References
- Adelstein, RS. (1983). Regulation of contractile proteins by phosphorylation. J. Clin. Invest., 72, 1863-1866 https://doi.org/10.1172/JCI111148
- Bai, R, Verdier-Pinard, P., Gangwar, S., Stessman, C.C., McClure, K.J., Sausville, E.A., Pettit, GR, Bates, RB. and Hamel, E. (2001). Dolastatin 11, a marine depsipeptide, arrests cells at cytokinesis and induces hyperpolymerization of purified actin. Mol. Pharmacal., 59, 462-469
- Birt, D.F., Hendrich, S. and Wang, W. (2001). Dietary agents in cancer prevention: flavonoids and isoflavonoids. Pharmacal. Ther., 90,157-177 https://doi.org/10.1016/S0163-7258(01)00137-1
- Bohl, M., Tietze, S., Sokoll, A., Madathil, S., Pfennig, F., Apostolakis, J., Fahmy, K. and Gutzeit, H.O. (2007). Flavonoids affect actin functions in cytoplasm and nucleus. Biophys. J., 93, 2767-2780 https://doi.org/10.1529/biophysj.107.107813
- Boyum, A (1976). Isolation of lymphocytes, granulocytes and macrophages. Scand. J. Immunol., 5, 9-15
- Bresnick, AR (1999). Molecular mechanisms of nonmuscle myosin-II regulation. Curr. Opin. Cell Bioi., 11, 26-33 https://doi.org/10.1016/S0955-0674(99)80004-0
- Chabner, BA and Roberts, Jr., T.G (2005). Timeline: Chemotherapy and the war on cancer. Nat. Rev. Cancer., 5, 65-72 https://doi.org/10.1038/nrc1529
- Clarke, M. and Spudich, JA (1977). Nonmuscle contractile proteins: The role of actin and myosin in cell motility and shape determination. Annu. Rev. Biochern., 46, 797-822 https://doi.org/10.1146/annurev.bi.46.070177.004053
- Connell, L.E. and Helfman, D.M. (2006). Myosin light chain kinase plays a role in the regulation of epithelial cell survival. J. Cell. Sci., 119, 2269-2281 https://doi.org/10.1242/jcs.02926
- De Lanerolle, P. and Paul, RJ. (1991). Myosin phosphorylation/dephosphorylation and regulation of airway smooth muscle contractility. Am. J. Physiol. Lung Cell Mol. Physiol., 261, 1-14
- Farah, M.E. and Amberg, D.C. (2007). Conserved actin cysteine residues are oxidative stress sensors that can regulate cell death in yeast. Mol. Bioi. Cell., 18, 1359-1365 https://doi.org/10.1091/mbc.E06-08-0718
- Fazal, F., Gu, L., Ihnatovych, I., Han, Y, Hu, W, Antic, N., Carreira, F., Blomquist, J.F., Hope, T.J. and Ucker, D.S. (2005). Inhibiting myosin light chain kinase induces apoptosis in vitro and in vivo. Mol. Cell. BioI., 25, 6259-6266 https://doi.org/10.1128/MCB.25.14.6259-6266.2005
- Fenteany, G and Zhu, S. (2003). Small-molecule inhibitors of actin dynamics and Cell Motility. Curr. Top. Med. Chem., 3, 593-616 https://doi.org/10.2174/1568026033452348
- Galati, G and O'Brien, P.J. (2004). Potential toxicity of flavonoids and other dietary phenolics: significance for their chemopreventive and anticancer properties. Free Radic. BioI. Med., 37, 287-303 https://doi.org/10.1016/j.freeradbiomed.2004.04.034
- Giganti, A and Friederich, E. (2003). The actin cytoskeleton as a therapeutic target: state of the art and future directions. Prog. Cell Cycle Res., 5, 511-526
- Goldie, J.H. (2001). Drug resistance in cancer: A perspective. Cancer Metastasis Rev., 20, 63-68 https://doi.org/10.1023/A:1013164609041
