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J. Biol. Chem., Vol. 275, Issue 41, 31946-31953, October 13, 2000

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Cell Type-dependent Differences in Thyroid Peroxidase Cell Surface Expression^*

Xiaoqing Zhang^§ and Peter Arvan^§¶

From the  Division of Endocrinology and ^§ Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York 10461

Recently, it has been suggested that only ~2% of human thyroid peroxidase (hTPO₉₃₃) reaches the surface of stably transfected (Chinese hamster ovary) cells, most being degraded intracellularly, and this might be representative of thyroid peroxidase (TPO) behavior in thyrocytes (Fayadat, L., Siffroi-Fernandez, S., Lanet, J., and Franc, J.-L. (2000) J. Biol. Chem. 275, 15948-15954). In agreement, in stably transfected Madin-Darby canine kidney clones, nonpermeabilized cells exhibit wild-type hTPO₉₃₃ immunofluorescence (apically) on <10% of that found in permeabilized cells, where an endoplasmic reticulum pattern is observed. Further, a C-terminally truncated, membrane-anchorless hTPO₈₄₈ is also retained in the endoplasmic reticulum of stably transfected Madin-Darby canine kidney cells. However, by contrast, in Chinese hamster ovary cells after transient transfection, hTPO₉₃₃ immunofluorescence is detected equally well in nonpermeabilized and permeabilized cells, indicating that a large portion of hTPO₉₃₃ is present at the cell surface; furthermore, hTPO₈₄₈ is efficiently secreted. Further, using an antiserum not cross-reacting with rat TPO, we find by immunofluorescence that in stable clones of PC Cl3 (rat) thyrocytes, considerably more (~50%) of the cells exhibit hTPO₉₃₃ at the cell surface. However, cell surface biotinylation and endoglycosidase H digestion assays appear to under-represent the extent of hTPO₉₃₃ transport, presumably because protein folding limits both Golgi carbohydrate modification and accessibility of lysines in the extracellular domain. We conclude that cell type-specific factors may facilitate stable expression of TPO at the cell surface of thyrocytes.

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