Stability of tyrosine sulfate in acidic solutions

Analytical Biochemistry

Volumn 363, Issue 1, 2007, Pages 70-76

  Balsved, Dorte ^a   Bundgaard, Jens R ^a   Sen, Jette W ^a  

^a Mental Health Services CPH   (Denmark)

Author keywords

Acid lability; Activation energy; Gastrins; Hydrogen ion concentration; Peptide hormones; Stability; Tyrosine O sulfation

Indexed keywords

ACTIVATION ENERGY; CONVERGENCE OF NUMERICAL METHODS; HORMONES; HYDROLYSIS; PEPTIDES; PH; PURIFICATION; SULFUR COMPOUNDS;

ACTIVATION ENERGIES (EA); AQUEOUS ACIDIC SOLUTION; GASTRINS; PEPTIDE HORMONES; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN PURIFICATION; SEQUENCING OF PEPTIDES; TYROSINE O SULFATIONS;

AMINO ACIDS;

ACETIC ACID; CERULETIDE; GASTRIN 17; PEPTIDE; TYROSINE SULFATE;

ACIDITY; ARTICLE; EUKARYOTE; GOLGI COMPLEX; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN SECRETION; SULFATION;

EUKARYOTA;

EID: 33847418755     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.12.003     Document Type: Article

References (34)

