[1. World Cancer Report 2014. World Health Organization. 2014. pp. Chapter 5.2.]Search in Google Scholar
[2. Siu, Albert L. Screening for Breast Cancer: U.S. Preventive Services Task Force Recommendation Statement. Annals of Internal Medicine. 2016, 164: 279-96.10.7326/M15-288626757170]Search in Google Scholar
[3. Kakde D., Jain D., Shrivastava V., Kakde R. and Patil A.T. Cancer therapeutics-opportunities, challenges and advances in drug delivery. Journal of Applied Pharmaceutical Science. 2011, 1 (9): 1-10.]Search in Google Scholar
[4. Zheleva D. I., Fischer P.M., Zhelev N. Z., Melville J. E., Gavine A-L., and Lane D. P. Design of cell-permeable peptides inhibitors of cyclin D1/ CDK4 complex. M. Nature Biotech. Sh.R.2000, 11: 25-30.]Search in Google Scholar
[5. Eldar-Finkelman H. and Eisenstein M. Peptide inhibitors targeting protein kinases. Current Pharmaceutical Design. 2009, 15 (21): 2463-2470.10.2174/13816120978868225319601843]Search in Google Scholar
[6. Rosca E.V., Koskimaki J.E., Rivera C.G., Pandey N.B., Tamiz A.P. and Popel A.S. Antiangiogenic peptides for cancer therapeutics. Current Pharmaceutical Biotechnology.2011, 12 (8): 1101-1116.10.2174/138920111796117300311425621470139]Search in Google Scholar
[7. McClue S.J., Blake D., Clarke R., Cowan A., Cummings L., Fischer P.M., MacKenzie M., Melville J., Stewart K., Wang S., Zhelev N., Zheleva D., Lane D.P. In vitro and in vivo antitumor properties of the cyclin dependent kinase inhibitor CYC202 (R-roscovitine). Int J Cancer. 2002, 102 (5):463-470.10.1002/ijc.1073812432547]Search in Google Scholar
[8. Mochly-Rosen D. and Qvit N. Peptide inhibitors of protein-protein interactions: from rational design to the clinic. Chimica Oggi. 2010, 28 (1): 14-16.]Search in Google Scholar
[9. Smolarczyk R., Cichon T., Graja K., Hucz J., Sochanik A., and Szala S. Antitumor effect of RGD- 4C-GG-D (KLAKLAK) 2 peptide in mouse B16(F10) melanoma model. Acta Biochimica Polonica. 2006, 53 (4): 801-805.10.18388/abp.2006_3309]Search in Google Scholar
[10. Liang J.F. and Yang V.C. Synthesis of doxorubicin-peptide conjugate with multidrug resistant tumor cell killing activity. Bioorg. Med. Chem. Lett. 2005.15: 5071-5075.10.1016/j.bmcl.2005.07.08716168650]Search in Google Scholar
[11. Akenteva N.P, Shushanov S.S, Kotelnikov A.I. Effects of RHAMM/ HMMR-Selective Peptides on Survival of Breast Cancer Cells. Bulletin of Experimental Biology and Medicine (Russia). 2015, 159 (5): 618-621.]Search in Google Scholar
[12. Luyt L.G., Turley E.A., Esguerra K.V. Rhamm binding peptides. International Patent WO2011/150495. London Health Sciences Centre Research Inc. 2011.]Search in Google Scholar
[13. Esguerra K.V., Tolg C., Akentieva N., Price M., Cho C.F., Lewis J.D., McCarthy J.B., Turley E.A., Luyt L.G. Identification, design and synthesis of tubulin-derived peptides as novel hyaluronan mimetic ligands for the receptor for hyaluronan-mediated motility (RHAMM/HMMR). Integr. Biol. (Camb).2015, 7 (12): 1547-1560.]Search in Google Scholar
[14. Akentieva N.P., Shushanov S.S. RHAMM (receptor hyaluronan-mediated motility)-target peptides induce apoptosis in prostate cancer cells. Problems in oncology. 2016, 62 (3):512-518.]Search in Google Scholar
