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• W2091247266 abstract "AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Abstract 12(S)-hydroxyeicosatetraenoic acid [12(S)-HETE], a lipoxygenase metabolite of arachidonic acid, has been shown to be involved in a wide variety of cellular activities (i.e., adhesion, spreading, motility, invasion) which promote metastasis to occur in tumor cells. In this study, several techniques (Western blotting, flow cytometry and DNase I assay) were performed to examine the alterations in the distribution of G- and F-actin expressed in B16a melanoma cells. Each of these methods independently revealed that 12(S)-HETE treatment (0.1 mM, 15 min) resulted in an increase in the F-actin content in the cytoskeletal preparations. Since the integrity of cytoskeletal networks (i.e., actin filaments) can be dynamically regulated through protein phosphorylation, we investigated the potential role of several protein kinases in the 12(S)-HETE-induced actin polymerization. By flow cytometric analysis, 12(S)-HETE was found to increase the actin filament contents. This effect could be inhibited by protein kinase C (PKC) inhibitors (calphostin C and staurosporine) as well as by protein tyrosine kinase (PTK) inhibitor (genistein) but not by protein kinase A inhibitor (H8), suggesting that the 12(S)-HETE effect involves PKC and PTK. This conclusion is consistent with the observations that phorbol 12-myristate-13-acetate (PMA) mimics the biological effect of 12(S)-HETE in promoting the F-actin formation in B16a cells. As a final analysis, direct protein phosphorylation studies indicate that 12(S)-HETE treatment led to enhanced phosphorylation of myosin light chain, which may contribute to the increased stress fiber formation following 12(S)-HETE stimulation. Int. J. Cancer 77:271–278, 1998.© 1998 Wiley-Liss, Inc. References Apgar, J. R., Activation of protein kinase C in rat basophilic leukemia cells stimulates increased production of phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate: correlation with actin polymerization. Mol. Biol. Cell., 6, 97– 108 (1995). Blikstad, I., Markey, F., Carelsson, L., Persson, T. and Lindberg, U., Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell, 15, 935– 948 (1978). Hall, A., Ras-related GTPases and the cytoskeleton. Mol. Biol. Cell, 3, 475– 479 (1992). Honn, K. V. and Tang, D. G., Adhesion molecules and tumor cell interaction with the endothelium and subendothelial matrix. Cancer Metastasis Rev., 11, 353– 375 (1992). Honn, K. V., Tang, D. G., Duniec, Z. M., Grossi, I. M., Timar, J., Renaud, C., Leithauser, M., Blair, I., Diglio, C. A., Kimler, V. A., Taylor, J. D. and Marnett, L. J., Tumor cell-derived 12(S)-hydroxyeicosatetraenoic acid induces microvascular endothelial cell retraction. Cancer Res., 54, 565– 574 (1994). Klemke, R. L., Cai, S., Giannini, A. L., Gallagher, P. J., de Lanerolle, P. and Cheresh, D. A., Regulation of cell motility by mitogen-activated protein kinase. J. Cell Biol., 137, 481– 492 (1997). Liu, B., Khan, W. A., Hannun, Y., Timar, J., Taylor, J. D., Lundy, S., Butovich, I. and Honn, K. V., 12(S)-hydroxyeicosatetraenoic acid and 13(S)-hydroxyoctadienoic acid regulation of protein kinase C-α in melanoma cells: role of receptor-mediated hydrolysis of inositol phospholipids. Proc. nat. Acad. Sci. (Wash.), 92, 9323– 9327 (1995). Melamed, I., Stein, L. and Roifman, C. M., Epstein-Barr virus induces actin polymerization in human B cells. J. Immunol., 153, 1998– 1998 (1994). Mochly-Rosen, D., Henrich, C. J., Cheever, L., Khaner, H. and Simpson, P. C., A protein kinase C isozyme is translocated to cytoskeletal elements on activation. Cell Regul., 1, 693– 705 (1990). Niu, M. Y. and Nachmias, V. T., Two-step mechanism for actin polymerization in human erythroleukemia cells induced by phorbol ester. Cell Motil. Cytoskel., 27, 327– 336 (1994). Pfeiffer, J. R. and Oliver, J. M., Tyrosine kinase-dependent assembly of actin plaques linking Fc-epsilon-R1 cross-linking to increased cell substrate adhesion in RBL-2H3 tumor mast cells. J. Immunol., 152, 270– 279 (1994). Phatak, P. D. and Packman, C. H., Engagement of the T-cell antigen receptor by anti-CD3 monoclonal antibody causes a rapid increase in lymphocyte F-actin. J. cell. Physiol., 159, 365– 370 (1994). Pienta, K. J. and Coffey, D. S., Nuclear-cytoskeletal interactions: evidence for physical connections between the nucleus and cell periphery and their alteration by transformation. J. cell. Biochem., 49, 357– 365 (1992). Piomelli, D., Volterra, A., Dale, N., Siegelbaum, S. A., Kandel, E. R., Schwartz, J. H. and Belardetti, F., Lipoxygenase metabolites of arachidonic acid as second messengers for presynaptic inhibition of Alpysiasensory cells. Nature (Lond.), 328, 38– 43 (1987). Rao, J. Y., Hemstreet, G. P., III, Hurst, R. E., Bonner, R. B., Min, K. W. and Jones, P. L., Cellular F-actin levels as a marker for cellular transformation: correlation with bladder cancer risk. Cancer Res., 51, 2762– 2767 (1991). Singer, H. A., Oren, J. W. and Benscoter, H. A., Myosin light chain phosphorylation of 32P-labeled rabbit aorta stimulated by phorbol 12,13-dibutyrate and phenylephrine. J. biol. Chem., 264, 21215– 21222 (1989). Steinert, B. W., Tang, D. G., Jones, C. L., Grossi, I. M., Umbarger, L. A. and Honn, K. V., Studies on the role of platelet eicosanoid metabolism and integrin αIIbβ3 in tumor cell induced platelet aggregation. Int. J. Cancer, 54, 92– 101 (1993). Sundareshan, P. and Hendrix, M. J. C., Growth, morphologic, and invasive characteristics of early and late passages of a human endothelial carcinoma cell line (RL95-2). In Vitro cell. Develop. Biol., 28A, 544– 552 (1992). Tang, D. G. and Honn, K. V., 12-Lipoxygenase, 12(S)-HETE, and cancer metastasis. Annals N. Y. Acad. Sci., 772, 199– 215 (1994). Tang, D. G., Tarrien, M., Dobrzynski, P. and Honn, K. V., Melanoma cell spreading in fibronectin induced by 12(S)-HETE involves both protein kinase C-and protein kinase-dependent focal adhesion formation and tyrosine phosphorylation of focal adhesion kinase (pp125fak). J. cell. Physiol., 165, 291– 306 (1995). Tang, D. G., Timar, J., Grossi, I. M., Renaud, C., Kimler, V. A., Taylor, J. D. and Honn, K. V., The lipoxygenase, 12(S)-HETE, induces a protein kinase C-dependent cytoskeletal rearrangement and retraction of microvascular endothelial cells. Exp. Cell Res., 207, 361– 375 (1993). Verschueren, H., Van der Taelen, I., Dewit, J., De Brakeleer, J. and De Baetselier, P., Metastatic competence of BW5147 T-lymphoma cell lines is correlated with in vitro, invasiveness, motility and F-actin content. J. Leukocyte Biol., 55, 552– 556 (1994). Citing Literature Volume77, Issue217 July 1998Pages 271-278 ReferencesRelatedInformation" @default.
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• W2091247266 title "12(S)-hydroxyeicosatetraenoic acid increases the actin microfilament content in B16a melanoma cells: A protein kinase-dependent process" @default.
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