Expression of 14-3-3γ in injured arteries and growth factor-and cytokine-stimulated human vascular smooth muscle cells

Cell Growth and Differentiation

Volumn 7, Issue 11, 1996, Pages 1453-1460

  Autieri, Michael V ^a   Haines, Dale S ^b   Romanic, Anne M ^c   Ohlstein, Eliot H ^c  

^a DEBORAH HEART AND LUNG CENTER   (United States)

^b DREXEL UNIVERSITY COLLEGE OF MEDICINE   (United States)

^c GLAXOSMITHKLINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; GROWTH FACTOR; INTERLEUKIN 1BETA; MESSENGER RNA; PLATELET DERIVED GROWTH FACTOR; PROTEIN; PROTEIN KINASE;

ANIMAL MODEL; ANIMAL TISSUE; ARTERY INJURY; ARTERY MEDIA; ARTICLE; CELL PROLIFERATION; CONTROLLED STUDY; DENSITOMETRY; HUMAN; HUMAN CELL; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; INTIMA; MALE; METABOLISM; NONHUMAN; NORTHERN BLOTTING; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INDUCTION; RAT; SMOOTH MUSCLE FIBER; STENOSIS; VASCULAR SMOOTH MUSCLE;

14-3-3 PROTEINS; ANGIOPLASTY, BALLOON; ANIMALS; CAROTID ARTERIES; CELLS, CULTURED; CYCLOHEXIMIDE; GENE EXPRESSION REGULATION; GROWTH SUBSTANCES; HUMANS; MALE; MUSCLE, SMOOTH, VASCULAR; ORGAN SPECIFICITY; PROTEIN BIOSYNTHESIS; PROTEIN SYNTHESIS INHIBITORS; PROTEINS; RATS; RATS, SPRAGUE-DAWLEY; RNA, MESSENGER; T-LYMPHOCYTES; TUNICA INTIMA; TYROSINE 3-MONOOXYGENASE;

ANIMALIA;

EID: 0029861449     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (44)

