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Article: The enhancement of phosphatidylcholine biosynthesis by angiotensin II in H9c2 cells

TitleThe enhancement of phosphatidylcholine biosynthesis by angiotensin II in H9c2 cells
Authors
KeywordsAngiotensin
Biosynthesis
Cardiac cell
Phosphatidylcholine
Phosphocholine cytidylyltransferase
Issue Date1995
PublisherElsevier BV.
Citation
Biochimica Et Biophysica Acta - Lipids And Lipid Metabolism, 1995, v. 1259 n. 3, p. 283-290 How to Cite?
AbstractThe effect of angiotensin II on the biosynthesis of phosphatidylcholine in rat heart myoblastic (H9c2) cells was investigated. Cells were incubated with [methyl-3H]choline, and the labelling of phosphatidylcholine at different time intervals was examined. When cells were pretreated with angiotensin II, a significant increase in the labelling of phosphatidylcholine was observed. Analysis of the labelled phosphatidylcholine precursors indicated that the conversion of phosphocholine to CDP-choline was enhanced by angiotensin II treatment. Determination of enzyme activities in the CDP-choline pathway revealed that the activities of choline kinase or CDP-choline: diacylglycerol cholinephosphotransferase were not changed, but the activities of CTP:phosphocholine cytidylyltransferase were stimulated in bath the particulate and soluble fractions. The stimulation of the cytidylyltransferase by angiotensin II was not abolished by okadaic acid, indicating that the activation of the enzyme was not mediated via the okadaic-sensitive dephosphorylation mechanism. Alternatively, the stimulation of the cytidylyltransferase activity was completely abolished by protein kinase C inhibitors. Immunoblotting studies revealed that levels of the cytidylyltransferase in the soluble and particulate fractions were not affected by angiotensin II treatment. We conclude that the increase in phosphatidylcholine biosynthesis by angiotensin II was a direct result of the enhancement of the cytidylyltransferase activity. The enhancement of enzyme activity was not mediated via enzyme translocation, but by a mechanism which was intimately associated with the protein kinase C cascade.
Persistent Identifierhttp://hdl.handle.net/10722/80312
ISSN
2000 Impact Factor: 2.973
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTran, Ken_HK
dc.contributor.authorMan, RYKen_HK
dc.contributor.authorChoy, PCen_HK
dc.date.accessioned2010-09-06T08:04:55Z-
dc.date.available2010-09-06T08:04:55Z-
dc.date.issued1995en_HK
dc.identifier.citationBiochimica Et Biophysica Acta - Lipids And Lipid Metabolism, 1995, v. 1259 n. 3, p. 283-290en_HK
dc.identifier.issn0005-2760en_HK
dc.identifier.urihttp://hdl.handle.net/10722/80312-
dc.description.abstractThe effect of angiotensin II on the biosynthesis of phosphatidylcholine in rat heart myoblastic (H9c2) cells was investigated. Cells were incubated with [methyl-3H]choline, and the labelling of phosphatidylcholine at different time intervals was examined. When cells were pretreated with angiotensin II, a significant increase in the labelling of phosphatidylcholine was observed. Analysis of the labelled phosphatidylcholine precursors indicated that the conversion of phosphocholine to CDP-choline was enhanced by angiotensin II treatment. Determination of enzyme activities in the CDP-choline pathway revealed that the activities of choline kinase or CDP-choline: diacylglycerol cholinephosphotransferase were not changed, but the activities of CTP:phosphocholine cytidylyltransferase were stimulated in bath the particulate and soluble fractions. The stimulation of the cytidylyltransferase by angiotensin II was not abolished by okadaic acid, indicating that the activation of the enzyme was not mediated via the okadaic-sensitive dephosphorylation mechanism. Alternatively, the stimulation of the cytidylyltransferase activity was completely abolished by protein kinase C inhibitors. Immunoblotting studies revealed that levels of the cytidylyltransferase in the soluble and particulate fractions were not affected by angiotensin II treatment. We conclude that the increase in phosphatidylcholine biosynthesis by angiotensin II was a direct result of the enhancement of the cytidylyltransferase activity. The enhancement of enzyme activity was not mediated via enzyme translocation, but by a mechanism which was intimately associated with the protein kinase C cascade.en_HK
dc.languageengen_HK
dc.publisherElsevier BV.en_HK
dc.relation.ispartofBiochimica et Biophysica Acta - Lipids and Lipid Metabolismen_HK
dc.rightsBiochimica et Biophysica Acta. Copyright © Elsevier BV.en_HK
dc.subjectAngiotensinen_HK
dc.subjectBiosynthesisen_HK
dc.subjectCardiac cellen_HK
dc.subjectPhosphatidylcholineen_HK
dc.subjectPhosphocholine cytidylyltransferaseen_HK
dc.titleThe enhancement of phosphatidylcholine biosynthesis by angiotensin II in H9c2 cellsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0006-3002&volume=&spage=&epage=&date=1995&atitle=The+enhancement+of+phosphatidylcholine+biosynthesis+by+angiotensin+II+in+H9c2+cellsen_HK
dc.identifier.emailMan, RYK: rykman@hkucc.hku.hken_HK
dc.identifier.authorityMan, RYK=rp00236en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/0005-2760(95)00175-1en_HK
dc.identifier.pmid8541336-
dc.identifier.scopuseid_2-s2.0-0029561014en_HK
dc.identifier.hkuros20682en_HK
dc.identifier.volume1259en_HK
dc.identifier.issue3en_HK
dc.identifier.spage283en_HK
dc.identifier.epage290en_HK
dc.identifier.isiWOS:A1995TM24600012-
dc.identifier.scopusauthoridTran, K=7102163210en_HK
dc.identifier.scopusauthoridMan, RYK=7004986435en_HK
dc.identifier.scopusauthoridChoy, PC=7006633002en_HK

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