Targeting the actin cytoskeleton: Selective antitumor action via trapping PKCε

Cell Death and Disease

Volumn 5, Issue 8, 2014, Pages

  Foerster, F ^a   Braig, S ^a   Moser, C ^a   Kubisch, R ^a   Busse, J ^a   Wagner, E ^a   Schmoeckel, E ^a   Mayr, D ^a   Schmitt, S ^b   Huettel, S ^a   Zischka, H ^b   Mueller, R ^c,d   Vollmar, A M ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b INSTITUTE OF EPIDEMIOLOGY   (Germany)

^c SAARLAND UNIVERSITY   (Germany)

^d SAARLAND UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHONDRAMIDE; CYTOCHROME C; CYTOTOXIC AGENT; HEXOKINASE; HEXOKINASE II; PROTEIN BAD; PROTEIN KINASE C EPSILON; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL; ACTIN; ANTINEOPLASTIC AGENT; CHONDRAMIDE A; DEPSIPEPTIDE; PHOSPHATIDYLSERINE; PROTEIN KINASE C;

ACTIN FILAMENT; ACTIN POLYMERIZATION; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTINEOPLASTIC ACTIVITY; APOPTOSIS; ARTICLE; BINDING SITE; BLEACHING; BREAST CANCER; BREAST CANCER CELL LINE; CANCER GROWTH; CELL SPECIFICITY; CONTROLLED STUDY; ENZYME PHOSPHORYLATION; HUMAN; HUMAN CELL; IN VITRO STUDY; MITOCHONDRIAL MEMBRANE; MITOCHONDRIAL PERMEABILITY; MITOCHONDRION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; SIGNAL TRANSDUCTION; TUMOR XENOGRAFT; ANIMAL; BREAST NEOPLASMS; CELL PROLIFERATION; DRUG EFFECTS; FEMALE; FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING; GENETICS; MCF 7 CELL LINE; METABOLISM; MITOCHONDRIAL MEMBRANE POTENTIAL; PATHOLOGY; SCID MOUSE; TUMOR CELL LINE; XENOGRAFT;

ACTIN CYTOSKELETON; ACTINS; ANIMALS; ANTINEOPLASTIC AGENTS; APOPTOSIS; BCL-ASSOCIATED DEATH PROTEIN; BINDING SITES; BREAST NEOPLASMS; CELL LINE, TUMOR; CELL PROLIFERATION; CYTOCHROMES C; DEPSIPEPTIDES; FEMALE; FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING; HEXOKINASE; HUMANS; MCF-7 CELLS; MEMBRANE POTENTIAL, MITOCHONDRIAL; MICE; MICE, SCID; MITOCHONDRIA; PHOSPHATIDYLSERINES; PROTEIN KINASE C; SIGNAL TRANSDUCTION; TRANSPLANTATION, HETEROLOGOUS; VOLTAGE-DEPENDENT ANION CHANNELS;

EID: 84906890367     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2014.363     Document Type: Article

References (46)

