Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-4-21
pubmed:abstractText
Phospholipase A2 (PLA2) activity is an important contributor to destructive cellular processes in the central nervous system. Two cytosolic forms of calcium dependent PLA2 have been characterized in the gerbil brain and the neuronal cultures from rat brain. PLA2 enzymatic activity in cell free extracts from cortical neuronal cultures is upregulated after cells are exposed to glutamate. Brief exposure to a calcium ionophore or phorbol 12-myristate 13-acetate (PMA) stably enhanced PLA2 activity. Stable activation of the two cytosolic forms of PLA2 occur prior to evidence of cell death and this activation is reversible. The larger molecular mass form was characterized as cPLA2. The smaller form (approximately 14 kDa) was distinct from Group I and II PLA2. Exposure to glutamate shifted the calcium activation curve of the smaller form to the left suggesting a novel mechanism of regulation of PLA2. Glutamate-induced stable enhancement of PLA2 activity, by processes involving calcium and protein kinase C activation, is a potential molecular switch likely mediating changes in synaptic function and contributing to excitotoxicity.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0929-7855
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Roles of phospholipases A2 in brain cell and tissue injury associated with ischemia and excitotoxicity.
pubmed:affiliation
Massachusetts General Hospital, Department of Medicine, Harvard Medical School, Boston 02114, USA. jbonvent@warren.med.harvard.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Corrected and Republished Article