The plasminogen-like molecule apically secreted by epithelial thyroid cells is sulfated

Biochemical and Biophysical Research Communications

Volumn 346, Issue 3, 2006, Pages 746-750

  Giraud, Annie ^a   Chabaud, Odile ^a   Lejeune, Pierre Jean ^a   Barbaria, Jocelyne ^a   Mallet, Bernard ^a  

^a INSERM   (France)

Author keywords

Plasminogen; Sulfation; Thyroid cells

Indexed keywords

OLIGOSACCHARIDE; PEPTIDE FRAGMENT; PROTEINASE; SERINE PROTEINASE; TYROSINE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING SITE; COMPUTER PROGRAM; ENZYME ACTIVITY; ENZYME RELEASE; EPITHELIUM CELL; MOLECULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN LOCALIZATION; SPECIES IDENTIFICATION; SULFATION; SWINE; THYROID CELL;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL POLARITY; CELLS, CULTURED; CHROMATOGRAPHY, GEL; EPITHELIAL CELLS; HUMANS; MOLECULAR SEQUENCE DATA; OLIGOSACCHARIDES; PLASMINOGEN; SULFATES; SWINE; THYROGLOBULIN; THYROID GLAND; TYROSINE;

EID: 33745212221     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.05.176     Document Type: Article

References (29)

1. Huttner W.B. Tyrosine sulfation and the secretory pathway. Annu. Rev. Physiol. 50 (1988) 363-376
2. Hille A., and Huttner W.B. Occurrence of tyrosine sulfate in proteins-a balance sheet. 2. Membrane proteins. Eur. J. Biochem. 188 (1990) 587-596
3. Hortin G., Fok K.F., Toren P.C., and Strauss A.W. Sulfation of a tyrosine residue in the plasmin-binding domain of alpha 2-antiplasmin. J. Biol. Chem. 262 (1987) 3082-3085
4. Hortin G.L. Sulfation of tyrosine residues in coagulation factor V. Blood 76 (1990) 946-952
5. Dong J.F., Li C.Q., and Lopez J.A. Tyrosine sulfation of the glycoprotein Ib-IX complex: identification of sulfated residues and effect on ligand binding. Biochemistry 33 (1994) 13946-13953
6. Bundgaard J.R., Vuust J., and Rehfeld J.F. Tyrosine O-sulfation promotes proteolytic processing of progastrin. EMBO J. 14 (1995) 3073-3079
7. Niehrs C., Beisswanger R., and Huttner W.B. Protein tyrosine sulfation, 1993-an update. Chem. Biol. Interact. 92 (1994) 257-271
8. Strott C.A. Sulfonation and molecular action. Endocr. Rev. 23 (2002) 703-732
9. Kehoe J.W., and Bertozzi C.R. Tyrosine sulfation: a modulator of extracellular protein-protein interactions. Chem. Biol. 7 (2000) R57-R61
10. Herzog V. Secretion of sulfated thyroglobulin. Eur. J. Cell Biol. 39 (1986) 399-409
11. Spiro R.G., and Bhoyroo V.D. Occurrence of sulfate in the asparagine-linked complex carbohydrate units of thyroglobulin. Identification and localization of galactose 3-sulfate and N-acetylglucosamine 6-sulfate residues in the human and calf proteins. J. Biol. Chem. 263 (1988) 14351-14358
12. 35S]sulfate: incorporation into chondroitin 6-sulfate and endoglycosidase-F-susceptible carbohydrate units. Endocrinology 122 (1988) 2428-2435
13. Kamerling J.P., Rijkse I., Maas A.A., van Kuik J.A., and Vliegenthart J.F. Sulfated N-linked carbohydrate chains in porcine thyroglobulin. FEBS Lett. 241 (1988) 246-250
14. Nlend M.C., Cauvi D., Venot N., Desruisseau S., and Chabaud O. Thyrotropin regulates tyrosine sulfation of thyroglobulin. Eur. J. Endocrinol. 141 (1999) 61-69
15. Venot N., Nlend M.C., Cauvi D., and Chabaud O. The hormonogenic tyrosine 5 of porcine thyroglobulin is sulfated. Biochem. Biophys. Res. Commun. 298 (2002) 193-197
16. Nlend M.C., Cauvi D., Venot N., and Chabaud O. Sulfated tyrosines of thyroglobulin are involved in thyroid hormone synthesis. Biochem. Biophys. Res. Commun. 262 (1999) 193-197
17. Nlend M.C., Cauvi D.M., Venot N., and Chabaud O. Role of sulfated tyrosines of thyroglobulin in thyroid hormonosynthesis. Endocrinology 146 (2005) 4834-4843
18. Giraud A., Dicristofaro J., De Micco C., Lejeune P.J., Barbaria J., and Mallet B. A plasminogen-like protein, present in the apical extracellular environment of thyroid epithelial cells, degrades thyroglobulin in vitro. Biochem. Biophys. Res. Commun. 338 (2005) 1000-1004
19. Chambard M., Mauchamp J., and Chabaud O. Synthesis and apical and basolateral secretion of thyroglobulin by thyroid cell monolayers on permeable substrate: modulation by thyrotropin. J. Cell Physiol. 133 (1987) 37-45
20. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
21. Blode H., Heinrich T., and Diringer H. A quantitative assay for tyrosine sulfation and tyrosine phosphorylation in peptides. Biol. Chem. Hoppe Seyler 371 (1990) 145-151
22. Heinemann F.S., Korza G., and Ozols J. A plasminogen-like protein selectively degrades stearoyl-CoA desaturase in liver microsomes. J. Biol. Chem. 278 (2003) 42966-42975
23. Monigatti F., Gasteiger E., Bairoch A., and Jung E. The sulfinator: predicting tyrosine sulfation sites in protein sequences. Bioinformatics 18 (2002) 769-770
24. Rejante M.R., and Llinas M. Solution structure of the epsilon-aminohexanoic acid complex of human plasminogen kringle 1. Eur. J. Biochem. 221 (1994) 939-949
25. Rejante M.R., and Llinas M. 1H-NMR assignments and secondary structure of human plasminogen kringle 1. Eur. J. Biochem. 221 (1994) 927-937
26. Koeller K.M., Smith M.E., and Wong C.H. Chemoenzymatic synthesis of PSGL-1 glycopeptides: sulfation on tyrosine affects glycosyltransferase-catalyzed synthesis of the O-glycan. Bioorg. Med. Chem. 8 (2000) 1017-1025
27. Meh D.A., Siebenlist K.R., Brennan S.O., Holyst T., and Mosesson M.W. The amino acid sequence in fibrin responsible for high affinity thrombin binding. Thromb. Haemost. 85 (2001) 470-474
28. Dong J., Ye P., Schade A.J., Gao S., Romo G.M., Turner N.T., McIntire L.V., and Lopez J.A. Tyrosine sulfation of glycoprotein I(b)alpha. Role of electrostatic interactions in von Willebrand factor binding. J. Biol. Chem. 276 (2001) 16690-16694
29. Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P., Gerwig G.J., van Halbeek H., and Vliegenthart J.F. The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns. Eur. J. Biochem. 173 (1988) 57-63