1. Franklin-Tong VE, Gourlay CW. A role for actin in regulating apoptosis/programmed cell death: evidence spanning yeast, plants and animals. Biochem J 2008; 413: 389-404.
2. Steinberg SF. Structural basis of protein kinase C isoform function. Physiol Rev 2008; 88: 1341-1378.
3. Prekeris R, Hernandez RM, Mayhew MW, White MK, Terrian DM. Molecular analysis of the interactions between protein kinase C-epsilon and filamentous actin. J Biol Chem 1998; 273: 26790-26798.
4. Baines CP, Song CX, Zheng YT, Wang GW, Zhang J, Wang OL et al. Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria. Circ Res 2003; 92: 873-880.
5. Zeidman R, Troller U, Raghunath A, Pahlman S, Larsson C. Protein kinase Cepsilon actin-binding site is important for neurite outgrowth during neuronal differentiation. Mol Biol Cell 2002; 13: 12-24.
6. Pan Q, Bao LW, Kleer CG, Sabel MS, Griffith KA, Teknos TN et al. Protein kinase C epsilon is a predictive biomarker of aggressive breast cancer and a validated target for RNA interference anticancer therapy. Cancer Res 2005; 65: 8366-8371.
7. Song MS, Park YK, Lee JH, Park K. Induction of glucose-regulated protein 78 by chronic hypoxia in human gastric tumor cells through a protein kinase C-epsilon/ERK/AP-1 signaling cascade. Cancer Res 2001; 61: 8322-8330.
8. Okhrimenko H, Lu W, Xiang C, Hamburger N, Kazimirsky G, Brodie C. Protein kinase C-epsilon regulates the apoptosis and survival of glioma cells. Cancer Res 2005; 65: 7301-7309.
9. Toton E, Ignatowicz E, Skrzeczkowska K, Rybczynska M. Protein kinase Cepsilon as a cancer marker and target for anticancer therapy. Pharmacol Rep 2011; 63: 19-29.
10. Basu A, Sivaprasad U. Protein kinase Cepsilon makes the life and death decision. Cell Signal 2007; 19: 1633-1642.
11. Garg R, Blando J, Perez CJ, Wang H, Benavides FJ, Kazanietz MG. Activation of nuclear factor kappaB (NF-kappaB) in prostate cancer is mediated by protein kinase C epsilon (PKCepsilon). J Biol Chem 2012; 287: 37570-37582.
12. Newton PM, Messing RO. The substrates and binding partners of protein kinase Cepsilon. Biochem J 2010; 427: 189-196.
13. Danial NN. BAD: undertaker by night, candyman by day. Oncogene 2008; 27(Suppl 1): S53-S70.
14. Galluzzi L, Kepp O, Tajeddine N, Kroemer G. Disruption of the hexokinase-VDAC complex for tumor therapy. Oncogene 2008; 27: 4633-4635.
15. Mathupala SP, Ko YH, Pedersen PL. Hexokinase II: cancer's double-edged sword acting as both facilitator and gatekeeper of malignancy when bound to mitochondria. Oncogene 2006; 25: 4777-4786.
16. McCommis KS, Baines CP. The role of VDAC in cell death: friend or foe? Biochim Biophys Acta 2012; 1818: 1444-1450.
17. Roy SS, Madesh M, Davies E, Antonsson B, Danial N, Hajnoczky G. Bad targets the permeability transition pore independent of Bax or Bak to switch between Ca2+-dependent cell survival and death. Mol Cell 2009; 33: 377-388.
18. Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 2007; 87: 99-163.
19. Green DR, Kroemer G. The pathophysiology of mitochondrial cell death. Science 2004; 305: 626-629.
20. Bernardi P, Krauskopf A, Basso E, Petronilli V, Blachly-Dyson E, Di Lisa F et al. The mitochondrial permeability transition from in vitro artifact to disease target. FEBS J 2006; 273: 2077-2099.
21. Halestrap AP. A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection. Biochem Soc Trans 2010; 38: 841-860.
22. Vander Heiden MG, Chandel NS, Williamson EK, Schumacker PT, Thompson CB. Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria. Cell 1997; 91: 627-637.
23. Brenner C, Grimm S. The permeability transition pore complex in cancer cell death. Oncogene 2006; 25: 4744-4756.
24. Reubold TF, Eschenburg S. A molecular view on signal transduction by the apoptosome. Cell Signal 2012; 24: 1420-1425.