- Gourlay, C.W and Ayscough, K.R (2003). The actin cytoskeleton: a key regulator of apoptosis and ageing? Proteomics, 422, 198-207
- Gourlay, C.W and Ayscough, K.R (2005). Identification of an upstream regulatory pathway controlling actin-mediated apoptosis in yeast. J. Cell. Sci., 118, 2119-2132 https://doi.org/10.1242/jcs.02337
- Gourlay, C.W and Ayscough, K.R (2006). Actin-induced hyperactivation of the ras signaling pathway leads to apoptosis in saccharomyces cerevisiae. Mol. Cell. Bioi., 26, 6487-6501 https://doi.org/10.1128/MCB.00117-06
- Gu, L.Z., Hu, WY, Antic, N., Mehta, R, Turner, J.R and de Lanerolle, P. (2006). Inhibiting myosin light chain kinase retards the growth of mammary and prostate cancer cells. Eur. J. Cancer., 42, 948-957 https://doi.org/10.1016/j.ejca.2005.12.017
- Hortobagyi, GN. (2001). Progress in systemic chemotherapy of primary breast cancer: an overview. J. Natl. Cancer Inst. Monographs, 2001, 72
- Jana, S.S., Kawamoto, S. and Adelstein, RS. (2006). A specific isoform of nonmuscle myosin II-C is required for cytokinesis in a tumor cell line. J. Bioi. Chem., 281, 24662-24670 https://doi.org/10.1074/jbc.M604606200
- Jay, P.Y. (1995). A mechanical function of myosin II in cell motility. J. Cell. Sci., 108, 387-393
- Jin, Y, Atkinson, S.J., Marrs, JA and Gallagher, P.J. (2001). Myosin II light chain phosphorylation regulates membrane localization and apoptotic signaling of tumor necrosis factor receptor-1. J. BioI. Chem., 276, 30342-30349 https://doi.org/10.1074/jbc.M102404200
- Jordan, MA and Wilson, L. (1998). Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr. Opin. Cell BioI., 10, 123-130 https://doi.org/10.1016/S0955-0674(98)80095-1
- Jordan, MA and Wilson, L. (2004). Microtubules as a target for anticancer drugs. Nat. Rev. Cancer, 4, 253-265 https://doi.org/10.1038/nrc1317
- Kamm, K.E. and Stull, J.T. (1985). The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu. Rev. Pharmacol. Toxicol., 25, 593-620 https://doi.org/10.1146/annurev.pa.25.040185.003113
- Kaneko, K., Satoh, K., Masamune, A, Satoh, A and Shimosegawa, T. (2002). Myosin light chain kinase inhibitors can block invasion and adhesion of human pancreatic cancer cell lines. Pancreas, 24, 34-41 https://doi.org/10.1097/00006676-200201000-00005
- Kolodney, M.S. and Elson, E.L. (1993). Correlation of myosin light chain phosphorylation with isometric contraction of fibroblasts. J. Biol. Chem., 268, 23850-23855
- Mahajan, RK., Vaughan, K.T., Johns, JA and Pardee, J.D. (1989). Actin filaments mediate dictyostelium myosin assembly in vitro. Proc. Natl. A cad. Sci. U.S.A., 86, 6161-6165 https://doi.org/10.1073/pnas.86.16.6161
- Nicoletti, I., Migliorati, G, Pagliacci, M.C., Grignani, F. and Riccardi, C. (1991). A rapid and simple method for measuring thymocyte apoptosis by propodium iodide staining and flow cytometry. J. Immunol. Methods, 139, 271-279 https://doi.org/10.1016/0022-1759(91)90198-O
- Nijveldt, RJ., van Nood, E., van Hoorn, D.E.C., Boelens, P.G, van Norren, K. and van Leeuwen, PAM. (2001). Flavonoids: a review of probable mechanisms of action and potential applications. Am. J. Clin. Nutr., 74, 418-425
