M. Kit, Qiagen) according to the manufacturer's instructions. RT was carried out with oligo(dT) and, pp.1-4

. ?g, I. Superscript, H. Rnase, and . Transcriptase, The expression of specific mRNAs was investigated by RT-PCR using primers for matrix metalloproteinase-2 and -9 (MMP-2, MMP-9), vascular endothelial growth factor (VEGF-A), tumor necrosis factor alpha (TNF-?), signal transducer and activator of transcription 1 (STAT-1), melanoma inhibitory activity (MIA), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). PCR was performed in a RoboCycler 96 (Stratagene) with the following primers: MMP-2 sense 5'-GAGTTGGCAGTGCAATACCT-3' and antisense 5'- GCCGTCCTTCTCAAAGTTGT-3'; MMP-9 sense 5'- AGTTTGGTGTCGCGGAGCAC-3' and antisense 5'- TACATGAGCGCTTCCGGCAC-3'; VEGF-A sense 5'- AGAGCAACATCACCATGCAG-3' and antisense 5'- AGGAATCCCAGAAACAACCC-3'; TNF-? sense 5'- ACTCCCAGAAAAGCAAGCAA-3' and antisense 5'- TGGAAGACTCCTCCCAGGTA-3'; STAT-1 sense 5

M. Srivastava and H. Pollard, Molecular dissection of nucleolin's role in growth and cell proliferation: new insights, FASEB J, vol.13, pp.1911-1922, 1999.

S. Storck, M. Shukla, S. Dimitrov, and P. Bouvet, Functions Of The Histone Chaperone Nucleolin In Diseases, Subcell Biochem, vol.41, pp.125-169, 2007.
DOI : 10.1007/1-4020-5466-1_7
URL : https://hal.archives-ouvertes.fr/hal-00337699

A. Hovanessian, F. Puvion-dutilleul, S. Nisole, J. Svab, E. Perret et al., The Cell-Surface-Expressed Nucleolin Is Associated with the Actin Cytoskeleton, Experimental Cell Research, vol.261, issue.2, pp.312-328, 2000.
DOI : 10.1006/excr.2000.5071

A. Hovanessian, Midkine, a cytokine that inhibits HIV infection by binding to the cell surface expressed nucleolin, Cell Research, vol.271, issue.2, pp.174-181, 2006.
DOI : 10.1056/NEJM199302043280508
URL : https://hal.archives-ouvertes.fr/hal-00104911

S. Nisole, B. Krust, and A. Hovanessian, Anchorage of HIV on Permissive Cells Leads to Coaggregation of Viral Particles with Surface Nucleolin at Membrane Raft Microdomains, Experimental Cell Research, vol.276, issue.2, pp.155-173, 2002.
DOI : 10.1006/excr.2002.5522

J. Sinclair, O. Brien, and A. , Intimin Types ??, ??, and ?? Bind to Nucleolin with Equivalent Affinity but Lower Avidity than to the Translocated Intimin Receptor, Journal of Biological Chemistry, vol.279, issue.32, pp.33751-33758, 2004.
DOI : 10.1074/jbc.M401616200

M. Barel, A. Hovanessian, K. Meibom, J. Briand, M. Dupuis et al., A novel receptor ??? ligand pathway for entry of Francisella tularensis in monocyte-like THP-1 cells: interaction between surface nucleolin and bacterial elongation factor Tu, BMC Microbiology, vol.8, issue.1, pp.145-163, 2008.
DOI : 10.1186/1471-2180-8-145
URL : https://hal.archives-ouvertes.fr/hal-00324631

M. Losfeld, D. Khoury, P. Mariot, M. Carpentier, B. Krust et al., The cell surface expressed nucleolin is a glycoprotein that triggers calcium entry into mammalian cells, Experimental Cell Research, vol.315, issue.2, pp.357-369, 2009.
DOI : 10.1016/j.yexcr.2008.10.039
URL : https://hal.archives-ouvertes.fr/hal-00347895

