A Cell-Free Protein Expression System Derived from Human Primary Peripheral Blood Mononuclear Cells

2020 ◽  
Vol 9 (8) ◽  
pp. 2188-2196
Author(s):  
David Burgenson ◽  
Jonathan Linton ◽  
Xudong Ge ◽  
Yordan Kostov ◽  
Leah Tolosa ◽  
...  
Keyword(s):  
Protein Expression ◽  
Peripheral Blood Mononuclear Cells ◽  
Peripheral Blood ◽  
Mononuclear Cells ◽  
Expression System ◽  
Peripheral Blood Mononuclear ◽  
Free Protein ◽  
Protein Expression System ◽  
Blood Mononuclear Cells ◽  
A Cell

Analysis of Protein Expression in Human Cells Cocultured with Porcine Peripheral Blood Mononuclear Cells

Intervirology ◽  
2018 ◽  
Vol 61 (5) ◽  
pp. 237-246
Author(s):  
Yuyuan Ma ◽  
Xiong Zhao ◽  
Junting Jia ◽  
Yongxian Yang ◽  
Rui Fan ◽  
...  
Keyword(s):  
Protein Expression ◽  
Peripheral Blood Mononuclear Cells ◽  
Peripheral Blood ◽  
Mononuclear Cells ◽  
Human Cells ◽  
Peripheral Blood Mononuclear ◽  
Blood Mononuclear Cells

High Frequency of Viral Protein Expression in Human T Cell Lymphotropic Virus Type 1-Infected Peripheral Blood Mononuclear Cells

2000 ◽  
Vol 16 (16) ◽  
pp. 1711-1715 ◽  
Author(s):  
Emmanuel Hanon ◽  
Rebecca E. Asquith ◽  
Graham P. Taylor ◽  
Yuetsu Tanaka ◽  
Jonathan N. Weber ◽  
...  
Keyword(s):  
Protein Expression ◽  
Peripheral Blood Mononuclear Cells ◽  
Peripheral Blood ◽  
High Frequency ◽  
Viral Protein ◽  
Mononuclear Cells ◽  
Peripheral Blood Mononuclear ◽  
Human T Cell ◽  
Blood Mononuclear Cells

scholarly journals The effect of aging on the autophagic and heat shock response in human peripheral blood mononuclear cells

2018 ◽  
Vol 105 (3) ◽  
pp. 247-256 ◽  
Author(s):  
JJ McCormick ◽  
TA VanDusseldorp ◽  
CG Ulrich ◽  
RL Lanphere ◽  
K Dokladny ◽  
...  
Keyword(s):  
Heat Shock ◽  
Protein Expression ◽  
Peripheral Blood Mononuclear Cells ◽  
Heat Shock Response ◽  
Peripheral Blood ◽  
Mononuclear Cells ◽  
Mrna Levels ◽  
Peripheral Blood Mononuclear ◽  
Shock Response ◽  
Blood Mononuclear Cells

Autophagy is a lysosome degradation pathway through which damaged organelles and macromolecules are degraded within the cell. A decrease in activity of the autophagic process has been linked to several age-associated pathologies, including triglyceride accumulation, mitochondrial dysfunction, muscle degeneration, and cardiac malfunction. Here, we examined the differences in the autophagic response using autophagy-inducer rapamycin (Rapa) in peripheral blood mononuclear cells (PBMCs) from young (21.8 ± 1.9 years) and old (64.0 ± 3.7 years) individuals. Furthermore, we tested the interplay between the heat shock response and autophagy systems. Our results showed a significant increase in LC3-II protein expression in response to Rapa treatment in young but not in old individuals. This was associated with a decreased response in MAP1LC3B mRNA levels, but not SQSTM1/p62. Furthermore, HSPA1A mRNA was upregulated only in young individuals, despite no differences in HSP70 protein expression. The combined findings suggest a suppressed autophagic response following Rapa treatment in older individuals.

scholarly journals Raltegravir Is a Substrate for SLC22A6: a Putative Mechanism for the Interaction between Raltegravir and Tenofovir

