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Detection of ret homodimers in MEN 2A-associated pheochromocytomas

M Wada1, N Asai, T Tsuzuki

  • 1Department of Pathology, Nagoya University School of Medicine, Japan.

Insights

Multiple endocrine neoplasia (MEN) 2A mutations activate the c-Ret protein by inducing homodimerization. Ret homodimers were detected in MEN 2A pheochromocytomas, but not sporadic tumors, confirming their presence in original tumors.

Area of Science:

  • Oncology
  • Molecular Biology
  • Genetics

Background:

  • Multiple Endocrine Neoplasia (MEN) 2A is a hereditary cancer syndrome.
  • Activating mutations in the c-Ret proto-oncogene are implicated in MEN 2A.
  • c-Ret protein activation involves disulfide-linked homodimerization.

Purpose of the Study:

  • To investigate the presence of c-Ret homodimers in original human pheochromocytoma tumors.
  • To determine if c-Ret homodimers are associated with MEN 2A-related pheochromocytomas.

Main Methods:

  • Analysis of c-Ret protein expression in eight sporadic and two MEN 2A-associated pheochromocytomas.
  • Immunoprecipitation of c-Ret protein from tumor tissues.
  • In vitro radioactive labeling of immunoprecipitated c-Ret protein with [gamma-32P]ATP.

Main Results:

  • c-Ret protein was expressed in all analyzed pheochromocytomas.
  • Ret homodimers were detected in pheochromocytomas from MEN 2A patients.
  • No Ret homodimers were found in the sporadic pheochromocytoma examined.

Conclusions:

  • This study provides the first evidence of Ret homodimers in original human pheochromocytoma tumors.
  • Ret homodimerization is a key mechanism in the pathogenesis of MEN 2A-associated pheochromocytomas.

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