Regulation of ghrelin structure and membrane binding by phosphorylation

Peptides

Volumn 29, Issue 6, 2008, Pages 904-911

  Dehlin, Eva ^a   Liu, Jianhua ^b   Yun, Samuel H ^a   Fox, Elizabeth ^a   Snyder, Sandra ^a   Gineste, Cyrille ^b   Willingham, Leslie ^b   Geysen, Mario ^b   Gaylinn, Bruce D ^b   Sando, Julianne J ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

Ghrelin phosphorylation; Ghrelin structure; Peptide membrane binding; PKC substrate

Indexed keywords

ALANINE; DES N OCTANOYL GHRELIN; DESACYLGHRELIN; GASTROINTESTINAL HORMONE; GHRELIN; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; PHOSPHODESACYLGHRELIN; PHOSPHOGHRELIN; PROTEIN KINASE C; SERINE; SERINE 18 PHOSPHOGHRELIN; SUCROSE; TRIFLUOROETHANOL;

ACYLATION; AMINO ACID SUBSTITUTION; ANTIINFLAMMATORY ACTIVITY; AQUEOUS SOLUTION; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; EVOLUTION; MEMBRANE BINDING; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; CELL MEMBRANE; CIRCULAR DICHROISM; GENE EXPRESSION REGULATION; GHRELIN; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE HORMONES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; TRIFLUOROETHANOL;

EID: 43049099290     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2008.02.001     Document Type: Article

References (54)