S. Aldi, D. Giovampaola, C. Focarelli, R. Armini, A. Ziche et al., A fucose-containing O-glycoepitope on bovine and human nucleolin, Glycobiology, vol.19, issue.4, pp.337-343, 2009.
DOI : 10.1093/glycob/cwn126

D. Destouches, E. Khoury, D. Hamma-kourbali, Y. Krust, B. Albanese et al., Suppression of Tumor Growth and Angiogenesis by a Specific Antagonist of the Cell-Surface Expressed Nucleolin, PLoS ONE, vol.22, issue.6, p.2518, 2008.
DOI : 10.1371/journal.pone.0002518.t001
URL : https://hal.archives-ouvertes.fr/hal-00294100

S. Christian, J. Pilch, M. Akerman, K. Porkka, P. Laakkonen et al., Nucleolin expressed at the cell surface is a marker of endothelial cells in angiogenic blood vessels, The Journal of Cell Biology, vol.53, issue.4, pp.871-878, 2003.
DOI : 10.1006/bbrc.1998.8754

Y. Huang, H. Shi, H. Z. Song, X. Yuan, S. Luo et al., The angiogenic function of nucleolin is mediated by vascular endothelial growth factor and nonmuscle myosin, Blood, vol.107, issue.9, pp.3564-3571, 2006.
DOI : 10.1182/blood-2005-07-2961

H. Shi, Y. Huang, H. Zhou, X. Song, S. Yuan et al., Nucleolin is a receptor that mediates antiangiogenic and antitumor activity of endostatin, Blood, vol.110, issue.8, pp.2899-2906, 2007.
DOI : 10.1182/blood-2007-01-064428

V. Fogal, K. Sugahara, E. Ruoslahti, and S. Christian, Cell surface nucleolin antagonist causes endothelial cell apoptosis and normalization of tumor vasculature, Angiogenesis, vol.355, issue.24, pp.91-100, 2009.
DOI : 10.1007/s10456-009-9137-5

B. Krust, R. Vienet, A. Cardona, C. Rougeot, E. Jacotot et al., The anti-HIV pentameric pseudopeptide HB-19 is preferentially taken up in vivo by lymphoid organs where it forms a complex with nucleolin, Proceedings of the National Academy of Sciences, vol.98, issue.24, pp.14090-14095, 2001.
DOI : 10.1073/pnas.221467298

K. Kadomatsu and T. Muramatsu, Midkine and pleiotrophin in neural development and cancer, Cancer Letters, vol.204, issue.2, pp.127-143, 2004.
DOI : 10.1016/S0304-3835(03)00450-6

I. Dumler, V. Stepanova, U. Jerke, O. Mayboroda, F. Vogel et al., Urokinase-induced mitogenesis is mediated by casein kinase 2 and nucleolin, Current Biology, vol.9, issue.24, pp.1468-1476, 1999.
DOI : 10.1016/S0960-9822(00)80116-5
URL : https://hal.archives-ouvertes.fr/hal-00023719

V. Stepanova, T. Lebedeva, A. Kuo, S. Yarovoi, S. Tkachuk et al., Nuclear translocation of urokinase-type plasminogen activator, Blood, vol.112, issue.1, pp.100-110, 2008.
DOI : 10.1182/blood-2007-07-104455

N. Turck, O. Lefebvre, I. Gross, P. Gendry, M. Kedinger et al., Effect of laminin-1 on intestinal cell differentiation involves inhibition of nuclear nucleolin, Journal of Cellular Physiology, vol.22, issue.2, pp.545-555, 2006.
DOI : 10.1002/jcp.20501

S. Larrucea, C. Gonzalez-rubio, R. Cambronero, B. Ballou, P. Bonay et al., Cellular Adhesion Mediated by Factor J, a Complement Inhibitor: EVIDENCE FOR NUCLEOLIN INVOLVEMENT, Journal of Biological Chemistry, vol.273, issue.48, pp.31718-31725, 1998.
DOI : 10.1074/jbc.273.48.31718

G. Harms, R. Kraft, G. Grelle, B. Volz, J. Dernedde et al., Identification of nucleolin as a new L-selectin ligand, Biochemical Journal, vol.360, issue.3, pp.531-538, 2001.
DOI : 10.1042/bj3600531

