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  • 1
    Keywords: brain ; COMBINATION ; Germany ; GENERATION ; SYSTEM ; liver ; PROTEIN ; PROTEINS ; HEART ; COMPLEX ; COMPLEXES ; MECHANISM ; RAT ; PHOSPHORYLATION ; TARGET ; RAT-LIVER ; SUBUNIT ; MEMBRANE ; STRESS ; MODULATION ; MITOCHONDRIA ; OXYGEN ; antioxidants ; PROTEOMICS ; reactive oxygen species ; glutathione-S-transferase ; GENE-EXPRESSION PROFILE ; ageing ; GEL-ELECTROPHORESIS ; assembly ; proteome ; REACTIVE OXYGEN ; ROS ; CALORIE RESTRICTION ; SHORT-TERM ; COMPLEX-I ; MEMBRANE-PROTEINS ; CYTOCHROME-C-OXIDASE ; DIGE ; Species ; ROS PRODUCTION ; SHIFT ; RESPIRATORY-CHAIN
    Abstract: Mitochondria being the major source and target of reactive oxygen species (ROS) play a crucial role during ageing. We analyzed ageing and calorie restriction (CR)-induced changes in abundance of rat liver mitochondrial proteins to understand key aspects behind the age-retarding mechanism of CR. The combination of blue-native (BN) gel system with fluorescence Difference Gel Electrophoresis (DIGE) facilitated an efficient analysis of soluble and membrane proteins, existing as monomers or multi-protein assemblies. Changes in abundance of specific key subunits of respiratory chain complexes I, IV and V, critical for activity and/or assembly of the complexes were identified. CR lowered complex I assembly and complex IV activity, which is discussed as a molecular mechanism to minimize ROS production at mitochondria. Notably, the antioxidant system was found to be least affected. The GSH:GSSG couple could be depicted as a rapid mean to handle the fluctuations in ROS levels led by reversible metabolic shifts. We evaluated the relative significance of ROS generation against quenching. We also observed parallel and unidirectional changes as effect of ageing and CR, in subunits of ATP synthase, cytochrome P450 and glutathione S-transferase. This is the first report on such 'putatively hormetic' ageing-analogous effects of CR, besides the age-retarding ones
    Type of Publication: Journal article published
    PubMed ID: 19894137
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  • 2
    Keywords: brain ; RECEPTOR ; CELLS ; Germany ; NETWORKS ; SYSTEM ; TOOL ; DISTINCT ; PROTEIN ; PROTEINS ; TRANSDUCTION ; COMPLEX ; MESSENGER-RNA ; RAT ; signal transduction ; MEMBRANE ; SIGNAL-TRANSDUCTION ; mass spectrometry ; MASS-SPECTROMETRY ; CHROMATOGRAPHY ; PROTEOMIC ANALYSIS ; glutathione-S-transferase ; BINDING PROTEIN ; signaling ; molecular ; NEURONS ; analysis ; cilia ; ENGLAND ; XENOBIOTIC-METABOLIZING ENZYMES ; affinity chromatography ; calcium-calmodulin ; CHEMOSENSORY CILIA ; NUCLEOTIDE-GATED CHANNEL ; olfaction ; olfactory receptor neurons ; PHOSPHOLIPID-BINDING ; SENSORY NEURONS
    Abstract: The olfactory neuroepithelium represents a unique interface between the brain and the external environment. Olfactory function comprises a distinct set of molecular tasks: sensory signal transduction, cytoprotection and adult neurogenesis. A multitude of biochemical studies has revealed the central role of Ca2+ signaling in the function of olfactory receptor neurons (ORNs). We set out to establish Ca2+-dependent signaling networks in ORN cilia by proteomic analysis. We subjected a ciliary membrane preparation to Ca2+/calmodulin-affinity chromatography using mild detergent conditions in order to maintain functional protein complexes involved in olfactory Ca2+ signaling. Thus, calmodulin serves as a valuable tool to gain access to novel Ca2+-regulated protein complexes. Tandem mass spectrometry (nanoscale liquid-chromatography-electrospray injection) identified 123 distinct proteins. Ninety-seven proteins (79%) could be assigned to specific olfactory functions, including 32 to sensory signal transduction and 40 to cytoprotection. We point out novel perspectives for research on the Ca2+-signaling networks in the olfactory system of the rat. (C) 2007 IBRO. Published by Elsevier Ltd. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 18155848
