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Department of Pharmacology and Physiology and the Cancer Center,
University of Rochester School of Medicine and Dentistry, Rochester,
New York 14642
The localization of an epitope-tagged receptor for
thyrotropin-releasing hormone (TRH) expressed in different cell
contexts was studied with immunofluorescence microscopy. In pituitary
lactotrophs, which normally express TRH receptors, and in AtT20
pituitary corticotrophs, TRH receptor immunoreactivity was primarily
confined to the plasma membrane. In HEK 293 and COS7 cells, TRH
receptors were predominantly intracellular. In transiently transfected
COS7 cells, the TRH receptor colocalized with endoplasmic reticulum and
Golgi markers. The pattern of TRH receptor immunofluorescence was the
same over a wide range of receptor expression in transiently
transfected COS7 cells, and all cell lines bound similar amounts of
3H- and rhodamine-labeled TRH analogs, suggesting that
cell-specific differences in TRH receptor localization were not simply
the result of overexpression. In all cell contexts, TRH receptors on
the plasma membrane underwent extensive ligand-driven endocytosis. Inhibitors of glycosylation did not alter the subcellular distribution of receptors. In HEK 293 cells expressing the transfected TRH receptor,
protein synthesis inhibitors caused translocation of intracellular
receptors to the cell surface, as shown by a marked increase in cell
surface immunofluorescence and
[3H][N3-methyl-His2]TRH
binding. These results demonstrate that the subcellular localization of
the TRH receptor depends on the cell context in which it is expressed
and that intracellular receptors are capable of translocation to the
plasma membrane.
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