Apolipoprotein A-I glycation by Glucose and Reactive Aldehydes Alters Phospholipid Affinity but Not Cholesterol Export from Lipid-Laden Macrophages.docVIP

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Apolipoprotein A-I glycation by Glucose and Reactive Aldehydes Alters Phospholipid Affinity but Not Cholesterol Export from Lipid-Laden Macrophages.doc

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Apolipoprotein A-I glycation by Glucose and Reactive Aldehydes Alters Phospholipid Affinity but Not Cholesterol Export from Lipid-Laden Macrophages

ApolipoproteinA-IglycationbyGlucoseandReactive AldehydesAltersPhospholipidAffinitybutNot CholesterolExportfromLipid-LadenMacrophages BronwynE.Brown1,3,EstelleNobecourt1,JingminZeng1,AliciaJ.Jenkins2,Kerry-AnneRye1,2,3, MichaelJ.Davies1,3 * 1TheHeartResearchInstitute,Sydney,NewSouthWales,Australia,2DepartmentofMedicine(StVincent’s),TheUniversityofMelbourne,Melbourne,Victoria,Australia, 3FacultyofMedicine,UniversityofSydney,Sydney,NewSouthWales,Australia Abstract Increasedproteinglycationinpeoplewithdiabetesmaypromoteatherosclerosis.Thisstudyexaminedtheeffectsofnon- enzymatic glycation on the association of lipid-free apolipoproteinA-I (apoA-I) with phospholipid, and cholesterol efflux fromlipid-loadedmacrophagestolipid-freeandlipid-associatedapoA-I.Glycationoflipid-freeapoA-Ibymethylglyoxaland glycolaldehyderesultedinArg,LysandTrploss,advancedglycationend-productformationandproteincross-linking.The association ofapoA-I glycated by glucose,methylglyoxalor glycolaldehyde withphospholipid multilamellarvesicles was impairedinaglycatingagentdose-dependentmanner,withexposureofapoA-Itoboth30mMglucose(42%decreasein kslow) and 3mM glycolaldehyde (50% decrease in kfast, 60% decrease in kslow) resulting is significantly reduced affinity. Cholesterol efflux to control or glycated lipid-free apoA-I, or discoidal reconstituted HDL containing glycated apoA-I (drHDL), was examined using cholesterol-loaded murine (J774A.1) macrophages treated to increase expression of ATP bindingcassettetransportersA1(ABCA1)orG1(ABCG1).CholesteroleffluxfromJ774A.1macrophagestoglycatedlipid-free apoA-I via ABCA1 or glycated drHDL via an ABCG1-dependent mechanism was unaltered, as was efflux to minimally modifiedapoA-IfrompeoplewithType1diabetes,orcontrols.Changestoproteinstructureandfunctionwereprevented bythereactivecarbonylscavengeraminoguanidine.Overallthesestudiesdemonstratethatglycationoflipid-freeapoA-I, particularly late glycation, modifies its structure, its capacity to bind phospholipids an