Trafficking of the vasopressin and oxytocin prohormone through the regulated secretory pathway

Journal of Neuroendocrinology

Volumn 12, Issue 6, 2000, Pages 589-594

  De Bree, F M ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

Oxytocin; Sorting; Trafficking; Vasopressin

Indexed keywords

HORMONE PRECURSOR; OXYTOCIN; VASOPRESSIN;

CONTROLLED STUDY; ENDOPLASMIC RETICULUM; HORMONE RELEASE; HORMONE TRANSPORT; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN FOLDING; REVIEW;

AMINO ACID SEQUENCE; ANIMALS; HUMANS; NEUROPHYSINS; OXYTOCIN; PROTEIN FOLDING; PROTEIN PRECURSORS; VASOPRESSINS;

EID: 0034026833     PISSN: 09538194     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2826.2000.00521.x     Document Type: Review

References (42)

1. De Bree FM, Burbach JPH. Structure-function relationships of the vasopressin prohormone domains. Cell Mol Neurobiol 1998; 18: 173-191.
2. Kim JK, Summer SN, Wood WM, Brown JL, Schrier RW. Arginine vasopressin secretion with mutants of wild-type and Brattleboro rats AVP gene. J Am Soc Nephrol 1997; 8: 1863-1869.
3. Huang HB, Breslow E. Identification of the unstable neurophysin tlisulfide and localisation to the hormone-binding site J Biol Chem 1992; 267: 6750-6756.
4. Breslow E, Burman S. Molecular, thermodynamic, and biological aspects of recognition and function in neurophysin-hormone systems; a model system for the analysis of protein peptide interactions. Adv Enzymol 1990; 63: 1-67.
5. Acher R, Light A, DuVigneaud V. Purification of oxytocin and vasopres sin by way of a protein complex. J Biol Chem 1958; 233: 116-120.
6. Dreifuss JJ. A review on neurosecretory granules; their contents and mechanisms of release. Ann NY Acad Sci 1975; 248: 184-201.
7. Kanmera T, Chaiken IM. Molecular properties of the oxytocin/bovine neurophysin biosynthetic precursor. J Biol Chem 1985; 260; 8474-8482.
8. Chaiken IM, Tamaoki H, Brownstein MJ, Gainer H. Onset of neurophysin self-association upon neurophysin/neuropeptide hormone precursor biosynthesis. FEBS Lett 1983; 164: 361-365.
9. De Bree FM, Burbach JPH. Heterologous biosynthesis and processing of preprovasopressin in Neuro2A neuroblastoma cells. Biochimie 1994; 76: 265-270.
10. Brakch N, Boileau G, Simonetti M, Nault C. Joseph-Bravo P, Rholam M, Cohen P. Prosomatostatin processing in Neuro2A cells. Role of beta-turn structure in the vicinity of the Arg-Lys cleavage site. Eur J Biochem 1993; 216: 39-47.
11. Tam WWH, Andreasson Kl, Loh YP. The amino-terminal sequence of pro-opiomelanocortin directs intracellular targeting to the regulated secretory pathway. Eur J Cell Biol 1993; 62: 294-306.
12. Burbach JP, Van Schaick HS, De Bree FM, Lopes da Silva S, Adan RA. Functional domains in the oxytocin gene for regulation of expression and biosynthesis of gene products. Adv Exp Med Biol 1995; 395: 9-21.
13. Nijenhuis M, ZaIm R, Burbach JPH. Mutations in the vasopressin prohormone involved in diabetes insipidus impair endoplasmic reticulum export but not sorting. J Biol Chem 1999; 274: 21200-21208.
14. Ito M, Jameson JL, Ito M. Molecular basis of autosomal dominant neurohypophyseal diabetes insipidus. Cellular toxicity caused by the accumulation of mutant vasopressin precursors within the endoplasmic reticulum. J Clin Invest 1997; 99: 1897-1905.
15. Rittig S, Siggaard C, Ozata M. Yetkin I, Gundagon MA, Robertson GL, Pedersen EB. In: Abstracts of the 1997 World Congress on Neurohypophysioal Hormones. Montreal, Canada, 1997: no. 40.
16. Nagasaki H, Ito M, Yuasa H. Saito H, Fukase M, Hamada K, Ishikawa E, Katakami H, Oiso Y. Two novel mutations in the coding region for neurophysin-II associated with familial central diabetes insipidus. J Clin Endocrinol Metabol 1995; 80: 1352-1356.
17. Yuasa H, Ito M, Nagasaki H, Oiso Y, Miyamoto S, Sasaki N, Saito H. Glu-47, which forms a salt bridge between neurophysin-II and arginine vasopressin, is deleted in patients with familial central diabetes insipidus. J Clin Endocrinol Metabol 1993; 77: 600-604.