E. Reyes-reyes and S. Akiyama, Cell-surface nucleolin is a signal transducing P-selectin binding protein for human colon carcinoma cells, Experimental Cell Research, vol.314, issue.11-12, pp.2212-2223, 2008.
DOI : 10.1016/j.yexcr.2008.03.016

A. Tate, S. Isotani, M. Bradley, R. Sikes, R. Davis et al., Met-Independent Hepatocyte Growth Factor-mediated regulation of cell adhesion in human prostate cancer cells, BMC Cancer, vol.5, issue.7, pp.197-212, 2006.
DOI : 10.1186/1471-2407-6-197

A. Said, B. Krust, S. Nisole, J. Briand, and A. Hovanessian, The Anti-HIV Cytokine Midkine Binds the Cell Surface-expressed Nucleolin as a Low Affinity Receptor, Journal of Biological Chemistry, vol.277, issue.40, pp.37492-37502, 2002.
DOI : 10.1074/jbc.M201194200

E. Said, J. Courty, J. Svab, J. Delbé, B. Krust et al., Pleiotrophin inhibits HIV infection by binding the cell surface-expressed nucleolin, FEBS Journal, vol.124, issue.18, pp.4646-4659, 2005.
DOI : 10.1002/art.10839
URL : https://hal.archives-ouvertes.fr/hal-00104912

S. Nisole, E. Said, C. Mische, M. Prevost, B. Krust et al., The Anti-HIV Pentameric Pseudopeptide HB-19 Binds the C-terminal End of Nucleolin and Prevents Anchorage of Virus Particles in the Plasma Membrane of Target Cells, Journal of Biological Chemistry, vol.277, issue.23, pp.20877-20886, 2002.
DOI : 10.1074/jbc.M110024200

M. Kato, M. Takahashi, A. Akhand, W. Liu, Y. Dai et al., Transgenic mouse model for skin malignant melanoma, Oncogene, vol.17, issue.14, pp.1885-1888, 1998.
DOI : 10.1038/sj.onc.1202077

R. Lengagne, L. Gal, F. Garcette, M. Fiette, L. et al., Spontaneous Vitiligo in an Animal Model for Human Melanoma: Role of Tumor-specific CD8+ T Cells, Cancer Research, vol.64, issue.4, pp.1496-14501, 2004.
DOI : 10.1158/0008-5472.CAN-03-2828

R. Lengagne, S. Graff-dubois, M. Garcette, L. Renia, M. Kato et al., Distinct Role for CD8 T Cells toward Cutaneous Tumors and Visceral Metastases, The Journal of Immunology, vol.180, issue.1, pp.130-1137, 2008.
DOI : 10.4049/jimmunol.180.1.130

T. Iwamoto, M. Takahashi, M. Ito, K. Hamatani, M. Ohbayashi et al., Aberrant melanogenesis and melanocytic tumour development in transgenic mice that carry a metallothionein/ret fusion gene, Embo J, vol.10, pp.3167-3175, 1991.

Y. Ohshima, I. Yajima, K. Takeda, M. Iida, M. Kumasaka et al., c-RET Molecule in Malignant Melanoma from Oncogenic RET-Carrying Transgenic Mice and Human Cell Lines, PLoS ONE, vol.5, issue.4, p.10279, 2010.
DOI : 10.1371/journal.pone.0010279.g009

D. Hoja-lukowicz, M. Przybylo, E. Poche?, A. Drabik, J. Silberring et al., The new face of nucleolin in human melanoma, Cancer Immunology, Immunotherapy, vol.373, issue.9, pp.1471-1480, 2009.
DOI : 10.1007/s00262-009-0705-8

V. Mourmouras, G. Cevenini, E. Cosci, M. Epistolato, M. Biagioli et al., Nucleolin protein expression in cutaneous melanocytic lesions, Journal of Cutaneous Pathology, vol.3, issue.6, pp.637-346, 2009.
DOI : 10.1111/j.1600-0560.2008.01126.x

