dc.contributor.author |
Abdalla, Eddie |
|
dc.contributor.author |
Carlton, Barnett |
|
dc.contributor.author |
Moore, Ernest |
|
dc.contributor.author |
Silliman, Christopher |
|
dc.contributor.author |
David, Patrick |
|
dc.contributor.author |
Curley, Steven |
|
dc.date.accessioned |
2015-11-10T08:58:08Z |
|
dc.date.available |
2015-11-10T08:58:08Z |
|
dc.date.copyright |
2001 |
|
dc.date.issued |
2015-11-10 |
|
dc.identifier.issn |
0022-4804 |
en_US |
dc.identifier.uri |
http://hdl.handle.net/10725/2506 |
|
dc.description.abstract |
Background. Some human malignancies such as virus-related hepatocellular cancer arise in a setting of chronic inflammation. Upregulation of ICAM-1 is a seminal late event in malignant transformation following chronic inflammation. Cytosolic phospholipase A2 (cPLA2) is a lipid-mediator activated by inflammatory stimuli, which has been shown to mediate ICAM-1 upregulation. As lipid mediators are known to work via calcium-dependent mechanisms in nearly all mammalian cells, we hypothesize that inflammatory-mediated ICAM-1 upregulation is dependent on both cPLA2 and intracellular calcium.
Materials and methods. HUVEC were chosen as a representative cell line as they emulate hepatic sinusoids and are a well-established cell model. These were grown to confluence in T-25 flasks and stimulated with TNF-α or LPS for 6 h. Additional groups were preincubated with AACOCF3 (a specific cPLA2 inhibitor) or BAPTA A.M. (a specific inhibitor of intracellular Ca2+) prior to being exposed to inflammatory stimuli. ICAM-1 expression was determined by mean fluorescent intensity (MFI) as measured by FITC-labeled moAb to ICAM-1 via FACS. The role of intracellular Ca2+ on cPLA2 activity was determined by thin-layer chromatography. Groups were compared using ANOVA with Scheffe's post hoc analysis; *P < 0.05 vs control, †P < 0.05 vs LPS and TNF-α was considered significant; N ≥ 4 all experimental groups.
Results. Both cPLA2 and Ca2+ inhibition significantly inhibited inflammatory upregulation of ICAM-1. Pretreatment with BAPTA A.M. attenuated HUVEC cPLA2 activity in response to LPS. These findings suggest that appropriate molecular target suppression may prevent malignant degeneration in the presence of chronic inflammation. |
en_US |
dc.language.iso |
en |
en_US |
dc.title |
Cytosolic Phospholipase A2-Mediated ICAM-1 Expression Is Calcium Dependent |
en_US |
dc.type |
Article |
en_US |
dc.description.version |
Published |
en_US |
dc.author.school |
SOM |
en_US |
dc.author.idnumber |
201100945 |
en_US |
dc.author.woa |
N/A |
en_US |
dc.author.department |
N/A |
en_US |
dc.description.embargo |
N/A |
en_US |
dc.relation.journal |
Journal of Surgical Research |
en_US |
dc.journal.volume |
99 |
en_US |
dc.journal.issue |
2 |
en_US |
dc.article.pages |
307-310 |
en_US |
dc.keywords |
Phospholipase A2 |
en_US |
dc.keywords |
Calcium |
en_US |
dc.keywords |
Endothelial cells |
en_US |
dc.keywords |
Cellular adhesion molecules |
en_US |
dc.keywords |
Intercellular adhesion molecule-1 |
en_US |
dc.identifier.doi |
http://dx.doi.org/10.1006/jsre.2001.6188 |
en_US |
dc.identifier.ctation |
Barnett, C. C., Moore, E. E., Silliman, C. C., Abdalla, E. K., Partrick, D. A., & Curley, S. A. (2001). Cytosolic phospholipase A 2-mediated ICAM-1 expression is calcium dependent. Journal of Surgical Research, 99(2), 307-310. |
en_US |
dc.author.email |
eddie.abdalla@lau.edu.lb |
|
dc.identifier.url |
http://www.sciencedirect.com/science/article/pii/S0022480401961888 |
|