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  • 3
    Keywords: MICE ; COMPLEX ; SUPERFAMILY ; TNF ; KAPPA-B ACTIVATION ; RHEUMATOID-ARTHRITIS ; STRUCTURAL BASIS ; CHAINS ; CHRONIC PROLIFERATIVE DERMATITIS ; K11-LINKED POLYUBIQUITINATION ; MEDIATED REGULATION ; NEMO
    Abstract: Members of the tumour necrosis factor (TNF) receptor superfamily have important functions in immunity and inflammation. Recently linear ubiquitin chains assembled by a complex containing HOIL-1 and HOIP (also known as RBCK1 and RNF31, respectively) were implicated in TNF signalling, yet their relevance in vivo remained uncertain. Here we identify SHARPIN as a third component of the linear ubiquitin chain assembly complex, recruited to the CD40 and TNF receptor signalling complexes together with its other constituents, HOIL-1 and HOIP. Mass spectrometry of TNF signalling complexes revealed RIP1 (also known as RIPK1) and NEMO (also known as IKK gamma or IKBKG) to be linearly ubiquitinated. Mutation of the Sharpin gene (Sharpin(cpdm/cpdm)) causes chronic proliferative dermatitis (cpdm) characterized by inflammatory skin lesions and defective lymphoid organogenesis. Gene induction by TNF, CD40 ligand and interleukin-1 beta was attenuated in cpdm-derived cells which were rendered sensitive to TNF-induced death. Importantly, Tnf gene deficiency prevented skin lesions in cpdm mice. We conclude that by enabling linear ubiquitination in the TNF receptor signalling complex, SHARPIN interferes with TNF-induced cell death and, thereby, prevents inflammation. Our results provide evidence for the relevance of linear ubiquitination in vivo in preventing inflammation and regulating immune signalling
    Type of Publication: Journal article published
    PubMed ID: 21455173
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  • 4
    Keywords: RECEPTOR ; Germany ; PATHWAY ; PROTEIN ; PROTEINS ; COMPLEX ; RAT ; signal transduction ; SIGNAL ; MOUSE ; MEMBRANE ; SIGNAL-TRANSDUCTION ; mass spectrometry ; PROTEOMIC ANALYSIS ; signaling ; NEURONS ; EPITHELIUM ; NUCLEOTIDE-GATED CHANNEL ; olfactory receptor neurons ; sensory cilia ; ADENYLYL-CYCLASE ; CHLORIDE ACCUMULATION ; MAMMALIAN ODORANT RECEPTORS ; ORGANELLAR PROTEOMICS
    Abstract: Olfactory sensory neurons expose to the inhaled air chemosensory cilia which bind odorants and operate as transduction organelles. Odorant receptors in the ciliary membrane activate a transduction cascade which uses cAMP and Ca2+ for sensory signaling in the ciliary lumen. Although the canonical transduction pathway is well established, molecular components for more complex aspects of sensory transduction, like adaptation, regulation, and termination of the receptor response have not been systematically identified. Moreover, open questions in olfactory physiology include how the cilia exchange solutes with the surrounding mucus, assemble their highly polarized set of proteins, and cope with noxious substances in the ambient air. A specific ciliary proteome would promote research efforts in all of these fields. We have improved a method to detach cilia from rat olfactory sensory neurons and have isolated a preparation specifically enriched in ciliary membrane proteins. Using LC-ESI-MS/MS analysis, we identified 377 proteins which constitute the olfactory cilia proteome. These proteins represent a comprehensive data set for olfactory research since more than 80% can be attributed to the characteristic functions of olfactory sensory neurons and their cilia: signal processing, protein targeting, neurogenesis, solute transport, and cytoprotection. Organellar proteomics thus yielded decisive information about the diverse physiological functions of a sensory organelle
    Type of Publication: Journal article published
    PubMed ID: 19086097
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