scholarly journals Developmental activation of the lysozyme gene in chicken macrophage cells is linked to core histone acetylation at its enhancer elements

2006 ◽  
Vol 34 (14) ◽  
pp. 4025-4035 ◽  
Author(s):  
Fiona A. Myers ◽  
Pascal Lefevre ◽  
Evangelia Mantouvalou ◽  
Kimberley Bruce ◽  
Claire Lacroix ◽  
...  
2020 ◽  
Vol 7 (4) ◽  
pp. 191561 ◽  
Author(s):  
Shan Zhang ◽  
Shu Wu ◽  
Yiru Shen ◽  
Yunqi Xiao ◽  
Lizeng Gao ◽  
...  

Magnetic Fe 3 O 4 nanoparticles (Fe 3 O 4 -NPs) have been widely investigated for their biomedical applications. The main purpose of this study was to evaluate the cytotoxic effects of different sizes of Fe 3 O 4 -NPs in chicken macrophage cells (HD11). Experimental groups based on three sizes of Fe 3 O 4 -NPs (60, 120 and 250 nm) were created, and the Fe 3 O 4 -NPs were added to the cells at different doses according to the experimental group. The cell activity, oxidative index (malondialdehyde (MDA), superoxide dismutase (SOD) and reactive oxygen species (ROS)), apoptosis and pro-inflammatory cytokine secretion level were detected to analyse the cytotoxic effects of Fe 3 O 4 -NPs of different sizes in HD11 cells. The results revealed that the cell viability of the 60 nm Fe 3 O 4 -NPs group was lower than those of the 120 and 250 nm groups when the same concentration of Fe 3 O 4 -NPs was added. No significant difference in MDA was observed among the three Fe 3 O 4 -NP groups. The SOD level and ROS production of the 60 nm group were significantly greater than those of the 120 and 250 nm groups. Furthermore, the highest levels of apoptosis and pro-inflammatory cytokine secretion were caused by the 60 nm Fe 3 O 4 -NPs. In conclusion, the smaller Fe 3 O 4 -NPs produced stronger cytotoxicity in chicken macrophage cells, and the cytotoxic effects may be related to the oxidative stress and apoptosis induced by increased ROS production as well as the increased expression of pro-inflammatory cytokines.


2007 ◽  
Vol 255 (1) ◽  
pp. 42-48 ◽  
Author(s):  
Hyung Jin Jeong ◽  
Jin Boo Jeong ◽  
Dae Seop Kim ◽  
Jae Ho Park ◽  
Jung Bok Lee ◽  
...  

1994 ◽  
Vol 224 (3) ◽  
pp. 885-892 ◽  
Author(s):  
Valerie Girardot ◽  
Thierry Rabilloud ◽  
Minoru Yoshida ◽  
Teruhiko Beppu ◽  
Jean-Jacques Lawrence ◽  
...  

Animals ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 307
Author(s):  
Fei Wang ◽  
Qinghe Li ◽  
Qiao Wang ◽  
Maiqing Zheng ◽  
Jie Wen ◽  
...  

Salmonellosis is a zoonosis that is not only harmful to the health of poultry but also poses a threat to human health. Although many measures have been put in place to reduce morbidity, they have not provided satisfactory results. Therefore, it is necessary to clarify the immune mechanisms involved in improving the resistance of chickens against Salmonella. BTB (Broad-complex Tramtrack and Bric-a-brac) Speckle-type POZ (poxvirus and zinc finger) protein (SPOP) regulates protein expression by promoting substrate ubiquitination and degradation. The correlation between SPOP expression and the immune response has not been fully described. Therefore, the aim of this study was to clarify this relationship. In vitro, we stimulated chicken macrophage cells (HD11) with lipopolysaccharide, then analyzed the correlation between SPOP and IL1β or IL8 expression using quantitative real-time polymerase chain reaction (qRT-PCR). In vivo, we infected 7-days-old chickens with Salmonella Typhimurium, then analyzed the association between SPOP expression and the immune response, including IL1β and IL8 expression, IgA production, and bacterial loads. We found that SPOP may participate in the regulation of the immune response in macrophage cells. SPOP expression was negatively correlated with IL-1β and IL-8 expression both in vivo and in vitro. SPOP expression was also negatively related to bacterial loads and immunoglobulin (Ig) A production. These results indicate that SPOP may have important functions in the response to Salmonella infection.


2004 ◽  
Vol 317 (1) ◽  
pp. 259-264 ◽  
Author(s):  
Tao Hong ◽  
Takeya Nakagawa ◽  
WeiJun Pan ◽  
Mi Young Kim ◽  
W Lee Kraus ◽  
...  

1998 ◽  
Vol 18 (8) ◽  
pp. 4629-4638 ◽  
Author(s):  
Christin Tse ◽  
Takashi Sera ◽  
Alan P. Wolffe ◽  
Jeffrey C. Hansen

ABSTRACT We have examined the effects of core histone acetylation on the transcriptional activity and higher-order folding of defined 12-mer nucleosomal arrays. Purified HeLa core histone octamers containing an average of 2, 6, or 12 acetates per octamer (8, 23, or 46% maximal site occupancy, respectively) were assembled onto a DNA template consisting of 12 tandem repeats of a 208-bp Lytechinus 5S rRNA gene fragment. Reconstituted nucleosomal arrays were transcribed in a Xenopus oocyte nuclear extract and analyzed by analytical hydrodynamic and electrophoretic approaches to determine the extent of array compaction. Results indicated that in buffer containing 5 mM free Mg2+ and 50 mM KCl, high levels of acetylation (12 acetates/octamer) completely inhibited higher-order folding and concurrently led to a 15-fold enhancement of transcription by RNA polymerase III. The molecular mechanisms underlying the acetylation effects on chromatin condensation were investigated by analyzing the ability of differentially acetylated nucleosomal arrays to fold and oligomerize. In MgCl2-containing buffer the folding of 12-mer nucleosomal arrays containing an average of two or six acetates per histone octamer was indistinguishable, while a level of 12 acetates per octamer completely disrupted the ability of nucleosomal arrays to form higher-order folded structures at all ionic conditions tested. In contrast, there was a linear relationship between the extent of histone octamer acetylation and the extent of disruption of Mg2+-dependent oligomerization. These results have yielded new insight into the molecular basis of acetylation effects on both transcription and higher-order compaction of nucleosomal arrays.


Methods ◽  
1997 ◽  
Vol 12 (1) ◽  
pp. 48-56 ◽  
Author(s):  
Colyn Crane-Robinson ◽  
Tim R. Hebbes ◽  
Alison L. Clayton ◽  
Alan W. Thorne

Sign in / Sign up

Export Citation Format

Share Document