Activation of pro-BDNF by the pericellular serine protease plasmin

Gray, Kelly and Ellis, Vincent (2008) Activation of pro-BDNF by the pericellular serine protease plasmin. FEBS Letters, 582 (6). pp. 907-910. ISSN 1873-3468

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Abstract

Brain-derived neurotrophic factor (BDNF) is secreted as either a mature furin-processed form or an unprocessed pro-form. Here, we characterise the extracellular processing of pro-BDNF by the serine protease plasmin. Using recombinant BDNF, maintained in the pro-form by site-directed mutagenesis or inhibition of furin, we demonstrate that plasmin (but not related proteases) is a specific and efficient activator of pro-BDNF. The proteolytic cleavage site is identified as Arg125-Val, within the consensus furin-cleavage motif (RVRR), generating an active form that stimulated neurite outgrowth on TrkB-transfected PC12 cells. Furthermore, we demonstrate that this processing can also occur in the pericellular environment by the action of cell-associated plasminogen activators.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Depositing User: LivePure Connector
Date Deposited: 28 Nov 2018 14:30
Last Modified: 24 Jun 2020 23:41
URI: https://ueaeprints.uea.ac.uk/id/eprint/69069
DOI: 10.1016/j.febslet.2008.02.026

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