Use of Cationized Ferritin Nanoparticles to Measure Renal Glomerular Microstructure with MRI

2015 ◽  
pp. 67-79 ◽  
Author(s):  
Kevin M. Bennett ◽  
Scott C. Beeman ◽  
Edwin J. Baldelomar ◽  
Min Zhang ◽  
Teresa Wu ◽  
...  
Keyword(s):  
Cationized Ferritin

The use of cationized ferritin as an ultrastructural stain for the visualization of bacterial surface structures by SEM

1987 ◽  
Vol 23 (2) ◽  
pp. 252
Author(s):  
Jenny Naimark ◽  
Eli Morgenstern ◽  
Edward A. Bayer ◽  
Raphael Lamed
Keyword(s):  
Surface Structures ◽  
Cationized Ferritin ◽  
Bacterial Surface

Chemical determination of cationized ferritin bound to synaptosomes

1981 ◽  
Vol 133 (2) ◽  
pp. 480-485 ◽  
Author(s):  
Sen Lin-Liu ◽  
W. Bondareff
Keyword(s):  
Cationized Ferritin ◽  
Chemical Determination

Dependence of the superficial layers of Spirillum putridiconchylium on Ca2+ or Sr2+

1976 ◽  
Vol 22 (9) ◽  
pp. 1233-1244 ◽  
Author(s):  
T. J. Beveridge ◽  
R. G. E. Murray
Keyword(s):  
Cell Surface ◽  
Outer Membrane ◽  
Growth Medium ◽  
Chelating Agents ◽  
Membrane Surface ◽  
Superficial Layer ◽  
Cationized Ferritin ◽  
Membrane Component ◽  
Casamino Acids ◽  
Amorphous Precipitate

Chelating agents disrupted the superficial layers on Spirillum putridiconchylium and adsorption of cationized ferritin indicated that both upper and lower surfaces of superficial layer fragments, as well as the outer membrane surface, possessed areas which were negatively charged. Growth of the bacterium in 1% casamino acids (vitamin free) resulted in cells which were devoid of the superficial layers, and negative staining of these cells revealed an amorphous precipitate together with a vesicular outer membrane component extruding from their surfaces into the medium. Addition of either 1 mM Ca2+ or 1 mM Sr2+ to the growth medium produced the typical regularly structured cell surface, whereas addition of equal concentrations of Li+, Na+, K+, Mg2+, Ba2+, Mn2+, Fe3+, or three polyamines produced the structureless surface.

Endocytosis of cationized ferritin to vesicles in the Golgi region of the glomus cells dissociated from the adult rat carotid body

1983 ◽  
Vol 207 (2) ◽  
pp. 357-363 ◽  
Author(s):  
Mats Grönblad ◽  
Karl Erik Åkerman ◽  
Olavi Eränkö
Keyword(s):  
Carotid Body ◽  
Cationized Ferritin ◽  
Glomus Cells ◽  
Adult Rat ◽  
Golgi Region

Use of cationized ferritin as a label of negative charges on cell surfaces

1972 ◽  
Vol 38 (5-6) ◽  
pp. 500-510 ◽  
Author(s):  
D. Danon ◽  
L. Goldstein ◽  
Y. Marikovsky ◽  
E. Skutelsky
Keyword(s):  
Cationized Ferritin ◽  
Cell Surfaces

Trypanosoma cruzi: cell surface dynamics in trypomastigotes of different strains

Parasitology ◽  
2019 ◽  
Vol 147 (3) ◽  
pp. 310-321
Author(s):  
Roberta Ferreira Cura das Neves ◽  
Camila Marques Adade ◽  
Anne Cristine Silva Fernandes ◽  
Angela Hampshire Lopes ◽  
Thaïs Souto-Padrón
Keyword(s):  
Cell Surface ◽  
Trypanosoma Cruzi ◽  
Binding Sites ◽  
Host Cells ◽  
Cationized Ferritin ◽  
Surface Dynamics ◽  
Con A ◽  
Low Intensity ◽  
Intense Labelling ◽  
Different Strains

AbstractCapping and shedding of ectodomains in Trypanosoma cruzi may be triggered by different ligands. Here, we analysed the mobility and shedding of cell surface components of living trypomastigotes of the Y strain and the CL Brener clone in the presence of poly-L-lysine, cationized ferritin (CF) and Concanavalin A (Con A). Poly-L-lysine and CF caused intense shedding in Y strain parasites. Shedding was less intense in CL Brener trypomastigotes, and approximately 10% of these parasites did not show any decrease in poly L-lysine or CF labelling. Binding of Con A induced low-intensity shedding in Y strain and redistribution of Con A-binding sites in CL Brener parasites. Trypomastigotes of the Y strain showed intense labelling with anti-〈-galactosyl antibodies, resulting in the lysis of approximately 30% of their population, in contrast with what was observed in CL Brener parasites. Incubation with Con A and CF protected trypomastigotes of the Y strain from lysis by anti-αGal. The last treatment did not interfere with the survival of the CL Brener parasites. This study corroborates with the idea that a ligand can differentially modulate the cell surface of T. cruzi, depending on the strain used, resulting in variable immune system responses and recognition by host cells.

scholarly journals Vesicular transport of cationized ferritin by the epithelium of the rat choroid plexus.

1981 ◽  
Vol 89 (1) ◽  
pp. 131-139 ◽  
Author(s):  
B Van Deurs ◽  
F Von Bülow ◽  
M Møller
Keyword(s):  
Choroid Plexus ◽  
Vesicular Transport ◽  
Apical Cell ◽  
Multivesicular Bodies ◽  
Apical Surface ◽  
Cationized Ferritin ◽  
Epithelial Surface ◽  
Apical Cell Membrane ◽  
Choroidal Epithelium ◽  
Limited Degree

We have studied the transport of ferritin that was internalized by coated micropinocytic vesicles at the apical surface of the choroid plexus epithelium in situ. After ventriculocisternal perfusion of native ferritin (NF) or cationized ferritin (CF), three routes followed by the tracers are revealed: (a) to lysosomes, (b) to cisternal compartments, and (c) to the basolateral cell surface. (a) NF is micropinocytosed to a very limited degree and appears in a few lysosomal elements whereas CF is taken up in large amounts and can be followed, via endocytic vacuoles and light multivesicular bodies, to dark multivesicular bodies and dense bodies. (b) Occasionally, CF particles are found in cisterns that may represent GERL or trans-Golgi elements, whereas stacked Golgi cisterns never contain CF. (c) Transepithelial vesicular transport of CF is distinctly revealed. The intercellular spaces of the epithelium, below the apical tight junctions, contain numerous clusters of CF particles, often associated with surface-connected, coated vesicles. Vesicles in the process of exocytosis of CF are also present at the basal epithelial surface, whereas connective tissue elements below the epithelium are unlabeled. Our conclusion is that fluid and solutes removed from the cerebrospinal fluid by endocytosis either become sequestered in the lysosomal apparatus of the choroidal epithelium or are transported to the basolateral surface. However, our results do not indicate any significant recycling via Golgi complexes of internalized apical cell membrane.

Sign in / Sign up

Export Citation Format

Share Document