Detection of Ret homodimers in MEN 2A-associated pheochromocytomas

Masaki Wada, Naoya Asai, Toyonori Tsuzuki, Shoichi Maruyama, Mikinao Ohiwa, Tsuneo Imai, Hiroomi Funahashi, Hiroshi Takagi, Masahide Takahashi

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10 Citations (Scopus)


Using transfection of NIH 3T3 cells, we have recently demonstrated that multiple endocrine neoplasia (MEN) 2A mutations activate the c-Ret protein by inducing its disulfide-linked homodimerization on the cell surface. To investigate whether the homodimers are present in original tumors, the expression of the c-Ret protein was analyzed in eight sporadic and two MEN 2A-associated pheochromocytomas, the latter two of which contained mutations in cysteine 618 or 634 of Ret. The c-Ret protein was expressed at variable levels in all pheochromocytomas examined. By labeling the c-Ret protein immunoprecipitated from tumor tissues with [γ-32P]ATP in vitro, its homodimers were detected in pheochromocytomas from MEN 2A patients but not in a sporadic tumor. This result represents the first demonstration of Ret homodimers in original tumors.

Original languageEnglish
Pages (from-to)606-609
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 17-01-1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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