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

  • A Yokoyama
  • , R Nomura
  • , M Kurosumi
  • , A Shimomura
  • , T Onouchi
  • , A Iizuka-Kogo
  • , Ron Smits
  • , N Oda
  • , Riccardo Fodde
  • , M Itoh
  • , T Senda

Research output: Contribution to journalArticleAcademic

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 - 2011

Research programs

  • EMC MM-03-24-01
  • EMC MM-04-20-01

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