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Article: Phospholipase C-induced aggregation and fusion of cholesterol-lecithin small unilamellar vesicles

TitlePhospholipase C-induced aggregation and fusion of cholesterol-lecithin small unilamellar vesicles
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1993
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistry
Citation
Biochemistry, 1993, v. 32 n. 27, p. 6965-6973 How to Cite?
AbstractWe have investigated the effects of the Ca2+-requiring enzyme phospholipase C on the stability of sonicated vesicles made with different molar ratios of cholesterol to lecithin. Vesicle aggregation is detected by following turbidity with time. Upon the addition of phospholipase C and after a short lag period, the turbidity of a vesicle dispersion increases continuously with time. The rate of increase of turbidity increases with both the enzyme-to-vesicle ratio and the cholesterol content of the vesicles. Vesicle fusion and leakage of contents are monitored by a contents-mixing fusion assay using 8-aminonaphthalene-1,3,6-trisulfonic acid (ANTS) and p-xylylenebis(pyridinium bromide) (DPX) as the fluorescence probes [Ellens, H., Bentz, J., & Szoka, F. C. (1985) Biochemistry 24, 3099-3106]. The results clearly show that phospholipase C induces vesicle fusion. The rate of vesicle fusion correlates with the enzyme-to-vesicle ratio but not with the cholesterol content of the membrane. Negligible aggregation and fusion of vesicles occurs when the experiment is repeated with buffer free of Ca2+. The membrane-destabilizing diacylglycerol, a product of lecithin hydrolysis by phospholipase C, is speculated to play a major role in driving the observed vesicle aggregation and fusion. The kinetics of vesicle aggregation and vesicle fusion can be predicted by linking Michaelis-Menten enzyme kinetics to a mass-action model. © 1993 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/92463
ISSN
2015 Impact Factor: 2.876
2015 SCImago Journal Rankings: 1.769
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLuk, ASen_HK
dc.contributor.authorKaler, EWen_HK
dc.contributor.authorLee, SPen_HK
dc.date.accessioned2010-09-17T10:47:00Z-
dc.date.available2010-09-17T10:47:00Z-
dc.date.issued1993en_HK
dc.identifier.citationBiochemistry, 1993, v. 32 n. 27, p. 6965-6973en_HK
dc.identifier.issn0006-2960en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92463-
dc.description.abstractWe have investigated the effects of the Ca2+-requiring enzyme phospholipase C on the stability of sonicated vesicles made with different molar ratios of cholesterol to lecithin. Vesicle aggregation is detected by following turbidity with time. Upon the addition of phospholipase C and after a short lag period, the turbidity of a vesicle dispersion increases continuously with time. The rate of increase of turbidity increases with both the enzyme-to-vesicle ratio and the cholesterol content of the vesicles. Vesicle fusion and leakage of contents are monitored by a contents-mixing fusion assay using 8-aminonaphthalene-1,3,6-trisulfonic acid (ANTS) and p-xylylenebis(pyridinium bromide) (DPX) as the fluorescence probes [Ellens, H., Bentz, J., & Szoka, F. C. (1985) Biochemistry 24, 3099-3106]. The results clearly show that phospholipase C induces vesicle fusion. The rate of vesicle fusion correlates with the enzyme-to-vesicle ratio but not with the cholesterol content of the membrane. Negligible aggregation and fusion of vesicles occurs when the experiment is repeated with buffer free of Ca2+. The membrane-destabilizing diacylglycerol, a product of lecithin hydrolysis by phospholipase C, is speculated to play a major role in driving the observed vesicle aggregation and fusion. The kinetics of vesicle aggregation and vesicle fusion can be predicted by linking Michaelis-Menten enzyme kinetics to a mass-action model. © 1993 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistryen_HK
dc.relation.ispartofBiochemistryen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titlePhospholipase C-induced aggregation and fusion of cholesterol-lecithin small unilamellar 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.pmid8334126-
dc.identifier.scopuseid_2-s2.0-0027304585en_HK
dc.identifier.volume32en_HK
dc.identifier.issue27en_HK
dc.identifier.spage6965en_HK
dc.identifier.epage6973en_HK
dc.identifier.isiWOS:A1993LN44200022-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLuk, AS=7004034631en_HK
dc.identifier.scopusauthoridKaler, EW=7007157989en_HK
dc.identifier.scopusauthoridLee, SP=7601417497en_HK

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