1. Ouyang Y., Lane W.S., and Moore K.L. Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins. Proc. Natl. Acad. Sci. USA 95 (1998) 2896-2901
2. Niehrs C., and Huttner W.B. Purification and characterization of tyrosylprotein sulfotransferase. EMBO J. 9 (1990) 35-42
3. Ouyang Y.B., and Moore K.L. Molecular cloning and expression of human and mouse tyrosylprotein sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in Caenorhabditis elegans. J. Biol. Chem. 273 (1998) 24770-24774
4. Beisswanger R., Corbeil D., Vannier C., Thiele C., Dohrmann U., Kellner R., Ashman K., Niehrs C., and Huttner W.B. Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2. Proc. Natl. Acad. Sci. USA 95 (1998) 11134-11139
5. Suiko M., Fernando P.H., Sakakibara Y., Nakajima H., Liu M.C., Abe S., and Nakatsu S. Post-translational modification of protein by tyrosine sulfation: active sulfate PAPS is the essential substrate for this modification. Nucleic Acids Symp. Ser. (1992) 183-184
6. Lee R.W., and Huttner W.B. (Glu62, Ala30, Tyr8)n serves as high-affinity substrate for tyrosylprotein sulfotransferase: a Golgi enzyme. Proc. Natl. Acad. Sci. USA 82 (1985) 6143-6147
7. Baeuerle P.A., and Huttner W.B. Tyrosine sulfation is a trans-Golgi-specific protein modification. J. Cell Biol. 105 (1987) 2655-2664
8. Lee R.W., and Huttner W.B. Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase. J. Biol. Chem. 258 (1983) 11326-11334
9. Hortin G.L., Farries T.C., Graham J.P., and Atkinson J.P. Sulfation of tyrosine residues increases activity of the fourth component of complement. Proc. Natl. Acad. Sci. USA 86 (1989) 1338-1342
10. Leyte A., van Schijndel H.B., Niehrs C., Huttner W.B., Verbeet M.P., Mertens K., and van Mourik J.A. Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor. J. Biol. Chem. 266 (1991) 740-746
11. Jensen R.T., Lemp G.F., and Gardner J.D. Interactions of COOH-terminal fragments of cholecystokinin with receptors on dispersed acini from guinea pig pancreas. J. Biol. Chem. 257 (1982) 5554-5559
12. Sako D., Comess K.M., Barone K.M., Camphausen R.T., Cumming D.A., and Shaw G.D. A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. Cell 83 (1995) 323-331
13. Pouyani T., and Seed B. PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. Cell 83 (1995) 333-343
14. Fong A.M., Alam S.M., Imai T., Haribabu B., and Patel D.D. CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion. J. Biol. Chem. 277 (2002) 19418-19423
15. Costagliola S., Panneels V., Bonomi M., Koch J., Many M.C., Smits G., and Vassart G. Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors. EMBO J. 21 (2002) 504-513
16. Farzan M., Mirzabekov T., Kolchinsky P., Wyatt R., Cayabyab M., Gerard N.P., Gerard C., Sodroski J., and Choe H. Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry. Cell 96 (1999) 667-676
17. Bundgaard J.R., Vuust J., and Rehfeld J.F. Tyrosine O-sulfation promotes proteolytic processing of progastrin. EMBO J. 14 (1995) 3073-3079
18. Friederich E., Fritz H.J., and Huttner W.B. Inhibition of tyrosine sulfation in the trans-Golgi retards the transport of a constitutively secreted protein to the cell surface. J. Cell Biol. 107 (1988) 1655-1667
19. Baeuerle P.A., and Huttner W.B. Inhibition of N-glycosylation induces tyrosine sulphation of hybridoma immunoglobulin G. EMBO J. 3 (1984) 2209-2215
20. Hille A., Rosa P., and Huttner W.B. Tyrosine sulfation: a post-translational modification of proteins destined for secretion?. FEBS Lett. 177 (1984) 129-134
21. Huttner W.B. Determination and occurrence of tyrosine O-sulfate in proteins. Methods Enzymol. 107 (1984) 200-223
22. Yagami T., Kitagawa K., Aida C., Fujiwara H., and Futaki S. Stabilization of a tyrosine O-sulfate residue by a cationic functional group: formation of a conjugate acid-base pair. J. Pept. Res. 56 (2000) 239-249
23. Hengge A.C. Isotope effects in the study of phosphoryl and sulfuryl transfer reactions. Accounts Chem. Res. 35 (2002) 105-112
24. Benkovic S.J., and Benkovic P.A. Studies on sulfate esters I: nucleophilic reactions of amines with P-nitrophenyl sulfate. J. Am. Chem. Soc. 88 (1966) 5504-&
25. Fendler E.J., and Fendler J.H. Hydrolysis of nitrophenyl and dinitrophenyl sulfate esters. J. Organ. Chem. 33 (1968) 3852
26. Hoff R.H., Larsen P., and Hengge A.C. Isotope effects and medium effects on sulfuryl transfer reactions. J. Am. Chem. Soc. 123 (2001) 9338-9344
27. Kice J.L., and Anderson J.M. Mechanism of acid hydrolysis of sodium aryl sulfates. J. Am. Chem. Soc. 88 (1966) 5242
28. Davis J.M., Cameron D.R., Kubanek J.M., Mizuyabu L., and Thatcher G.R.J. Acceleration of sulfate ester hydrolysis in hydrophobic environments. Tetrahedr. Lett. 32 (1991) 2205-2206
29. Gorman G.S., Speir J.P., Turner C.A., and Amster I.J. Proton affinities of the 20 common alpha-amino-acids. J. Am. Chem. Soc. 114 (1992) 3986-3988
30. Bundgaard J.R., Cowland J.B., Vuust J., and Rehfeld J.F. An efficient cellular system for mutational analysis of prohormone processing. DNA Cell Biol. 15 (1996) 147-157
31. Guthrie J.P. Free-energy of formation of sulfur-trioxide in aqueous-solution-methods for determining the energy-level of an unobservable intermediate. J. Am. Chem. Soc. 102 (1980) 5177-5180
32. D.R. Lide, CRC Handbook of Chemistry and Physics, Eightieth ed., 1999-2000.
33. Chesnut D.B., and Quin L.D. Nature of bonding in the sulfuryl group. J. Comput. Chem. 25 (2004) 734-738
34. Baeuerle P.A., and Huttner W.B. Tyrosine sulfation of yolk proteins 1, 2, and 3 in Drosophila melanogaster. J. Biol. Chem. 260 (1985) 6434-6439