Intracellular transport, sorting, and proteolytic processing of regulated secretory proteins does not require protein sulfation

Molecular and Cellular Endocrinology

Volumn 136, Issue 1, 1998, Pages 29-35

  Van Kuppeveld, Frank J M ^a   Van Horssen, A Martin ^a   Martens, Gerard J M ^a  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

Author keywords

Protein sulfation; Regulated secretory pathway; Xenopus laevis

Indexed keywords

APOMORPHINE; CHLORATE; FURIN; PROOPIOMELANOCORTIN; SECRETOGRANIN III; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; HYPOPHYSIS; HYPOPHYSIS INTERMEDIATE LOBE; INTRACELLULAR TRANSPORT; PRIORITY JOURNAL; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; SULFATION; XENOPUS LAEVIS;

ANIMALS; APOMORPHINE; BIOLOGICAL TRANSPORT; CHLORATES; CHROMOGRANINS; DOPAMINE AGONISTS; FURIN; METHIONINE; ORGAN CULTURE TECHNIQUES; PITUITARY GLAND; PRO-OPIOMELANOCORTIN; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEINS; SUBTILISINS; SULFATES; XENOPUS LAEVIS;

EID: 0344157833     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(97)00211-6     Document Type: Article

References (38)

1. Anderson R.G.W., Stadil F. Sulfation of gastrin in Zollinger-Ellison sera: Evidence for association between sulfation and proteolytic processing. Regul. Pept. 6:1983;231-239.
2. Baeuerle P.A., Huttner W.B. Chlorate-A potent inhibitor of protein sulfation in intact cells. Biochem. Biophys. Res. Commun. 141:1986;870-877.
3. Baeuerle P.A., Lottspeich F., Huttner W.B. Purlfication of yolk protein 2 of Drosophila melanogaster and identification of its site of tyrosine sulfation. J. Biol. Chem. 263:1988;14925-14929.
4. Bodanszky M., Martinez J., Priestley G.P., Gardner J.D., Mutt V. Cholecystokinin (pancreozymin). 4. Synthesis and properties of a biologically active analogue of the C-terminal heptapeptide with epsilon-hydroxynorleucine sulfate replacing tyrosine sulfate. J. Med. Chem. 21:1978;1030-1035.
5. Braks J.A.M., Martens G.J.M. 7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway. Cell. 78:1994;263-273.
6. Braks J.A.M., Goldenmond K.C.W., van Riel M.C.H.M., Coenen A.J.M., Martens G.J.M. Structure and expression of Xenopus prohormone convertase PC2. FEBS Lett. 305:1992;45-50.
7. Burgess T.L., Kelly R.B. Constitutive and regulated secretion of proteins. Annu. Rev. Cell. Biol. 3:1987;243-293.
8. Chanat E., Huttner W.B. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell. Biol. 115:1991;1505-1519.
9. fat mice. Cell. 88:1997;73-83.
10. Fricker L.D. Carboxypeptidase E. Annu. Rev. Physiol. 50:1988;309-321.
11. Friederich E., Fritz H.J., 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.
12. Holthuis J.C.M., Martens G.J.M. The neuroendocrine proteins secretogranin II and III are regionally conserved and coordinately expressed with proopiomelanocortin in Xenopus intermediate pituitary. J. Neurochem. 66:1996;2248-2256.
13. Holthuis J.C.M., Jansen E.J.R., van Riel M.C.H.M., Martens G.J.M. Molecular probing of the secretory pathway in peptide hormone-producing cells. J. Cell. Sci. 108:1995;3295-3305.
14. Holthuis J.C.M., Jansen E.J.R., Martens G.J.M. Secretogranin III is a sulfated protein undergoing proteolytic processing in the regulated secretory pathway. J. Biol. Chem. 271:1996;17755-17760.
