NTAKα and β isoforms stimulate breast tumor cell growth by means of different receptor combinations

Norihiko Nakano, Shigeki Higashiyama, Kenichi Kajihara, Takeshi Endo, Hiroshi Ishiguro, Kouji Yamada, Toshiharu Nagatsu, Naoyuki Taniguchi

研究成果: Article

12 引用 (Scopus)

抄録

Neural- and thymus-derived activator for ErbB kinases (NTAK) is a recently described member of the neuregulin family that binds directly to ErbB3 and ErbB4 and transactivates ErbB2. Rat NTAK has at least five alternative-spliced isoforms: α1, α2a, α2b, β, and γ. In order to understand their biological properties, this study focused on the NTAKα2a and β isoforms, which have different EGF-like domains. The effect of these isoforms on cell growth and tyrosine phosphorylation in human breast cancer cells, MDA-MB-453 and T47D, was examined using the recombinant proteins. In terms of cell growth, NTAKα2a and NTAKβ preferentially stimulate T47D cells and MDA-MB-453 cells, respectively, in a dose-dependent manner. Although both NTAKs induce the highest level of tyrosine phosphorylation of ErbB2, NTAKα2a and NTAKβ preferentially induce ErbB3 and ErbB4 phosphorylation, respectively. Thus, NTAKα2a and NTAKβ stimulate cell growth in different ways, by means of different combinations of receptors.

元の言語English
ページ(範囲)925-930
ページ数6
ジャーナルJournal of Biochemistry
127
発行部数5
DOI
出版物ステータスPublished - 01-01-2000

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Thymus
Cell growth
Thymus Gland
Tumors
Protein Isoforms
Phosphotransferases
Phosphorylation
Breast Neoplasms
Growth
Tyrosine
Neuregulins
Recombinant Proteins
Epidermal Growth Factor
Rats
Cells

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Nakano, Norihiko ; Higashiyama, Shigeki ; Kajihara, Kenichi ; Endo, Takeshi ; Ishiguro, Hiroshi ; Yamada, Kouji ; Nagatsu, Toshiharu ; Taniguchi, Naoyuki. / NTAKα and β isoforms stimulate breast tumor cell growth by means of different receptor combinations. :: Journal of Biochemistry. 2000 ; 巻 127, 番号 5. pp. 925-930.
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Nakano, N, Higashiyama, S, Kajihara, K, Endo, T, Ishiguro, H, Yamada, K, Nagatsu, T & Taniguchi, N 2000, 'NTAKα and β isoforms stimulate breast tumor cell growth by means of different receptor combinations', Journal of Biochemistry, 巻. 127, 番号 5, pp. 925-930. https://doi.org/10.1093/oxfordjournals.jbchem.a022688

NTAKα and β isoforms stimulate breast tumor cell growth by means of different receptor combinations. / Nakano, Norihiko; Higashiyama, Shigeki; Kajihara, Kenichi; Endo, Takeshi; Ishiguro, Hiroshi; Yamada, Kouji; Nagatsu, Toshiharu; Taniguchi, Naoyuki.

:: Journal of Biochemistry, 巻 127, 番号 5, 01.01.2000, p. 925-930.

研究成果: Article

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T1 - NTAKα and β isoforms stimulate breast tumor cell growth by means of different receptor combinations

AU - Nakano, Norihiko

AU - Higashiyama, Shigeki

AU - Kajihara, Kenichi

AU - Endo, Takeshi

AU - Ishiguro, Hiroshi

AU - Yamada, Kouji

AU - Nagatsu, Toshiharu

AU - Taniguchi, Naoyuki

PY - 2000/1/1

Y1 - 2000/1/1

N2 - Neural- and thymus-derived activator for ErbB kinases (NTAK) is a recently described member of the neuregulin family that binds directly to ErbB3 and ErbB4 and transactivates ErbB2. Rat NTAK has at least five alternative-spliced isoforms: α1, α2a, α2b, β, and γ. In order to understand their biological properties, this study focused on the NTAKα2a and β isoforms, which have different EGF-like domains. The effect of these isoforms on cell growth and tyrosine phosphorylation in human breast cancer cells, MDA-MB-453 and T47D, was examined using the recombinant proteins. In terms of cell growth, NTAKα2a and NTAKβ preferentially stimulate T47D cells and MDA-MB-453 cells, respectively, in a dose-dependent manner. Although both NTAKs induce the highest level of tyrosine phosphorylation of ErbB2, NTAKα2a and NTAKβ preferentially induce ErbB3 and ErbB4 phosphorylation, respectively. Thus, NTAKα2a and NTAKβ stimulate cell growth in different ways, by means of different combinations of receptors.

AB - Neural- and thymus-derived activator for ErbB kinases (NTAK) is a recently described member of the neuregulin family that binds directly to ErbB3 and ErbB4 and transactivates ErbB2. Rat NTAK has at least five alternative-spliced isoforms: α1, α2a, α2b, β, and γ. In order to understand their biological properties, this study focused on the NTAKα2a and β isoforms, which have different EGF-like domains. The effect of these isoforms on cell growth and tyrosine phosphorylation in human breast cancer cells, MDA-MB-453 and T47D, was examined using the recombinant proteins. In terms of cell growth, NTAKα2a and NTAKβ preferentially stimulate T47D cells and MDA-MB-453 cells, respectively, in a dose-dependent manner. Although both NTAKs induce the highest level of tyrosine phosphorylation of ErbB2, NTAKα2a and NTAKβ preferentially induce ErbB3 and ErbB4 phosphorylation, respectively. Thus, NTAKα2a and NTAKβ stimulate cell growth in different ways, by means of different combinations of receptors.

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