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Article: Protein lipid interaction in bile: Effects of biliary proteins on the stability of cholesterol-lecithin vesicles

TitleProtein lipid interaction in bile: Effects of biliary proteins on the stability of cholesterol-lecithin vesicles
Authors
KeywordsBile
Gallstone
Kinetics
Scattering
Issue Date1998
Citation
Biochimica Et Biophysica Acta - Lipids And Lipid Metabolism, 1998, v. 1390 n. 3, p. 282-292 How to Cite?
AbstractThe nucleation of cholesterol crystals is an obligatory precursor to cholesterol gallstone formation. Nucleation, in turn, is believed to be preceded by aggregation and fusion of cholesterol-rich vesicles. We have investigated the effects of two putative pro-nucleating proteins, a concanavalin A-binding protein fraction and a calcium-binding protein, on the stability of sonicated small unilamellar cholesterol-lecithin vesicles. Vesicle aggregation is followed by monitoring absorbance, and upon addition of the concanavalin A-binding protein fraction the absorbance of a vesicle dispersion increases continuously with time. Vesicle fusion is probed by a fluorescence contents-mixing assay. Vesicles apparently fuse slowly after the addition of the concanavalin A-binding protein, although inner filter effects confound the quantitative measurement of fusion rates. The rates of change of absorbance and fluorescence increase with the concentration of the protein, and the second-order dimerization rate constant increases with both the protein concentration and the cholesterol content of the vesicles. On the other hand, the calcium-binding protein has no effect on the stability of the vesicle dispersion. This protein may therefore affect cholesterol crystal formation not by promoting the nucleation process, but by enhancing crystal growth and packaging. Our results demonstrate that biliary proteins can destabilize lipid vesicles and that different proteins play different roles in the mechanism of cholesterol gallstone formation.
Persistent Identifierhttp://hdl.handle.net/10722/92493
ISSN
2000 Impact Factor: 2.973
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLuk, ASen_HK
dc.contributor.authorKaler, EWen_HK
dc.contributor.authorLee, SPen_HK
dc.date.accessioned2010-09-17T10:47:56Z-
dc.date.available2010-09-17T10:47:56Z-
dc.date.issued1998en_HK
dc.identifier.citationBiochimica Et Biophysica Acta - Lipids And Lipid Metabolism, 1998, v. 1390 n. 3, p. 282-292en_HK
dc.identifier.issn0005-2760en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92493-
dc.description.abstractThe nucleation of cholesterol crystals is an obligatory precursor to cholesterol gallstone formation. Nucleation, in turn, is believed to be preceded by aggregation and fusion of cholesterol-rich vesicles. We have investigated the effects of two putative pro-nucleating proteins, a concanavalin A-binding protein fraction and a calcium-binding protein, on the stability of sonicated small unilamellar cholesterol-lecithin vesicles. Vesicle aggregation is followed by monitoring absorbance, and upon addition of the concanavalin A-binding protein fraction the absorbance of a vesicle dispersion increases continuously with time. Vesicle fusion is probed by a fluorescence contents-mixing assay. Vesicles apparently fuse slowly after the addition of the concanavalin A-binding protein, although inner filter effects confound the quantitative measurement of fusion rates. The rates of change of absorbance and fluorescence increase with the concentration of the protein, and the second-order dimerization rate constant increases with both the protein concentration and the cholesterol content of the vesicles. On the other hand, the calcium-binding protein has no effect on the stability of the vesicle dispersion. This protein may therefore affect cholesterol crystal formation not by promoting the nucleation process, but by enhancing crystal growth and packaging. Our results demonstrate that biliary proteins can destabilize lipid vesicles and that different proteins play different roles in the mechanism of cholesterol gallstone formation.en_HK
dc.languageengen_HK
dc.relation.ispartofBiochimica et Biophysica Acta - Lipids and Lipid Metabolismen_HK
dc.subjectBileen_HK
dc.subjectGallstoneen_HK
dc.subjectKineticsen_HK
dc.subjectScatteringen_HK
dc.titleProtein lipid interaction in bile: Effects of biliary proteins on the stability of cholesterol-lecithin vesiclesen_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/S0005-2760(97)00161-6en_HK
dc.identifier.pmid9487149-
dc.identifier.scopuseid_2-s2.0-0032559566en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032559566&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume1390en_HK
dc.identifier.issue3en_HK
dc.identifier.spage282en_HK
dc.identifier.epage292en_HK
dc.identifier.isiWOS:000072758400005-
dc.identifier.scopusauthoridLuk, AS=7004034631en_HK
dc.identifier.scopusauthoridKaler, EW=7007157989en_HK
dc.identifier.scopusauthoridLee, SP=7601417497en_HK

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