Mol. Cells 2012; 34(3): 323-328
Published online July 27, 2012
https://doi.org/10.1007/s10059-012-0163-6
© The Korean Society for Molecular and Cellular Biology
Correspondence to : *Correspondence: s0huh@hallym.ac.kr
Lysophosphatidic acid (LPA) is a lipid growth factor that induces proliferation of fibroblasts by activating the cAMP response element binding protein (CREB). Here, we further investigated whether LPA induces proliferation of P19 cells, a line of pluripotent embryonic carcinoma cells. 5?-Bromo-2-deoxyuridine incorporation and cell viability assays showed that LPA stimulated proliferation of P19 cells. Immunoblot experiments with P19 cells revealed that the mitogen activated protein kinases, including p-ERK, p38, pAKT, glycogen synthase kinase 3?, and CREB were phosphorylated by treatment with 10 ?M LPA. LPA-indu-ced phosphorylation of CREB was efficiently blocked by U0126 and H89, inhibitors of the MAP kinases ERK1/2 and mitogen- and stress-activated protein kinase 1, respec-tively. Involvement of cyclin D1 in LPA-induced P19 cell proliferation was verified by immunoblot analysis in combination with pharmacological inhibitor treatment. Furthermore, LPA up-regulated CRE-harboring cyclin D1 promoter activity, suggesting that CREB and cyclin D1 play significant roles in LPA-induced proliferation of P19 embryonic carcinoma cells.
Keywords cAMP response element binding protein (CREB), cyclin D1, lysophosphatidic acid, P19 embryonic carcinoma cell, proliferation
Mol. Cells 2012; 34(3): 323-328
Published online September 30, 2012 https://doi.org/10.1007/s10059-012-0163-6
Copyright © The Korean Society for Molecular and Cellular Biology.
Min-Jung Kim, Yuanjie Sun, Haijie Yang, Nam-Ho Kim, Sung Ho Jeon1, and Sung-Oh Huh*
Department of Pharmacology, College of Medicine, Institute of Natural Medicine, Hallym University, Chuncheon 200-702, Korea, 1Department of Life Science, Hallym University, Chuncheon 200-702, Korea
Correspondence to:*Correspondence: s0huh@hallym.ac.kr
Lysophosphatidic acid (LPA) is a lipid growth factor that induces proliferation of fibroblasts by activating the cAMP response element binding protein (CREB). Here, we further investigated whether LPA induces proliferation of P19 cells, a line of pluripotent embryonic carcinoma cells. 5?-Bromo-2-deoxyuridine incorporation and cell viability assays showed that LPA stimulated proliferation of P19 cells. Immunoblot experiments with P19 cells revealed that the mitogen activated protein kinases, including p-ERK, p38, pAKT, glycogen synthase kinase 3?, and CREB were phosphorylated by treatment with 10 ?M LPA. LPA-indu-ced phosphorylation of CREB was efficiently blocked by U0126 and H89, inhibitors of the MAP kinases ERK1/2 and mitogen- and stress-activated protein kinase 1, respec-tively. Involvement of cyclin D1 in LPA-induced P19 cell proliferation was verified by immunoblot analysis in combination with pharmacological inhibitor treatment. Furthermore, LPA up-regulated CRE-harboring cyclin D1 promoter activity, suggesting that CREB and cyclin D1 play significant roles in LPA-induced proliferation of P19 embryonic carcinoma cells.
Keywords: cAMP response element binding protein (CREB), cyclin D1, lysophosphatidic acid, P19 embryonic carcinoma cell, proliferation
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