| Literature DB >> 20049656 |
Abstract
Plasmalogen-selective phospholipase A(2) (PlsEtn-PLA(2)) has been purified from pig brain using multiple column chromatographic procedure. The purified enzyme migrates as a single band on polyacrylamide. It is stimulated by Triton X-100 and inhibited by sodium deoxycholate. Purified PlsEtn-PLA(2) is inhibited by iodoacetate, and this inhibition can be prevented by beta-meracaptoethanol. Treatment of neuronal cell cultures with kainic acid stimulates PlsEtn-PLA(2) activity in a dose-dependent manner, and this stimulation can be blocked by Ly294486, a selective kainic acid receptor antagonist. Activities of PlsEtn-PLA(2) are markedly increased in plasma membrane and synaptosomal plasma membrane fraction prepared from nucleus basalis and hippocampal region of brains from Alzheimer disease patients compared to age-matched controls. It is proposed that accumulation of ceramide and increased expression of cytokines may be responsible for the stimulation of PlsEtn-PLA(2) in Alzheimer disease.Entities:
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Year: 2010 PMID: 20049656 DOI: 10.1007/s12035-009-8091-y
Source DB: PubMed Journal: Mol Neurobiol ISSN: 0893-7648 Impact factor: 5.590