1. Ross, R. The pathogenesis of atherosclerosis: a prospective for the 1990s. Nature (Lond), 362: 801-809, 1993.
2. Nilsson, J. Cytokines and smooth muscle cells in atherosclerosis. Cardiovasc. Res., 27: 1184-1189, 1992.
3. Clowes A. W., Reidy, M. A., and Clowes, M. M. Mechanisms of stenosis after arterial injury. Lab. Invest., 49: 208-215, 1983.
4. Liu, M. W., Roubin, G. S., and King, S. B. Restenosis after coronary angioplasty: potential biologic determinants and role of intimal hyperplasia. Circulation, 79: 1374-1378, 1989.
5. Austin, G. E., Ratliff, N. B., Hollman, J., Tabei, S., and Phillips, D. F. Intimal proliferation of smooth muscle cells as an explanation for recurrent coronary artery stenosis after percutaneous transluminal coronary angioplasty. J. Am. Coll. Cardiol., 6: 369-375, 1985.
6. O'Brien, E. R., Alpers, C. E., Stewart, D. K., Ferguson, M., Tran, N., Gordon, D., Benditt, E. P., Hinohara, T., Simpson, J. B., and Schwarte, S. M. Proliferation in primary and restenotic coronary atherectomy tissue. Circ. Res., 73: 223-231, 1993.
7. Feig, L. A. The many roads that lead to Ras. Science (Washington), 260: 767-768, 1993.
8. Marx, J. Forging a path to the nucleus. Science (Washington), 260: 1588-1590, 1993.
9. Roberts, T. M. A signal chain of events. Nature (Lond.), 360: 534-535, 1992.
10. Aitken, A., Collinge, D. B., van Heusden, B., Isobe, T., and Rosenboom, P. H. 14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins. Trends Biochem. Sci., 17: 498-501, 1992.
11. Aitken, A., Amess, B., Howell, S., Jones, D., Martin, H., Patel, Y., Robinson, K., and Toker, A. The role of specific isoformsof 14-3-3 protein in regulating protein kinase activity in the brain. Biochem. Soc. Trans., 20: 607-611, 1992.
12. Isobe, T., Ichimura, T., Sunaya, T., Okuyama, T., Takashi, N., Kuwano, R., and Takahashi, Y. Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases. J. Mol. Biol., 277: 125-132, 1991.
13. Watanabe, M., Isobe, T., Ichimura, T., Kuwano, R., Takashi, Y., and Kondo, H. Molecular cloning of rat cDNAs for β and γ subtypes of 14-3-3 protein and developmental changes in expression of their mRNAs in the nervous system. Mol. Brain Res., 17: 136-146, 1993.
14. Pallas, D. C., Fu, H., Haehnel, L. C., Weller, W., Collier, R. J., and Roberts, T. M. Association of polyomavirus middle tumor antigen with 14-3-3 proteins. Science (Washington), 265: 535-537, 1994.
15. Ford, J. C., Al-Khodairy, F., Fotou, E., Sheldrick, K. S., Griffiths, D. J. F., and Carr, A. M. 14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast. Science (Washington), 265: 533-534, 1994.
16. Morrison, D. 14-3-3: modulators of signalling proteins? Science (Washington), 266: 56-57, 1994.
17. Freed, E., Symons, M., Macdonald, S. G., McCormick, F., and Ruggieri, R. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science (Washington), 265: 1713-1716, 1994.
18. Ire, K., Gotoh, Y., Yashar, B. M., Errede, B., Nishida, E., and Matsumoto, K. Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science (Washington), 265: 1716-1719, 1994.
19. Fu, H., Xia, K., Pallas, D. C., Cui, M. C., Conroy, K., Narsimhan, R. P., Mamon, H., Collier, R. J., and Roberts, T. M. Interaction of the protein kinase Raf-1 with 14-3-3 proteins. Science (Washington), 266: 126-129, 1994.
20. Fantl, W. J., Muslin, A. J., Kikuchi, A., Martin, J. A., MacMicol, A. M., Gross, R. W., and Williams, L. T. Activation of Raf-1 by 14-3-3 proteins. Nature (Lond.), 371: 612-614, 1894.
21. Reuther, G. W., Fu, H., Cripe, L. D., Collier, J. R., and Pendergast, A. M. Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family. Science (Washington), 266: 129-143, 1994.
22. Xiao, B., Smerdon, S. J., Jones, D. H., Dodson, G. G., Soneji, Y., Aitken, A., and Gamblin, S. Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature (Lond.), 370: 188-191, 1995.
23. Liu, D., Bienkowska, J., Petosa, C., Collier, R. J., Fu, H., and Liddington, R. Crystal structure of the ζ isoform of the 14-3-3 protein. Nature (Lond.), 376: 191-194, 1995.
24. Muslin, A. J., Tanner, J. W., Allen, P. M., and Shaw, A. S. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell, 84: 889-397, 1996.
