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1

Recent controversy surrounding lipid rafts

100%
Skwarek M.
Archivum Immunologiae et Therapiae Experimentalis
|
2004
|
tom 52
|
nr 6
2

Role of lipid rafts in T cells

100%
Thomas S., Rajeev Kumar R. S., Brumeanu T. D.
Archivum Immunologiae et Therapiae Experimentalis
|
2004
|
tom 52
|
nr 4
3
Content available remote

Molecular targets of [-]-epigallocatechin-3-gallate [EGCG]: specificity and interaction with membrane lipid rafts

84%
Patra S. K., Rizzi F., Silva A., Rugina D. O., Bettuzzi S.
Journal of Physiology and Pharmacology. Supplement
|
2008
|
tom 59
|
nr 9
217-235
4

Giant unilamellar vesicles - a perfect tool to visualize phase separation and lipid rafts in model systems

84%
Wesolowska O., Michalak K., Maniewska J., Hendrich A. B.
Acta Biochimica Polonica
|
2009
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tom 56
|
nr 1
33-39
 Model systems such as black lipid membranes or conventional uni- or multilamellar liposomes are commonly used to study membrane properties and structure. However, the construction and dimensions of these models excluded their direct optical microscopic observation. Since the introduction of the simple method of liposome electroformation in alternating electric field giant unilamellar vesicles (GUVs) have become an important model imitating biological membranes. Due to the average diameter of GUVs reaching up to 100 µm, they can be easily observed under a fluorescent or confocal microscope provided that the appropriate fluorescent probe was incorporated into the lipid phase during vesicle formation. GUVs can be formed from different lipid mixtures and they are stable in a wide range of physical conditions such as pH, pressure or temperature. This mini-review presents information about the methods of GUV production and their usage. Particularly, the use of GUVs in studying lipid phase separation and the appearance and behavior of lipid domains (rafts) in membranes is discussed but also other examples of GUVs use in membrane research are given. The experience of the authors in setting up the GUV-forming equipment and production of GUVs is also presented.
5

Accumulation of aquaporin-1 during hemolysin-induced necrotic cell death

84%
Schweitzer K., Li E., Sidhaye V., Leitch V., Kuznetsov S., King L. S.
Cellular and Molecular Biology Letters
|
2008
|
tom 13
|
nr 2
195-211
Altered tissue water homeostasis may contribute to edema formation during various stresses including bacterial infection. We observed induction of aquaporin-1 (AQP1) during Staphylococcus aureus infection of cultured cells indicating a potential mechanism underlying altered water homeostasis during infection. To investigate mechanisms of AQP1 induction, we examined the effects of the S. aureus alpha-hemolysin on AQP1 abundance in Balb/c fibroblasts. Fibroblasts incubated with 30 microg/ml hemolysin exhibited a 5-10 fold increase in AQP1 protein within 4-6 hours of exposure. The use of multiple signaling cascade inhibitors failed to affect hemolysin-mediated accumulation of AQP1. However, immunoprecipitation revealed an initial accumulation of ubiquitinated AQP1 followed by a decrease to baseline levels after 4 hours. Immunofluorescence indicated that following hemolysin exposure, AQP1 was no longer on the plasma membrane, but was found in a population of submembrane vacuoles. AQP1 redistribution was further indicated by surface biotinylation experiments suggesting diminished AQP1 abundance on the plasma membrane as well as redistribution out of lipid raft fractions. Live cell confocal microscopy revealed that the pattern of cell volume change observed following hemolysin exposure was altered in cells in which AQP1 was silenced. We conclude that alpha-toxin alters proteasomal processing and leads to intracellular accumulation of AQP1, which may likely contribute to disrupted cell volume homeostasis in infection.
6

Mouse Ly-6 proteins and their extended family: markers of cell differentiation and regulators of cell signalling

84%
Bamezai A.
Archivum Immunologiae et Therapiae Experimentalis
|
2004
|
tom 52
|
nr 4
7

Rewinding the DISC

84%
Chaigne-Delalande B., Moreau J-F., Legembre P.
Archivum Immunologiae et Therapiae Experimentalis
|
2008
|
tom 56
|
nr 1
8
Content available remote

Lipid rafts mediate epigallocatechin-3-gallate- and green tea extract-dependent viability of human colon adenocarcinoma COLO 205 cells; clusterin affects lipid rafts-associated signaling pathways

67%
Pajak B., Kania E., Gajkowska B., Orzechowski A.
Journal of Physiology and Pharmacology
|
2011
|
tom 62
|
nr 4
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