ArticleBiophysical journal2000
Different sphingolipids show differential partitioning into sphingolipid/cholesterol-rich domains in lipid bilayers.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
35 citing papers in PubMed, 136 citations in OpenAlex.
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- Nutrient Regulation of Pancreatic Islet β-Cell Secretory Capacity and Insulin Production.Biomolecules · 2022Review
- Inside the Insulin Secretory Granule.Metabolites · 2021Review
- HDL-Mediated Lipid Influx to Endothelial Cells Contributes to Regulating Intercellular Adhesion Molecule (ICAM)-1 Expression and eNOS Phosphorylation.International journal of molecular sciences · 2018Article
- Alterations in endo-lysosomal function induce similar hepatic lipid profiles in rodent models of drug-induced phospholipidosis and Sandhoff disease.Journal of lipid research · 2017Article
- Label-free in situ imaging of oil body dynamics and chemistry in germination.Journal of the Royal Society, Interface · 2016Article
- Recent progress on lipid lateral heterogeneity in plasma membranes: From rafts to submicrometric domains.Progress in lipid research · 2016Review
- Lipid dynamics in boar sperm studied by advanced fluorescence imaging techniques.European biophysics journal : EBJ · 2016Article
- Microscopy tools for the investigation of intracellular lipid storage and dynamics.Molecular metabolism · 2016Review
- Biophysics of cell membrane lipids in cancer drug resistance: Implications for drug transport and drug delivery with nanoparticles.Advanced drug delivery reviews · 2013Review
- Sphingomyelin organization is required for vesicle biogenesis at the Golgi complex.The EMBO journal · 2012Article
- Tip-enhanced Raman detection of antibody conjugated nanoparticles on cellular membranes.Analytical chemistry · 2012Article
- STED nanoscopy reveals molecular details of cholesterol- and cytoskeleton-modulated lipid interactions in living cells.Biophysical journal · 2011Article
- FCS diffusion laws in two-phase lipid membranes: determination of domain mean size by experiments and Monte Carlo simulations.Biophysical journal · 2011Article
- Fatty acid-dependent globotriaosyl ceramide receptor function in detergent resistant model membranes.Journal of lipid research · 2009Article
- A fluorescent glycolipid-binding peptide probe traces cholesterol dependent microdomain-derived trafficking pathways.PloS one · 2008Article
- Ceramide signaling in cancer and stem cells.Future lipidology · 2008Article
- Lipid microdomain formation: characterization by infrared spectroscopy and ultrasonic velocimetry.Biophysical journal · 2008Article
- Membrane lipids: where they are and how they behave.Nature reviews. Molecular cell biology · 2008Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two fluorescence-based approaches have been applied to examine the differential partitioning of fluorescent phospho- and sphingolipid molecules into sphingolipid-enriched domains modeling membrane "lipid rafts." Fluorescence-quenching measurements reveal that N-(diphenylhexatrienyl)propionyl- (DPH3:0-)-labeled gluco- and galactocerebroside partition into sphingolipid-enriched domains in sphingolipid/phosphatidylcholine/cholesterol bilayers with substantially higher affinity than do analogous sphingomyelin, ceramide, or phosphatidylcholine molecules. By contrast, the affinity of sphingomyelin and ceramide for such domains is only marginally greater than that of a phosphatidylcholine with similar hydrocarbon chains. By using direct measurements of molecular partitioning between vesicles of different compositions, we show that the relative affinities of different C(6)-NBD- and C(5)-Bodipy-labeled sphingolipids for sphingolipid-enriched domains are quantitatively, and in most circumstances even qualitatively, quite different from those found for species whose N-acyl chains more closely resemble the long saturated chains of cellular sphingolipids. These findings lend support in principle to previous suggestions that differential partitioning of different sphingolipids into "raft" domains could contribute to the differential trafficking of these species in eukaryotic cells. However, our findings also indicate that short-chain sphingolipid probes previously used to examine this phenomenon are in general ill-suited for such applications.
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Registered trials
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