Gene expression changes during Giardia–host cell interactions in serum-free medium

2014 ◽  
Vol 197 (1-2) ◽  
pp. 21-23 ◽  
Author(s):  
Marcela Ferella ◽  
Barbara J. Davids ◽  
Michael J. Cipriano ◽  
Shanda R. Birkeland ◽  
Daniel Palm ◽  
...  
Keyword(s):  
Gene Expression ◽  
Host Cell ◽  
Cell Interactions ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Host Cell Interactions

scholarly journals Pivotal Roles for Ribonucleases in Streptococcus pneumoniae Pathogenesis

mBio ◽  
2021 ◽  
Author(s):  
Dhriti Sinha ◽  
Jacob P. Frick ◽  
Kristen Clemons ◽  
Malcolm E. Winkler ◽  
Nicholas R. De Lay
Keyword(s):  
Gene Expression ◽  
Streptococcus Pneumoniae ◽  
Host Cell ◽  
Cell Interactions ◽  
Human Pathogen ◽  
Protein Coding ◽  
Content Type ◽  
Key Players ◽  
Host Cell Interactions ◽  
Host Tissues

Streptococcus pneumoniae is a notorious human pathogen that adapts to conditions in distinct host tissues and responds to host cell interactions by adjusting gene expression. RNases are key players that modulate gene expression by mediating the turnover of regulatory and protein-coding transcripts.

scholarly journals Beta 1 integrin-mediated interaction with extracellular matrix proteins regulates cytokine gene expression in synovial fluid cells of rheumatoid arthritis patients.

1993 ◽  
Vol 177 (3) ◽  
pp. 863-868 ◽  
Author(s):  
S Miyake ◽  
H Yagita ◽  
T Maruyama ◽  
H Hashimoto ◽  
N Miyasaka ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Gene Expression ◽  
Cytokine Gene Expression ◽  
Serum Free Medium ◽  
Cytokine Gene ◽  
Free Medium ◽  
Serum Free ◽  
Ecm Proteins ◽  
Beta 1 Integrin

Inflammatory cytokines have been implicated in the pathogenesis of rheumatoid arthritis (RA), whereas the mechanisms for constitutive production of inflammatory cytokines in affected joints are largely unknown. Recently, integrin-mediated interaction with extracellular matrix (ECM) proteins has been demonstrated to play a role in regulating cytokine production in T cells and monocytes. In this study, we investigated the contribution of the beta 1 integrin-mediated interaction with ECM proteins to the persistent cytokine gene expression in RA synovial fluid mononuclear cells (SFMNC). We examined mRNA expression of 14 cytokines in the SFMNC of three RA patients, which were either fresh or cultured overnight in serum-free medium on ECM-coated plates, by polymerase chain reaction with a panel of oligonucleotide primers specific for each cytokine. The persistent expression of various cytokine mRNA found in fresh SFMNC was maintained after overnight culture in serum-free medium on ECM proteins, especially on laminin (LM), but not on serum albumin. This effect of LM was inhibited by an anti-integrin beta 1 chain (CD29) mAb, as well as by an anti-CD3 mAb, indicating an important role of the beta 1 integrin-mediated interaction with ECM proteins in regulating persistent cytokine gene expression in RA SFMNC, and a key role of T cells in regulating inflammatory monokine production.

Gene expression of nestin, collagen type I and type III in human dental follicle cells after cultivation in serum-free medium

2008 ◽  
Vol 12 (2) ◽  
pp. 89-92 ◽  
Author(s):  
Christian Morsczeck ◽  
Wolfgang Ernst ◽  
Christian Florian ◽  
Torsten Eugen Reichert ◽  
Peter Proff ◽  
...  
Keyword(s):  
Gene Expression ◽  
Collagen Type ◽  
Collagen Type I ◽  
Follicle Cells ◽  
Type I ◽  
Dental Follicle ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Dental Follicle Cells

Exogeneous factors are not necessary in attachment, spreading and polarization of hela cells

1978 ◽  
Vol 36 (2) ◽  
pp. 310-311
Author(s):  
W. Liebrich
Keyword(s):  
Hela Cells ◽  
Calf Serum ◽  
Glass Tube ◽  
Serum Free Medium ◽  
Nacl Solution ◽  
Free Medium ◽  
Minimum Essential Medium ◽  
Serum Free ◽  
All Solutions ◽  
Glass Support

HeLa cells were grown for 2-3 days in EAGLE'S minimum essential medium with 10% calf serum (S-MEM; Seromed, München) and then incubated for 24 hours in serum free medium (MEM). After detaching the cells with a solution of 0. 14 % EDTA and 0. 07 % trypsin (Difco, 1 : 250) they were suspended in various solutions (S-MEM = control, MEM, buffered salt solutions with or without Me++ions, 0. 9 % NaCl solution) and allowed to settle on glass tube slips (Leighton-tubes). After 5, 10, 15, 20, 25, 30, 1 45, 60 minutes 2, 3, 4, 5 hours cells were prepared for scanning electron microscopy as described by Paweletz and Schroeter. The preparations were examined in a Jeol SEM (JSM-U3) at 25 KV without tilting.The suspended spherical HeLa cells are able to adhere to the glass support in all solutions. The rate of attachment, however, is faster in solutions without serum than in the control. The latter is in agreement with the findings of other authors.

Hemoglobin Enhances the Binding of Bacterial Endotoxin to Human Endothelial Cells

1996 ◽  
Vol 76 (02) ◽  
pp. 258-262 ◽  
Author(s):  
Robert I Roth
Keyword(s):  
Endothelial Cells ◽  
Binding Protein ◽  
Bacterial Endotoxin ◽  
Dependent Manner ◽  
Serum Free Medium ◽  
Free Medium ◽  
Human Endothelial Cells ◽  
Serum Factors ◽  
Serum Free ◽  
Lps Binding

SummaryHuman endothelial cells, when incubated with bacterial endotoxin (lipopolysaccharide, LPS), modify their surface in association with prominent production of procoagulant tissue factor (TF) activity. This deleterious biological effect of LPS has been shown previously to be enhanced approximately 10-fold by the presence of hemoglobin (Hb), a recently recognized LPS binding protein that causes disaggregation of LPS and increases the biological activity of LPS in a number of in vitro assays. The present study was performed to test the hypothesis that Hb enhances the LPS-induced procoagulant activity of human umbilical vein endothelial cells (HUVEC) by increasing LPS binding to the cells. The binding of 3H-LPS to HUVEC was determined in the absence or presence of Hb or two other known LPS-binding proteins, human serum albumin (HSA) and IgG. LPS binding was substantially increased in the presence of Hb, in a Hb concentration-dependent manner, but was not increased by HSA or IgG. Hb enhancement of LPS binding was observed in serum-free medium, indicating that there was no additional requirement for any of the serum factors known to participate in the interaction of LPS with cells (e.g., lipopolysaccharide (LPS)-binding protein (LBP) and soluble CD14 (sCD14)). Hb enhancement of LPS binding also was observed in the more physiologic condition of 100% plasma. LPS-induced TF activity was stimulated by Hb, but not by HSA or IgG. In serum-free medium, TF activity was not stimulated under any of the conditions tested. Ultrafiltration of LPS was dramatically increased after incubation with Hb but not with HSA or IgG, suggesting that LPS disaggregation by Hb was responsible for the enhanced binding of LPS to HUVEC and the subsequent stimulation of TF activity.

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