Imaging plasma membrane microviscosity in cancer cells during chemotherapy

2020 ◽  
Author(s):  
Liubov E. Shimolina ◽  
Marina V. Shirmanova ◽  
Marina Kuimova ◽  
Maria M. Lukina ◽  
Nadezhda I. Ignatova ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cancer Cells ◽  
Membrane Microviscosity

scholarly journals Phenothiazines alter plasma membrane properties and sensitize cancer cells to injury by inhibiting annexin-mediated repair

2021 ◽  
pp. 101012
Author(s):  
Anne Sofie Busk Heitmann ◽  
Ali Asghar Hakami Zanjani ◽  
Martin Berg Klenow ◽  
Anna Mularski ◽  
Stine Lauritzen Sønder ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cancer Cells ◽  
Membrane Properties

scholarly journals Glycosylation Modulates Plasma Membrane Trafficking of CD24 in Breast Cancer Cells

2021 ◽  
Vol 22 (15) ◽  
pp. 8165
Author(s):  
Amanda Chantziou ◽  
Kostas Theodorakis ◽  
Hara Polioudaki ◽  
Eelco de Bree ◽  
Marilena Kampa ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Plasma Membrane ◽  
Subcellular Localization ◽  
Cancer Cells ◽  
Membrane Trafficking ◽  
Breast Cancer Cells ◽  
Endocytic Pathway ◽  
Cell Periphery ◽  
Wild Type ◽  
Mcf 7

In breast cancer, expression of Cluster of Differentiation 24 (CD24), a small GPI-anchored glycoprotein at the cell periphery, is associated with metastasis and immune escape, while its absence is associated with tumor-initiating capacity. Since the mechanism of CD24 sorting is unknown, we investigated the role of glycosylation in the subcellular localization of CD24. Expression and localization of wild type N36- and/or N52-mutated CD24 were analyzed using immunofluorescence in luminal (MCF-7) and basal B (MDA-MB-231 and Hs578T) breast cancer cells lines, as well as HEK293T cells. Endogenous and exogenously expressed wild type and mutated CD24 were found localized at the plasma membrane and the cytoplasm, but not the nucleoplasm. The cell lines showed different kinetics for the sorting of CD24 through the secretory/endocytic pathway. N-glycosylation, especially at N52, and its processing in the Golgi were critical for the sorting and expression of CD24 at the plasma membrane of HEK293T and basal B type cells, but not of MCF-7 cells. In conclusion, our study highlights the contribution of N-glycosylation for the subcellular localization of CD24. Aberrant N-glycosylation at N52 of CD24 could account for the lack of CD24 expression at the cell surface of basal B breast cancer cells.

scholarly journals RAS Function in cancer cells: translating membrane biology and biochemistry into new therapeutics

2020 ◽  
Vol 477 (15) ◽  
pp. 2893-2919
Author(s):  
Walaa E. Kattan ◽  
John F. Hancock
Keyword(s):  
Plasma Membrane ◽  
Cell Growth ◽  
Cancer Cells ◽  
Special Focus ◽  
Ras Proteins ◽  
Membrane Interactions ◽  
Multiple Methods ◽  
Membrane Biology ◽  
The Past ◽  
Cell Growth And Proliferation

The three human RAS proteins are mutated and constitutively activated in ∼20% of cancers leading to cell growth and proliferation. For the past three decades, many attempts have been made to inhibit these proteins with little success. Recently; however, multiple methods have emerged to inhibit KRAS, the most prevalently mutated isoform. These methods and the underlying biology will be discussed in this review with a special focus on KRAS-plasma membrane interactions.

