Mutated ras induced PLD1 gene expression through increased Sp1 transcription factor.

Siqiang Gao, Masashi Murakami, Hiromi Ito, Ayako Furuhata, Kayo Yoshida, Yoko Tagawa, Kazumi Hagiwara, Akira Takagi, Tetsuhito Kojima, Motoshi Suzuki, Yoshiko Banno, Yoshinori Nozawa, Takashi Murate

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The underlying mechanisms of oncogene-induced phospholipase D (PLD) activation have not been fully elucidated. The effect of the mutated-ras on PLD mRNA was examined using colon cancer cell lines as well as mock- and mutated ras-transfected NIH3T3 cells. Ras-mutation and activation were correlated, and cells with enhanced ras-activation showed increased PLD1 mRNA and protein. Analysis of the 5' PLD1 promoter using a representative cell line, DLD-1 and also mutated ras-NIH3T3, showed one Sp1-site as the important ras-responsible motif. Spl inhibition with mithramycin A and Spl siRNA inhibited PLD1 protein expression and its promoter activity. Sp1 but not Sp3 protein level and increased Sp1-motif binding activity were correlated with ras activation. Furthermore, overexpression of Sp1 in drosophila SL2 cells lacking Sp family proteins increased PLD1 promoter activity. EMSA and chromatin immunoprecipitation assay confirmed the importance of Sp1 protein binding to the Sp1-motif in ras-induced PLD1 mRNA expression.

Original languageEnglish
Pages (from-to)127-136
Number of pages10
JournalNagoya Journal of Medical Science
Volume71
Issue number3-4
Publication statusPublished - 01-09-2009
Externally publishedYes

Fingerprint

Sp1 Transcription Factor
Gene Expression
Phospholipase D
Messenger RNA
Proteins
Cell Line
Chromatin Immunoprecipitation
Oncogenes
Protein Binding
Colonic Neoplasms
Small Interfering RNA
Drosophila
Mutation

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

Gao, S., Murakami, M., Ito, H., Furuhata, A., Yoshida, K., Tagawa, Y., ... Murate, T. (2009). Mutated ras induced PLD1 gene expression through increased Sp1 transcription factor. Nagoya Journal of Medical Science, 71(3-4), 127-136.
Gao, Siqiang ; Murakami, Masashi ; Ito, Hiromi ; Furuhata, Ayako ; Yoshida, Kayo ; Tagawa, Yoko ; Hagiwara, Kazumi ; Takagi, Akira ; Kojima, Tetsuhito ; Suzuki, Motoshi ; Banno, Yoshiko ; Nozawa, Yoshinori ; Murate, Takashi. / Mutated ras induced PLD1 gene expression through increased Sp1 transcription factor. In: Nagoya Journal of Medical Science. 2009 ; Vol. 71, No. 3-4. pp. 127-136.
@article{16e398bdbcbc4720a57f30b254646352,
title = "Mutated ras induced PLD1 gene expression through increased Sp1 transcription factor.",
abstract = "The underlying mechanisms of oncogene-induced phospholipase D (PLD) activation have not been fully elucidated. The effect of the mutated-ras on PLD mRNA was examined using colon cancer cell lines as well as mock- and mutated ras-transfected NIH3T3 cells. Ras-mutation and activation were correlated, and cells with enhanced ras-activation showed increased PLD1 mRNA and protein. Analysis of the 5' PLD1 promoter using a representative cell line, DLD-1 and also mutated ras-NIH3T3, showed one Sp1-site as the important ras-responsible motif. Spl inhibition with mithramycin A and Spl siRNA inhibited PLD1 protein expression and its promoter activity. Sp1 but not Sp3 protein level and increased Sp1-motif binding activity were correlated with ras activation. Furthermore, overexpression of Sp1 in drosophila SL2 cells lacking Sp family proteins increased PLD1 promoter activity. EMSA and chromatin immunoprecipitation assay confirmed the importance of Sp1 protein binding to the Sp1-motif in ras-induced PLD1 mRNA expression.",
author = "Siqiang Gao and Masashi Murakami and Hiromi Ito and Ayako Furuhata and Kayo Yoshida and Yoko Tagawa and Kazumi Hagiwara and Akira Takagi and Tetsuhito Kojima and Motoshi Suzuki and Yoshiko Banno and Yoshinori Nozawa and Takashi Murate",
year = "2009",
month = "9",
day = "1",
language = "English",
volume = "71",
pages = "127--136",
journal = "Nagoya Journal of Medical Science",
issn = "0027-7622",
publisher = "Nagoya University, School of Medicine",
number = "3-4",

}

Gao, S, Murakami, M, Ito, H, Furuhata, A, Yoshida, K, Tagawa, Y, Hagiwara, K, Takagi, A, Kojima, T, Suzuki, M, Banno, Y, Nozawa, Y & Murate, T 2009, 'Mutated ras induced PLD1 gene expression through increased Sp1 transcription factor.', Nagoya Journal of Medical Science, vol. 71, no. 3-4, pp. 127-136.