- Odaka, C., Sanders, M.L. and Crews, P. (2000). Jasplakinolide iduces apoptosis in various transformed cell lines by a caspase-3-like protease-dependent pathway. Clin. Vaccine Immunol., 7, 947-952 https://doi.org/10.1128/CDLI.7.6.947-952.2000
- Ostrow, B.D. (1994). Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells. J. Cell Bioi., 127, 1945-1955 https://doi.org/10.1083/jcb.127.6.1945
- Posey, S.C. and Bierer, B.E. (1999). Actin Stabilization by Jasplakinolide Enhances apoptosis induced by cytokine deprivation. J. Biol. Chem., 274, 4259-4265 https://doi.org/10.1074/jbc.274.7.4259
- Rao, J.Y., Jin, YS., Zheng, Q.L., Cheng, J., Tai, J. and Hemstreet, GP. (1999). Alterations of the actin polymerization status as an apoptotic morphological effector in HL-60 cells. J. Cell. Biochem., 75, 686-697 https://doi.org/10.1002/(SICI)1097-4644(19991215)75:4<686::AID-JCB14>3.0.CO;2-F
- Shen, L., Black, E.D., Witkowski, E.D., Lencer, WI., Guerriero, V., Schneeberger, E.E. and Turner, J.R (2006). Myosin light chain phosphorylation regulates barrier function by remodeling tight junction structure. J. Cell. Sci., 119, 2095-2106 https://doi.org/10.1242/jcs.02915
- Singh, N.P., McCoy, M.T., Tice, RR and Schneider, E.L. (1988). A simple technique for quantitation of low levels of DNA damage in individual cells. Exp. Cell Res., 175, 184-191 https://doi.org/10.1016/0014-4827(88)90265-0
- Skibola, C.F. and Smith, M.T. (2000). Potential health impacts of excessive f1avonoids intake. Free Radic. BioI. Med., 29, 375-383 https://doi.org/10.1016/S0891-5849(00)00304-X
- Suzuki, E., Ota, T., Tsukuda, K., Okita, A, Matsuoka, K., Murakami, M., Doihara, H. and Shimizu, N. (2004). nm23-H1 reduces in vitro cell migration and the liver metastatic potential of colon cancer cells by regulating myosin light chain phosphorylation. Int. J. Cancer, 108, 207-211 https://doi.org/10.1002/ijc.11546
- Thomas, M.G, Santa Coloma, TA, Correale, J. and Boccaccio, GL. (2002). Myosin light chain kinase inhibitors induce retraction of mature oligodendrocyte processes. Neurochem. Res., 27,1305-1312 https://doi.org/10.1023/A:1021615530960
- Verin, AD., Birukova, A, Wang, P., Liu, F., Becker, P., Birukov, K. and Garcia, J.GN. (2001). Microtubule disassembly increases endothelial cell barrier dysfunction: role of MLC phosphorylation. Am. J. Physiol. Lung Cell Mol. Physiol., 281, 565-574
- Wilson, AK. (1991). An increase or a decrease in myosin II phosphorylation inhibits macrophage motility. J. Cell Bioi., 114, 277-283 https://doi.org/10.1083/jcb.114.2.277
- Wysolmerski, R.B. and Lagunoff, D. (1990). Involvement of myosin light-chain kinase in endothelial cell retraction. Proc. Natl. Acad. Sci. U.S.A., 87, 16-20 https://doi.org/10.1073/pnas.87.1.16
- Wysolmerski, R.B. and Lagunoff, D. (1991). Regulation of permeabilized endothelial cell retraction by myosin phosphorylation. Am. J. Physiol., Cell Physiol., 261, 32-40
- Yamakita, Y. (1994). In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells. J. Cell Bioi., 124,129-137 https://doi.org/10.1083/jcb.124.1.129
- Zhou, X., Liu, Y., You, J., Zhang, H., Zhang, X. and Ye, L. (2008). Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2. Cancer Lett., 270, 312-327 https://doi.org/10.1016/j.canlet.2008.05.028