2010 ◽  
Vol 55 (2) ◽  
pp. 879-887 ◽  
Author(s):  
Darren M. Moss ◽  
Wai San Kwan ◽  
Neill J. Liptrott ◽  
Darren L. Smith ◽  
Marco Siccardi ◽  
...  
Keyword(s):  
Peripheral Blood Mononuclear Cells ◽  
Peripheral Blood ◽  
Mononuclear Cells ◽  
Expression System ◽  
Dependent Manner ◽  
Renal Cells ◽  
Peripheral Blood Mononuclear ◽  
Blood Mononuclear Cells ◽  
Oocyte Expression ◽  
Oocyte Expression System

ABSTRACTThe identification of transporters of the HIV integrase inhibitor raltegravir could be a factor in an understanding of the pharmacokinetic-pharmacodynamic relationship and reported drug interactions of raltegravir. Here we determined whether raltegravir was a substrate for ABCB1 or the influx transporters SLCO1A2, SLCO1B1, SLCO1B3, SLC22A1, SLC22A6, SLC10A1, SLC15A1, and SLC15A2. Raltegravir transport by ABCB1 was studied with CEM, CEMVBL100, and Caco-2 cells. Transport by uptake transporters was assessed by using aXenopus laevisoocyte expression system, peripheral blood mononuclear cells, and primary renal cells. The kinetics of raltegravir transport and competition between raltegravir and tenofovir were also investigated using SLC22A6-expressing oocytes. Raltegravir was confirmed to be an ABCB1 substrate in CEM, CEMVBL100, and Caco-2 cells. Raltegravir was also transported by SLC22A6 and SLC15A1 in oocyte expression systems but not by other transporters studied. TheKmandVmaxfor SLC22A6 transport were 150 μM and 36 pmol/oocyte/h, respectively. Tenofovir and raltegravir competed for SLC22A6 transport in a concentration-dependent manner. Raltegravir inhibited 1 μM tenofovir with a 50% inhibitory concentration (IC50) of 14.0 μM, and tenofovir inhibited 1 μM raltegravir with an IC50of 27.3 μM. Raltegravir concentrations were not altered by transporter inhibitors in peripheral blood mononuclear cells or primary renal cells. Raltegravir is a substrate for SLC22A6 and SLC15A1 in the oocyte expression system. However, transport was limited compared to endogenous controls, and these transporters are unlikely to have a great impact on raltegravir pharmacokinetics.

scholarly journals CRP and TNF-α  Induce PAPP-A Expression in Human Peripheral Blood Mononuclear Cells

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Weiping Li ◽  
Hongwei Li ◽  
Fusheng Gu
Keyword(s):  
Protein Expression ◽  
Peripheral Blood Mononuclear Cells ◽  
Peripheral Blood ◽  
Mononuclear Cells ◽  
Human Peripheral Blood ◽  
Human Pbmcs ◽  
Peripheral Blood Mononuclear ◽  
Protein Levels ◽  
Blood Mononuclear Cells ◽  
Mrna And Protein Expression

Objective. The effects of C-reactive protein (CRP) and tumor necrosis factor-α(TNF-α) on pregnancy-associated plasma protein-A (PAPP-A) expression in human peripheral blood mononuclear cells (PBMCs) require further investigation.Methods. The PAPP-A levels in culture supernatants, PAPP-A mRNA expression, and cellular PAPP-A expression were measured in human PBMCs isolated from fresh blood donations provided by 6 healthy volunteers (4 donations per volunteer). Analyses were conducted by ultrasensitive ELISA, western blotting, and RT-PCR following stimulation with CRP or TNF-αcytokines.Results. PAPP-A mRNA and protein levels after CRP stimulation peaked at 24 hours, whereas peak PAPP-A mRNA and protein levels were achieved after TNF-αstimulation at only 2 and 8 hours, respectively. These findings indicate the dose-dependent effect of CRP and TNF-αstimulation. Actinomycin D treatment completely prevented CRP and TNF-αinduction of PAPP-A mRNA and protein expression. Additionally, nuclear factor- (NF-)κB inhibitor (BAY11-7082) potently inhibited both CRP and TNF-αstimulated PAPP-A mRNA and protein expression.Conclusions. Human PBMCs are capable of expressing PAPP-Ain vitro, expression that may be regulated by CRP and TNF-αthrough the NF-κB pathway. This mechanism may play a significant role in the observed increase of serum PAPP-A levels in acute coronary syndrome (ACS).

Sign in / Sign up

Export Citation Format

Share Document