Vai al contenuto| Home page|

   Ti trovi in: HOME »Programmi, progetti e risultati »I progetti »PRIN - Programmi di ricerca di Rilevante Interesse Nazionale»Programma di ricerca
INIZIO_TESTO_DA_INDICIZZARE

RESEARCH PROGRAM

italiano - inglese
Similar research programs:
Scientific and education field classification
International Patent Classification
Geographical classification
Bibliografia
1. S. Krantic et al., Eur.J Endocrinol. 151, 643-655 (2004).
2. S. Krantic, Peptides. 21, 1941-1964 (2000).
3. L. de Lecea et al., Nature. 381, 242-245 (1996).
4. V. A. Dalm et al., Clin.Endocrinol.(Oxf). 60, 625-629 (2004).
5. M. Papotti et al., J Endocrinol.Invest. 26, RC15-RC18 (2003).
6. G. Notas et al., J Hepatol. 40, 792-798 (2004).
7. E. G. Lichtenauer-Kaligis et al., Eur.J Endocrinol. 150, 565-577 (2004).
8. H. Hosoda, M. Kojima, H. Matsuo, K. Kangawa, J Biol.Chem. 275, 21995-22000 (2000).
9. M. Kojima et al., Nature. 402, 656-660 (1999).
10. H. Ariyasu et al., J Clin.Endocrinol.Metab. 86, 4753-4758 (2001).
11. Y. Date et al., Endocrinology. 141, 4255-4261 (2000).
12. C. Tomasetto, C. Wendling, M. C. Rio, P. Poitras, Peptides. 22, 2055-2059 (2001).
13. A. Yabuki et al., J Anat. 205, 239-246 (2004).
14. H. Hosoda, M. Kojima, H. Matsuo, K. Kangawa, Biochem.Biophys.Res.Commun. 279, 909-913 (2000).
15. I. Sakata et al., Peptides. 23, 531-536 (2002).
16. Y. Date et al., Diabetes. 51, 124-129 (2002).
17. C. L. Prado, A. E. Pugh-Bernard, L. Elghazi, B. Sosa-Pineda, L. Sussel, Proc.Natl.Acad.Sci.U.S.A. 101, 2924-2929 (2004).
18. N. Wierup, H. Svensson, H. Mulder, F. Sundler, Regul.Pept. 107, 63-69 (2002).
19. N. Wierup, S. Yang, R. J. McEvilly, H. Mulder, F. Sundler, J Histochem.Cytochem. 52, 301-310 (2004).
20. S. Lu et al., Neurosci.Lett. 321, 157-160 (2002).
21. M. A. Cowley et al., Neuron. 20, 649-661 (2003).
22. G. S. Tannenbaum, J. Epelbaum, C. Y. Bowers, Endocrinology 144, 967-974 (2003).
23. C. D. Breder et al., J Neurosci. 12, 3920-3934 (1992).
24. J. F. Bruno, Y. Xu, J. Song, M. Berelowitz, Endocrinology. 133, 2561-2567 (1993).
25. Y. C. Patel, Front Neuroendocrinol. 20, 157-198 (1999).
26. V. A. Dalm et al., J Endocrinol.Invest. 26, 94-102 (2003).
27. C. Bruns, I. Lewis, U. Briner, G. Meno-Tetang, G. Weckbecker, Eur.J Endocrinol. 146, 707-716 (2002).
28. J. P. Allen et al., Eur.J Neurosci. 17, 1881-1895 (2003).
29. P. Dutar et al., Neuroscience. 112, 455-466 (2002).
30. C. Viollet et al., Eur.J Neurosci. 12, 3761-3770 (2000).
31. V. Martinez et al., Gastroenterology. 114, 1125-1132 (1998).
32. L. Piqueras, Y. Tache, V. Martinez, J Physiol. 549, 889-901 (2003).
33. M. Z. Strowski et al., Mol.Endocrinol. 17, 93-106 (2003).
34. T. A. Tirone et al., Pancreas. 26, e67-e73 (2003).
35. H. J. Kreienkamp, E. Akgun, H. Baumeister, W. Meyerhof, D. Richter, FEBS Lett. 462, 464-466 (1999).
36. G. Casini et al., Eur.J Neurosci. 19, 43-54 (2004).
37. C. Lanneau et al., Endocrinology. 141, 967-979 (2000).
38. S. G. Ren et al., J Clin.Endocrinol.Metab. 88, 5414-5421 (2003).
39. M. Pollak, Digestion. 57 Suppl 1:29-33., 29-33 (1996).
40. E. Bajetta et al., Cancer. 94, 299-304 (2002).
41. G. Ferjoux et al., J Physiol Paris. 94, 205-210 (2000).
42. P. Dasgupta, Pharmacol.Ther. 102, 61-85 (2004).
43. L. Buscail et al., Proc.Natl.Acad.Sci.U.S.A. 91, 2315-2319 (1994).
44. L. Buscail et al., Proc.Natl.Acad.Sci.U.S.A. 92, 1580-1584 (1995).
45. V. A. Dalm et al., Am.J Physiol Endocrinol.Metab. 285, E344-E353 (2003).
46. V. A. Dalm et al., J Clin.Endocrinol.Metab. 88, 270-276 (2003).
47. N. Robas, E. Mead, M. Fidock, J Biol.Chem. 278, 44400-44404 (2003).
48. A. D. Howard et al., Science. 273, 974-977 (1996).
49. O. C. Palyha et al., Mol.Endocrinol. 14, 160-169 (2000).
50. R. G. Smith, S. Feighner, K. Prendergast, X. Guan, A. Howard, Trends Endocrinol.Metab. 10, 128-135 (1999).
51. R. G. Smith et al., Endocrine. 14, 9-14 (2001).
52. X. M. Guan et al., Brain Res.Mol.Brain Res. 48, 23-29 (1997).
53. M. Nakazato et al., Nature. 409, 194-198 (2001).
54. P. A. Bennett et al., Endocrinology. 138, 4552-4557 (1997).
55. S. Gnanapavan et al., J Clin.Endocrinol.Metab. 87, 2988 (2002).
56. N. Hattori et al., J Clin.Endocrinol.Metab. 86, 4284-4291 (2001).
57. M. Kojima, H. Hosoda, K. Kangawa, Horm.Res. 56 Suppl 1:93-7., 93-97 (2001).
58. F. Broglio, C. Gottero, E. Arvat, E. Ghigo, Horm.Res. 59, 109-117 (2003).
59. M. Murata et al., J Biol.Chem. 277, 5667-5674 (2002).
Keywords
PEPTIDES, ENDOCRINE CELLS, NEURONS, SOMATOSTATIN, CORTISTATIN, GHRELIN, METABOLISM, NEUROTRANSMISSION, TUMORS

