Lovastatin suppresses erythropoietin receptor surface expression through dual inhibition of glycosylation and geranylgeranylation

Biochemical Pharmacology

Volumn 74, Issue 4, 2007, Pages 590-600

  Hamadmad, Sumaya N ^a   Hohl, Raymond J ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

Erythropoietin; Erythropoietin receptor; Geranylgeranylation; GGPP; Glycosylation; Lovastatin

Indexed keywords

DOLICHOL; ENZYME INHIBITOR; ERYTHROPOIETIN; ERYTHROPOIETIN RECEPTOR; GGTI 286; MEVALONIC ACID; MEVINOLIN; TUNICAMYCIN; UNCLASSIFIED DRUG;

ARTICLE; BIOTINYLATION; CELL PROLIFERATION; CELL SURVIVAL; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG MECHANISM; ERYTHROLEUKEMIA CELL; GERANYLGERANYLATION; GLYCOSYLATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN MODIFICATION;

ANTI-BACTERIAL AGENTS; ANTICHOLESTEREMIC AGENTS; ANTIVIRAL AGENTS; BIOTINYLATION; BLOTTING, WESTERN; CELL LINE, TUMOR; CELL SURVIVAL; DOLICHOL; DOSE-RESPONSE RELATIONSHIP, DRUG; ERYTHROPOIETIN; GLYCOSYLATION; HUMANS; IODINE RADIOISOTOPES; JANUS KINASE 2; LEUCINE; LOVASTATIN; MEVALONIC ACID; PHOSPHORYLATION; POLYISOPRENYL PHOSPHATES; PROTEIN ISOPRENYLATION; RECEPTORS, ERYTHROPOIETIN; STAT5 TRANSCRIPTION FACTOR; TUNICAMYCIN;

EID: 34447309075     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2007.04.028     Document Type: Article

References (43)

