RUB » Biochemistry I - Receptor Biochemistry

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09.02.2018

NMDA receptor peptidesUp to 20% of the population carry anti­bodies against glutamate receptors of the NMDA type independent of any disease, with pre­valence increasing with age. In colla­bo­ration with the Clinical Neuroscience Group of Hannelore Ehrenreich at the Max Planck Institute for Experimental Medicine in Göttingen, we have now shown a similar prevalence of antibodies against NMDA receptors in other mammals. Dogs, cats, rats and mice also displayed the age de­penden­cy found in most humans, whereas baboons and rhesus macaques in captivity did not. Based on this result and the observation that human migrants also show a weaker age dependency, we hypothesise that chronic stress triggers the antibody production.

When we immunised mice against NMDA receptors, they produced large amounts of antibodies. When the animals had a disrupted blood-brain barrier, they showed psychosis-like symptoms like the ones known to be caused by drug-induced NMDA receptor block. However, none of the animals had any signs of brain inflammation (encephalitis). This indicates that some of the symptoms observed in encephalitis patients carrying antibodies against NMDA receptors may indeed be caused by the antibodies, whereas the encephalitis itself has another cause.

Abstract. The complete article is openly accessible.

Publications

07.04.2017

GluD2 hingeThe delta receptor GluD2 is an unusual mem­ber of the ionotropic glutamate receptor (iGluR) family. Most iGluRs can be activated by the neurotransmitter glutamate, with some additionally requring glycine or D-serine as a co-agonist. The activation leads to opening of a channel that allows the influx of ions into the cell. GluD2 has a functional ion channel and can bind glycine or D-serine, yet the binding is weak and does not open the channel. In collaboration with the group of Jette Kastrup at the Department of Drug Design and Phar­ma­col­ogy at the University of Copenhagen, we have now investigated why D-serine binds so weakly to GluD2. We found that a small, so-called hinge region is responsible for the weak binding. This region is located in the domain of the receptor that binds D-serine and serves as a hinge for a closing movement trapping D-serine inside the protein. Replacing this hinge region with that of another iGluR, GluN1, that binds D-serine much more strongly, transfers the strong binding to GluD2.

Abstract. The complete article is openly accessible.

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