No abstract

A tumor of 60 years' duration overlying the sternum of an 87-year-old woman is described. Histologically, the tumor was composed of lobules and cords of epithelial cells with finely granular, eosinophilic cytoplasm. The epithelial nests were floating in large pools of mucinous stroma, separated by thin fibrovascular septa. Cytoplasmic argyrophilia was seen by Grimelius silver stain. Positive reactions of the tumor cells were also found for chromogranin and neuron-specific enolase. Ultrastructural study revealed that the cytoplasm of the tumor cells contained two types of granules: neurosecretory and mucinous. From these findings, the present tumor is considered to be a carcinoid tumor with amphicrine cells, and the term "mucinous carcinoid" of the skin seems to be appropriate for the diagnosis of the present case.

No abstract

UDP-Glucuronosyltransferase (UGT) plays an important role in the metabolism of endogenous and exogenous compounds. UGT is a type I membrane protein, and has a dilysine motif (KKXX/KXKXX) in its C-terminal cytoplasmic domain. Although a dilysine motif is defined as an endoplasmic reticulum (ER) retrieval signal, it remains a matter of debate whether this motif functions in the ER localization of UGT. To address this issue, we generated systematic deletion mutants of UGT2B7, a major human isoform, and compared their subcellular localizations with that of an ER marker protein calnexin (CNX), using subcellular fractionation and immunofluorescent microscopy. We found that although the dilysine motif functioned as the ER retention signal in a chimera that replaced the cytoplasmic domain of CD4 with that of UGT2B7, UGT2B7 truncated mutants lacking this motif extensively colocalized with CNX, indicating dilysine motif-independent ER retention of UGT2B7. Moreover, deletion of the C-terminal transmembrane and cytoplasmic domains did not affect ER localization of UGT2B7, suggesting that the signal necessary for ER retention of UGT2B7 is present in its luminal domain. Serial deletions of the luminal domain, however, did not affect the ER retention of the mutants. Further, a cytoplasmic and transmembrane domain-deleted mutant of UGT2B7 was localized to the ER without being secreted. These results suggest that UGT2B7 could localize to the ER without any retention signal, and lead to the conclusion that the static localization of UGT results from lack of a signal for export from the ER.

No abstract