1. D'Andrea A.D., Fasman G.D., and Lodish H.F. Erythropoietin receptor and interleukin-2 receptor beta chain: a new receptor family. Cell 58 6 (1989) 1023-1024
2. Youssoufian H., Longmore G., Neumann D., Yoshimura A., and Lodish H.F. Structure, function, and activation of the erythropoietin receptor. Blood 81 9 (1993) 2223-2236
3. Krantz S.B. Erythropoietin. Blood 77 3 (1991) 419-434
4. Remy I., Wilson I.A., and Michnick S.W. Erythropoietin receptor activation by a ligand-induced conformation change. Science 283 5404 (1999) 990-993
5. Witthuhn B.A., Quelle F.W., Silvennoinen O., Yi T., Tang B., Miura O., et al. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell 74 2 (1993) 227-236
6. Klingmuller U., Bergelson S., Hsiao J.G., and Lodish H.F. Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5. Proc Natl Acad Sci USA 93 16 (1996) 8324-8328
7. Gouilleux F., Pallard C., Dusanter-Fourt I., Wakao H., Haldosen L.A., Norstedt G., et al. Prolactin, growth hormone, erythropoietin and granulocyte-macrophage colony stimulating factor induce MGF-Stat5 DNA binding activity. Embo J 14 9 (1995) 2005-2013
8. Damen J.E., Wakao H., Miyajima A., Krosl J., Humphries R.K., Cutler R.L., et al. Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation. Embo J 14 22 (1995) 5557-5568
9. Quelle F.W., Wang D., Nosaka T., Thierfelder W.E., Stravopodis D., Weinstein Y., et al. Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response. Mol Cell Biol 16 4 (1996) 1622-1631
10. Damen J.E., Liu L., Cutler R.L., and Krystal G. Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-kDa tyrosine phosphorylated protein. Blood 82 8 (1993) 2296-2303
11. Koury M.J., and Bondurant M.C. The molecular mechanism of erythropoietin action. Eur J Biochem 210 3 (1992) 649-663
12. Komatsu N., Adamson J.W., Yamamoto K., Altschuler D., Torti M., Marzocchini R., et al. Erythropoietin rapidly induces tyrosine phosphorylation in the human erythropoietin-dependent cell line, UT-7. Blood 80 1 (1992) 53-59
13. Torti M., Marti K.B., Altschuler D., Yamamoto K., and Lapetina E.G. Erythropoietin induces p21ras activation and p120GAP tyrosine phosphorylation in human erythroleukemia cells. J Biol Chem 267 12 (1992) 8293-8298
14. Miura Y., Miura O., Ihle J.N., and Aoki N. Activation of the mitogen-activated protein kinase pathway by the erythropoietin receptor. J Biol Chem 269 47 (1994) 29962-29969
15. Lester R.D., Jo M., Campana W.M., and Gonias S.L. Erythropoietin promotes MCF-7 breast cancer cell migration by an ERK/mitogen-activated protein kinase-dependent pathway and is primarily responsible for the increase in migration observed in hypoxia. J Biol Chem 280 47 (2005) 39273-39277
16. Lai S.Y., Childs E.E., Xi S., Coppelli F.M., Gooding W.E., Wells A., et al. Erythropoietin-mediated activation of JAK-STAT signaling contributes to cellular invasion in head and neck squamous cell carcinoma. Oncogene 24 27 (2005) 4442-4449
17. Yoshimura A., D'Andrea A.D., and Lodish H.F. Friend spleen focus-forming virus glycoprotein gp55 interacts with the erythropoietin receptor in the endoplasmic reticulum and affects receptor metabolism. Proc Natl Acad Sci USA 87 11 (1990) 4139-4143
18. Neumann D., Wikstrom L., Watowich S.S., and Lodish H.F. Intermediates in degradation of the erythropoietin receptor accumulate and are degraded in lysosomes. J Biol Chem 268 18 (1993) 13639-13649
19. D'Andrea A.D., and Zon L.I. Erythropoietin receptor. Subunit structure and activation. J Clin Invest 86 3 (1990) 681-687
20. Walrafen P., Verdier F., Kadri Z., Chretien S., Lacombe C., and Mayeux P. Both proteasomes and lysosomes degrade the activated erythropoietin receptor. Blood 105 2 (2005) 600-608
21. Goldstein J.L., and Brown M.S. Regulation of the mevalonate pathway. Nature 343 6257 (1990) 425-430
22. Schafer W.R., Kim R., Sterne R., Thorner J., Kim S.H., and Rine J. Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans. Science 245 4916 (1989) 379-385
23. Hancock J.F., Magee A.I., Childs J.E., and Marshall C.J. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57 7 (1989) 1167-1177
24. Casey P.J., Solski P.A., Der C.J., and Buss J.E. p21ras is modified by a farnesyl isoprenoid. Proc Natl Acad Sci U S A 86 21 (1989) 8323-8327
25. Zhang F.L., and Casey P.J. Protein prenylation: molecular mechanisms and functional consequences. Annu Rev Biochem 65 (1996) 241-269
26. Sinensky M. Recent advances in the study of prenylated proteins. Biochim Biophys Acta 1484 2-3 (2000) 93-106
27. Casey P.J. Mechanisms of protein prenylation and role in G protein function. Biochem Soc Trans 23 1 (1995) 161-166
28. Hori Y., Kikuchi A., Isomura M., Katayama M., Miura Y., Fujioka H., et al. Post-translational modifications of the C-terminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins. Oncogene 6 4 (1991) 515-522
29. Lowy D.R., and Willumsen B.M. Protein modification: new clue to Ras lipid glue. Nature 341 6241 (1989) 384-385
30. Schenk B., Fernandez F., and Waechter C.J. The ins(ide) and out(side) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum. Glycobiology 11 5 (2001) 61R-70R
31. Cottalasso D., Bellocchio A., Domenicotti C., Dapino D., Pronzato M.A., and Nanni G. 1,1,2,2-Tetrachloroethane-induced early decrease of dolichol levels in rat liver microsomes and Golgi apparatus. J Toxicol Environ Health A 54 2 (1998) 133-144
32. Chojnacki T., and Dallner G. The biological role of dolichol. Biochem J 251 1 (1988) 1-9
33. Hwang J.B., and Frost S.C. Effect of alternative glycosylation on insulin receptor processing. J Biol Chem 274 32 (1999) 22813-22820
34. Collier E., Carpentier J.L., Beitz L., Carol H., Taylor S.I., and Gorden P. Specific glycosylation site mutations of the insulin receptor alpha subunit impair intracellular transport. Biochemistry 32 30 (1993) 7818-7823
35. Carlberg M., Dricu A., Blegen H., Wang M., Hjertman M., Zickert P., et al. Mevalonic acid is limiting for N-linked glycosylation and translocation of the insulin-like growth factor-1 receptor to the cell surface. Evidence for a new link between 3-hydroxy-3-methylglutaryl-coenzyme a reductase and cell growth. J Biol Chem 271 29 (1996) 17453-17462
36. Hamadmad S.N., Henry M.K., and Hohl R.J. Erythropoietin receptor signal transduction requires protein geranylgeranylation. J Pharmacol Exp Ther 316 1 (2006) 403-409
37. Miyazaki Y., Kuriyama K., Higuchi M., Tsushima H., Sohda H., Imai N., et al. Establishment and characterization of a new erythropoietin-dependent acute myeloid leukemia cell line, AS-E2. Leukemia 11 11 (1997) 1941-1949
38. Huang L.J., Constantinescu S.N., and Lodish H.F. The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor. Mol Cell 8 6 (2001) 1327-1338
39. Verdier F., Walrafen P., Hubert N., Chretien S., Gisselbrecht S., Lacombe C., et al. Proteasomes regulate the duration of erythropoietin receptor activation by controlling down-regulation of cell surface receptors. J Biol Chem 275 24 (2000) 18375-18381
40. Van Aelst L., and D'Souza-Schorey C. Rho GTPases and signaling networks. Genes Dev 11 18 (1997) 2295-2322
41. Efuet E.T., and Keyomarsi K. Farnesyl and geranylgeranyl transferase inhibitors induce G1 arrest by targeting the proteasome. Cancer Res 66 2 (2006) 1040-1051
42. Nagao M., Matsumoto S., Masuda S., and Sasaki R. Effect of tunicamycin treatment on ligand binding to the erythropoietin receptor: conversion from two classes of binding sites to a single class. Blood 81 10 (1993) 2503-2510
43. Nagao M., Morishita E., Hanai Y., Kobayashi K., and Sasaki R. N-glycosylation-defective receptor for erythropoietin can transduce the ligand-induced cell proliferation signal. FEBS Lett 373 3 (1995) 225-228