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| Beteiligung des Calciumsensors VILIP- 1 (Visinin-like protein-1) an synaptischer Plastizität Brackmann, Marian |
| Main title | Beteiligung des Calciumsensors VILIP- 1 (Visinin-like protein-1) an synaptischer Plastizität |
| Subtitle | Regulation der Expression in Modellen der hippokampalen Plastizität und Einfluss auf Signaltransduktionsmechanismen |
| Title variations | Involvement of the calcium-sensor visinin-like protein-1 (VILIP-1) in synaptic plasticity |
| Subtitle for translated title | Regulation of expression in models of hippocampal plasticity and influence on signal transductionprocesses |
| Author(s) | Brackmann, Marian
Place of birth: Bad Oeynhausen, Deutschland |
| 1. Referee | Prof. Dr. Uwe Heinemann |
| Further Referee(s) | Prof. Dr. Ferdinand Hucho - |
| Keywords | calcium, neuronal calcium-binding proteins, guanylyl cyclase, synaptic plasticity, protein regulation |
| Classification (DDC) | 570 Life sciences |
| Summary | An effect of VILIP-1 on guanylyl cyclases in different cell types has been well documented. The current data show, that an increased VILIP-1 protein expression leads to an increased cGMP accumulation and that therefore VILIP-1 affects the activity of guanylyl cyclases in hippocampal neurons. The underlying molecular mechanisms seem to be an increased surface expression of the receptor, which depends on a reinforced recycling of the internalised GC-B. Since VILIP-1 also increases surface expression of the α4 subunit of the nicotinic acetylcholine receptor and also influences the subcellular distribution of clathrin, it is likely that VILIP-1 might have a general effect on membrane trafficking. Furthermore VILIP-1 influences the phosphorylation state of the GC-B after ligand binding, but it is not clear yet, whether this is a secondary effect, as homolgous desensitization, which induces dephosphorylation and ligand-dependent internalization are closely linked to each other. The stimulation of group I metabotropic glutamate receptors induces a specific upregulation of VILIP-1 and NCS-1 in vivo after 8 and 24 hours. A similar regulation can be observed in LTP-stimulated denate gyri of rat in vivo. Therefore an increased protein expression of VILIP-1, as well as NCS-1, can be evoked by a variety plasticity inducing stimuli. In addition, it was shown, that regulation of VILIP-1 also occurs during an early phase of protein expression, which is independent of gene transcription and can be observed already half an hour after stimulation of hippocampal cell cultures with DHPG. Similarly, LTP-induction in rat subiculum slices leads to moderate, but significant increase in VILIP-1 protein expression half an hour after the induction. The regulation of the VILIP-1 protein, expression at different phases of synaptic plasticity processes, by mGluR-dependent mechanisms, suggests that VILIP-1 contributes to the expression of synaptic plasticity. It was shown for the first time that the activity of GC-B is linked to synaptic potentiation in subiculum slices in vitro, where a stimulation of GC-B enhances the expression of LTP up to 50 %. An increased cGMP accumulation via GC-B, which can be stimulated by VILIP-1, may be part of processes that, so far have been attributed to the activity of soluble guanylyl cyclase. These data support the hypothesized function of VILIP-1 in plasticity processes. In summary, these data suggest, that the regulation of VILIP-1 after plasticity induction may lead to a long term change of synaptic transmission in neurons via increased surface presentation or recycling of receptors, which sensitizes the cell for subsequent stimuli and thus contribute to synaptic plasticity. |
| Documents |
FUDISS_derivate_000000001496
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| FU Department | Department of Biology, Chemistry and Pharmacy |
| Year of publication | 2004 |
| Document type | Doctoral thesis |
| Media type/Format | Text |
| Language | German |
| Terms of use/Rights | Nutzungsbedingungen |
| Date of defense | 2004-08-20 |
| Created at | 2004-08-31 : 12:00:00 |
| Last changed | 2010-02-19 : 10:10:01 |
| Old Darwin URL | http://www.diss.fu-berlin.de/2004/232/ |
| Static URL | http://www.diss.fu-berlin.de/diss/receive/FUDISS_thesis_000000001496 |
| NBN | urn:nbn:de:kobv:188-2004002327 |
| Statistics | |
