Receptor protein tyrosine kinase DDR is up-regulated by p53 protein

Shirou Sakuma, Hideyuki Saya, Mitsuhiro Tada, Mitsuyoshi Nakao, Toshiyoshi Fujiwara, Jack A. Roth, Yutaka Sawamura, Yumiko Shinohe, Abe Hiroshi

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

We have previously reported on radiation-induction of ptk-3 in rat astr ocyte culture [Sakuma et al. (1995) Radiat. Res. 143, 1-7]. Ptk-3 was considered to be a rat version of human DDR (discoidin domain receptor). We cloned and analyzed genomic DNA of the DDR and its promoter region. We discovered that the promoter region contained a consensus sequence of the p53 tumor suppressor binding site. Adenovirus-mediated p53 transfection induced a high level of DDR mRNA in SAOS2 human osteosarcoma cells. These results indicate that DDR is up-regulated by the p53 protein.

Original languageEnglish
Pages (from-to)165-169
Number of pages5
JournalFEBS Letters
Volume398
Issue number2-3
DOIs
Publication statusPublished - Dec 2 1996

Keywords

  • Genomic DNA structure
  • Human DDR gene
  • p53 regulatory element

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Sakuma, S., Saya, H., Tada, M., Nakao, M., Fujiwara, T., Roth, J. A., Sawamura, Y., Shinohe, Y., & Hiroshi, A. (1996). Receptor protein tyrosine kinase DDR is up-regulated by p53 protein. FEBS Letters, 398(2-3), 165-169. https://doi.org/10.1016/S0014-5793(96)01234-3