[15. Aina O.H., Sroka T.C., Chen M.L. and Lam K.S. Therapeutic cancer targeting peptides. Biopolymers. 2002, 66 (3): 184-199.10.1002/bip.1025712385037]Open DOISearch in Google Scholar
[16. Zhasloff, M. Antimicrobial peptides of multicellular organisms. Nature. 2002, 415: 389-395.10.1038/415389a11807545]Search in Google Scholar
[17. Brogden K.A. Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev.Microbiol. 2005, 3: 238-250.10.1038/nrmicro109815703760]Open DOISearch in Google Scholar
[18. Mader J.S., Hoskin, D.W. Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment. Expert Opin. Investig. Drugs. 2006, 15: 933-946.10.1517/13543784.15.8.93316859395]Search in Google Scholar
[19. Kim Y.J., Varki, A. Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconj.J. 1997, 14: 569-576.10.1023/A:1018580324971]Search in Google Scholar
[20. Lindgren M., Rosenthal-Aizman K., Saar, K., Eiriksdottir, E., Jiang, Y., Sassian, M., Ostlund, P., Hallbrink, M., and Langel, U. Overcoming methotrexate resistance in breast cancer tumour cells by the use of a new cell-penetrating peptide. Biochem. Pharmacol. 2006, 71: 416-425.10.1016/j.bcp.2005.10.048]Search in Google Scholar
[21. Liang, J.F., and Yang, V.C. Synthesis of doxorubicin-peptide conjugate with multidrug resistant tumor cell killing activity. Bioorg. Med. Chem. Lett. 2005, 15: 5071-5075.10.1016/j.bmcl.2005.07.087]Open DOISearch in Google Scholar
[22. Steiner H, Hultmark D., Engstrom A, Bennich H, Boman HG. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature. 1981; 292 (5820):246-248.10.1038/292246a0]Search in Google Scholar
[23. Lehrer RI. Primate defensins. Nat. Rev. Microbiol. 2004, 2 (9): 727-738.]Search in Google Scholar
[24. Hancock REW. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 2001, 1 (3):156-164.10.1016/S1473-3099(01)00092-5]Search in Google Scholar
[25. Koczulla AR, Bals R. Antimicrobial peptides: current status and therapeutic potential. Drugs. 2003, 63 (4):389-406.10.2165/00003495-200363040-0000512558461]Search in Google Scholar
[26. Otvos L. Jr. Antibacterail paptides and proteins with multiple cellular targets. J. Pept. Sci. 2005, 11 (11): 697-706.10.1002/psc.69816059966]Open DOISearch in Google Scholar
[27. Powers J-PS., Hanckock REW. The relationship between peptide structure and antibacterial activity. Peptides 2003, 24 (11):1681-1691.10.1016/j.peptides.2003.08.02315019199]Search in Google Scholar
[28. Nicolaou KC, Murphy F., Barluenga S., Ohshima T., Wei H, Xu J., Gray DLF, Baudoin O. Total synthesis of the novel immunosuppressant sanglifehrin A, J.Am.Chem.Soc. 2000, 122: 3830-3838.10.1021/ja994285v]Search in Google Scholar
[29. White J.D., Hong J., Robarge LA. Total synthesis of cryptophycins- 1, -3, -4 and -24 (arenastatin A0 and -29, cytotoxic depsipeptides from cyanobacteria of the nostocacae. J. Org. Chem. 1999, 64: 6206-6216.10.1021/jo9907585]Search in Google Scholar
[30. Xia Z., Smith CD. Total synthesis of dendroamide A, a novel cyclic peptide that reverses multiple drug resistance. J. Org. Chem. 2001, 66:3459-3466.10.1021/jo005783l11348130]Search in Google Scholar
[31. Boger DL, Zhou J., Borzilleri RM., Nukii S., Castle SL. Synthesis of (9R, 12 S)- and (9S, 12 S)-cycloisodityrosine and their N-methyl derivatives. J. Org. Chem. 1997, 62:2054-2069.10.1021/jo961346o11671510]Open DOISearch in Google Scholar
