Linked Life Data

8281293

Source:http://linkedlifedata.com/resource/pubmed/id/8281293

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1994-2-15
pubmed:abstractText
Depolarization induced in rat hippocampal slices by a high concentration of extracellular K+ leads to an increase in the phosphorylation of microtubule-associated protein MAP2. The comparison of the major phosphopeptides derived from in situ and in vitro phosphorylated MAP2 suggests the implication of calcium-dependent protein kinases, including calcium/calmodulin-dependent protein kinase type II and protein kinase C, in the up-phosphorylation of MAP2. In particular, a peptide containing the tubulin-binding domain of the MAP2 molecule may be phosphorylated by protein kinase C. As the association of MAP2 with the cytoskeleton may be regulated by phosphorylation, we suggest that changes in the phosphorylation level of MAP2 might be involved in synaptic remodelling in hippocampal neurons.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0953-816X
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
818-24
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
High external potassium induces an increase in the phosphorylation of the cytoskeletal protein MAP2 in rat hippocampal slices.
pubmed:affiliation
Centro de Biología Molecular, Universidad Autónoma de Madrid, Spain.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't