25. Crompton M, Ellinger H, Costi A. Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem J 1988; 255: 357-360.
26. Broekemeier KM, Dempsey ME, Pfeiffer DR. Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria. J Biol Chem 1989; 264: 7826-7830.
27. Sasse F, Kunze B, Gronewold TM, Reichenbach H. The chondramides: cytostatic agents from myxobacteria acting on the actin cytoskeleton. J Natl Cancer Inst 1998; 90: 1559-1563.
28. Eggert U, Diestel R, Sasse F, Jansen R, Kunze B, Kalesse M. Chondramide C: synthesis, configurational assignment, and structure-activity relationship studies. Angew Chem Int Ed Engl 2008; 47: 6478-6482.
29. Herrmann J, Huttel S, Muller R. Discovery and biological activity of new Chondramides from Chondromyces sp. Chembiochem 2013; 14: 1573-1580.
30. Hall A. The cytoskeleton and cancer. Cancer Metastasis Rev 2009; 28: 5-14.
31. Kuppens IE. Current state of the art of new tubulin inhibitors in the clinic. Curr Clin Pharmacol 2006; 1: 57-70.
32. Posey SC, Martelli MP, Azuma T, Kwiatkowski DJ, Bierer BE. Failure of gelsolin overexpression to regulate lymphocyte apoptosis. Blood 2000; 95: 3483-3488.
33. Bubb MR, Spector I, Beyer BB, Fosen KM. Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations. J Biol Chem 2000; 275: 5163-5170.
34. Lazaro-Dieguez F, Aguado C, Mato E, Sanchez-Ruiz Y, Esteban I, Alberch J et al. Dynamics of an F-actin aggresome generated by the actin-stabilizing toxin jasplakinolide. J Cell Sci 2008; 121: 1415-1425.
35. Mochly-Rosen D, Das K, Grimes KV. Protein kinase C, an elusive therapeutic target? Nat Rev Drug Discov 2012; 11: 937-957.
36. Oliva JL, Caino MC, Senderowicz AM, Kazanietz MG. S-Phase-specific activation of PKC alpha induces senescence in non-small cell lung cancer cells. J Biol Chem 2008; 283: 5466-5476.
37. Lau E, Kluger H, Varsano T, Lee K, Scheffler I, Rimm DL et al. PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Cell 2012; 148: 543-555.
38. Aziz MH, Manoharan HT, Church DR, Dreckschmidt NE, Zhong W, Oberley TD et al. Protein kinase Cepsilon interacts with signal transducers and activators of transcription 3 (Stat3), phosphorylates Stat3Ser727, and regulates its constitutive activation in prostate cancer. Cancer Res 2007; 67: 8828-8838.
39. Chiang CW, Kanies C, Kim KW, Fang WB, Parkhurst C, Xie M et al. Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis. Mol Cell Biol 2003; 23: 6350-6362.
40. Meshki J, Caino MC, von Burstin VA, Griner E, Kazanietz MG. Regulation of prostate cancer cell survival by protein kinase Cepsilon involves bad phosphorylation and modulation of the TNFalpha/JNK pathway. J Biol Chem 2010; 285: 26033-26040.
41. Murakoshi H, Lee SJ, Yasuda R. Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP. Brain Cell Biol 2008; 36: 31-42.
42. Zamzami N, Metivier D, Kroemer G. Quantitation of mitochondrial transmembrane potential in cells and in isolated mitochondria. Methods Enzymol 2000; 322: 208-213.
43. von Schwarzenberg K, Wiedmann RM, Oak P, Schulz S, Zischka H, Wanner G et al. Mode of cell death induction by pharmacological vacuolar H+-ATPase (V-ATPase) inhibition. J Biol Chem 2013; 288: 1385-1396.
44. Rudy A, Lopez-Anton N, Barth N, Pettit GR, Dirsch VM, Schulze-Osthoff K et al. Role of Smac in cephalostatin-induced cell death. Cell Death Differ 2008; 15: 1930-1940.
45. Schmitt S, Saathoff F, Meissner L, Schropp EM, Lichtmannegger J, Schulz S et al. A semiautomated method for isolating functionally intact mitochondria from cultured cells and tissue biopsies. Anal Biochem 2013; 443: 66-74.
46. Cenni V, Doppler H, Sonnenburg ED, Maraldi N, Newton AC, Toker A. Regulation of novel protein kinase C epsilon by phosphorylation. Biochem J 2002; 363: 537-545.