Linked Life Data

17046687

Source:http://linkedlifedata.com/resource/pubmed/id/17046687

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-10-18
pubmed:abstractText
Long-lasting changes in synaptic strength are thought to play a pivotal role in activity-dependent plasticity and memory. There is ample evidence indicating that in hippocampal long-term potentiation (LTP) the synthesis of new proteins is crucial for enduring changes. However, whether protein degradation also plays a role in this process has only recently begun to receive attention. Here, we examine the effects of blocking protein degradation on LTP. We show that pharmacological inhibition of proteasome-dependent protein degradation, just like inhibition of protein synthesis, disrupts expression of late (L-)LTP. However, when protein degradation and protein synthesis are inhibited at the same time, LTP is restored to control levels, calling into question the commonly held hypothesis that synthesis of new proteins is indispensable for L-LTP. Instead, these findings point to a more facetted model, in which L-LTP is determined by the combined action of synthesis and degradation of plasticity proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
239-45
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP.
pubmed:affiliation
Department of Cellular and Systems Neurobiology, Max Planck Institute of Neurobiology, Am Klopferspitz 18, 82152 München-Martinsried, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't