[32. Inoue T., Inaba T., Umezawa I., Yuasa M., Itokawa H., Ogura K., Komatsu K, Hara H, Hoshino O. Reglose-lective synthesis of 14-membered blaryl ethers. Total synthesis of RA V11 and deoxybouvardin. Chem. Pharm. Bull. 1995, 43: 1325-1335.10.1248/cpb.43.1325]Open DOISearch in Google Scholar
[33. Davies J.S. REW. The cyclization of peptides and depsipeptides. J. Peptide Sci. 2003, 9:471-501.10.1002/psc.49112952390]Search in Google Scholar
[34. Vives, E., Schmidt, J., and Pelegrin, A. Cell-penetrating and cell-targeting peptides in drug delivery. Biochim. Biophys. Acta. 2008, 1786: 126-38.10.1016/j.bbcan.2008.03.00118440319]Search in Google Scholar
[35. Myrberg, H., Zhang, L., Mae, M., and Langel, U. Design of a tumor- homing cell-penetrating peptide. Bioconjug.Chem. 2008, 19: 70-75.10.1021/bc070113918001077]Search in Google Scholar
[36. Jiang, T., Olson, E.S., Nguyen, Q.T., Roy, M., Jennings, P.A., and Tsien, R.Y. Tumor imaging by means of proteolytic activation of cell-penetrating peptides. Proc. Natl. Acad. Sci. USA. 2004, 101:17867-72.10.1073/pnas.040819110153931415601762]Search in Google Scholar
[37. Pipkorn, R., Waldeck, W., Spring, H., Jenne, J.W., and Braun, K. Delivery of substances and their target-specific topical activation. Biochim. Biophys. Acta. 2006, 1758: 606-10.10.1016/j.bbamem.2006.03.03616730647]Search in Google Scholar
[38. Telmer, P. G.; Tolg, C.; McCarthy, J. B.; and Turley, E. A. How does protein with dual mitotic spindle and extracellular matrix receptor functions affect tumor susceptibility and progression? Commun. Integr. Biol. 2011, 4(2): 182-185.]Search in Google Scholar
[39. Laurent, T. C., and Fraser, J. R. E. Hyaluronan. FASEB J. 1992, 6: 2397-2404.10.1096/fasebj.6.7.1563592]Search in Google Scholar
[40. Laurent, T. C. Biochemistry of Hyaluronan. Acta Otolaryngol Suppl. 1987, 442: 7-24.10.3109/000164887091028333124495]Search in Google Scholar
[41. Lee, J. Y.; and Spicer, A. P. Hyaluronan: a multifunctional, megaDalton, stealth molecule. Curr. Opin. Cell Biol. 2000, 12(5): 581-586.10.1016/S0955-0674(00)00135-6]Open DOISearch in Google Scholar
[42. Tzircotis G, Thorne RF, Isacke CM. Chemotaxis towards hyaluronan is dependent on CD44 expression and modulated by cell type variation in CD44-hyaluronan binding. J Cell Sci. 2005, 118:5119-5128.10.1242/jcs.02629]Open DOISearch in Google Scholar
[43. Udabage L, Brownlee GR, Nilsson SK, Brown TJ. The over-expression of HAS2, Hyal-2 and CD44 is implicated in the invasiveness of breast cancer. Exp Cell Res. 2005, 310:205-217.10.1016/j.yexcr.2005.07.026]Search in Google Scholar
[44. Bourguignon LY, Singleton PA, Zhu H, Zhou B. Hyaluronan promotes signaling interaction between CD44 and the transforming growth factor beta receptor I in metastatic breast tumor cells. J. Biol. Chem. 2002, 277:39703-39712.10.1074/jbc.M204320200]Search in Google Scholar
[45. Naot, D., Sionov, R.V., and Ish-Shalom, D. CD44: Structure, function, and association with the malignant process. Adv. Cancer Res.1997, 71: 241-319.10.1016/S0065-230X(08)60101-3]Search in Google Scholar
[46. Turley E.A., Noble P.W., Bourguignon L.Y. Signaling properties of hyaluronan receptors. J. Biol. Chem. 2002, 277: 4589-4592.10.1074/jbc.R100038200]Search in Google Scholar
