First author: Hoeche, Nicole (poster)
Poster board B108 - Mon 05/07/2010, 13:30 - Hall 1
Session 105 - Synapses 1
Abstract n° 105.7
Publication ref.: FENS Abstr., vol.5, 105.7, 2010
||Hoeche N. (1, 2), Kaehne T. (4), Kobler O. (3), Richter K. (5), Tischmeyer W. (1), Dieterich D. C. (2) & Smalla K. H. (1)
||(1) Leibniz Institute for Neurobiology, Lab. Mol. Biol. Tec., Magdeburg, Germany; (2) Leibniz Institute for Neurobiology, RG Emmy Noether, Magdeburg, Germany; (3) Leibniz Institute for Neurobiology, Dept. Neurochemistry, Magdeburg, Germany; (4) Inst. of Experimental Internal Medicine, OvG University, Magdeburg, Germany; (5) Inst. of Biochemistry and Cell Biology, OvG University, Magdeburg, Germany
||Mapping fucosylated synaptic proteins
||The brain is a highly complex entity comprising a variety of proteins with posttranslational modifications, such as glycosylation. Fucosylated carbohydrate structures in the brain are crucial for neuronal plasticity. Plasticity phenomena like hippocampal long-term potentiation (LTP) and memory formation are accompanied by a transient increase in the incorporation of fucose into membrane glycoproteins. Interestingly, inhibition of protein fucosylation does not interfere with LTP induction or memory acquisition, but prevents specifically the long-term maintenance of LTP and memory. The mechanisms underlying the particular importance of protein fucosylation for phenomena of long-term synaptic plasticity as well as the identity of synaptic fucosylated proteins are largely unknown. Therefore, as a first step to better understand the role of protein fucosylation in the context of neuronal plasticity, we attempted to identify fucosylated synaptic proteins.
In the present study, the fucose-specific lectin from Aleuria aurantia (AAL) was used to investigate the distribution of fucose-containing carbohydrate moieties in the rat brain. We found strong AAL staining of membrane structures especially in synaptic neuropilar regions. To identify fucosylated synaptic proteins, extracts from synaptic junctions were analysed either in a targeted approach using immunoprecipitations and lectin blotting or in an unbiased approach using tandem AAL-affinity chromatography with subsequent identification of glycopeptides by LC-MS/MS. For the targeted approach we focused on proteins previously implicated in neuroplasticity, i.e. neurotransmitter receptors, cell adhesion molecules, extracellular matrix proteins, voltage gated potassium and calcium channels, growth factor receptors and ligand-gated ion channels. We identified 19 proteins that were previously not known to be fucosylated.
Supported as IfN Special Project (WT, KHS, DCD), DFG SFB 779 (TK, WT), EU Structural Funds 2007-2013 (WT, KHS) and the DFG Emmy Noether Program (DCD).
||B - Excitability, synaptic transmission, network functions
Synapses / Other
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