Role of a putative tyrosine-O-sulfate receptor in the targeting and/or intracellular transport of tyrosine-sulfated proteins.

Cytotechnology
M C LiuM Suiko

Abstract

By employing the affinity gel fraction technique, we have detected a 175 kDa tyrosine-O-sulfate (TyrS)-binding protein in sodium choleate extracts of the microsomal membrane fractions of bovine liver and pancreas, as well as canine liver and pancreas. Western blot analysis revealed the presence of the bovine liver TyrS-binding protein in complexes with tyrosine-sulfated proteins both in vivo and in vitro, suggesting the putative role of the former being the receptor for the latter. Using filter-grown Madin-Darby canine kidney (MDCK) cells as a model, it was demonstrated that the tyrosine-sulfated proteins synthesized were predominantly secreted into the apical medium. The results further indicate the production and differential polarized secretion of different sulfated forms of the two major secretory proteins produced by MDCK cells, fibronectin (FN) and an 80 kDa glycoprotein (gp 80), with their tyrosine-sulfated forms being predominantly secreted from the apical surface. Treatment of filter-grown MDCK cells with glycosylation inhibitors, swainsonine and 1-deoxymannojirimycin, appeared to enhance the apical secretion of tyrosine-sulfated FN and gp 80. A similar 175 kDa membrane-bound 'TyrS receptor', cross-reactive toward anti...Continue Reading

References

Mar 1, 1989·The Journal of Membrane Biology·M SargiacomoE Rodriguez-Boulan
Apr 1, 1986·The Journal of Cell Biology·T A GottliebD D Sabatini
Dec 15, 1986·Biochemical and Biophysical Research Communications·P A Baeuerle, W B Huttner
Dec 1, 1987·The Journal of Cell Biology·P A Baeuerle, W B Huttner
Jan 1, 1988·Annual Review of Physiology·W B Huttner
Jun 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·M C Liu, F Lipmann

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