[47. Adamia S., Maxwell C.A., Pilarski L.M. Hyaluronan and hyaluronan synthases: potential therapeutic targets in cancer. Curr. Drug Targets Cardiovasc. Haematol. Disord. 2005, 5: 3-1410.2174/1568006053005056]Search in Google Scholar
[48. Hardwick C., Hoare K., Owens R., Hohn H.P., Hook M., Moore D., Cripps V., Austen L., Nance D.M., Turley E.A. Molecular cloning of a novel hyaluronan receptor that mediates tumor cell motility. J. Cell. Biol. 1992, 117:1343-1350.10.1083/jcb.117.6.1343]Search in Google Scholar
[49. Hall C.L., Yang B., Yang X., Zhang S., Turley M., Samuel S., Lange L.A., Wang C., Curpen G.D., Savani R.C., Greenberg A.H., Turley E.A. Overexpression of the hyaluronan receptor RHAMM is transforming and is also required for H-ras transformation. Cell. 1995, 82:19-26.10.1016/0092-8674(95)90048-9]Search in Google Scholar
[50. Maxwell C.A., Keats J.J., Crainie M., Sun X., Yen T., Shibuya E., Hendzel M., Chan G., Pilarski L.M. RHAMM is a centrosomal protein that interacts with dynein and maintains spindle pole stability. Mol. Biol. Cell. 2003,14:2262-2276.10.1091/mbc.E02-07-037719487612808028]Open DOISearch in Google Scholar
[51. Assmann V., Jenkinson D., Marshall J.F., Hart I.R. The intracellular hyaluronan receptor RHAMM/IHABP interacts with microtubule and actin filaments. J. Cell. Sci. 1999, 112 (Pt 22):3943-3954.10.1242/jcs.112.22.3943]Search in Google Scholar
[52. Joukov V., Groen A.C., Prokhorova T., Gerson R., White E., Rodriguez A., Walter J.C., Livingston D.M. The BRCA1/BARD1 heterodimer modulates ran-dependent mitotic spindle assembly. Cell. 2006, 127:539-552.10.1016/j.cell.2006.08.053]Search in Google Scholar
[53. Gust K. M., Hofer M. D., Perner S.R., Chinnaiyan A. M., VaramballyS., Moller P., Rinnab L., Rubin M. A., Greiner J., Schmitt M., Kuefer R., and Ringhoffer M. RHAMM (CD168) is overexpressed at the protein level and may constitute an immunogenic antigen in advanced prostate cancer disease. Neoplasia. 2009, 11(9): 956-963.10.1593/neo.09694]Open DOISearch in Google Scholar
[54. Wang C., Thor A.D., Moore D.H., Zhao Y., Kerschmann R., Stern R., Watson P.H., and Turley E. A. The overexpression of RHAMM, a hyaluronan- binding protein that regulates ras signalling, correlates with overexpression of mitogen-activated protein kinase and is a significant parameter in breast cancer rogression. Clin. Cancer Res.1998, 4(3): 567-576.]Search in Google Scholar
[55. Greiner J., Ringhoffer M., Taniguchi M., Schmitt A., Kirchner D., Krahn G., Heilmann V., Gschwend J., Bergmann L., Dohner H., and Schmitt M. Receptor for hyaluronan acid-mediated motility (RHAMM) is a new immunogenic leukemia-associated antigen in acute and chromic myeloid leukemia. Exp. Hematol. 2002, 30(9): 1029-1035.10.1016/S0301-472X(02)00874-3]Open DOISearch in Google Scholar
[56. Assmann V., Marshall J. F., Fieber C., Hofmann M., and Hart I.R. The human hyaluronan receptor RHAMM is expressed as an intracellular protein in breast cancer. J. Cell Sci. 1998, 111: 1685-1694.10.1242/jcs.111.12.16859601098]Search in Google Scholar
[57. Maxwell C. A., Rasmussen E., Zhan F., Keats J. J., Adarnia S., Strachan E., Crainie M., Walker R., Belch A. R., Pilarski L. M., Barlogie B., Shaughnessy J. Jr., and Reiman T. RHAMM expression and isoform balance predict aggressive disease and poor survival in multiple myeloma. Blood. 2004, 104(4): 1151-1158.10.1182/blood-2003-11-407915105292]Search in Google Scholar