1. Alvaro V., Lévy L., Dubray C., Roche A., Peillon F., Quérat B., and Joubert D. Invasive human pituitary tumors express a point-mutated α-protein kinase-C. J Clin Endocrinol Metab 7 (1993) 1125-1129
2. Ariyasu H., Takjaya K., Tagami T., Ogawa Y., Hosoda K., Akamizu T., et al. Stomach is a major source of circulating ghrelin, and feeding state determines plasma ghrelin-like immunoreactivity levels in humans. J Clin Endocrinol Metab 86 (2001) 4753-4758
3. Baldanzi G., Filigheddu N., Cutrupi S., Catapano F., Bonissoni S., Fubini A., et al. Ghrelin and des-acylghrelin inhibit cell death in cardiomyocytes and endothelial cells through ERK1/2 and PI 3-kinase/AKT. J Cell Biol 159 (2002) 1029-1037
4. Banan A., Fields J.Z., Farhadi A., Talmage D.A., Shang L., and Keshavarzian A. Activation of δ-isoform of protein kinase C is required for oxidant-induced disruption of both the microtubule cytoskeleton and permeability barrier of intestinal epithelia. J Pharmacol Exp Ther 303 (2002) 17-28
5. Beaumont N.J., Skinner V.O., Tan T.M.M., Ramesh B.S., Byrne D.J., MacColl G.S., et al. Ghrelin can bind to a species of high density lipoprotein associated with paraoxonase. J Biol Chem 278 (2003) 8877-8880
6. Bednarek M.A., Feighner S.D., Pong S.S., McKee K.K., Hreniuk D.L., Silva M.V., et al. Structure-Function studies on the new Growth Hormone-releasing peptide, Ghrelin: minimal sequence of ghrelin necessary for activation of growth hormone secretgogue receptor 1a. J Med Chem 43 (2000) 4370-4376
7. Beevers A.J., and Kukol A. Conformational flexibility of the peptide hormone ghrelin in solution and lipid membrane bound: a molecular dynamics study. J Biomol Struct Dyn 23 (2006) 357-363
8. Bi K., and Altman A. Membrane lipid microdomains and the role of PKCθ in T cell activation. Semin Immunol 13 (2001) 139-146
9. Binder H., and Lindblom G. Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes. Biophys J 85 (2003) 982-995
10. Böhm G., Muhr R., and Jaenicke R. Quantitative analysis of protein far UV circular dichrosim spectra by neural networks. Protein Eng 5 (1992) 191-195
11. Camiña J.P. Cell biology of the ghrelin receptor. J Neuroendocrinol 18 (2006) 65-76
12. Crane J.K., and Vezina C.M. Externalization of host cell protein kinase C during enteropathogenic Escherichia coli infection. Cell Death Differ 12 (2005) 115-127
13. D'Costa A.M., Robinson J.K., Maududi T., Chaturvedi V., Nickoloff B.J., and Denning M.F. The proapoptotic tumor suppressor protein kinase C-δ is lost in human squamous cell carcinomas. Oncogene 25 (2006) 378-386
14. De Vriese C., Gregoire R., Lema-Kisoka R., Waelbroeck M., Robberecht P., and Delporte C. Ghrelin degradation by serum and tissue homogenates: identification of the cleavage sites. Endocrinology 145 (2004) 4997-5005
15. De Vriese C., Gregoire F., De Neef P., Robberecht P., and Delporte C. Ghrelin is produced by the human erythroleukemic HEL cell line and involved in an autocrine pathway leading to cell proliferation. Endocrinology 146 (2005) 1514-1522
16. Dixit V.D., Schaffer E.M., Pyle R.S., Collins G.D., Sakthivel S.K., Palaniappan R., et al. Ghrelin inhibits leptin- and activation-induced proinflammatory cytokine expression by human monocytes and T cells. J Clin Invest 114 (2004) 57-66
17. 1NMR structural analysis of human ghrelin and its truncated analogs. Biopolymers 59 (2001) 489-501
18. Foster-Schubert KE, Overduin J, Prudom CE, Liu J, Callahan HS, Gaylinn BD, et al. Acyl and total ghrelin are suppressed strongly by ingested proteins, weakly by lipids, and biphasically by carbohydrates. J Clin Endocrinol Metab 2008, doi:10.1210/jc.2007-2289, epub ahead of print.
19. Garcia J.M., Garcia-Touza M., Hijazi R.A., Taffet G., Epner D., Mann D., et al. Active ghrelin levels and active to total ghrelin ratio in cancer-induced cachexia. J Clin Endo Metab 90 (2005) 2920-2926
20. Garg A. Commentary: the ongoing saga of obestatin. Is it a hormone?. J Clin Endocrinol Metab 92 (2007) 3396-3398
21. Giorgione J., and Newton A.C. Measuring the binding of protein kinase C to sucrose-loaded vesicles. In: Newton A.C. (Ed). Meth Mol Biol 233: Protein kinase C protocols (2003), Humana Press, Totowa, NJ 105-113
22. Glavaski-Joksimovic A., Jeftinija K., Scanes C.G., Anderson L.L., and Jeftinija S. Stimulatory effect of ghrelin on isolated porcine somatotropes. Neuroendocrinol 77 (2003) 367-379
23. Holst B., Holliday N.D., Bach A., Eling C.E., Cox H.M., and Schwartz T.W. Common structural basis for constitutive activity of the ghrelin receptor family. J Biol Chem 279 (2004) 53806-53817
24. Hosoda H., Kojima M., Mizushima T., Shimizu S., and Kangawa K. Structural divergence of human ghrelin. Identification of multiple ghrelin-derived molecules produced by post-translational processing. J Biol Chem 278 (2003) 64-70
25. Isomoto H., Ueno H., Nishi Y., Yasutake T., Tanaka K., Nakazato M., and Kohno S. Circulating ghrelin levels in patients with various upper gastrointestinal diseases. Dig Dis Sci 50 (2005) 833-838
26. Jeffery P.L., Murray R.E., Yeh A.H., McNamara J.F., Duncan R.P., Francis G.D., et al. Expression and function of the ghrelin axis, including a novel preproghrelin isoform, in human breast cancer tissues and cell lines. Endo-Relat Cancer 12 (2005) 839-850
