Differences in surface chemistry of iron oxide nanoparticles result in different routes of internalization

• Barbora Svitkova,
• Vlasta Zavisova,
• Veronika Nemethova,
• Martina Koneracka,
• Miroslava Kretova,
• Filip Razga,
• Monika Ursinyova and
• Alena Gabelova

Beilstein J. Nanotechnol. 2021, 12, 270–281, doi:10.3762/bjnano.12.22

• cellular uptake of nanoparticles. Therefore, initial experiments were focused on the expression of clathrin heavy chain (CLHC), dynamin (Dyn), caveolin-1 (Cav1), and its phosphorylated form (pCav1) in A549 cells. The expression of CLHC and Cav1 was determined at the protein (Supporting Information File 1

• internalization of BSA-SO-MNPs via CME was also observed in murine primary podocytes and mesangial cells (unpublished results). In endothelial cells, albumin has been shown to bind to albondin, a 60 kDa glycoprotein (gp60) receptor localized in caveolae. The interaction between gp60 and caveolin-1, which is

• proteins were boiled in Laemmli buffer and separated on a 10% polyacrylamide SDS-PAGE gel. After transfer of proteins onto nitrocellulose membranes the following primary antibodies were used: anti-Clathrin Heavy Chain (P1663) (#2410), anti-Caveolin-1 (#3238), anti-Phospho-Caveolin-1 (Tyr14) (#3251), anti

Key for crossing the BBB with nanoparticles: the rational design

• Sonia M. Lombardo,
• Marc Schneider,
• Akif E. Türeli and
• Nazende Günday Türeli

Beilstein J. Nanotechnol. 2020, 11, 866–883, doi:10.3762/bjnano.11.72

• functionalized with glycopeptide g7 or with a mutated form of diphtheria toxin (CRM197) have been shown to significantly increase the analgesic effect of loperamide in mice [94]. Furthermore, it was shown that CRM197 allowed the carrier system to cross the BBB by RMT as well as by up-regulation of caveolin-1

Interactions at the cell membrane and pathways of internalization of nano-sized materials for nanomedicine

• Valentina Francia,
• Daphne Montizaan and
• Anna Salvati

Beilstein J. Nanotechnol. 2020, 11, 338–353, doi:10.3762/bjnano.11.25

• ]. 4.2 Cell models The cell type investigated and its tissue organization are other important factors that can affect the uptake mechanisms of nanoparticles. For example, not all pathways are active in all cell types: HepG2 cells have no endogenous caveolin-1, and therefore they are unable to internalize

• molecules by microscopy. However, also this might lead to additional artefacts. For example, it has been shown that overexpression of GFP-tagged caveolin 1 (CAV1-GFP), the main constituent of caveolae-mediated endocytosis, leads to the creation of artefacts, such as the observation of a specialized

Internalization mechanisms of cell-penetrating peptides

• Ivana Ruseska and
• Andreas Zimmer

Beilstein J. Nanotechnol. 2020, 11, 101–123, doi:10.3762/bjnano.11.10

• escape the endosomolytic intracellular path. Caveolae on the plasma membrane: The shape and structural organization of caveolae are conferred by members of the caveolin gene family, caveolin

Evaluation of quantum dot conjugated antibodies for immunofluorescent labelling of cellular targets

• Jennifer E. Francis,
• David Mason and
• Raphaël Lévy

Beilstein J. Nanotechnol. 2017, 8, 1238–1249, doi:10.3762/bjnano.8.125

• fibrillary acidic proteins (GFAPs) [12], mortalin [23], erythrocytes [24], GRP78 protein [25], caveolin-1 [26], golgi [20], and nuclear HER2 targets [6]. The majority of this labelling, however, was done with in-house synthesised Qdots rather than commercially available Qdots [27]. The use of commercially

Comparative evaluation of the impact on endothelial cells induced by different nanoparticle structures and functionalization

• Lisa Landgraf,
• Ines Müller,
• Peter Ernst,
• Miriam Schäfer,
• Christina Rosman,
• Isabel Schick,
• Oskar Köhler,
• Hartmut Oehring,
• Vladimir V. Breus,
• Thomas Basché,
• Carsten Sönnichsen,
• Wolfgang Tremel and
• Ingrid Hilger

Beilstein J. Nanotechnol. 2015, 6, 300–312, doi:10.3762/bjnano.6.28

• to be a cell-type-specific process [61][62][63]. In this context, the mouse macrophages cell line J774A.1 used macropinocytosis and clathrin-mediated endocytosis for the uptake of 40 nm sized polystyrene nanoparticles, depending on the lack of caveolin-1 expression in this cell line. In contrast, the

Caveolin-1 and CDC42 mediated endocytosis of silica-coated iron oxide nanoparticles in HeLa cells

• Nils Bohmer and
• Andreas Jordan

Beilstein J. Nanotechnol. 2015, 6, 167–176, doi:10.3762/bjnano.6.16

• line. Cells were transfected with specific siRNAs against Caveolin-1, Dynamin 2, Flotillin-1, Clathrin, PIP5Kα and CDC42. Knockdown of Caveolin-1 reduces endocytosis of superparamagnetic iron oxide nanoparticles (SPIONs) and silica-coated iron oxide nanoparticles (SCIONs) between 23 and 41%, depending

• in HeLa cells of iron oxide nanoparticles, used in this study, is mainly mediated by Caveolin-1 and CDC42. It is shown here for the first time, which proteins of the endocytotic pathway mediate the endocytosis of silica-coated iron oxide nanoparticles in HeLa cells in vitro. In future studies more

• experiments should be carried out with different cell lines and other well-defined nanoparticle species to elucidate possible general principles. Keywords: Caveolin-1; CDC42; endocytosis inhibition; iron oxide nanoparticles; nanoparticle uptake; Introduction Nanotechnology is expected to be a very powerful

Different endocytotic uptake mechanisms for nanoparticles in epithelial cells and macrophages

• Dagmar A. Kuhn,
• Dimitri Vanhecke,
• Benjamin Michen,
• Fabian Blank,
• Peter Gehr,
• Alke Petri-Fink and
• Barbara Rothen-Rutishauser

Beilstein J. Nanotechnol. 2014, 5, 1625–1636, doi:10.3762/bjnano.5.174

• caveolin-1. A549 cells expressed clathrin heavy chain and caveolin-1, but no flotillin-1 uptake-related proteins. Our data revealed an impeded uptake of 40 nm polystyrene nanoparticles by J774A.1 macrophages when actin polymerization and clathrin-coated pit formation was blocked. From this result, it is

• high amounts of cholesterol [27]. The protein which gives shape and structure in caveolin-mediated endocytosis is caveolin-1, a dimeric protein which binds cholesterol onto the cellular surface for uptake and intracellular trafficking (lipid homeostasis) [28]. Also located at the site of lipid rafts is

• presence of the endocytotic proteins which are involved in endocytosis in both cell types (Figure 2). To achieve this, laser scanning microscopy (LSM) was applied as the primary tool for this investigations. Flotillin-1 and clathrin heavy chain could be visualized in J774A.1 cells, but caveolin-1 was not