[58. Crainie M., Belch A. R., Mant M. J., and Pilarski L. M. Overexpression of the receptor for hyaluronan-mediated motility (RHAMM) characterizes the malignant clone in multiple myeloma: identification of three distinct RHAMM variants. Blood. 1999, 93(5): 1684-1696.10.1182/blood.V93.5.1684]Search in Google Scholar
[59. Wang C., Thor A. D., Moore D. H., Zhao Y., Kerschmann R., Stern R., Watson P. H., Turley E. A. The overexpression of RHAMM, a hyaluronan binding protein that regulates ras signalling, correlates with overexpression of mitogen-activated protein kinase and is a significant parameter in breast cancer P Progression. Clin. Cancer Res. 1998, 4(3): 567-576.]Search in Google Scholar
[60. Assman V., Gillett C. E., Poulsom R., Ryder K., Hart I. R., and Hanby A. M. The pattern of expression of the microtubule-binding protein RHAMM/IHAMP im mammary carcinoma suggests a role in the invasive behaviour of tumour cells. J. Pathol. 2001, 195(2): 191-196.]Search in Google Scholar
[61. Tolg C., Hamilton S. J., Morningstar L., Zhang J., Esguerra K. V., Telmer P. G., Luyt L. G., Harrison R., McCarthy J. B., Turley E. A. RHAMM promotes interphase microtubule instability and mitotic spindle integrity trough MEK1/ERK1, 2 activity. J Biol. Chem., 2010, 285: 26461-26474.10.1074/jbc.M110.121491292407920558733]Search in Google Scholar
[62. Kurokawa H., Kazuto N., Fukumoto H., Tomonari A., Suzuki T., Saijo N. Alteration of caspase-3 (CPP32/Yama/apopaim) in wild-type MCF-7 breast cancer cells. Oncology Rep.1999, 6: 33-37.10.3892/or.6.1.339864397]Search in Google Scholar
[63. Rizzardi A.E., Vogel R.I., Koopmeiners J.S., Forster C.L., Marston L.O., Rosener N.K., Akentieva N., Price M.A., Metzger G.J., Warlick C.A., Henriksen J.C., Turley E.A., McCarthy J.B., Schmechel S.C. 2014. Elevated hyaluronan and hyaluronan-mediated motility receptor are associated with biochemical failure in patients with intermediate-grade prostate tumors. Cancer. 120 (12), 1800-1809.]Search in Google Scholar
[64. Sliva D., Rizzo M.T., English D. Phosphatidylinositol 3-kinase and NF-κB regulate motility of invasive MDA-MB-231 human breast cancer cells by the secretion of urokinase-type plasminogen activator. J. Biol. Chem. 2002, 277:3150-7.10.1074/jbc.M10957920011689575]Search in Google Scholar
[65. Brunet A., Bonni A., Zigmond M.J., et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell. 1999, 96:857-68.10.1016/S0092-8674(00)80595-4]Open DOISearch in Google Scholar
[66. Byeong-Chel Lee, Tae-Hee Lee, Shalom Avraham and Hava Karsenty Avraham. Involvement of the Chemokine Receptor CXCR4 and Its Ligand Stromal Cell-Derived Factor 1α in Breast Cancer Cell Migration Through Human Brain Microvascular Endothelial Cells. Mol. Cancer. Res. 2004, 2: 327-337.10.1158/1541-7786.327.2.6]Search in Google Scholar
[67. Muller A., Homey B., Soto H., et al. Involvement of chemokine receptors in breast cancer metastasis. Nature. 2001, 410:50-6.10.1038/35065016]Search in Google Scholar
[68. Soule H.D., Vazguez J., Long, A., Albert S. and Brennan M. A human cell line from a pleural effusion derived from a breast carcinoma. J. Natl. Cancer Inst. 1973, 51:1409-1416.10.1093/jnci/51.5.1409]Open DOISearch in Google Scholar
[69. Levenson A.S., Jordan V.C. MCF-7: the first hormone-responsive breast cancer cell line. Cancer Res. 1997, 57: 3071-3078.]Search in Google Scholar
