Is there structural specificity in the reversible protein aggregates that are stored in secretory granules?

Journal of Molecular Neuroscience

Volumn 22, Issue 1-2, 2004, Pages 43-49

  Keeler, Camille ^a   Hodsdon, Michael E ^a   Dannies, Priscilla S ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

NMR spectroscopy; Prolactin; Reversible protein aggregation; Secretory granule formation

Indexed keywords

AMINO ACID; MEMBRANE PROTEIN; OLIGOMER; SECRETORY PROTEIN; PROLACTIN; PROTEIN;

AMINO ACID ANALYSIS; CELL FUNCTION; CELL SPECIFICITY; CONCENTRATION RESPONSE; CONFERENCE PAPER; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN AGGREGATION; PROTEIN DETERMINATION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN STRUCTURE; SECRETORY GRANULE; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; HUMAN; INTRACELLULAR MEMBRANE; MACROMOLECULE; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PHYSIOLOGY; REVIEW; SECRETION; SECRETIONS; SECRETORY VESICLE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BODILY SECRETIONS; HUMANS; INTRACELLULAR MEMBRANES; MACROMOLECULAR SUBSTANCES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROLACTIN; PROTEINS; SECRETORY VESICLES;

EID: 3042704069     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1385/JMN:22:1-2:43     Document Type: Conference Paper

References (35)

