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K Ohta, T Endo, K Gunji, and T Onaya


We have cloned a cDNA whose mRNA levels are increased in malignantly transformed rat thyroid FRTL cells (FRTL-Tc cells). We constructed a cDNA library from FRTL-Tc cells in λgt10 and screened the cDNAs by differential plaque filter hybridization. Twenty-five thousand clones were screened and one cDNA (C140) was selected which corresponded to a mRNA whose expression was 5·8 times higher in FRTL-Tc cells than in FRTL cells. A 0·8 kb specific C140 mRNA was detected by Northern blot analysis of FRTL-Tc and FRTL mRNAs. The C140 cDNA was sequenced and found to encode a protein of 227 amino acids.

We have found that C140 mRNA is conserved in human thyroid cells, but it is encoded by a smaller 0·7 kb transcript. C140 mRNA was highly expressed in neoplastic thyroid tissues and weakly in normal thyroid tissues in the same patients. Additionally, we found that C140 mRNA was also increased in the thyroid tissue of a patient with Graves' disease. These results suggest that C140 expression might be higher in rapidly growing thyroid cells than in normal cells, and might provide a new aspect for the study of thyroid tumours.

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K Haraguchi, T Saito, M Kaneshige, T Endo, and T Onaya


To understand the functional significance of the carboxy-terminal half of the intracellular region of the human TSH receptor (hTSHR), a mutant hTSHR lacking amino acids from the carboxyterminal to His726 was constructed.

Wild type hTSHR cDNA and truncated hTSHR cDNA were subcloned into a eukaryotic expression vector, pRc/CMV, and transfected into Chinese hamster ovary cells to obtain cell lines which stably expressed hTSHRs at high levels. This allowed us to observe highly efficient coupling of hTSHR and adenylyl cyclase as well as desensitization and internalization of hTSHR.

Despite the differences in potential phosphorylation sites and internalization signals, dose-dependent stimulation of adenylyl cyclase by TSH, TSH-dependent desensitization and the rate of hTSHR internalization were similar for wild type and truncated hTSHRs. We conclude that the carboxy-terminal half of the intracellular region of hTSHR does not have a major functional role in TSH-dependent signal transduction.