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|Title:||IL-10 synergistically enhances GM-CSF-induced CCR1 expression in myelomonocytic cells||Authors:||Li, H.
Fred, Wong W.S.
|Issue Date:||2003||Citation:||Li, H., Choo, H.H., Chan, J.H.P., Fred, Wong W.S., Cheung, W., Lai, P.S. (2003). IL-10 synergistically enhances GM-CSF-induced CCR1 expression in myelomonocytic cells. Biochemical and Biophysical Research Communications 304 (2) : 417-424. ScholarBank@NUS Repository. https://doi.org/10.1016/S0006-291X(03)00612-0||Abstract:||CC chemokine receptor 1 (CCR1) has been implicated in inflammation. The present study examined the signaling mechanisms that mediate GM-CSF/IL-10-induced synergistic CCR1 protein expression in monocytic U937 cells. GM-CSF alone markedly increased both the mRNA and protein expression of CCR1. IL-10 augmented GM-CSF-induced CCR1 protein expression with no effect on mRNA expression. PD098059 and U0126 (two MEK inhibitors), and LY294002 (a PI3K inhibitor) inhibited GM-CSF/IL-10-induced CCR1 gene and protein expression. PD098059, U0126, and LY294002 also attenuated chemotaxis of GM-CSF/IL-10-primed U937 cells in response to MIP-1α. Immunoblotting studies show that GM-CSF alone induced ERK2 phosphorylation; whereas, IL-10 alone induced p70S6k phosphorylation in U937 cells. Neither cytokine when used alone induced PKB/Akt phosphorylation. Combined GM-CSF/IL-10 treatment of U937 cells induced phosphorylation of ERK2, p70S6k, and PKB/Akt. PD098059 and U0126 completely abrogated ERK2 phosphorylation; whereas, LY294002 completely blocked PKB/Akt and p70S6k phosphorylation. Our findings indicate that IL-10 may potentiate GM-CSF-induced CCR1 protein expression in U937 cells via activation of PKB/Akt and p70S6k. © 2003 Elsevier Science (USA). All rights reserved.||Source Title:||Biochemical and Biophysical Research Communications||URI:||http://scholarbank.nus.edu.sg/handle/10635/32274||ISSN:||0006291X||DOI:||10.1016/S0006-291X(03)00612-0|
|Appears in Collections:||Staff Publications|
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