Linked Life Data

8740440

Source:http://linkedlifedata.com/resource/pubmed/id/8740440

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-10-29
pubmed:abstractText
The observation that autophosphorylation converts CaM kinase II from the Ca(2+)-dependent form to the Ca(2+)-independent form has led to speculation that the formation of the Ca(2+)-independent form of the enzyme could encode frequency of synaptic usage and serve as a molecular explanation of "memory". In cultured rat hippocampal neurons, glutamate elevated the Ca(2+)-independent activity of CaM kinase II through autophosphorylation, and this response was blocked by an NMDA receptor antagonist, D-2-amino-5-phosphonopentanoate (AP5). In addition, we confirmed that high, but not low frequency stimulation, applied to two groups of CA1 afferents in the rat hippocampus, resulted in LTP induction with concomitant long-lasting increases in Ca(2+)-independent and total activities of CaM kinase II. In experiments with 32P-labeled hippocampal slices, the LTP induction in the CA1 region was associated with increases in autophosphorylation of both alpha and beta subunits of CaM kinase II 1 h after LTP induction. Significant increases in phosphorylation of endogenous CaM kinase II substrates, synapsin I and microtubule-associated protein 2 (MAP2), which are originally located in presynaptic and postsynaptic regions, respectively, were also observed in the same slice. All these changes were prevented when high frequency stimulation was applied in the presence of AP5 or a calmodulin antagonist, calmidazolium. Furthermore, in vitro phosphorylation of the AMPA receptor by CaM kinase II was reported in the postsynaptic density and infusion of the constitutively active CaM kinase II into the hippocampal neurons enhanced kainate-induced response. These results support the idea that CaM kinase II contributes to the induction of hippocampal LTP in both postsynaptic and presynaptic regions through phosphorylation of target proteins such as the AMPA receptor, MAP2 and synapsin I.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0197-0186
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
343-58
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8740440-2-Amino-5-phosphonovalerate, pubmed-meshheading:8740440-Afferent Pathways, pubmed-meshheading:8740440-Animals, pubmed-meshheading:8740440-Calcium-Calmodulin-Dependent Protein Kinase Type 2, pubmed-meshheading:8740440-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:8740440-Hippocampus, pubmed-meshheading:8740440-Homeostasis, pubmed-meshheading:8740440-Long-Term Potentiation, pubmed-meshheading:8740440-Memory, pubmed-meshheading:8740440-Models, Neurological, pubmed-meshheading:8740440-Neurons, pubmed-meshheading:8740440-Phosphoprotein Phosphatases, pubmed-meshheading:8740440-Phosphorylation, pubmed-meshheading:8740440-Protein Kinases, pubmed-meshheading:8740440-Pyramidal Cells, pubmed-meshheading:8740440-Rats, pubmed-meshheading:8740440-Receptors, N-Methyl-D-Aspartate, pubmed-meshheading:8740440-Synapses
pubmed:year
1996
pubmed:articleTitle
CaM kinase II in long-term potentiation.
pubmed:affiliation
Department of Pharmacology, Kumamoto University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't