25. Shimizu, K., Kuroda, S., Yamamori, B., Matsuda, S., Kaibuchi, K., Yamauchi, T., Isobe, T., Irie, K., Matsumoto, K., and Taka, Y. Synergistic activation by ras and 14-3-3 protein of a mitogen-activated protein kinase kinase kinase named Ras-dependent extracellular signal-regulated kinase kinase stimulator. J. Biol. Chem., 269: 22917-22920, 1994.
26. Autieri, M. V., Feuerstein, G. Z., Yue, T-L., Ohlstein, E. H., and Douglas, S. A. Use of differential display to identify differentially expressed mRNAs induced by rat carotid artery balloon angioplasty. Lab. Invest., 72: 656-671, 1995.
27. Sabath, D. E., Podolin, P. L., Comber, P. G., and Prystowsky, M. B. cDNA cloning and characterization of interleukin 2-induced genes in a cloned T helper lymphocyte. J. Biol. Chem., 265: 12671-12678, 1990.
28. Glasbrook, A. L., Sarmiento, M., Loken, M. R., Dialynas, D. P., Quintans, J., Eisenberg, L., Lutz, C. T., Wilde, D., and Fitch, F. W. Murine T-lymphocyte clones with distinct immunologic functions. Immunol. Rev., 54: 225-266, 1981.
29. Shipman, P. M., Sabath, D. E., Fischer, A. H., Camber, P. G., Sullivan, K., Tan, E. M., and Prystowsky, M. B. Cyclin mRNA and protein expression in recombinant interleukin 2-stimulated cloned murine T lymphocytes. J. Cell. Biochem., 38: 39-48, 1988.
30. Gadeau, A. P., Campan, M., and Desgranges, C. Induction of cell cycle-dependent genes during cell cycle progression of arterial smooth muscle cells in culture. J. Cell. Physiol., 146: 356-361, 1991.
31. Campan, M., Desgranges, C., Gadeau, A. P., Millet, D., and Belloc, F. Cell cycle-dependent gene expression in quiescent stimulated and asynchronously cycling arterial smooth muscle cells in culture. J. Cell. Physiol., 150: 493-500, 1991.
32. Cells, J. E., Dejgaard, K., Madsen, P., Letters, H., Gesser, B., Honore, B., Rasmussen, H. H., Olsen, E., Lauridsen, J. B., and Ratz, G. The MRC-5 human embryonal lung fibroblast two-dimensional gel cellular protein database: quantitative identification of polypeptides whose relative abundance differs between quiescent, proliferating, and SV40-transformed cells. Electrophoresis, 11: 1072-1113, 1990.
33. Rosenfeld, G. C., Samborn, B., and Loose-Mitchell, D. Cloning, distribution, and expression of rat 14-3-3 protein. FASEB J., 5: A834, 1991.
34. Katoch, S. S., and Moreland, R. S. Agonist and membrane depolarization-induced activation of MAP kinase in the swine carotid artery. Am. J. Physiol., 269: 222-229, 1995.
35. Adam, L. P., Gapinski, C. J., and Hathaway, D. R. Phosphorylation sequences in h-caldesmon from phorbol ester-stimulated canine aortas. FEBS Lett, 302: 223-226, 1992.
36. Adam, L. P., Haeberle, J. R., and Hathaway, D. R. Phosphorylation of caldesmon in arterial smooth muscle. J. Biol. Chem., 264: 7698-7703, 1989.
37. Adam, L. P., and Hathaway, D. R. Identification of mitogen-activated protein kinase phosphorylation sequences in mammalian h-caldesmon. FEBS Lett., 322: 56-60, 1993.
38. Pardee, A. B. A restriction point for control of normal animal cell proliferation. Proc. Natl. Acad. Sci. USA, 71: 4901-4905, 1974.
39. Coppock, D. L., and Pardee, A. B. Control of thymidine kinase mRNA during the cell cycle. Mol. Cell. Biol., 7: 2925-2932, 1987.
40. Hipskind, R. A., Baccarini, M., and Nordheim, A. Transient activation of RAF-1, MEK, and ERK2 coincides kinetically with ternary complex factor phosphorylation and immediate early gene promoter activity. Mol. Cell. Biol., 14: 6219-6231, 1994.
41. Ohlstein, E. H., Douglas, S. A., Sung, C. P., Yue, T. L., Louden, C., Arleth, A., Poste, G., Ruffolo, R. R., Jr., and Feuerstein, G. Z. Carvedilol, a cardiovascular drug, prevents vascular smooth muscle cell proliferation, migration, and neointima formation following vascular injury. Proc. Natl. Acad. Sci. USA, 90: 6189-6193, 1993.
42. Yue, T. L., McKenna, P. J., Gu, J. L., and Feuerstein, G. Z. Interleukin-8 is chemotactic for vascular smooth muscle cells. Eur. J. Pharmacol., 240: 81-84, 1993.
43. Autieri, M. V., Olson, B. A., Yue, T-L., and Feuerstein, G. Z. Antisense oligonucleotides to the p65 subunit of NF-kB inhibit human vascular smooth muscle cell adherence and proliferation. Biochem. Biophys. Res. Commun., 213: 827-831, 1995.
44. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.), 227: 680-685, 1970.