Activation of pro-BDNF by the pericellular serine protease plasmin
In: FEBS Letters, Jg. 582 (2008-03-19), Heft 6, S. 907-910
Online
academicJournal
Zugriff:
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. [Copyright &y& Elsevier]
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Activation of pro-BDNF by the pericellular serine protease plasmin
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Autor/in / Beteiligte Person: | Gray, Kelly ; Ellis, Vincent |
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Zeitschrift: | FEBS Letters, Jg. 582 (2008-03-19), Heft 6, S. 907-910 |
Veröffentlichung: | 2008 |
Medientyp: | academicJournal |
ISSN: | 0014-5793 (print) |
DOI: | 10.1016/j.febslet.2008.02.026 |
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