966 Activation of a plasma membrane-cationic channel and apoptosis in prostate cancer cells overexpressing Bax

2003 ◽  
Vol 1 (5) ◽  
pp. S290
Author(s):  
A.A. Gutiérrez ◽  
D. González-Espinosa ◽  
J. Hernández ◽  
A. Guerrero-Hernández ◽  
F. Martinez ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Plasma Membrane ◽  
Cancer Cells ◽  
Prostate Cancer Cells ◽  
Cationic Channel

scholarly journals Decrease in Multidrug Resistance-associated Protein 2 Activities by Knockdown of Phosphatidylinositol 4-phosphate 5-kinase in Hepatocytes and Cancer Cells

2019 ◽  
Vol 22 ◽  
pp. 576-584 ◽  
Author(s):  
Atsushi Kawase ◽  
Yuta Inoue ◽  
Miho Hirosoko ◽  
Yuka Sugihara ◽  
Hiroaki Shimada ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Multidrug Resistance ◽  
Cancer Cells ◽  
Hepg2 Cells ◽  
Carcinoma Cells ◽  
Efflux Transporters ◽  
Membrane Localization ◽  
Intracellular Accumulation ◽  
Primary Hepatocytes ◽  
Phosphatidylinositol 4

Purpose: The plasma membrane localization and transport activity of multidrug resistance-associated protein 2 (MRP2/ABCC2) and P-glycoprotein (P-gp/ABCB1) efflux transporters are governed by transporter-associated proteins. Phosphatidylinositol 4,5-bisphosphate (PIP2) formed by phosphatidylinositol 4-phosphate 5-kinase type 1 (PIP5K1) activates the linker function of radixin for efflux transporters. Radixin is involved in the plasma membrane localization of efflux transporters. We examined whether PIP5K1 could be a target for the modulation of transporter activities in hepatocytes and cancer cells. Methods: The effects of PIP5K1 depletion by siRNA in mouse primary hepatocytes, PANC1 human pancreatic carcinoma cells, and HepG2 human hepatocellular carcinoma cells on the intracellular accumulation of MRP2 and P-gp substrates were examined. Results: PIP5K1A depletion resulted in increased intracellular accumulation of carboxydichlorofluorescein, a MRP2 fluorescent substrate, in mouse primary hepatocytes, PANC1 cells, and HepG2 cells. In PANC1 and HepG2 cells, the transport activities of MRP2 were significantly decreased by PIP5K1C depletion. However, the transport activities of P-gp were unchanged by PIP5K1 depletion. PIP2 levels were unchanged between control and PIP5K1A- or PIP5K1C-depleted HepG2 cells. MRP2 mRNA levels showed few changes in HepG2 cells following PIP5K1A or PIP5K1C depletion. The expression of phosphorylated radixin was decreased by PIP5K1A and PIP5K1C depletion, although total radixin levels were unchanged. Conclusions: These data suggest that PIP5K1A and PIP5K1C could be target proteins for modulating MRP2 function, partly because of the resulting changes of the linker function of radixin.

scholarly journals Interaction of the Anti-Proliferative GPER Inverse Agonist ERα17p with the Breast Cancer Cell Plasma Membrane: From Biophysics to Biology

Cells ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 447 ◽  
Author(s):  
Michaël Trichet ◽  
Rosamaria Lappano ◽  
Mathilde Belnou ◽  
Lilian Salazar Vazquez ◽  
Isabel Alves ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Plasma Membrane ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Breast Cancer Cells ◽  
Direct Interaction ◽  
Lipid Vesicles ◽  
Estrogen Receptor Α ◽  
Cd Spectroscopy

The peptide ERα17p, which corresponds to the 295-311 fragment of the hinge/AF2 domains of the human estrogen receptor α (ERα), exerts apoptosis in breast cancer cells through a mechanism involving the G protein-coupled estrogen-dependent receptor GPER. Besides this receptor-mediated mechanism, we have detected a direct interaction (Kd value in the micromolar range) of this peptide with lipid vesicles mimicking the plasma membrane of eukaryotes. The reversible and not reversible pools of interacting peptide may correspond to soluble and aggregated membrane-interacting peptide populations, respectively. By using circular dichroism (CD) spectroscopy, we have shown that the interaction of the peptide with this membrane model was associated with its folding into β sheet. A slight leakage of the 5(6)-fluorescein was also observed, indicating lipid bilayer permeability. When the peptide was incubated with living breast cancer cells at the active concentration of 10 μM, aggregates were detected at the plasma membrane under the form of spheres. This insoluble pool of peptide, which seems to result from a fibrillation process, is internalized in micrometric vacuoles under the form of fibrils, without evidence of cytotoxicity, at least at the microscopic level. This study provides new information on the interaction of ERα17p with breast cancer cell membranes as well as on its mechanism of action, with respect to direct membrane effects.

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