[70. Reed E. Platinum-DNA adduct, nucleotide excision repair and platinum-based anti-cancer chemotherapy. Cancer Treat. Rev. 1998, 24: 331-344.10.1016/S0305-7372(98)90056-1]Open DOISearch in Google Scholar
[71. Maxwell C.A., McCarthy J., Turley E. Cell-surface and mitotic-spindle Rhamm: moonlighting or dual oncogenic functions? J. Cell. Sci. 2008, 121: 925-932.10.1242/jcs.02203818354082]Search in Google Scholar
[72. Hus I., Kawiak J., Tabarkiewicz J., Radej S., Hoser G., Bojarska-Junak A., Schmitt M., Giannopoulos K., Dmoszynska A., Rolinski J. Immunotherapy with irradiated autologous leukemic cells in patients with B-CLL in early stages. Oncol Rep. 2008, 20(2):443-51.]Search in Google Scholar
[73. Zlobec I., Terraciano L., Tornullo L., Gunhert U., Vuong T., Jass J.R., Lugli A. Role of Rhamm within the hierarchy of well-established prognostic factors in colorectal cancer. Gur. 2008.10.1136/gut.2007.14119218436576]Search in Google Scholar
[74. Yamano Y., Uzawa K., Shinozuka K., Fushimi K., Ishigami T., Nomura H., Ogawara K., Shiiba M., Yokoe H., Tanzawa H. Hyaluronan-mediated motility: a target in oral squamous cell carcinoma. Int. J. Oncol. 2008, 32: 10001-9.10.3892/ijo.32.5.1001]Search in Google Scholar
[75. Tolg C., Poon R., Fodde R., Turley E.A., Alman B.A. Genetic deletion of receptor for hyaluronan-mediated motility (Rhamm) attenuates the formation of aggressive fibromatosis (desmoids tumor). Oncogene. 2003, 22: 6873-82.10.1038/sj.onc.120681114534534]Open DOISearch in Google Scholar
[76. Rein D.T., Roehrig K., Schondorf T., Lazar A., Fleisch M., Niederacher D., Bender H.G., Dall P. Expression of the hyaluronan receptor Rhamm in endometrial carcinoma suggests a role in tumor progression and metastasis. J. Cancer Res. Clin. Oncol. 2003, 129: 161-4.10.1007/s00432-003-0415-012712331]Search in Google Scholar
[77. Sohr S. and Engeland K. Rhamm is differentially expressed in the cell cycle and downregulated by the tumor suppressor p53. Cell Cycle. 2008, 7 (21): 3448-3460.10.4161/cc.7.21.701418971636]Search in Google Scholar
[78. Lippman M.E. and Bolan G. Oestrogen-responsive human breast cancer in long-term tissue culture. Nature. 1975, 256:592-593.10.1038/256592a0170527]Search in Google Scholar
[79. Seals D.F. et al. The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells. Cancer Cell. 2005, 7:155-165.10.1016/j.ccr.2005.01.00615710328]Open DOISearch in Google Scholar
[80. Yamaguchi H. et al. Molecular mechanisms of invadopodium formation: the role of the N-WASP-Arp2/3 complex pathway and cofilin. J. Cell. Biol. 2005, 168: 441-452.10.1083/jcb.200407076217173115684033]Search in Google Scholar
[81. Weaver A.M. Invadopodia : specialized cell structures for cancer invasion. Clin. Exp. Metastasis. 2006, 23: 97-105.10.1007/s10585-006-9014-116830222]Search in Google Scholar
[82. Diaz B. et al. Tks5-dependent, Nox-mediated generation of reactive oxygen species is necessary for invadopodia formation. Sci. Signal. 2009, 2:ra53.10.1126/scisignal.2000368281064019755709]Search in Google Scholar
[83. Clark E.S. and Weaver A.M. A new role for cortactin in invadopodia: regulation of protease secretion. Eur. J. Cell Biol. 2008, 87:581-590.10.1016/j.ejcb.2008.01.008256693318342393]Search in Google Scholar