Temperature‐dependent localization of GPI‐anchored intestinal alkaline phosphatase in model rafts

Giocondi, Marie-Cécile; Besson, Françoise; Dosset, Patrice; Milhiet, Pierre-Emmanuel; Grimellec, Christian Le

doi:10.1002/jmr.835

Cited by 17 publications

(13 citation statements)

References 43 publications

(55 reference statements)

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“…This finding lent strong support to our earlier suggestions that PM is involved in the sensing of temperature elevations through changes in the physical state of the membrane [36,42,43]. Interestingly, in artificial bilayer systems, atomic force microscopy studies have shown that GPI-anchored proteins can be released from the liquid ordered phase by an increase in temperature [44]. Thus, a similar mechanism may apparently account for the observed dissociation of mGFP-GPI homo-associates in the CHO cell membrane.…”

Section: Membranes Are Key Determinants Of Cellular Stress Adaptationsupporting

confidence: 87%

Membrane fluidity matters: Hyperthermia from the aspects of lipids and membranes

Csoboz

Balogh

Kúsz

et al. 2013

International Journal of Hyperthermia

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Hyperthermia is a promising treatment modality for cancer in combination both with radio-and chemotherapy. In spite of its great therapeutic potential, the underlying molecular mechanisms still remain to be clarified. Due to lipid imbalances and 'membrane defects' most of the tumour cells possess elevated membrane fluidity. However, further increasing membrane fluidity to sensitise to chemo-or radiotherapy could have some other effects. In fact, hyperfluidisation of cell membrane induced by membrane fluidiser initiates a stress response as the heat shock protein response, which may modulate positively or negatively apoptotic cell death. Overviewing some recent findings based on a technology allowing direct imaging of lipid rafts in live cells and lipidomics, novel aspects of the intimate relationship between the 'membrane stress' of tumour cells and the cellular heat shock response will be highlighted. Our findings lend support to both the importance of membrane remodelling and the release of lipid signals initiating stress protein response, which can operate in tandem to control the extent of the ultimate cellular thermosensitivity. Overall, we suggest that the fluidity variable of membranes should be used as an independent factor for predicting the efficacy of combinational cancer therapies.

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Section: Membranes Are Key Determinants Of Cellular Stress Adaptationsupporting

confidence: 87%

Membrane fluidity matters: Hyperthermia from the aspects of lipids and membranes

Csoboz

Balogh

Kúsz

et al. 2013

International Journal of Hyperthermia

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“…It is thus attractive to speculate that the plasma membrane may be involved in sensing small temperature elevations. Interestingly, in artificial bilayer systems, atomic force microscopy studies have shown that GPI-anchored proteins can be released from the liquid-ordered phase by an increase in temperature (44); a similar mechanism may account for the observed dissociation of mGFP-GPI homo-associates in the CHO cell membrane.…”

Section: Resultsmentioning

confidence: 99%

Imaging of Mobile Long-lived Nanoplatforms in the Live Cell Plasma Membrane

Brameshuber

Weghuber

Ruprecht

et al. 2010

Journal of Biological Chemistry

104

120

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The plasma membrane has been hypothesized to contain nanoscopic lipid platforms, which are discussed in the context of “lipid rafts” or “membrane rafts.” Based on biochemical and cell biological studies, rafts are believed to play a crucial role in many signaling processes. However, there is currently not much information on their size, shape, stability, surface density, composition, and heterogeneity. We present here a method that allows for the first time the direct imaging of nanoscopic long-lived platforms with raft-like properties diffusing in the live cell plasma membrane. Our method senses these platforms by their property to assemble a characteristic set of fluorescent marker proteins or lipids on a time scale of seconds. A special photobleaching protocol was used to reduce the surface density of labeled mobile platforms down to the level of well isolated diffraction-limited spots without altering the single spot brightness. The statistical distribution of probe molecules per platform was determined by single molecule brightness analysis. For demonstration, we used the consensus raft marker glycosylphosphatidylinositol-anchored monomeric GFP and the fluorescent lipid analog BODIPY-GM1, which preferentially partitions into liquid-ordered phases. For both markers, we found cholesterol-dependent homo-association in the plasma membrane of living CHO and Jurkat T cells in the resting state, thereby demonstrating the existence of small, mobile, long-lived platforms containing these probes. We further applied the technology to address structural changes in the plasma membrane during fever-type heat shock: at elevated temperatures, the glycosylphosphatidylinositol-anchored monomeric GFP homo-association disappeared, accompanied by an increase in the expression of the small heat shock protein Hsp27.

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“…Considering the insertion and the redistribution of the lipids it is probable that GPI-anchored proteins, once in the lipid bilayer, recruit the most suitable lipid environment most likely by exploiting the hydrophobic matching interaction. The AFM can also be exploited to observe the redistribution of GPI-anchored proteins after a temperature variation (Giocondi et al, 2007b). The obtained information can be fruitfully compared with results obtained from DRM extraction at low temperature.…”

Section: Chapter 2: Lipid/protein Interaction Studied By Afmmentioning

confidence: 99%

Unraveling lipid/protein interaction in model lipid bilayers by Atomic Force Microscopy

Alessandrini

Facci

2011

J of Molecular Recognition

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The current view of the biological membrane is that in which lipids and proteins mutually interact to accomplish membrane functions. The lateral heterogeneity of the lipid bilayer can induce partitioning of membrane-associated proteins, favoring protein-protein interaction and influence signaling and trafficking. The Atomic Force Microscope allows to study the localization of membrane-associated proteins with respect to the lipid organization at the single molecule level and without the need for fluorescence staining. These features make AFM a technique of choice to study lipid/protein interactions in model systems or native membranes. Here we will review the technical aspects inherent to and the main results obtained by AFM in the study of protein partitioning in lipid domains concentrating in particular on GPI-anchored proteins, lipidated proteins, and transmembrane proteins. Whenever possible, we will also discuss the functional consequences of what has been imaged by Atomic Force Microscopy.

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Temperature‐dependent localization of GPI‐anchored intestinal alkaline phosphatase in model rafts

Cited by 17 publications

References 43 publications

Membrane fluidity matters: Hyperthermia from the aspects of lipids and membranes

Membrane fluidity matters: Hyperthermia from the aspects of lipids and membranes

Imaging of Mobile Long-lived Nanoplatforms in the Live Cell Plasma Membrane

Unraveling lipid/protein interaction in model lipid bilayers by Atomic Force Microscopy

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