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Article: The catabolism of exogenous lysophosphatidylcholine in isolated perfused rat and guinea pig hearts: A comparative study

TitleThe catabolism of exogenous lysophosphatidylcholine in isolated perfused rat and guinea pig hearts: A comparative study
Authors
Issue Date1991
Citation
Biochimica Et Biophysica Acta - Lipids And Lipid Metabolism, 1991, v. 1084 n. 2, p. 167-172 How to Cite?
AbstractLysophosphatidylcholine (lysoPC) is an arrhythmogenic phospholipid metabolite which accumulates in the ischemic myocardium. Reduced catabolism of lysoPC has been proposed to be one of the biochemical mechanisms responsible for the increase in lysoPC content. In this investigation we compared the microsomal catabolism of exogenous labeled lysoPC in isolated perfused rat and guinea pig hearts. Analysis of the amount of radioactivity in microsomal phosphatidylcholine (PC) and free fatty acid (FFA) was used as an index of the participation in lysoPC clearance by acylation catalyzed by acyl-CoA:lysoPC acyltransferase and deacylation catalyzed by lysophospholipase, respectively. There was no significant difference in the incorporation of radioactivity into rat and guinea pig heart microsomes; however, the patterns of radioactivity in lysoPC metabolites were notably different. Equal participation by deacylation and reacylation was observed in rat microsomes, whereas deacylation was clearly the preferred route for lysoPC clearance in guinea pig microsomes. Modulation of enzyme activity by treatment of the isolated heart with pHMB, a sulfhydryl agent, was used to probe the relationship among acylation, deacylation and the extent of lysoPC clearance. In guinea pig microsomes impairment of lysoPC acylation was not associated with any change in the amount of radioactivity in lysoPC because of a compensatory increase in deacylation. In contrast, impaired deacylation in rat microsomes led to significant elevations in the amount of radioactivity in lysoPC. We conclude, therefore, that in intact perfused rat and guinea pig hearts the relative participation of acylation and deacylation in lysoPC clearance differs. Moreover, we propose that the level of deacylation by lysophospholipase is an important factor in the extent of clearance of lysoPC.
Persistent Identifierhttp://hdl.handle.net/10722/171006
ISSN
2000 Impact Factor: 2.973
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMock, Ten_US
dc.contributor.authorMan, RYKen_US
dc.date.accessioned2012-10-30T06:11:48Z-
dc.date.available2012-10-30T06:11:48Z-
dc.date.issued1991en_US
dc.identifier.citationBiochimica Et Biophysica Acta - Lipids And Lipid Metabolism, 1991, v. 1084 n. 2, p. 167-172en_US
dc.identifier.issn0005-2760en_US
dc.identifier.urihttp://hdl.handle.net/10722/171006-
dc.description.abstractLysophosphatidylcholine (lysoPC) is an arrhythmogenic phospholipid metabolite which accumulates in the ischemic myocardium. Reduced catabolism of lysoPC has been proposed to be one of the biochemical mechanisms responsible for the increase in lysoPC content. In this investigation we compared the microsomal catabolism of exogenous labeled lysoPC in isolated perfused rat and guinea pig hearts. Analysis of the amount of radioactivity in microsomal phosphatidylcholine (PC) and free fatty acid (FFA) was used as an index of the participation in lysoPC clearance by acylation catalyzed by acyl-CoA:lysoPC acyltransferase and deacylation catalyzed by lysophospholipase, respectively. There was no significant difference in the incorporation of radioactivity into rat and guinea pig heart microsomes; however, the patterns of radioactivity in lysoPC metabolites were notably different. Equal participation by deacylation and reacylation was observed in rat microsomes, whereas deacylation was clearly the preferred route for lysoPC clearance in guinea pig microsomes. Modulation of enzyme activity by treatment of the isolated heart with pHMB, a sulfhydryl agent, was used to probe the relationship among acylation, deacylation and the extent of lysoPC clearance. In guinea pig microsomes impairment of lysoPC acylation was not associated with any change in the amount of radioactivity in lysoPC because of a compensatory increase in deacylation. In contrast, impaired deacylation in rat microsomes led to significant elevations in the amount of radioactivity in lysoPC. We conclude, therefore, that in intact perfused rat and guinea pig hearts the relative participation of acylation and deacylation in lysoPC clearance differs. Moreover, we propose that the level of deacylation by lysophospholipase is an important factor in the extent of clearance of lysoPC.en_US
dc.languageengen_US
dc.relation.ispartofBiochimica et Biophysica Acta - Lipids and Lipid Metabolismen_US
dc.subject.mesh1-Acylglycerophosphocholine O-Acyltransferase - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshFatty Acids, Nonesterified - Isolation & Purification - Metabolismen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshHydroxymercuribenzoates - Pharmacologyen_US
dc.subject.meshKineticsen_US
dc.subject.meshLysophosphatidylcholines - Metabolismen_US
dc.subject.meshLysophospholipase - Metabolismen_US
dc.subject.meshMicrosomes - Enzymologyen_US
dc.subject.meshMyocardium - Metabolismen_US
dc.subject.meshPerfusionen_US
dc.subject.meshPhosphatidylcholines - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Inbred Strainsen_US
dc.titleThe catabolism of exogenous lysophosphatidylcholine in isolated perfused rat and guinea pig hearts: A comparative studyen_US
dc.typeArticleen_US
dc.identifier.emailMan, RYK:rykman@hkucc.hku.hken_US
dc.identifier.authorityMan, RYK=rp00236en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0005-2760(91)90216-5en_US
dc.identifier.pmid1854801-
dc.identifier.scopuseid_2-s2.0-0025832994en_US
dc.identifier.volume1084en_US
dc.identifier.issue2en_US
dc.identifier.spage167en_US
dc.identifier.epage172en_US
dc.identifier.isiWOS:A1991FY61300008-
dc.identifier.scopusauthoridMock, T=35954418100en_US
dc.identifier.scopusauthoridMan, RYK=7004986435en_US

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