Platelet derived growth factor increases phospholipase D1 but not phospholipase D2 expression via NFκB signaling pathway and enhances invasion of breast cancer cells

Dong Woo Kang, Do Sik Min

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Phospholipase D (PLD) has emerged as a critical element in the cell growth signaling. Despite extensive information regarding the regulation of PLD activity in cell survival, the signaling mechanisms that regulate PLD expression in cancer remains poorly understood. Here we investigate that platelet derived growth factor (PDGF) increases PLD1 but not PLD2 expression via Ras-ERK/PI3K-NFκB signaling cascade in SK-BR3 breast cancer cells. The two NFκB-binding sites are functionally critical for transcriptional activation of PLD1 induced by PDGF. Furthermore, depletion of PLD1 using siRNA significantly abolished PDGF-induced upregulation of matrix metalloproteinase-2 or -9 and invasion of breast cancer cells. Thus, we propose that PDGF-induced PLD1 expression via NFκB signaling pathway might contribute to carcinogenesis.

Original languageEnglish
Pages (from-to)125-133
Number of pages9
JournalCancer Letters
Volume294
Issue number1
DOIs
Publication statusPublished - 2010 Aug 1

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Platelet-Derived Growth Factor
Phospholipase D
Breast Neoplasms
Matrix Metalloproteinase 2
Phosphatidylinositol 3-Kinases
Small Interfering RNA
Transcriptional Activation
Cell Survival
Carcinogenesis
Up-Regulation
Binding Sites
phospholipase D2
phospholipase D1
Growth
Neoplasms

All Science Journal Classification (ASJC) codes

  • Oncology
  • Cancer Research

Cite this

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title = "Platelet derived growth factor increases phospholipase D1 but not phospholipase D2 expression via NFκB signaling pathway and enhances invasion of breast cancer cells",
abstract = "Phospholipase D (PLD) has emerged as a critical element in the cell growth signaling. Despite extensive information regarding the regulation of PLD activity in cell survival, the signaling mechanisms that regulate PLD expression in cancer remains poorly understood. Here we investigate that platelet derived growth factor (PDGF) increases PLD1 but not PLD2 expression via Ras-ERK/PI3K-NFκB signaling cascade in SK-BR3 breast cancer cells. The two NFκB-binding sites are functionally critical for transcriptional activation of PLD1 induced by PDGF. Furthermore, depletion of PLD1 using siRNA significantly abolished PDGF-induced upregulation of matrix metalloproteinase-2 or -9 and invasion of breast cancer cells. Thus, we propose that PDGF-induced PLD1 expression via NFκB signaling pathway might contribute to carcinogenesis.",
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AU - Min, Do Sik

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N2 - Phospholipase D (PLD) has emerged as a critical element in the cell growth signaling. Despite extensive information regarding the regulation of PLD activity in cell survival, the signaling mechanisms that regulate PLD expression in cancer remains poorly understood. Here we investigate that platelet derived growth factor (PDGF) increases PLD1 but not PLD2 expression via Ras-ERK/PI3K-NFκB signaling cascade in SK-BR3 breast cancer cells. The two NFκB-binding sites are functionally critical for transcriptional activation of PLD1 induced by PDGF. Furthermore, depletion of PLD1 using siRNA significantly abolished PDGF-induced upregulation of matrix metalloproteinase-2 or -9 and invasion of breast cancer cells. Thus, we propose that PDGF-induced PLD1 expression via NFκB signaling pathway might contribute to carcinogenesis.

AB - Phospholipase D (PLD) has emerged as a critical element in the cell growth signaling. Despite extensive information regarding the regulation of PLD activity in cell survival, the signaling mechanisms that regulate PLD expression in cancer remains poorly understood. Here we investigate that platelet derived growth factor (PDGF) increases PLD1 but not PLD2 expression via Ras-ERK/PI3K-NFκB signaling cascade in SK-BR3 breast cancer cells. The two NFκB-binding sites are functionally critical for transcriptional activation of PLD1 induced by PDGF. Furthermore, depletion of PLD1 using siRNA significantly abolished PDGF-induced upregulation of matrix metalloproteinase-2 or -9 and invasion of breast cancer cells. Thus, we propose that PDGF-induced PLD1 expression via NFκB signaling pathway might contribute to carcinogenesis.

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