Extracellular proteolysis of reelin by tissue plasminogen activator following synaptic potentiation.

@article{Trotter2014ExtracellularPO,
  title={Extracellular proteolysis of reelin by tissue plasminogen activator following synaptic potentiation.},
  author={Justin H. Trotter and April L. Lussier and Kelly E Psilos and H L Mahoney and Ashley E Sponaugle and H-S Hoe and G. William Rebeck and Edwin J. Weeber},
  journal={Neuroscience},
  year={2014},
  volume={274},
  pages={299-307}
}
The secreted glycoprotein reelin plays an indispensable role in neuronal migration during development and in regulating adult synaptic functions. The upstream mechanisms responsible for initiating and regulating the duration and magnitude of reelin signaling are largely unknown. Here we report that reelin is cleaved between EGF-like repeats 6-7 (R6-7) by tissue plasminogen activator (tPA) under cell-free conditions. No changes were detected in the level of reelin and its fragments in the brains… CONTINUE READING

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