1. Allan, B. B. and Balch, W. E. (1999) Protein sorting by directed maturation of Golgi compartments. Science 285, 63-66.
2. Arvan, P. and Castle, D. (1998) Sorting and storage during secretory granule biogenesis: looking backward and looking forward. Biochem. J. 332 (Pt. 3), 593-610.
3. Baertschi, A. J., Monnier, D., Schmidt, U., Levitan, E. S., Fakan, S., and Roatti, A. (2001) Acid prohormone sequence determines size, shape, and docking of secretory vesicles in atrial myocytes. Circ. Res. 89, E23-E29.
4. Bannykh, S. I. and Balch, W. E. (1997) Membrane dynamics at the endoplasmic reticulum-Golgi interface. J. Cell Biol. 138, 1-4.
5. Bernado, P., Akerud, T., de la Torre, J. G., Akke, M., and Pons, M. (2003) Combined use of NMR relaxation measurements and hydrodynamic calculations to study protein association. Evidence for tetramers of low molecular weight protein tyrosine phosphatase in solution. J. Am. Chem. Soc. 125, 916-923.
6. Canaff, L., Brechler, V., Reudelhuber, T. L., and Thibault, G. (1996) Secretory granule targeting of atrial natriuretic peptide correlates with its calcium-mediated aggregation. Proc. Natl. Acad. Sci. USA 93, 9483-9487.
7. Castle, A. M., Huang, A. Y., and Castle, J. D. (1997) Passive sorting in maturing granules of AtT-20 cells: the entry and exit of salivary amylase and proline-rich protein. J. Cell Biol. 138, 45-54.
8. Dannies, P. S. (1999) Protein hormone storage in secretory granules: mechanisms for concentration and sorting. Endocr. Rev. 20, 3-21.
9. Deladoey J., Stocker, P., and Mullis, P. E. (2001) Autosomal dominant GH deficiency due to an Arg183His GH-1 gene mutation: clinical and molecular evidence of impaired regulated GH secretion. J. Clin. Endocrinol. Metab. 86, 3941-3947.
10. Farquhar, M. G., Reid, J. J., and Daniell, L. W. (1978) Intracellular transport and packaging of prolactin: a quantitative electron microscope autoradiographic study of mammotrophs dissociated from rat pituitaries. Endocrinology 102, 296-311.
11. Gerdes, H. H. and Glombik, M. M. (2000) Signal-mediated sorting of chromogranins to secretory granules. Adv. Exp. Med. Biol. 482, 41-54.
12. Giannattasio, G., Zanini, A., and Meldolesi, J. (1975) Molecular organization of rat prolactin granules. I. In vitro stability of intact and "membraneless" granules. J. Cell Biol. 64, 246-251.
13. Ishima, R. and Torchia, D. A. (2000) Protein dynamics from NMR. Nat. Struct. Biol. 7, 740-743.
14. Jahn, R. and Sudhof, T. C. (1999) Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911.
15. Kasimova, M. R., Kristensen, S. M., Howe, P. W., Christensen, T., Matthiesen F., Petersen, J., et al. (2002) NMR studies of the backbone flexibility and structure of human growth hormone: a comparison of high and low ph conformations. J. Mol. Biol. 318, 679-695.
16. Kay L. E. (1998) Protein dynamics from NMR. Biochem. Cell Biol. 76, 145-152.
17. Keeler, C., Dannies, P. S., and Hodsdon, M. E. (2003) The tertiary structure and backbone dynamics of human prolactin. J. Mol. Biol. 328, 1105-1121.
18. Lee, M. S., Zhu, Y. L., Chang, J. E., and Dannies, P. S. (2001) Acquisition of Lubrol insolubility, a common step for growth hormone and prolactin in the secretory pathway of neuroendocrine cells. J. Biol. Chem. 276, 715-721.
19. Marx, R., El Meskini, R., Johns, D. C., and Mains, R. E. (1999) Differences in the ways sympathetic neurons and endocrine cells process, store, and secrete exogenous neuropeptides and peptide-processing enzymes. J. Neurosci. 19, 8300-8311.
20. Michael, J., Carroll, R., Swift, H. H., and Steiner, D. F. (1987) Studies on the molecular organization of rat insulin secretory granules. J. Biol. Chem. 262, 16531-16535.
21. Mironov, A. A., Beznoussenko, G. V., Nicoziani, P., Martella, O., Trucco, A., Kweon, H. S., et al. (2001) Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae. J. Cell Biol. 155, 1225-1238.
22. Molinete, M., Irminger, J. C., Tooze, S. A., and Halban, P. A. (2000) Trafficking/sorting and granule biogenesis in the beta-cell. Semin. Cell Dev. Biol. 11, 243-251.
23. Orci, L., Ravazzola, M., Amherdt, M., Madsen, O., Vassalli, J. D., and Perrelet, A. (1985) Direct identification of prohormone conversion site in insulin-secreting cells. Cell 42, 671-681.
24. Orci, L., Ravazzola, M., Storch, M. J., Anderson, R. G., Vassalli, J. D., and Perrelet, A. (1987) Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles. Cell 49, 865-868.
25. Ort, T., Maksimova, E., Dirkx, R., Kachinsky A. M., Berghs, S., Froehner, S. C., and Solimena, M. (2000) The receptor tyrosine phosphatase-like protein ICA512 binds the PDZ domains of beta2-syntrophin and nNOS in pancreatic beta-cells. Eur. J. Cell Biol. 79, 621-630.
26. Rambourg, A., Clermont, Y., Chretien, M., and Olivier, L. (1992) Formation of secretory granules in the Golgi apparatus of prolactin cells in the rat pituitary gland: a stereoscopic study. Anat. Rec. 232, 169-179.
27. 1 cells, but their storage is differentially regulated. Mol. Endocrinol. 4, 1017-1026.
28. Scammell, J. G., Burrage, T. G., and Dannies, P. S. (1986) Hormonal induction of secretory granules in a pituitary tumor cell line. Endocrinology 119, 1543-1548.
29. Slot, J. W., Garruti, G., Martin, S., Oorschot, V., Posthuma, G., Kraegen, E. W., et al. (1997) Glucose transporter (GLUT-4) is targeted to secretory granules in rat atrial cardiomyocytes. J. Cell Biol. 137, 1243-1254.
30. Sossin, W. S., Fisher, J. M., and Scheller, R. H. (1990a) Sorting within the regulated secretory pathway occurs in the trans-Golgi network. J. Cell Biol. 110, 1-12.
31. Sossin, W. S., Sweet-Cordero, A., and Scheller, R. H. (1990b) Dale's hypothesis revisited: different neuropeptides derived from a common prohormone are targeted to different processes. Proc. Natl. Acad. Sci. USA 87, 4845-4848.
32. Tooze, S. A., Martens, G. J., and Huttner, W. B. (2001) Secretory granule biogenesis: rafting to the SNARE. Trends Cell Biol. 11, 116-122.
33. Wajnrajch, M. P., Gertner, J. M., Mullis, P. E., Deladoey J., Cogan, J. D., Lekhakula, S., et al. (2000) Arg183His, a new mutational "hot-spot" in the growth hormone (GH) gene causing isolated GH deficiency type II. J. Endocr. Genet. 1, 125-135.
34. Wand, A. J. (2001) Dynamic activation of protein function: a view emerging from NMR spectroscopy. Nat. Struct. Biol. 8, 926-931.
35. Zhu, Y. L., Conway-Campbell, B. L., Waters, M. J., and Dannies, P. S. (2002) Prolonged retention after aggregation into secretory granules of R183H-growth hormone, a mutant that causes autosomal growth hormone deficiency type II. Endocrinology 1443, 4243-4248.