β-Lactonization of fluorinated porphyrin enhances LDL binding affinity, cellular uptake with selective intracellular localization

2014 ◽  
Vol 5 (2) ◽  
pp. 558-566 ◽  
Author(s):  
Juan Tang ◽  
Juan-Juan Chen ◽  
Jing Jing ◽  
Jia-Zhen Chen ◽  
Hongbin Lv ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Cellular Uptake ◽  
Intracellular Localization ◽  
Ldl Binding

scholarly journals Interplay between Cellular Uptake, Intracellular Localization and the Cell Death Mechanism in Triphenylamine-Mediated Photoinduced Cell Death

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Rahima Chennoufi ◽  
Ngoc-Duong Trinh ◽  
Françoise Simon ◽  
Guillaume Bordeau ◽  
Delphine Naud-Martin ◽  
...  
Keyword(s):  
Cell Death ◽  
Cellular Uptake ◽  
Intracellular Localization ◽  
Cell Death Mechanism

Efficient cleavage of RNA, enhanced cellular uptake, and controlled intracellular localization of conjugate DNAzymes

2005 ◽  
Vol 15 (1) ◽  
pp. 167-170 ◽  
Author(s):  
Takanori Kubo ◽  
Kengo Takamori ◽  
Ken-ichi Kanno ◽  
Bakalova Rumiana ◽  
Hideki Ohba ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Intracellular Localization

scholarly journals Characterization of Rab3A, Rab3B and Rab3C: different biochemical properties and intracellular localization in bovine chromaffin cells

1997 ◽  
Vol 324 (1) ◽  
pp. 85-90 ◽  
Author(s):  
Chong-Gee LIN ◽  
Yu-Chi LIN ◽  
Hwan-Wun LIU ◽  
Lung-Sen KAO
Keyword(s):  
Subcellular Localization ◽  
Binding Affinity ◽  
Chromaffin Cells ◽  
Intracellular Localization ◽  
Biochemical Properties ◽  
Amino Acid Residues ◽  
C Terminus ◽  
Bovine Chromaffin Cells ◽  
Adrenal Chromaffin

In this study we examined the biochemical properties and subcellular localization of Rab3A, Rab3B and Rab3C in bovine adrenal chromaffin cells. The Kd for guanosine 5′-[γ-thio]triphosphate (GTP[S]) of the three Rab3 proteins was 15, 2700 and 204 nM for Rab3A, Rab3B and Rab3C respectively. The intrinsic GTPase activity of the three Rab3 proteins seemed similar and was increased approx. 3-fold by bovine chromaffin cell lysate. Truncation of the C-terminal 31 amino acid residues decreased the binding affinity for GTP[S] of the three Rab3 proteins. When the C-terminus of Rab3C was replaced with that of Rab3A, the binding affinity of Rab3C for GTP[S] was decreased, but the replacement did not affect the affinity of Rab3B for GTP[S]. Immunostaining experiments showed that Rab3A, Rab3B and Rab3C are localized separately within chromaffin cells. Anti-Rab3A and anti-Rab3C antibodies stained vesicle-like structures, whereas anti-Rab3B antibody distinctly stained the plasma membrane. In summary, bovine chromaffin cells express the three Rab3 proteins but the subcellular localization and biochemical properties of the three Rab3 proteins are distinct.

scholarly journals Cellular Uptake Behaviors of Rigidity-Tunable Dendrimers

Pharmaceutics ◽  
2018 ◽  
Vol 10 (3) ◽  
pp. 99 ◽  
Author(s):  
Hui Liu ◽  
Jingjing Wang ◽  
Wenchao Li ◽  
Jie Hu ◽  
Min Wang ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Cellular Uptake ◽  
Biomedical Applications ◽  
Intracellular Localization ◽  
Hydrodynamic Size ◽  
Limited Information ◽  
Flow Cytometry Analysis ◽  
Core Flow ◽  
Microscopic Evaluation ◽  
Gold Nps

Understanding of the interaction between cells and nanoparticles (NPs) is critical. Despite numerous attempts to understand the effect of several parameters of NPs on their cellular uptake behaviors, such as size, shape, surface chemistry, etc., limited information is available regarding NP rigidity. Herein, we investigate the effect of rigidity on cellular uptake behaviors of NPs, using generation 5 poly(amidoamine) dendrimer as a model. By harnessing the abundant inner cavity, their rigidity could be effectively regulated by forming size-tunable gold NPs. The NPs thus formed were well characterized and displayed similar hydrodynamic size, surface potential, fluorescence intensity, and distinct rigidity (owing to differences in the size of the Au core). Flow cytometry analysis revealed a positive correlation between NP rigidity and cellular uptake of NPs. Confocal microscopic evaluation revealed that the entrapped gold NPs may affect the intracellular localization of the internalized dendrimers. The present findings can potentially guide the preparation of suitable NPs for biomedical applications.

Intracellular Behavior of Nanoparticles Based on their Physicochemical Properties

2015 ◽  
pp. 10-35 ◽  
Author(s):  
Charmainne Cruje ◽  
Darren Yohan ◽  
Celina Yang ◽  
Devika B. Chithrani
Keyword(s):  
Physicochemical Properties ◽  
Cellular Uptake ◽  
Treatment Options ◽  
Intracellular Localization ◽  
Disease Diagnosis ◽  
Current Treatment ◽  
Model System ◽  
Medical Applications ◽  
Gold Nps ◽  
Intracellular Pathway

This chapter addresses physicochemical properties that affect Nanoparticle (NP) intracellular behavior using Gold NPs (GNPs) as a model system. The main objective is to outline what is known about the effect of GNP size, shape, and surface properties on cellular uptake and intracellular pathway. The authors propose that the entry of GNPs into cells is related to its effectiveness in applications that favor intracellular localization of such GNPs. The authors also discuss how such properties are used to optimize GNP designs for medical applications. Finally, the authors discuss how GNPs may improve disease diagnosis and treatment. Furthermore, how they may be incorporated or used as alternatives to current treatment options is defined.