Mutated ras induced PLD1 gene expression through increased Sp1 transcription factor. / Gao, Siqiang; Murakami, Masashi; Ito, Hiromi; Furuhata, Ayako; Yoshida, Kayo; Tagawa, Yoko; Hagiwara, Kazumi; Takagi, Akira; Kojima, Tetsuhito; Suzuki, Motoshi; Banno, Yoshiko; Nozawa, Yoshinori; Murate, Takashi.

In: Nagoya Journal of Medical Science, Vol. 71, No. 3-4, 01.09.2009, p. 127-136.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Mutated ras induced PLD1 gene expression through increased Sp1 transcription factor.

AU - Gao, Siqiang

AU - Murakami, Masashi

AU - Ito, Hiromi

AU - Furuhata, Ayako

AU - Yoshida, Kayo

AU - Tagawa, Yoko

AU - Hagiwara, Kazumi

AU - Takagi, Akira

AU - Kojima, Tetsuhito

AU - Suzuki, Motoshi

AU - Banno, Yoshiko

AU - Nozawa, Yoshinori

AU - Murate, Takashi

PY - 2009/9/1

Y1 - 2009/9/1

N2 - The underlying mechanisms of oncogene-induced phospholipase D (PLD) activation have not been fully elucidated. The effect of the mutated-ras on PLD mRNA was examined using colon cancer cell lines as well as mock- and mutated ras-transfected NIH3T3 cells. Ras-mutation and activation were correlated, and cells with enhanced ras-activation showed increased PLD1 mRNA and protein. Analysis of the 5' PLD1 promoter using a representative cell line, DLD-1 and also mutated ras-NIH3T3, showed one Sp1-site as the important ras-responsible motif. Spl inhibition with mithramycin A and Spl siRNA inhibited PLD1 protein expression and its promoter activity. Sp1 but not Sp3 protein level and increased Sp1-motif binding activity were correlated with ras activation. Furthermore, overexpression of Sp1 in drosophila SL2 cells lacking Sp family proteins increased PLD1 promoter activity. EMSA and chromatin immunoprecipitation assay confirmed the importance of Sp1 protein binding to the Sp1-motif in ras-induced PLD1 mRNA expression.

AB - The underlying mechanisms of oncogene-induced phospholipase D (PLD) activation have not been fully elucidated. The effect of the mutated-ras on PLD mRNA was examined using colon cancer cell lines as well as mock- and mutated ras-transfected NIH3T3 cells. Ras-mutation and activation were correlated, and cells with enhanced ras-activation showed increased PLD1 mRNA and protein. Analysis of the 5' PLD1 promoter using a representative cell line, DLD-1 and also mutated ras-NIH3T3, showed one Sp1-site as the important ras-responsible motif. Spl inhibition with mithramycin A and Spl siRNA inhibited PLD1 protein expression and its promoter activity. Sp1 but not Sp3 protein level and increased Sp1-motif binding activity were correlated with ras activation. Furthermore, overexpression of Sp1 in drosophila SL2 cells lacking Sp family proteins increased PLD1 promoter activity. EMSA and chromatin immunoprecipitation assay confirmed the importance of Sp1 protein binding to the Sp1-motif in ras-induced PLD1 mRNA expression.

UR - http://www.scopus.com/inward/record.url?scp=73949124424&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=73949124424&partnerID=8YFLogxK

M3 - Article

VL - 71

SP - 127

EP - 136

JO - Nagoya Journal of Medical Science

JF - Nagoya Journal of Medical Science

SN - 0027-7622

IS - 3-4

ER -

Gao S, Murakami M, Ito H, Furuhata A, Yoshida K, Tagawa Y et al. Mutated ras induced PLD1 gene expression through increased Sp1 transcription factor. Nagoya Journal of Medical Science. 2009 Sep 1;71(3-4):127-136.