Serum Proteins Opsonization and Phagocytic Uptake of PEG-Modified PLGA Nanoparticles: Effect of Particle Size

2011 ◽  
Vol 393-395 ◽  
pp. 939-942 ◽  
Author(s):  
An Shu Yang ◽  
Wei Liu ◽  
Xiang Liang Yang
Keyword(s):  
Particle Size ◽  
Serum Protein ◽  
Complement Activation ◽  
Serum Proteins ◽  
Enzyme Linked Immunosorbent Assay ◽  
Spontaneous Emulsification ◽  
Protein Assay ◽  
Effect Of Particle Size ◽  
Serum Dependent

The purpose of this study is to evaluate the effect of particle size on serum protein opsonization and in vitro macrophage uptake of polyethyleneglycol modified poly (D, L-lactide-co-glycolide) nanoparticles (PEG-PLGA-NPs). PEG-PLGA-NPs were prepared by modified-spontaneous emulsification solvent diffusion (modified-SESD) method. Serum protein adsorptions to PEG-PLGA-NPs were evaluated by bicinchoninic acid (BCA) protein assay and enzyme-linked immunosorbent assay (ELISA). Complement activation was also investigated by ELISA for complement fragments iC3b. Uptake of PEG-PLGA-NPs by macrophages was measured by fluorescence spectrometer. The results showed that serum protein adsorption and complement activation were augmented for nanoparticles with a larger size below 400 nm. Phagocytosis of PEG-PLGA-NPs by murine peritoneal macrophages involved serum-independent and serum-dependent phagocytosis. Serum-independent phagocytosis decreased, while serum-dependent phagocytosis increased with the increase of particle size in the nanometer and submicrometer range. Consequently, nanoparticles with size of about 400 nm were phagocytosed more readily than either smaller or larger particles

In vitro permeation of gold nanoparticles through rat skin and rat intestine: Effect of particle size

2008 ◽  
Vol 65 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Ganeshchandra Sonavane ◽  
Keishiro Tomoda ◽  
Akira Sano ◽  
Hiroyuki Ohshima ◽  
Hiroshi Terada ◽  
...  
Keyword(s):  
Particle Size ◽  
Gold Nanoparticles ◽  
Rat Skin ◽  
Rat Intestine ◽  
In Vitro Permeation ◽  
Effect Of Particle Size

Rutin nanosuspension for potential management of osteoporosis: effect of particle size reduction on oral bioavailability, in vitro and in vivo activity

2020 ◽  
Vol 25 (8) ◽  
pp. 971-988
Author(s):  
Sonia Gera ◽  
Venkatesh Pooladanda ◽  
Chandraiah Godugu ◽  
Veerabhadra Swamy Challa ◽  
Jitendra Wankar ◽  
...  
Keyword(s):  
Particle Size ◽  
Oral Bioavailability ◽  
Size Reduction ◽  
Particle Size Reduction ◽  
Effect Of Particle Size

Effect of particle size on in vitro fermentation of silages differing in dry matter content

1997 ◽  
Vol 1997 ◽  
pp. 197-197
Author(s):  
R. Sanderson ◽  
S.J. Lister ◽  
A. Sargeant ◽  
M.S. Dhanoa
Keyword(s):  
Particle Size ◽  
Dry Matter ◽  
Matter Content ◽  
Dry Matter Content ◽  
In Vitro Fermentation ◽  
Freeze Dried ◽  
Effect Of Particle Size

The objectives of this study were a) to examine the effect of particle size and silage dry matter (DM) content on the rate and pattern of fermentation of fresh silages in vitro as an aid to modelling the in vivo situation and b) to compare the rate and pattern of fermentation of fresh silage samples with those obtained for freeze-dried material.

Effect of particle size on macrophage-osteoclast differentiation in vitro

2001 ◽  
Vol 6 (1) ◽  
pp. 53-58 ◽  
Author(s):  
Takahisa Hirayama ◽  
Yosuke Fujikawa ◽  
Ichiro Itonaga ◽  
Takehiko Torisu
Keyword(s):  
Particle Size ◽  
Osteoclast Differentiation ◽  
Effect Of Particle Size

scholarly journals Leptospiral LruA Is Required for Virulence and Modulates an Interaction with Mammalian Apolipoprotein AI

2013 ◽  
Vol 81 (10) ◽  
pp. 3872-3879 ◽  
Author(s):  
Kunkun Zhang ◽  
Gerald L. Murray ◽  
Torsten Seemann ◽  
Amporn Srikram ◽  
Thanatchaporn Bartpho ◽  
...  
Keyword(s):  
Serum Protein ◽  
Serum Proteins ◽  
Acute Infection ◽  
Cellular Interactions ◽  
Wild Type ◽  
Hamster Model ◽  
Content Type ◽  
Truncation Mutant ◽  
Separation Of Proteins

ABSTRACTLeptospirosis is a worldwide zoonosis caused by spirochetes of the genusLeptospira. While understanding of pathogenesis remains limited, the development of mutagenesis inLeptospirahas provided a powerful tool for identifying novel virulence factors. LruA is a lipoprotein that has been implicated in leptospiral uveitis as a target of the immune response. In this study, twolruAmutants, M754 and M765, generated by transposon mutagenesis fromLeptospira interrogansserovar Manilae, were characterized. In M754, the transposon inserted in the middle oflruA, resulting in no detectable expression of LruA. In M765, the transposon inserted toward the 3′ end of the gene, resulting in expression of a truncated protein. LruA was demonstrated to be on the cell surface in M765 and the wild type (WT). M754, but not M765, was attenuated in a hamster model of acute infection. A search for differential binding to human serum proteins identified a serum protein of around 30 kDa bound to the wild type and the LruA deletion mutant (M754), but not to the LruA truncation mutant (M765). Two-dimensional separation of proteins from leptospiral cells incubated with guinea pig serum identified the 28-kDa apolipoprotein A-I (ApoA-I) as a major mammalian serum protein that bindsLeptospirain vitro. Interestingly, M754 (with no detectable LruA) bound more ApoA-I than did the LruA-expressing strains Manilae wild type and M765. Our data thus identify LruA as a surface-exposed leptospiral virulence factor that contributes to leptospiral pathogenesis, possibly by modulating cellular interactions with serum protein ApoA-I.

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