Somatostatin and related peptides: distribution, biological effects, and characterization of transgenic models

Università degli Studi di Torino
Abstract
This project derives from the collaboration of four research groups each possessing specific expertise/background in cellular and structural morphology, electrophysiology, pathology and histopathology, pharmacology and endocrinology. By such a mutifaceted approach this program will aim to clarify some cellular and molecular mechanisms that undierlie the biological effects of somatostatin and two related peptides (cortistatin and ghrelin) in different experimental models in vitro and in vivo, and in human tissues. These biologically active peptides display pleiotropic functions, many of which are of potential applicative interest. Therefore we will primarily address:
- the comparative distribution in the neuroendocrine system on KO mice, human fetal and adult material, tumors of nervous and/or neuroendocrine origin;
- the regulatory effects on proliferation and apoptosis in normal and pathological nerve cells, endocrine cells or hematological cells;
- the analysis of the endocrine-metabolic profile and evaluation of the physio-pathological and pharmacological responses in phlogistic conditions and somatic and visceral hyperalgesia in single/double KO mice;
- the short-term modulation of excitatory glutamatergic neurotransmission within the superficial laminae of the spinal dorsal horn with particular emphasis on pain neurotrasmission in acute and chronic conditions;
- the short and long-term modulation of inhibitory >>>

Principal Investigator
Adalberto Merighi Università degli Studi di TORINO
Research Objectives
The main goal of this program will be to clarify some cellular and molecular mechanisms that undierlie the biological effects of somatostatin and two related peptides (cortistatin and ghrelin) by using a multidisciplinary approach in different experimental models in vitro and in vivo.
The four units collaborating to the project will liaise with each others in term of exchange of technical expertise and cultural background. Each group will primarily address one or more of the following major issues of somatostatin biology:
- Comparative distribution in the neuroendocrine system on KO mice, human fetal and adult material, tumors of nervous and/or neuroendocrine origin;
- Regulatory effects on proliferation and apoptosis in normal and pathological nerve cells, endocrine cells or hematological cells;
- Analysis of the endocrine-metabolic profile and evaluation of the physio-pathological and pharmacological responses in phlogistic conditions and somatic and visceral hyperalgesia in single/double KO mice;
- Short-term modulation of excitatory glutamatergic neurotransmission within the superficial laminae of the spinal dorsal horn with particular emphasis on pain neurotrasmission in acute and chronic conditions;
- Short and long-term modulation of inhibitory GABAergic neurotrasmission within the superficial laminae of the spinal dorsal horn with particular emphasis on the regulation of the inhibitory tone of substantia >>>

Timescale
24 months
National and international background
Somatostatin as a pleiotropic peptide
Bioactive peptides, cytokines and growth factors represent the principal types of chemical messengers. Classically, the term bioactive peptides designate a group of hormones and neuromediators of petidic nature. Cytokines are mediators of the cell communication in the immune system whereas, growth factors represent signal molecules controlling cell division and/or differentiation notably during embryonic development. Distinction between these three families of polypeptides/glycoproteins is more historical and didactic than functional. Indeed, there is often no clear distinction between the three families and, more importantly, the same peptide might functionally belong to all three families, being released by a multitude of cell types and thus displaying pleiotropic effects [1].
Concerning the relevant receptors, there are slight differences in the way the ligand triggers the initial
receptor activation upon binding, but the final cellular response is elaborated according to a common, general principle consisting in activation of different types of protein kinases. In the case of bioactive peptides, receptors are made of a single polypeptide chain spanning the plasma membrane in seven transmembrane domains and are coupled to G-proteins (G-protein-coupled receptors or GPCRs). In all cases, protein kinase-driven phosphorylation results in functional alteration of down-stream effectors (ion channels >>>