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Article: Interaction of apolipoprotein A-I with lecithin-cholesterol vesicles in the presence of phospholipase C

TitleInteraction of apolipoprotein A-I with lecithin-cholesterol vesicles in the presence of phospholipase C
Authors
KeywordsApo A-I
Apo A-I complex
Bile
Cholesterol
PLC
Vesicle
Issue Date2003
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbalip
Citation
Biochimica Et Biophysica Acta - Molecular And Cell Biology Of Lipids, 2003, v. 1635 n. 2-3, p. 127-141 How to Cite?
AbstractHere we study the anti-nucleating mechanism of apolipoprotein A-I (apo A-I) on model biliary vesicles in the presence of phospholipase C (PLC) utilizing dynamic light scattering (DLS), steady-state fluorescence spectroscopy, cryogenic transmission electron microscopy (cryo-TEM), and UV/Vis spectroscopy. PLC induces aggregation of cholesterol-free lecithin vesicles from an initial, average size of 100 nm to a maximal size of 600 nm. The presence of apo A-I likely inhibits vesicle aggregation by shielding the PLC-generated hydrophobic moieties, which results in vesicles of an average size of 200 nm. A similar phenomenon is observed in cholesterol-enriched lecithin vesicles. Whereas PLC alone produces aggregates of 300 nm, no aggregation is observed when apo A-I is present along with PLC. However, the ability of apo A-I to inhibit aggregation is temporary, and after 8 h, a broad particle size distribution with sizes as high as 800 nm is observed. Apo A-I possibly induces the formation of small apo A-I/lecithin/cholesterol complexes of about 5-20 nm similar to the discoidal pre-HDL complexes found in blood when it can no longer effectively shield all the DAG molecules. Concomitant with formation of complexes, DAG molecules coalesce into large oil droplets, which account for the large particles observed by light scattering. Thus, apo A-I acts as an anti-nucleating agent by two mechanisms, anti-aggregation and microstructural transition. The mode of protection is dependent on the cholesterol content and the relative amounts of DAG and apo A-I present. This study supports the possibility of apo A-I solubilizing lipids in bile in a similar fashion as it does in blood and also delineates the mechanism of formation of the complexes. © 2003 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/92472
ISSN
2015 Impact Factor: 4.779
2015 SCImago Journal Rankings: 2.467
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGudheti, MVen_HK
dc.contributor.authorGonzalez, YIen_HK
dc.contributor.authorLee, SPen_HK
dc.contributor.authorWrenn, SPen_HK
dc.date.accessioned2010-09-17T10:47:17Z-
dc.date.available2010-09-17T10:47:17Z-
dc.date.issued2003en_HK
dc.identifier.citationBiochimica Et Biophysica Acta - Molecular And Cell Biology Of Lipids, 2003, v. 1635 n. 2-3, p. 127-141en_HK
dc.identifier.issn1388-1981en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92472-
dc.description.abstractHere we study the anti-nucleating mechanism of apolipoprotein A-I (apo A-I) on model biliary vesicles in the presence of phospholipase C (PLC) utilizing dynamic light scattering (DLS), steady-state fluorescence spectroscopy, cryogenic transmission electron microscopy (cryo-TEM), and UV/Vis spectroscopy. PLC induces aggregation of cholesterol-free lecithin vesicles from an initial, average size of 100 nm to a maximal size of 600 nm. The presence of apo A-I likely inhibits vesicle aggregation by shielding the PLC-generated hydrophobic moieties, which results in vesicles of an average size of 200 nm. A similar phenomenon is observed in cholesterol-enriched lecithin vesicles. Whereas PLC alone produces aggregates of 300 nm, no aggregation is observed when apo A-I is present along with PLC. However, the ability of apo A-I to inhibit aggregation is temporary, and after 8 h, a broad particle size distribution with sizes as high as 800 nm is observed. Apo A-I possibly induces the formation of small apo A-I/lecithin/cholesterol complexes of about 5-20 nm similar to the discoidal pre-HDL complexes found in blood when it can no longer effectively shield all the DAG molecules. Concomitant with formation of complexes, DAG molecules coalesce into large oil droplets, which account for the large particles observed by light scattering. Thus, apo A-I acts as an anti-nucleating agent by two mechanisms, anti-aggregation and microstructural transition. The mode of protection is dependent on the cholesterol content and the relative amounts of DAG and apo A-I present. This study supports the possibility of apo A-I solubilizing lipids in bile in a similar fashion as it does in blood and also delineates the mechanism of formation of the complexes. © 2003 Elsevier B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbalipen_HK
dc.relation.ispartofBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipidsen_HK
dc.subjectApo A-Ien_HK
dc.subjectApo A-I complexen_HK
dc.subjectBileen_HK
dc.subjectCholesterolen_HK
dc.subjectPLCen_HK
dc.subjectVesicleen_HK
dc.titleInteraction of apolipoprotein A-I with lecithin-cholesterol vesicles in the presence of phospholipase Cen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, SP: sumlee@hku.hken_HK
dc.identifier.authorityLee, SP=rp01351en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bbalip.2003.11.003en_HK
dc.identifier.pmid14729075en_HK
dc.identifier.scopuseid_2-s2.0-0346056939en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0346056939&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume1635en_HK
dc.identifier.issue2-3en_HK
dc.identifier.spage127en_HK
dc.identifier.epage141en_HK
dc.identifier.isiWOS:000188511000008-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridGudheti, MV=16024338300en_HK
dc.identifier.scopusauthoridGonzalez, YI=8648217700en_HK
dc.identifier.scopusauthoridLee, SP=7601417497en_HK
dc.identifier.scopusauthoridWrenn, SP=6603940041en_HK

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