sciences, Vol 22, Iss 4772, p

    2021  Volume 4772

    Abstract: The tetratricopeptide repeat-containing Rab8b-interacting protein (TRIP8b/PEX5R) is an interaction partner and auxiliary subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, which are key for rhythm generation in the brain and ... ...

    Abstract The tetratricopeptide repeat-containing Rab8b-interacting protein (TRIP8b/PEX5R) is an interaction partner and auxiliary subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, which are key for rhythm generation in the brain and in the heart. Since TRIP8b is expressed in central neurons but not in cardiomyocytes, the TRIP8b-HCN interaction has been studied intensely in the brain, but is deemed irrelevant in the cardiac conduction system. Still, to date, TRIP8b has not been studied in the intrinsic cardiac nervous system (ICNS), a neuronal network located within epicardial fat pads. In vitro electrophysiological studies revealed that TRIP8b-deficient mouse hearts exhibit increased atrial refractory and atrioventricular nodal refractory periods, compared to hearts of wild-type littermates. Meanwhile, heart rate, sino-nodal recovery time, and ventricular refractory period did not differ between genotypes. Trip8b mRNA was detected in the ICNS by quantitative polymerase chain reaction. RNAscope in situ hybridization confirmed Trip8b localization in neuronal somata and nerve fibers. Additionally, we found a very low amount of mRNAs in the sinus node and atrioventricular node, most likely attributable to the delicate fibers innervating the conduction system. In contrast, TRIP8b protein was not detectable. Our data suggest that TRIP8b in the ICNS may play a role in the modulation of atrial electrophysiology beyond HCN-mediated sino-nodal control of the heart.
    Keywords autonomic nervous system ; TRIP8b ; HCN channels ; cardiac electrophysiology ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 572
    Language English
    Publishing date 2021-04-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: The RAS-Effector Interface

    Hossein Nakhaeizadeh / Ehsan Amin / Saeideh Nakhaei-Rad / Radovan Dvorsky / Mohammad Reza Ahmadian

    PLoS ONE, Vol 11, Iss 12, p e

    Isoform-Specific Differences in the Effector Binding Regions.

    2016  Volume 0167145

    Abstract: RAS effectors specifically interact with the GTP-bound form of RAS in response to extracellular signals and link them to downstream signaling pathways. The molecular nature of effector interaction by RAS is well-studied but yet still incompletely ... ...

    Abstract RAS effectors specifically interact with the GTP-bound form of RAS in response to extracellular signals and link them to downstream signaling pathways. The molecular nature of effector interaction by RAS is well-studied but yet still incompletely understood in a comprehensive and systematic way. Here, structure-function relationships in the interaction between different RAS proteins and various effectors were investigated in detail by combining our in vitro data with in silico data. Equilibrium dissociation constants were determined for the binding of HRAS, KRAS, NRAS, RRAS1 and RRAS2 to both the RAS binding (RB) domain of CRAF and PI3Kα, and the RAS association (RA) domain of RASSF5, RALGDS and PLCε, respectively, using fluorescence polarization. An interaction matrix, constructed on the basis of available crystal structures, allowed identification of hotspots as critical determinants for RAS-effector interaction. New insights provided by this study are the dissection of the identified hotspots in five distinct regions (R1 to R5) in spite of high sequence variability not only between, but also within, RB/RA domain-containing effectors proteins. Finally, we propose that intermolecular β-sheet interaction in R1 is a central recognition region while R3 may determine specific contacts of RAS versus RRAS isoforms with effectors.
    Keywords Medicine ; R ; Science ; Q
    Subject code 500
    Language English
    Publishing date 2016-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Biophysical Characterization of Nucleophosmin Interactions with Human Immunodeficiency Virus Rev and Herpes Simplex Virus US11.

    Kazem Nouri / Jens M Moll / Lech-Gustav Milroy / Anika Hain / Radovan Dvorsky / Ehsan Amin / Michael Lenders / Luitgard Nagel-Steger / Sebastian Howe / Sander H J Smits / Hartmut Hengel / Lutz Schmitt / Carsten Münk / Luc Brunsveld / Mohammad R Ahmadian

    PLoS ONE, Vol 10, Iss 12, p e

    2015  Volume 0143634

    Abstract: Nucleophosmin (NPM1, also known as B23, numatrin or NO38) is a pentameric RNA-binding protein with RNA and protein chaperon functions. NPM1 has increasingly emerged as a potential cellular factor that directly associates with viral proteins; however, the ...

    Abstract Nucleophosmin (NPM1, also known as B23, numatrin or NO38) is a pentameric RNA-binding protein with RNA and protein chaperon functions. NPM1 has increasingly emerged as a potential cellular factor that directly associates with viral proteins; however, the significance of these interactions in each case is still not clear. In this study, we have investigated the physical interaction of NPM1 with both human immunodeficiency virus type 1 (HIV-1) Rev and Herpes Simplex virus type 1 (HSV-1) US11, two functionally homologous proteins. Both viral proteins show, in mechanistically different modes, high affinity for a binding site on the N-terminal oligomerization domain of NPM1. Rev, additionally, exhibits low-affinity for the central histone-binding domain of NPM1. We also showed that the proapoptotic cyclic peptide CIGB-300 specifically binds to NPM1 oligomerization domain and blocks its association with Rev and US11. Moreover, HIV-1 virus production was significantly reduced in the cells treated with CIGB-300. Results of this study suggest that targeting NPM1 may represent a useful approach for antiviral intervention.
    Keywords Medicine ; R ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2015-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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