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首页> 外文期刊>American Journal of Dermatopathology >Immunohistochemical Localization of Phosphorylated and Unphosphorylated Form of β-catenin With Regard to Shadow Cell and Squamous Differentiation in Cutaneous Pilomatricoma.
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Immunohistochemical Localization of Phosphorylated and Unphosphorylated Form of β-catenin With Regard to Shadow Cell and Squamous Differentiation in Cutaneous Pilomatricoma.

机译：Immunohistochemical Localization of Phosphorylated and Unphosphorylated Form of β-catenin With Regard to Shadow Cell and Squamous Differentiation in Cutaneous Pilomatricoma.

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Pilomatricoma usually contains a mutation in CTNNB1 that encodes β-catenin (BC). It also shows nuclear accumulation of BC protein, which plays an important role in tumorigenesis of pilomatricoma. In vitro studies have indicated that mutant BC protein is unphosphorylated and shows nuclear accumulation, but this theory has not been confirmed in various tumors with CTNNB1 mutation. We examined immunohistochemical localization of phosphorylated BC (pBC) and unphosphorylated BC (npBC) with regard to the modes of cell death or differentiation in 25 cases of pilomatricoma. As for the component showing shadow cell differentiation, BC was detected in cytoplasm/nucleus and along cell membrane in basaloid cells, whereas only in the latter in transitional cells in all cases. Meanwhile, npBC was localized along cell membrane of transitional cells, but not in basaloid cells, nor in nucleus of any components. The components with squamous differentiation also revealed the staining patterns similar to those seen in shadow cell differentiation in some cases. pBC was found in some cell fragments in the amorphous debris containing apoptotic bodies among shadow cell nests. These results suggested that npBC plays an important role in cell adhesion during differentiation and that pBC expression is associated with apoptosis of basaloid cells in pilomatricoma. BC accumulated in the nucleus was not immunoreactive for npBC possibly due to post-translational modification or conformational changes that resulted in loss of or masked antigenicity when BC is assumed to be unphosphorylated.

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