The C-terminal domain of the adenomatous polyposis coli (Apc) protein is involved in thyroid morphogenesis and function

Atsushi Yokoyama, Ryuji Nomura, Masafumi Kurosumi, Atsushi Shimomura, Takanori Onouchi, Akiko Iizuka-Kogo, Ron Smits, Naohisa Oda, Riccardo Fodde, Mitsuyasu Itoh, Takao Senda

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5 Citations (Scopus)

Abstract

Adenomatous polyposis coli (APC) is a multifunctional protein as well as a tumor suppressor. To determine the functions of the C-terminal domain of Apc, we have investigated Apc 1638T/1638T mice, which express a truncated Apc that lacks the C-terminal domain. Apc 1638T/1638T mice are tumor free and exhibit growth retardation. In the present study, we analyzed the morphology and functions of the thyroid gland in Apc 1638T/1638T mice. There was no significant difference in the basal concentration of serum thyroid hormones between Apc 1638T/1638T and Apc +/+ mice. Thyroid follicle size was significantly larger in Apc 1638T/1638T mice than in Apc +/+ mice. The extent of serum T4 elevation following exogenous thyroid-stimulating hormone (TSH) injection was lower in Apc 1638T/1638T mice than in Apc +/+ mice. TSH also induced a greater reduction in thyroid follicle size in Apc 1638T/1638T mice than in Apc +/+ mice. Analyses using immunohistochemistry and electron microscopy indicated that follicular epithelial cells in Apc 1638T/1638T mice had an enlarged rough endoplasmic reticulum of irregular shape. These results suggest that the C-terminal domain of Apc is involved in thyroid morphology and function.

Original languageEnglish
Pages (from-to)207-212
Number of pages6
JournalMedical Molecular Morphology
Volume44
Issue number4
DOIs
Publication statusPublished - 01-12-2011

All Science Journal Classification (ASJC) codes

  • Pathology and Forensic Medicine
  • Molecular Biology

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    Yokoyama, A., Nomura, R., Kurosumi, M., Shimomura, A., Onouchi, T., Iizuka-Kogo, A., Smits, R., Oda, N., Fodde, R., Itoh, M., & Senda, T. (2011). The C-terminal domain of the adenomatous polyposis coli (Apc) protein is involved in thyroid morphogenesis and function. Medical Molecular Morphology, 44(4), 207-212. https://doi.org/10.1007/s00795-010-0529-9