Exogenous phospholipase C specifically inhibits ApoE expression in mouse peritoneal macrophages

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Abstract

Treatment of cholesterol-loaded mouse peritoneal macrophages with exogenous phospholipase C results in a specific and dose-dependent inhibition of apoE secretion. The inhibition of apoE secretion is secondary to the rapid and specific inhibition of its synthesis. The profound changes in rates of apoE synthesis are not accompanied by changes in the level of apoE mRNA, an observation strongly suggestive of translational regulation of expression. The changes in apoE expression coincide with, or are preceeded by a three-fold increase in membrane-bound protein kinase C activity, pointing out the potential importance of this signal transduction pathway in regulating apoE expression at a posttranscriptional locus.

Original languageEnglish
Pages (from-to)842-847
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume194
Issue number2
DOIs
StatePublished - 1 Jan 1993

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Macrophages
Peritoneal Macrophages
Type C Phospholipases
Apolipoproteins E
Signal transduction
Protein Kinase C
Signal Transduction
Membrane Proteins
Cholesterol
Observation
Membranes
Messenger RNA

Cite this

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abstract = "Treatment of cholesterol-loaded mouse peritoneal macrophages with exogenous phospholipase C results in a specific and dose-dependent inhibition of apoE secretion. The inhibition of apoE secretion is secondary to the rapid and specific inhibition of its synthesis. The profound changes in rates of apoE synthesis are not accompanied by changes in the level of apoE mRNA, an observation strongly suggestive of translational regulation of expression. The changes in apoE expression coincide with, or are preceeded by a three-fold increase in membrane-bound protein kinase C activity, pointing out the potential importance of this signal transduction pathway in regulating apoE expression at a posttranscriptional locus.",
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AB - Treatment of cholesterol-loaded mouse peritoneal macrophages with exogenous phospholipase C results in a specific and dose-dependent inhibition of apoE secretion. The inhibition of apoE secretion is secondary to the rapid and specific inhibition of its synthesis. The profound changes in rates of apoE synthesis are not accompanied by changes in the level of apoE mRNA, an observation strongly suggestive of translational regulation of expression. The changes in apoE expression coincide with, or are preceeded by a three-fold increase in membrane-bound protein kinase C activity, pointing out the potential importance of this signal transduction pathway in regulating apoE expression at a posttranscriptional locus.

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