Please use this identifier to cite or link to this item: https://doi.org/10.1194/jlr.M700543-JLR200
DC FieldValue
dc.titleA fluorescent sphingolipid binding domain peptide probe interacts with sphingolipids and cholesterol-dependent raft domains[s]
dc.contributor.authorHebbar, S.
dc.contributor.authorLee, E.
dc.contributor.authorManna, M.
dc.contributor.authorSteinert, S.
dc.contributor.authorKumar, G.S.
dc.contributor.authorWenk, M.
dc.contributor.authorWohland, T.
dc.contributor.authorKraut, R.
dc.date.accessioned2014-10-16T08:47:50Z
dc.date.available2014-10-16T08:47:50Z
dc.date.issued2008-05-01
dc.identifier.citationHebbar, S., Lee, E., Manna, M., Steinert, S., Kumar, G.S., Wenk, M., Wohland, T., Kraut, R. (2008-05-01). A fluorescent sphingolipid binding domain peptide probe interacts with sphingolipids and cholesterol-dependent raft domains[s]. Journal of Lipid Research 49 (5) : 1077-1089. ScholarBank@NUS Repository. https://doi.org/10.1194/jlr.M700543-JLR200
dc.identifier.issn00222275
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/95437
dc.description.abstractWe have designed a tagged probe [sphingolipid binding domain (SBD)] to facilitate the tracking of intracellular movements of sphingolipids in living neuronal cells. SBD is a small peptide consisting of the SBD of the amyloid precursor protein. It can be conjugated to a fluorophore of choice and exogenously applied to cells, thus allowing for in vivo imaging. Here, we present evidence to describe the characteristics of the SBD association with the plasma membrane. Our experiments demonstrate that SBD binds to isolated raft fractions from human neuroblastomas and insect neuronal cells. In protein-lipid overlay experiments, SBD interacts with a subset of glycosphingolipids and sphingomyelin, consistent with its raft association in neurons. We also provide evidence that SBD is taken up by neuronal cells in a cholesterol- and sphingolipid-dependent manner via detergent-resistant microdomains. Furthermore, using fluorescence correlation spectroscopy to assay the mobility of SBD in live cells, we show that SBD's behavior at the plasma membrane is similar to that of the previously described raft marker cholera toxin B, displaying both a fast and a slow component- Our data suggest that fluorescently tagged SBD can be used to investigate the dynamic nature of glycosphingolipid-rich detergent-resistant microdomains that are cholesterol-dependent Copyright © 2008 by the American Society for Biochemistry and Molecular Biology, Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1194/jlr.M700543-JLR200
dc.sourceScopus
dc.subjectAmyloid β peptide, fluorescence correlation spectroscopy
dc.subjectDetergent-resistant microdomains
dc.subjectFluorescent probe
dc.subjectLipid rafts
dc.typeConference Paper
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1194/jlr.M700543-JLR200
dc.description.sourcetitleJournal of Lipid Research
dc.description.volume49
dc.description.issue5
dc.description.page1077-1089
dc.description.codenJLPRA
dc.identifier.isiut000255753700020
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

40
checked on Oct 22, 2020

WEB OF SCIENCETM
Citations

40
checked on Oct 13, 2020

Page view(s)

66
checked on Oct 11, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.