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Melanoma cells

Human GAL1 receptor mRNA has been detected in multiple cell and tissue samples including Bowes melanoma cells, brain, gastrointestinal tract (from esophagus to rectum), heart, prostate, and testes. Rat GAL1 mRNA was detected in olfactory regions, many hypothalamic nuclei (including supraoptic nucleus),... [Pg.520]

Anderson, R.L., Tao, T.W., Betten, D.A., Hahn, G.M. (1986). Heat shock protein levels are not elevated in heat resistant B16 melanoma cells. Radiat Res. 105,240-246. [Pg.450]

Villa R., Folini M., Lualdi S., Veronese S., Daidone M.C., Zaffaroni N. Inhibition of telomerase activity by a cell-penetrating peptide nucleic acid construct in human melanoma cells. FEB.S. Lett. 2000 473 241-248. [Pg.176]

RECORD I R, BROADBENT J L, KING R A, DREOSTI I E, HEAD R J, TONKIN A L (1997) Geuisteiu inhibits growth of B16 melanoma cells in vivo and in vitro and promotes differentiation in vitro. In J Cancer 72 860-64. [Pg.85]

IC50 values of cisplatin and AU55 and Figures 29a and b show the course of cell viabilities in dependence of the molar concentrations in case of melanoma cells. [Pg.18]

Besides melanoma cells with the extraordinary sensitivity towards AU55, the difference in toxicity is also very obvious for Hek-12 and U-20S where the effectiveness of AU55 is 32 and 18 times higher than that of cisplatin. [Pg.18]

Figure 29. Comparison of the viability of melanoma cells treated with cisplatin (a) and Au55(Ph2PC6H4S03H)i2Cl6 (b) in dependence of the molar concentrations. (Reprinted from Ref [77], 2005, with permission from Wiley-VCH.)... Figure 29. Comparison of the viability of melanoma cells treated with cisplatin (a) and Au55(Ph2PC6H4S03H)i2Cl6 (b) in dependence of the molar concentrations. (Reprinted from Ref [77], 2005, with permission from Wiley-VCH.)...
Bolton, J. L. Pisha, E. Shen, L. Krol, E. S. Iverson, S. L. Huang, Z. van Breemen, R. B. Pezzuto, J. M. The reactivity of o-quinones which do not isomerize to quinone methides correlates with alkylcatechol-induced toxicity in human melanoma cells. Chem.-Biol. Interact. 1997, 106, 133-148. [Pg.354]

Murakami T, Maki W, Cardones AR, et al. Expression of CXC chemokine receptor-4 enhances the pulmonary metastatic potential of murine B16 melanoma cells. Cancer Res 2002 62 7328-7334. [Pg.345]

Robledo MM, Bartolome RA, Longo N, et al. Expression of functional chemokine receptors CXCR3 and CXCR4 on human melanoma cells. J Biol Chem 2001 48 45098—45105. [Pg.347]

Kawada K, Sonoshita M, Sakashita H, et al. Pivotal role of CXCR3 in melanoma cell metastasis to lymph nodes. Cancer Res 2004 64 4010 1017. [Pg.347]

Mori T, Kim J, Yamano T, et al. Epigenetic up-regulation of C-C chemokine receptor 7 and C-X-C chemokine receptor 4 expression in melanoma cells. Cancer Res 2005 65 180-187. [Pg.347]

Ramjeesingh R, Leung R, Siu C-H. Interleukin-8 secreted by endothelial cell induces chemotaxis of melanoma cells through the chemokine receptor CXCR1. FASEB J 2003 17 1292-1294. [Pg.348]

Ponnazhagan and Kwon (1992) reported a putative tissue-specific ds-element (TE-1) located at-236 bp of the mouse tyrosinase promoter. They partially purified a TE-1 binding protein (approximately 49 kDa in size), but tissue specificity remains to be confirmed by a more detailed analysis. For the human tyrosinase promoter, Shibata et al. (1992) identified a 200-bp pigment cell-specific enhancer, located between -2.0 and -1.8 kb. A minimum core sequence of 39 bp was shown to be sufficient to confer the specific activity, although other regions (not identified so far) within the 200-bp fragment are required for more efficient expression in melanoma cells (Shibata et al., 1992). [Pg.170]

Jara, J. R., Martinez-Liarte, J. H., Solano, F., and Penafiel, R. (1988). Transport of L-tyrosine by B16 F10 melanoma cells the effect of the intracellular content of other amino acids. J. Cell Sci. 97 479-485. [Pg.173]

Kemeny-Beke A, Aradi J, Damjanovich J, et al. Apoptotic response of uveal melanoma cells upon treatment with chelidonine, sanguinarine and chelerythrine. Cancer Lett 2005, in press. [Pg.225]

It has been demonstrated in other cell types that lutein can inhibit expression of MMPs and/ or activity (Philips et al., 2007). For example, in dermal fibroblasts lutein inhibits expression of MMP-1 and decreases levels of MMP-2 protein (Philips et al., 2007). In melanoma cells, lutein inhibits MMP-1 expression while stimulating TIMP-2 (Philips et al., 2007). Moreover it has been shown that lutein inhibits elastin expression in fibroblasts subjected to oxidative stress by exposure to ultraviolet light (Philips et al., 2007). These results clearly indicate that lutein can play an important role in remodeling of the extracellular matrix. [Pg.336]

Philips, N, Keller, T, Hendrix, C, Hamilton, S, Arena, R, Tuason, M, and Gonzalez, S, 2007. Regulation of the extracellular matrix remodeling by lutein in dermal fibroblasts, melanoma cells, and ultraviolet radiation exposed fibroblasts. Arch Dermatol Res 299, 373-379. [Pg.349]


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B16 melanoma cell lines

B16 melanoma cells

B16F10 melanoma cells

Binding to melanoma cells

Bowes melanoma cell line

Central melanoma cells

Human cancer cell lines melanoma

Human melanoma cell line

Melanoma cancer cell lines

Melanoma cells and

Melanoma cells human

Murine melanoma cell

Murine melanoma cell lines

Murine melanoma cells and

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