18. Chen L, Rose JP, Breslow E, Yang D. Chang WR, Furey WF Jr, Sax M, Wang BC. Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 Å determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom. Proc Natl Acad Sci USA 1991; 88: 4240-4244.
19. Rose JP, Wu CK, Hsiao CD, Breslow E, Wang BC. Crystal structure of the neurophysin-oxytocin complex. Nature Struct Biol 1995; 3: 163-169.
20. Schmale H, Richter D. Single base deletion in the vasopressin gene is the cause of diabetes insipidus in Brattleboro rats. Nature 1984; 308: 705-709.
21. Schmale H, Borowiak B, Holtgreve-Grez H, Richter D. Impact of altered protein structures on the intracellular traffic of a mutated vasopressin precursor from Brattleboro rats. Eur J Biochem 1989; 182: 621-627.
22. Morris JF, Budd TC, Epton MJ, Ma D, Pow DV, Wang H. Functions of the perikaryon and dendrites in magnocellular vasopressin-secreting neurons: new insights from ultrastructural studies. In: Urban IJA, Burbach JPH, De Wied D. eds. Progress in Brain Research. Amsterdam: Elsevier Science. 1998
23. Evans DAP, Van der Kleij AAM, Sonnemans MAF, Burbach JPH, Van Leeuwen FW. Frameshift mutations at two hotspots in vasopressin transcripts in post-mitotic neurons. Proc Natl Acad Sci USA 1994; 91: 6059-6063.
24. Evans DAP, De Bree FM, Nijenhuis M, Van der Kleij AAM, ZaIm R, Korteweg N, Van Leeuwen FW, Burbach JPH. Processing of frameshifted vasopressin precursors. J Neuroendocrinol, in press.
25. Deeb R, Breslow E. Thermodynamic role of the pro region of the neurophysin precursor in neurophysin folding: evidence from the effects of ligand peptides on folding. Biochemstry 1996; 35: 864-873.
26. Zhu X, Ohta Y, Jordan F. lnouye M. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolccular process. Nature 1989; 339: 483-484.
27. Shinde U, Inouye M. Intramolecular chaperones and protein folding. TIBS 1993; 18: 442-445.
28. Baker D. Sohl JL, Agard DA. A protein-folding reaction under kinetic control. Nature 1992; 356: 263-265.
29. Weissman JS, Kim PS. The pro region of BPTI facilitates folding. Cell 1992; 71: 841-851.
30. Hurtlcy SM, Helenius A. Protein oligomerization in the endoplasmic reticulum. Anna Rev Cell Biol 1989; 5: 277-307.
31. Mizuno M, Singer SJ. A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus. Proc Natl Acad Sci USA 1993: 90: 5732-5736.
32. Ito M, Yu RN, Jameson JL. Mutant vasopressin precursors that cause autosomal dominant neurohypophyseal diabetes insipidus retain dimerization and impair the secretion of wild-type proteins. J Biol Chem 1999; 274: 9029-9037.
33. Arvan P, Castle D. Sorting and storage during secretory granule biogenesis: looking backward and looking forward. Biochem J 1998; 332: 592-610.
34. Loh YP, Snell CR, Cool DR. Receptor-mediated targeting of hormones to secretory granules. TEM 1997; 8: 130-137.
35. Breslow E, Aaning HL, Abrash L, Schmir M. Phsyical and chemical properties of the bovine neurophysins. J Biol Chem 1971; 246: 5179-5188.
36. Tooze SA, Flatmark T, Tooze J, Huttner WB. Characterization of the immature secretory granule, and intermediate in granule biogenesis. J Cell Biol 1991; 115: 1491-1503.
37. Dannies PS. Protein hormone storage in secretory granules: mechanisms for concentration and sorting. Endocr Rev 1999; 20: 3-21.
38. Tooze SA. Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells. Bioch Biophys Acta 1998; 1404: 231-244.
39. Kromer A, Glombik MM, Huttner WB, Gerdes HH. Essential role of the disulfide-bonded loop of chromogranin B for sorting to secretory granules is revealed by expression of a deletion mutant in the absence of endogenous granin synthesis. J Cell Biol 1998; 140: 1331-1346.
40. Matsuuchi L, Kelly RB. Constitutive and basal secretion from the endocrine cell line, AtT-20. J Cell Biol 1991; 112: 843-852.
41. Orci L, Ravazzola M, Amherdt M, Perrelet A, Powell SK, Quinn DL, Moore HP. The trans-most cisternac of the Golgi complex: a compartment for sorting of secretory and plasma membrane proteins. Cell 1987; 51: 1039-1051.
42. Moore HPH, Walker MD, Lee F, Kelly RB. Expressing a human proinsulin cDNA in a mouse ACTH-secreting cell, Intracellular storage, proteolytic processing, and secretion on stimulation. Cell 1983; 35: 531-538.