Cytosolic Phospholipase A2-Mediated ICAM-1 Expression Is Calcium Dependent

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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

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