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Published on: May 31, 2018
Se-methylselenocysteine enhances PMA-mediated CD11c expression via phospholipase D1 activation in U937 cells
Tae-Jin Lee1, Young Ho Kim, Do Sik Min
1Department of Immunology and Chronic Disease Research Center and Institute for Medical Science, School of Medicine, Keimyung University, 194 DongSan-Dong Jung-Gu, Taegu 700-712, Republic of Korea. taejin@kmu.ac.kr
Abstract:
CD11c/CD18 is expressed primarily on myeloid cells, where its expression is regulated both during differentiation and during monocyte maturation into tissue macrophages, and is also a receptor for fibrinogen and lipopolysaccharide (LPS). We focused on the molecular mechanisms leading to the activation of CD11c expression in differentiating U937 cells. During phorbol myristate acetate (PMA)-induced differentiation of U937 cells, we found that the mRNA expression of CD11c was increased. Se-methylselenocysteine (Se-MSC) potentiated up-regulation of CD11c expression and its promoter activity and increased PLD1 activity without affecting the level of PLD1 protein in PMA-treated cells. To examine the regulation mechanism of PMA and Se-MSC on CD11c gene expression through the activation of PLD1, we analyzed changes in the CD11c mRNA level and the promoter activity following treatment of a selective PLD inhibitor n-butanol. The combinatory effect of PMA and Se-MSC on CD11c gene expression was abolished by n-butanol in a dose-dependent manner. Further, introduction of PLD1 gene into U937 cells increased CD11c mRNA expression and activated CD11c promoter activity in a dose-dependent manner. These results showed that Se-MSC increased PMA-induced CD11c expression through the activation of PLD1 signaling pathway. To our knowledge, this is the first report that expression of the CD11c gene is regulated by PLD1 and is enhanced by Se-MSC during PMA-induced U937 differentiation.
Insights
Se-methylselenocysteine (Se-MSC) enhances CD11c expression during U937 cell differentiation by activating the Phospholipase D1 (PLD1) signaling pathway. This study reveals a novel regulatory mechanism for CD11c gene expression.
Area of Science:
- Immunology
- Molecular Biology
- Cell Biology
Background:
- CD11c/CD18 is a key molecule on myeloid cells, involved in cell differentiation, maturation, and acting as a receptor for fibrinogen and lipopolysaccharide (LPS).
- Understanding the molecular mechanisms regulating CD11c expression is crucial for comprehending myeloid cell function and immune responses.
Purpose of the Study:
- To investigate the molecular mechanisms underlying CD11c expression during U937 cell differentiation.
- To elucidate the role of Se-methylselenocysteine (Se-MSC) and Phospholipase D1 (PLD1) in regulating CD11c gene expression.
Main Methods:
- U937 cells were induced to differentiate using phorbol myristate acetate (PMA).
- The effects of Se-MSC on CD11c mRNA expression, promoter activity, and PLD1 activity were analyzed.
- A selective PLD inhibitor, n-butanol, was used to assess the involvement of PLD1.
- The impact of introducing the PLD1 gene into U937 cells was evaluated.
Main Results:
- PMA-induced differentiation increased CD11c mRNA expression in U937 cells.
- Se-MSC potentiated CD11c expression and promoter activity, alongside increased PLD1 activity.
- The effects of PMA and Se-MSC on CD11c expression were abrogated by n-butanol, indicating PLD1 dependence.
- Overexpression of PLD1 enhanced CD11c mRNA expression and promoter activity.
Conclusions:
- Se-MSC enhances PMA-induced CD11c expression in U937 cells via the activation of the PLD1 signaling pathway.
- This study presents the first evidence that PLD1 regulates CD11c gene expression, with Se-MSC acting as an enhancer during U937 differentiation.