27. Kim J., Shishido T., Jiang X., Aderem A., and McLaughlin S. Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipids vesicles. J Biol Chem 269 (1994) 28214-28219
28. Kojima M., Hosoda H., Date Y., Nakazoto M., Matsuo H., and Kangawa K. Ghrelin is a growth-hormone-releasing acylated peptide from stomach. Nature 402 (1999) 656-660
29. Lai J.K., Cheng C.H., Ko W.H., and Leung P.S. Ghrelin system in pancreatic AR42J cells: its ligand stimulation evokes calcium signaling through ghrelin receptors. Int J Biochem Cell Biol 37 (2005) 887-900
30. Larsen L.H., Gjesing A.P., Sorensen T.I.A., Hamid Y.H., Echwald S.M., Toubro S., et al. Mutation analysis of the preproghrelin gene: no association with obesity and type 2 diabetes. Clin Biochem 38 (2005) 420-424
31. Li W.G., Gavrila D., Liu X., Wang L., Gunnlaugsson S., Stoll L.L., et al. Ghrelin inhibits proinflammatory responses and nuclear factor-κB activation in human endothelial cells. Circulation 109 (2004) 2221-2226
32. Lin Y., Matsumura K., Fukuhara M., Kagiyama S., Fujii K., and Iida M. Ghrelin acts at the nucleus of the solitary tract to decrease arterial pressure in rats. Hypertension 43 (2004) 977-982
33. Lindgren M., Hallbrink M., Prochiantz A., and Langel U. Cell penetrating peptides. Trends Pharmacol Sci 21 (2000) 99-103
34. Liu J, Prudom CE, Nass R, Pezzoli SS, Oliveri MC, Johnson ML, et al. Novel ghrelin assays provide evidence for independent regulation of ghrelin acylation and secretion in healthy young men. J Clin Endocrinol Metab 2008; in press.
35. Matsumura K., Tsuchihashi T., Fujii K., Abe I., and Iida M. Central ghrelin modulates sympathetic activity in conscious rabbits. Hypertension 40 (2002) 694-699
36. McCabe J.B., and Berthiaume L.G. N-terminal acylation confers localization to cholesterol, sphingolipid-enriched membranes but not to lipid rafts/caveole. Mol Biol Cell 12 (2001) 3601-3617
37. Mosior M., and Epand R.M. Mechanism of activation of protein kinase C: roles of diolein and phosphatidylserine. Biochemistry 32 (1993) 66-75
38. Peracchi M., Bardella M.T., Caprioli F., Massironi S., Conte D., Valenti L., et al. Circulating ghrelin levels in patients with inflammatory bowel disease. Gut 55 (2006) 432-433
39. Pöykkö S.M., Kellokoski E., Hörkkö S., Kauma H., Kesäniemi Y.A., and Ukkola O. Low plasma ghrelin is associated with insulin resistance, hypertension, and the prevalence of type 2 diabetes. Diabetes 52 (2003) 2546-2553
40. Purnell J.Q., Weigle D.S., Breen P., and Cummings D.E. Ghrelin levels correlate with insulin levels, insulin resistance, and high-density lipoprotein cholesterol, but not with gender, menopausal status, or cortisol levels in humans. J Clin Endocrinol Metab 88 (2003) 5747-5752
41. Rebecchi M., Peterson A., and McLaughlin S. Phosphoinositide-specific phospholipase C-δ1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4,5-bisphosphate. Biochem 31 12 (1992) 474-574
42. Sando J.J., and Chertihin O.I. Activation of protein kinase C by lysophosphatidic acid: dependence on composition of phospholipids vesicles. Biochem J 317 (1996) 583-588
43. Solodukhin A.S., Kretsinger R.H., and Sando J.J. Initial three-dimensional reconstruction of protein kinase C δ from two-dimensional crystals on lipid monolayers. Cell Signal 19 (2007) 2035-2045
44. Stultz C.M., White J.V., and Smith T.F. Structural analysis based on state-space modeling. Protein Sci 2 (1993) 305-314
45. Torsello A., Ghe C., Bresciani E., Catapano F., Chigo E., Deghenghi R., et al. Short ghrelin peptides neither displace ghrelin binding in vitro nor stimulate GH release in vivo. Endocrinology 143 (2002) 1968-1971
46. Ukkola O., Ravussin E., Jacobson P., Snyder E.E., Chagnon M., Sjöström L., and Bouchard C. Mutations in the preproghrelin/ghrelin gene associated with obesity in humans. J Clin Endo Metab 86 (2001) 3996-3999
47. VanderLely A.J., Tschöp M., Heiman M.L., and Ghigo E. Biological, physiological, pathophysiological and pharmacological aspects of ghrelin. Endocr Rev 25 (2004) 426-457
48. Vinton B.B., Wertz S.L., Jacob J., Grisham C.M., Cafiso D.S., and Sando J.J. Influence of lipid on the structure and phosphorylation of protein kinase C α substrate peptides. Biochem J 330 (1998) 1433-1442
49. Vivenza D., Rapa A., Castellino N., Bellone S., Petri A., Vacca G., et al. Ghrelin gene polymorphisms and ghrelin, insulin, IGF-I, leptin: anthropometric data in children and adolescents. Eur J Endocrinol 151 (2004) 127-133
50. Walker J.W., and Sando J.J. Activation of protein kinase C by short chain phosphatidylcholines. J Biol Chem 263 (1988) 4537-4540
51. Yeh A.H., Jeffery P.L., Duncan R.P., Herington A.C., and Chopin L.K. Ghrelin and a novel preproghrelin isoform are highly expressed in prostate cancer and ghrelin activates mitogen-activated protein kinase in prostate cancer. Clin Cancer Res 11 (2005) 8295-8303
52. Yoshimoto A., Mori K., Sugawara A., Mukoyama M., Yahata K., Suganami T., et al. Plasma ghrelin and desacyl ghrelin concentrations in renal failure. J Am Soc Nephrol 13 (2002) 2748-2752
53. Zhang J.V., Ren P.-G., Avsian-Kretchmer O., Luo C.-W., Rauch R., Klein C., and Hjsueh A.J. Obestatin a peptide encoded by the ghrelin gene, opposes ghrelin's effects on food intake. Science 310 (2005) 996-999
54. Zhu X., Cao Y., Voogd K., and Steiner D.F. On the processing of proghrelin to ghrelin. J Biol Chem 281 (2006) 38867-38870