RGD Reference Report - The synaptic glycoprotein neuroplastin is involved in long-term potentiation at hippocampal CA1 synapses. - Rat Genome Database

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The synaptic glycoprotein neuroplastin is involved in long-term potentiation at hippocampal CA1 synapses.

Authors: Smalla, KH  Matthies, H  Langnase, K  Shabir, S  Bockers, TM  Wyneken, U  Staak, S  Krug, M  Beesley, PW  Gundelfinger, ED 
Citation: Smalla KH, etal., Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):4327-32.
RGD ID: 8553916
Pubmed: (View Article at PubMed) PMID:10759566
DOI: Full-text: DOI:10.1073/pnas.080389297

Neuroplastin-65 and -55 (previously known as gp65 and gp55) are glycoproteins of the Ig superfamily that are enriched in rat forebrain synaptic membrane preparations. Whereas the two-Ig domain isoform neuroplastin-55 is expressed in many tissues, the three-Ig domain isoform neuroplastin-65 is brain-specific and enriched in postsynaptic density (PSD) protein preparations. Here, we have assessed the function of neuroplastin in long-term synaptic plasticity. Immunocytochemical studies with neuroplastin-65-specific antibodies differentially stain distinct synaptic neuropil regions of the rat hippocampus with most prominent immunoreactivity in the CA1 region and the proximal molecular layer of the dentate gyrus. Kainate-induced seizures cause a significant enhancement of neuroplastin-65 association with PSDs. Similarly, long-term potentiation (LTP) of CA1 synapses in hippocampal slices enhanced the association of neuroplastin-65 with a detergent-insoluble PSD-enriched protein fraction. Several antibodies against the neuroplastins, including one specific for neuroplastin-65, inhibited the maintenance of LTP. A similar effect was observed when recombinant fusion protein containing the three extracellular Ig domains of neuroplastin-65 was applied to hippocampal slices before LTP induction. Microsphere binding experiments using neuroplastin-F(c) chimeric proteins show that constructs containing Ig1-3 or Ig1 domains, but not Ig2-3 domains mediate homophilic adhesion. These data suggest that neuroplastin plays an essential role in implementing long-term changes in synaptic activity, possibly by means of a homophilic adhesion mechanism.


Gene Ontology Annotations    

Cellular Component

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Nptn  (neuroplastin)

Additional Information