A flow cytometry assay to quantify intercellular exchange of membrane components

Poulcharidis, Dimitrios; Belfor, Kimberley; Kros, Alexander; Kasteren, Sander I. van

doi:10.1039/c7sc00260b

Cited by 6 publications

(1 citation statement)

References 60 publications

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“…These data not only highlight the involvement of PM integrity in HSR but also suggest that altered dynamics of specific cholesterol pools could represent a mechanism to fine tune HSP expression. Considering that cholesterol exchange between cells through direct cell-cell contacts has recently been shown [49], membrane-compound exchange through cell-to-cell communication could in fact represent an hitherto less recognized mechanism through which stress adaptation could spread throughout a larger cell population.…”

Section: Discussionmentioning

confidence: 99%

Modulation of Plasma Membrane Composition and Microdomain Organization Impairs Heat Shock Protein Expression in B16-F10 Mouse Melanoma Cells

Crul

Csoboz

Gombos

et al. 2020

Cells

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The heat shock response (HSR) regulates induction of stress/heat shock proteins (HSPs) to preserve proteostasis during cellular stress. Earlier, our group established that the plasma membrane (PM) acts as a sensor and regulator of HSR through changes in its microdomain organization. PM microdomains such as lipid rafts, dynamic nanoscale assemblies enriched in cholesterol and sphingomyelin, and caveolae, cholesterol-rich PM invaginations, constitute clustering platforms for proteins functional in signaling cascades. Here, we aimed to compare the effect of cyclodextrin (MβCD)- and nystatin-induced cholesterol modulations on stress-activated expression of the representative HSPs, HSP70, and HSP25 in mouse B16-F10 melanoma cells. Depletion of cholesterol levels with MβCD impaired the heat-inducibility of both HSP70 and HSP25. Sequestration of cholesterol with nystatin impaired the heat-inducibility of HSP25 but not of HSP70. Imaging fluorescent correlation spectroscopy marked a modulated lateral diffusion constant of fluorescently labelled cholesterol in PM during cholesterol deprived conditions. Lipidomics analysis upon MβCD treatment revealed, next to cholesterol reductions, decreased lysophosphatidylcholine and phosphatidic acid levels. These data not only highlight the involvement of PM integrity in HSR but also suggest that altered dynamics of specific cholesterol pools could represent a mechanism to fine tune HSP expression.

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Section: Discussionmentioning

confidence: 99%