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dc.contributor.authorMei, Fan
dc.contributor.authorNagappan, Guhan
dc.contributor.authorKe, Yang
dc.contributor.authorSacktor, Todd C.
dc.contributor.authorLu, Bai
dc.contributor.editorMei, Lin
dc.date.accessioned2012-10-26T16:27:00Z
dc.date.available2012-10-26T16:27:00Z
dc.date.issued2011-06-29en_US
dc.identifier.citationPLoS One. 2011 Jun 29; 6(6):e21568en_US
dc.identifier.issn1932-6203en_US
dc.identifier.pmid21747912en_US
dc.identifier.doi10.1371/journal.pone.0021568en_US
dc.identifier.urihttp://hdl.handle.net/10675.2/662
dc.description.abstractLate-phase long term potentiation (L-LTP) is thought to be the cellular basis for long-term memory (LTM). While LTM as well as L-LTP is known to depend on transcription and translation, it is unclear why brain-derived neurotrophic factor (BDNF) could sustain L-LTP when protein synthesis is inhibited. The persistently active protein kinase f (PKMf) is the only molecule implicated in perpetuating L-LTP maintenance. Here, in mouse acute brain slices, we show that inhibition of PKMf reversed BDNF-dependent form of L-LTP. While BDNF did not alter the steady-state level of PKMf, BDNF together with the L-LTP inducing theta-burst stimulation (TBS) increased PKMf level even without protein synthesis. Finally, in the absence of de novo protein synthesis, BDNF maintained TBS-induced PKMf at a sufficient level. These results suggest that BDNF sustains L-LTP through PKMf in a protein synthesis-independent manner, revealing an unexpected link between BDNF and PKMf.
dc.rightsMei et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_US
dc.subjectResearch Articleen_US
dc.subjectBiologyen_US
dc.subjectNeuroscienceen_US
dc.subjectDevelopmental Neuroscienceen_US
dc.subjectSynaptic Plasticityen_US
dc.subjectMolecular Neuroscienceen_US
dc.subjectSignaling Pathwaysen_US
dc.subjectNeurophysiologyen_US
dc.subjectSynapsesen_US
dc.subjectLearning and Memoryen_US
dc.titleBDNF Facilitates L-LTP Maintenance in the Absence of Protein Synthesis through PKMfen_US
dc.typeArticleen_US
dc.identifier.pmcidPMC3126837en_US
dc.contributor.corporatenameDepartment of Neurology
refterms.dateFOA2019-04-10T00:29:02Z
html.description.abstractLate-phase long term potentiation (L-LTP) is thought to be the cellular basis for long-term memory (LTM). While LTM as well as L-LTP is known to depend on transcription and translation, it is unclear why brain-derived neurotrophic factor (BDNF) could sustain L-LTP when protein synthesis is inhibited. The persistently active protein kinase f (PKMf) is the only molecule implicated in perpetuating L-LTP maintenance. Here, in mouse acute brain slices, we show that inhibition of PKMf reversed BDNF-dependent form of L-LTP. While BDNF did not alter the steady-state level of PKMf, BDNF together with the L-LTP inducing theta-burst stimulation (TBS) increased PKMf level even without protein synthesis. Finally, in the absence of de novo protein synthesis, BDNF maintained TBS-induced PKMf at a sufficient level. These results suggest that BDNF sustains L-LTP through PKMf in a protein synthesis-independent manner, revealing an unexpected link between BDNF and PKMf.


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