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, Koji Yamada, Toshiharu Nagatsu, Naoyuki Taniguchi

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)925-930
Number of pages6
JournalJournal of Biochemistry
Volume127
Issue number5
DOIs
Publication statusPublished - 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

Cite this

Nakano, Norihiko ; Higashiyama, Shigeki ; Kajihara, Kenichi ; Endo, Takeshi ; Ishiguro, Hiroshi ; Yamada, Koji ; Nagatsu, Toshiharu ; Taniguchi, Naoyuki. / NTAKα and β isoforms stimulate breast tumor cell growth by means of different receptor combinations. In: Journal of Biochemistry. 2000 ; Vol. 127, No. 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, vol. 127, no. 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, Koji; Nagatsu, Toshiharu; Taniguchi, Naoyuki.

In: Journal of Biochemistry, Vol. 127, No. 5, 01.01.2000, p. 925-930.

Research output: Contribution to journalArticle

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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, Koji

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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