Effects of a fluorescent myosin light chain phosphatase inhibitor on prostate cancer cells

Frontiers in Oncology

Volumn 1, Issue SEP, 2011, Pages

  Grindrod, Scott ^a   Suy, Simeng ^a   Fallen, Shannon ^a   Eto, Masumi ^b   Toretsky, Jeffrey ^a   Brown, Milton L ^a  

^a GEORGETOWN UNIVERSITY MEDICAL CENTER   (United States)

^b THOMAS JEFFERSON UNIVERSITY   (United States)

Author keywords

Chemotaxis; Myosin phosphatase; Prostate cancer

Indexed keywords

EID: 84891591212     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2011.00027     Document Type: Article

References (26)

1. Bollen, M., Peti, W., Ragusa, M. J., and Beullens, M. (2010). The extended PP1 toolkit: designed to create specificity. Trends Biochem. Sci. 35, 450-458.
2. Bridges, A. (2001). Chemical inhibitors of protein kinases. Chem. Rev. 101, 2541-2572.
3. Eto, M., Kitazawa, T., and Brautigan, D. L. (2004). Phosphoprotein inhibitor CPI-17 specificity depends on allosteric regulation of protein phosphatase-1 by regulatory subunits. Proc. Natl. Acad. Sci. U.S.A. 101, 8888-8893.
4. Eto, M., Ohmori, T., Suzuki, M., Furuya, K., and Morita, F. (1995). A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J. Biochem. 118, 1104-1107.
5. Eto, M., Wong, L., Yazawa, M., and Brautigan, D. L. (2000). Inhibition of myosin/moesin phosphatase by expression of the phosphoinhibitor protein CPI-17 alters microfilament organization and retards cell spreading. Cell Motil. Cytoskeleton 46, 222-234.
6. Evans, D. A., Gage, J. R., and Leighton, J. L. (1992). Total synthesis of (+)-calyculin A. J. Am. Chem. Soc. 114, 9434-9453.
7. Forsyth, C. J., Sabes, S. F., and Urbanek, R. A. (1997). An efficient total synthesis of okadaic acid. J. Am. Chem. Soc. 119, 8381-8382.
8. Garber, K. (2006). The second wave in kinase cancer drugs. Nat. Biotechnol. 24, 127-136.
9. Ghosh, A., Wang, X., Klein, E., and Heston, W. (2005). Novel role of prostate-specific membrane antigen in suppressing prostate cancer invasiveness. Cancer Res. 65, 727-731.
10. Goldberg, J., Huang, H., Kwon, Y., Greengard, P., Nairn, A. C., and Kuriyan, J. (1995). Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376, 745-753.
11. Gupta, V., Ogawa, A. K., Du, X., Houk, K. N., and Armstrong, R. W. (1997). A model for binding of structurally diverse natural product inhibitors of protein phosphatases PP1 and PP2A. J. Med. Chem. 40, 3199-3206.
12. Hartshorne, D. J. (1998). Myosin phosphatase: subunits and interactions. Acta Physiol. Scand. 164, 483-493.
13. Hirano, K., Phan, B. C., and Hartshorne, D. J. (1997). Interactions of the subunits of smooth muscle myosin phosphatase. J. Biol. Chem. 272, 3683-3688.
14. Huai, Q., Kim, H.-Y., Liu, Y., Zhao, Y., Mondragon, A., Liu, J. O., and Ke, H. (2002). Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc. Natl. Acad. Sci. U.S.A. 99, 12037-12042.
15. Humphrey, J. M., Aggen, J. B., and Chamberlin, A. R. (1996). Total synthesis of the serine-threonine phosphatase inhibitor microcystin-LA. J. Am. Chem. Soc. 118, 11759-11770.
16. Kenefick, K. (2006). Small-molecule kinase inhibitors: from lab bench to clinic. Cell Notes 26-29.
17. Kita, A., Matsunaga, S., Takai, A., Kataiwa, H., Wakimoto, T., Fusetani, N., Isobe, M., and Miki, K. (2002). Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1. Structure 10, 715-724.
18. Kitazawa, T., Eto, M., Woodsome, T. P., and Khalequzzaman, M. (2002). Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca2+ sensitization in rabbit smooth muscle. J. Physiol. 546, 879-889.
19. Martin, B. I., Shriner, C. L., Brautigan, and David, L. (1994). Concurrent purification of type-1 and type-2A protein phosphatase catalytic subunits. Protein Exp. Purif. 15, 211-217.
20. Matsumura, F., and Hartshorne, D. J. (2008). Myosin phosphatase target subunit: many roles in cell function. Biochem. Biophys. Res. Commun. 369, 149-156.
21. Maynes, J. T., Bateman, K. S., Cherney, M. M., Das, A. K., Luu, H. A., Holmes, C. F., and James, M. N. (2001). Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1. J. Biol. Chem. 276, 44078-44082.
22. Mills, J. C., Stone, N. L., Erhardt, J., and Pittman, R. N. (1998). Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation. J. Cell Biol. 140, 627-636.
23. Sogawa, K., Masaki, T., Miyauchi, A., Sugita, A., Kito, K., Ueda, N., Miyamoto, K., Okazaki, K., Okutani, K., and Matsumoto, K. (1997). Enhanced expression of PPlyl, a catalytic subunit isoform of protein phosphatase type 1, in invasive ductal carcinoma of the breast. Cancer Lett. 112, 263-268.
24. Somlyo, A. P., and Somlyo, A. V. (2003). Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol. Rev. 83, 1325-1358.
25. Xia, D., Stull, J. T., and Kamm, K. E. (2005). Myosin phosphatase targeting subunit 1 affects cell migration by regulating myosin phosphorylation and actin assembly. Exp. Cell Res. 304, 506-517.
26. Yoshida, M., and Yagi, K. (1988). Two kinds of myosin phosphatases with different enzymatic properties from fresh chicken gizzard smooth muscle. Purification and characterization. J. Biochem. 103, 380-385.