Airborne organic particulate matter (PM) activates phospholipase A2 through extracellular signal-regulated kinase in lung epithelial cells | Health & Environmental Research Online (HERO)

HERO ID

2579704

Reference Type

Journal Article

Subtype

Abstract

Title

Airborne organic particulate matter (PM) activates phospholipase A2 through extracellular signal-regulated kinase in lung epithelial cells

Author(s)

Parinandi, NL; Kotha, SR

Year

2008

Is Peer Reviewed?

Yes

Journal

Free Radical Biology and Medicine
ISSN: 0891-5849
EISSN: 1873-4596

Volume

45

Issue

Suppl.

Page Numbers

S47-S47

Language

English

Web of Science Id

WOS:000260867900129

URL

http://www.sciencedirect.com/science/article/pii/S0891584908006217
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Relationship(s)

is part of a larger document 3452652 SFRBM's 15th Annual Meeting: Program and Abstracts

Abstract

The precise mechanism(s) of poultry (agricultural organic) particulate matter (PM)-induced respiratory disorders is not established. Hence, it is hypothesized here that poultry PM induces the release of the calcium-dependent phospholipase A2 (cPLA2) by lung epithelium under the modulation of extracellular signal-regulated kinase (ERK) through serine phosphorylation. To test this hypothesis, human lung epithelial cells (A549) in culture, were treated with poultry PM (0.1-1.0 mg) for 0-60 min following which PLA2 activity, cPLA2 serine phosphorylation, and ERK1/2 phosphorylation (activation) were determined. the results showed a significant activation of PLA2 induced by poultry PM (1.0 mg/mL) at 1 h which was significantly attenuated by AACOCF3 (cPLA2 inhibitor) and PD98057 (ERK1/2 upstream inhibitor), suggesting the modulation of cPLA2 activity by ERK1/2 in cells. ERK1/2 phosphorylation was also induced by poultry PM which paralleled with cPLA2 serine phosphorylation. cPLA2 immunoprecipitates from poultry PM-treated cells exhibited enhanced association of ERK1/2 and cPLA2 in a time-dependent fashion. ERK1/2 inhibition with PD98057 also attenuated the poultry PM-induced serine phosphorylation of cPLA2 in cells. Furthermore, the poultry PM-induced cPLA2 serine phosphorylation was significantly inhibited by PD98057 and by transfection with dominant-negative ERK1/2 DNA in cells. for the first time, this study demonstrated that the agricultural PM induced cPLA2 activation through ERK-mediated serine phosphorylation.

Conference Name

Society for Free Radical Biology and Medicine 15th Annual Meeting

Conference Location

Indianapolis, IN

Conference Dates

November 19-23, 2008