Modulation of the cellular uptake efficiency and the intracellular localization of conjugated Trojan peptides

2007 ◽  
Author(s):  
Fabienne Burlina ◽  
Baptiste Aussedat ◽  
Soline Aubry ◽  
Diane Delaroche ◽  
Edmond Dupont ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Intracellular Localization ◽  
Uptake Efficiency ◽  
Cellular Uptake Efficiency

scholarly journals Thiazolidinediones reduce the LDL binding affinity of non-human primate vascular cell proteoglycans

Diabetologia ◽  
2004 ◽  
Vol 47 (5) ◽  
pp. 837-843 ◽  
Author(s):  
L. R. Tannock ◽  
P. J. Little ◽  
C. Tsoi ◽  
P. H. R. Barrett ◽  
T. N. Wight ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Vascular Cell ◽  
Ldl Binding ◽  
Human Primate

scholarly journals Cellular uptake and intracellular localization of benzo(a)pyrene by digital fluorescence imaging microscopy.

1985 ◽  
Vol 100 (4) ◽  
pp. 1295-1308 ◽  
Author(s):  
A L Plant ◽  
D M Benson ◽  
L C Smith
Keyword(s):  
Fluorescence Imaging ◽  
Cellular Uptake ◽  
Intracellular Localization ◽  
Low Density Lipoproteins ◽  
High Density Lipoproteins ◽  
Low Density ◽  
Very Low Density Lipoproteins ◽  
Intracellular Location ◽  
Fluorescence Imaging Microscopy ◽  
Digital Fluorescence Imaging

Uptake of benzo(a)pyrene by living cultured cells has been visualized in real time using digital fluorescence-imaging microscopy. Benzo(a)pyrene was noncovalently associated with lipoproteins, as a physiologic mode of presentation of the carcinogen to cells. When incubated with either human fibroblasts or murine P388D1 macrophages, benzo(a)pyrene uptake occurred in the absence of endocytosis, with a halftime of approximately 2 min, irrespective of the identity of the delivery vehicles, which were high density lipoproteins, low density lipoproteins, very low density lipoproteins, and 1-palmitoyl-2-oleoylphosphatidylcholine single-walled vesicles. Thus, cellular uptake of benzo(a)pyrene from these hydrophobic donors occurs by spontaneous transfer through the aqueous phase. Moreover, the rate constant for uptake, the extent of uptake, and the intracellular localization of benzo(a)pyrene were identical for both living and fixed cells. Similar rate constants for benzo(a)pyrene efflux from cells to extracellular lipoproteins suggests the involvement of the plasma membrane in the rate-limiting step. The intracellular location of benzo(a)pyrene at equilibrium was coincident with a fluorescent cholesterol analog, N-(7-nitrobenz-2-oxa-1,3-diazole)-23,24-dinor-5-cholen-22-amine-3 beta-ol. Benzo(a)pyrene did not accumulate in acidic compartments, based on acridine orange fluorescence, or in mitochondria, based on rhodamine-123 fluorescence. When the intracellular lipid volume of isolated mouse peritoneal macrophages was increased by prior incubation of these cells with either acetylated low density lipoproteins or with very low density lipoproteins from a hypertriglyceridemic individual, cellular accumulation of benzo(a)pyrene increased proportionately with increased [1-14C]oleate incorporation into cellular triglycerides and cholesteryl esters. Thus, benzo(a)pyrene uptake by cells is a simple partitioning phenomenon, controlled by the relative lipid volumes of extracellular donor lipoproteins and of cells, and does not involve lipoprotein endocytosis as an obligatory step.

Cellular localization and photodynamic effect of chlorin e6-monoclonal antibody conjugate

2005 ◽  
Vol 09 (02) ◽  
pp. 138-141 ◽  
Author(s):  
Shun-ichiro Ogura ◽  
Toshiaki Kamachi ◽  
Ichiro Okura
Keyword(s):  
Monoclonal Antibody ◽  
Tumor Cells ◽  
Binding Affinity ◽  
Cellular Localization ◽  
Specific Binding ◽  
Intracellular Localization ◽  
Chlorin E6 ◽  
Binding Affinities ◽  
High Accumulation ◽  
Peptide Bonds

Chlorin e6(Ce6) was conjugated with anti-tumor monoclonal antibody ( IgG ) to increase its binding affinity for tumors. Ce 6 was activated by N -hydroxysulfosuccinimide and conjugated with IgG via peptide bonds, and Ce 6 molecules were conjugated with IgG ( IgG - Ce 6) and their binding affinities to tumor cells were investigated. Intracellular localization of IgG - Ce 6 was observed, and IgG - Ce 6 was accumulated in tumor cells much higher than Ce 6, indicating that the IgG - Ce 6 has specific binding affinity to tumor cells. The effective photocytotoxicity of the cells with IgG - Ce 6 is caused by the high accumulation of IgG - Ce 6 in tumor cells.

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