E. Deryugina and J. Quigley, Matrix metalloproteinases and tumor metastasis, Cancer and Metastasis Reviews, vol.60, issue.Pt 1, pp.9-34, 2006.
DOI : 10.1007/s10555-006-7886-9

A. Byrne, D. Bouchier-hayes, and J. Harmey, Angiogenic and cell survival functions of Vascular Endothelial Growth Factor (VEGF), Journal of Cellular and Molecular Medicine, vol.8, issue.4, pp.777-794, 2005.
DOI : 10.1073/pnas.2135406100

S. Huang, C. Bucana, M. Van-arsdall, and I. Fidler, Stat1 negatively regulates angiogenesis, tumorigenicity and metastasis of tumor cells, Oncogene, vol.21, issue.16, pp.2504-2512, 2002.
DOI : 10.1038/sj.onc.1205341

I. Poser, J. Tatzel, S. Kuphal, and A. Bosserhoff, Functional role of MIA in melanocytes and early development of melanoma, Oncogene, vol.23, issue.36, pp.6115-6124, 2004.
DOI : 10.1038/sj.onc.1207797

B. Bachmeier, A. Albini, R. Vené, R. Benelli, D. Noonan et al., Cell density-dependent regulation of matrix metalloproteinase and TIMP expression in differently tumorigenic breast cancer cell lines, Experimental Cell Research, vol.305, issue.1, pp.83-98, 2005.
DOI : 10.1016/j.yexcr.2004.12.019

M. Takahashi, J. Ritz, and G. Cooper, Activation of a novel human transforming gene, ret, by DNA rearrangement, Cell, vol.42, issue.2, pp.581-588, 1985.
DOI : 10.1016/0092-8674(85)90115-1

N. Narita, A. Tanemura, R. Murali, R. Scolyer, S. Huang et al., Functional RET G691S polymorphism in cutaneous malignant melanoma, Functional RET G691S polymorphism in cutaneous malignant melanoma, pp.3058-3068, 2009.
DOI : 10.1038/nrc2037

L. Coussens and Z. Werb, Inflammation and cancer, Nature, vol.2, issue.6917, pp.860-867, 2002.
DOI : 10.1006/cyto.1996.0074

W. Lin and K. M. , A cytokine-mediated link between innate immunity, inflammation, and cancer, Journal of Clinical Investigation, vol.117, issue.5, pp.1175-1183, 2007.
DOI : 10.1172/JCI31537

M. Ahmadzadeh, L. Johnson, B. Heemskerk, J. Wunderlich, M. Dudley et al., Tumor antigen-specific CD8 T cells infiltrating the tumor express high levels of PD-1 and are functionally impaired, Blood, vol.114, issue.8, pp.1537-1544, 2009.
DOI : 10.1182/blood-2008-12-195792

M. Polak, N. Borthwick, F. Gabriel, P. Johnson, B. Higgins et al., Mechanisms of local immunosuppression in cutaneous melanoma, British Journal of Cancer, vol.5, issue.12, pp.961879-1887, 2007.
DOI : 10.1158/1078-0432.CCR-05-2431

B. Hansen, H. Schmidt, V. Der-maase, H. Sjoegren, P. Agger et al., Tumour-associated macrophages are related to progression in patients with metastatic melanoma following interleukin-2 based immunotherapy, Acta Oncologica, vol.19, issue.1, pp.400-405, 2006.
DOI : 10.1186/bcr589

S. Nisole, B. Krust, E. Dam, A. Blanco, N. Seddiki et al., N)PR]-TASP Inhibits Attachment of T Lymphocyte- and Macrophage-Tropic HIV to Permissive Cells, AIDS Research and Human Retroviruses, vol.16, issue.3, pp.237-249, 2000.
DOI : 10.1089/088922200309331

V. Heath and R. Bicknell, Anticancer strategies involving the vasculature, Nature Reviews Clinical Oncology, vol.68, issue.7, pp.395-404, 2009.
DOI : 10.1038/nrclinonc.2009.52