15. 35S]sulfate. Proc. Natl. Acad. Sci. USA. 78:1981;7468-7472.
16. Hortin G.L., Farries T.C., Graham J.P., Atkinson J.P. Sulfation of tyrosine residues increases activity of the fourth component of complement. Proc. Natl. Acad. Sci. USA. 86:1989;1338-1342.
17. Huttner W., Niehrs C., Vannier C. Bind or bleed. Curr. Biol. 1:1991;309-310.
18. Huttner W.B., Gerdes H.H., Rosa P. The granin (chromogranin/secretogranin) family. Trends Biochem. Sci. 16:1991;27-30.
19. Huttner W.B. Tyrosine sulfation and the secretory pathway. Annu. Rev. Physiol. 50:1988;363-376.
20. Jenks B.G., Leenders H.J., Martens G.J.M., Roubos E.W. Adaptation physiology: the functioning of pituitary melanotrope cells during background adaptation of the amphibian Xenopus laevis. Zool. Sci. 10:1993;1-11.
21. Jensen S.L., Rehfeld J.F., Holst J.J., Fahrenkrug J., Nielsen O.V., Schaffalitzky de Muckadell O.B. Secretory effects of gastrins on isolated porcine pancreas. Am. J. Physiol. 238:1980;186-192.
22. Kelly R.B. Pathways of protein secretion in eucaryotes. Science. 230:1985;25-32.
23. Kornfeld S. Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors. Annu. Rev. Biochem. 61:1992;307-330.
24. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
25. 1680 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.
26. Lodish H.F., Kong N. Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex. J. Cell. Biol. 98:1984;1720-1729.
27. Martens G.J.M., Jenks B.G., van Overbeeke A.P. Microsuperfusion of neurointermediate lobes of Xenopus laevis: concomitant and coordinately controlled release of newly synthesized peptides. Comp. Biochem. Physiol. 69:1981;75-82.
28. Mian N., Anderson G.E., Kent P.W. Neuroaminidase inhibition by chemically sulfated glycopeptides. Biochem. J. 181:1979;377-385.
29. Niehrs C., Huttner W.B. Purlfication and characterization of tyrosylprotein sulfotransferase. EMBO J. 9:1990;35-42.
30. Parsons T.F., Pierce J.G. Oligosaccharide moieties of glycoprotein hormones: bovine lutropin resists enzymatic deglycosylation because of terminal O-sulfated N-acetyl-hexosamines. Proc. Natl. Acad. Sci. USA. 77:1980;7089-7093.
31. Ragg H., Uhlshofer T., Gerewitz J. Glycosaminoglycan-mediated leuserpin-2/thrombin interaction. Structure-function relationships. J. Biol. Chem. 265:1990;22386-22391.
32. Song L., Fricker L.D. Calcium- and pH-dependent aggregation of carboxypeptidase E. J. Biol. Chem. 270:1995;7963-7967.
33. Stone S.R., Hofsteenge J. Kinetics of the inhibition of thrombin by hirudin. Biochemistry. 25:1986;4622-4628.
34. Suiko M., Liu M.C. Change in binding affinities of 3Y1 secreted fibronectin upon desulfation of tyrosine-O-sulfate. Biochem. Biophys. Res. Commun. 154:1988;1094-1098.
35. Tooze S.A., Huttner W.B. Cell-free sorting to the regulated and constitutive secretory pathways. Cell. 60:1990;837-847.
36. Unsworth C.D., Hughes J., Morley J.S. O-sulphated leu-enkephalin in brain. Nature. 295:1982;519-522.
37. Vannier C., Huttner W.B. Expression of tyrosine-sulfated secretory proteins in Xenopus laevis oocytes. Differential export of constitutive and regulated proteins. Eur. J. Biochem. 239:1996;111-116.
38. 2+-dependent aggregation property of secretory vesicle matrix proteins and the potential role of chromogranins A and B in secretory vesicle biogenesis. J. Biol. Chem. 271:1996;1558-1565.