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International Journal of Cell Biology
Volume 2015, Article ID 537560, 25 pages
http://dx.doi.org/10.1155/2015/537560
Review Article

Utilization of Glycosaminoglycans/Proteoglycans as Carriers for Targeted Therapy Delivery

1Department of Regenerative Medicine and Cell Biology, Medical University of South Carolina, Charleston, SC 29425, USA
2Department of Biomedical Engineering/ND20, Cleveland Clinic, Cleveland, OH, USA
3Division of Rheumatology & Immunology, Department of Medicine, Medical University of South Carolina, 114 Doughty Street, Charleston, SC 29425, USA

Received 20 September 2014; Revised 19 January 2015; Accepted 15 February 2015

Academic Editor: Pavel Hozak

Copyright © 2015 Suniti Misra et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. K. Wolf, Y. I. Wu, Y. Liu et al., “Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion,” Nature Cell Biology, vol. 9, no. 8, pp. 893–904, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. F. Sabeh, R. Shimizu-Hirota, and S. J. Weiss, “Protease-dependent versus-independent cancer cell invasion programs: three-dimensional amoeboid movement revisited,” The Journal of Cell Biology, vol. 185, no. 1, pp. 11–19, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. T. E. Hardingham and A. J. Fosang, “Proteoglycans: many forms and many functions,” The FASEB Journal, vol. 6, no. 3, pp. 861–870, 1992. View at Google Scholar · View at Scopus
  4. B. Mulloy and C. C. Rider, “Cytokines and proteoglycans: an introductory overview,” Biochemical Society Transactions, vol. 34, no. 3, pp. 409–413, 2006. View at Publisher · View at Google Scholar · View at Scopus
  5. J. R. Bishop, M. Schuksz, and J. D. Esko, “Heparan sulphate proteoglycans fine-tune mammalian physiology,” Nature, vol. 446, no. 7139, pp. 1030–1037, 2007. View at Publisher · View at Google Scholar · View at Scopus
  6. K. Mythreye and G. C. Blobe, “Proteoglycan signaling co-receptors: roles in cell adhesion, migration and invasion,” Cellular Signalling, vol. 21, no. 11, pp. 1548–1558, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. M. Bernfield, M. Götte, P. W. Park et al., “Functions of cell surface heparan sulfate proteoglycans,” Annual Review of Biochemistry, vol. 68, pp. 729–777, 1999. View at Publisher · View at Google Scholar · View at Scopus
  8. J. Yang, M. A. Price, C. L. Neudauer et al., “Melanoma chondroitin sulfate proteoglycan enhances FAK and ERK activation by distinct mechanisms,” Journal of Cell Biology, vol. 165, no. 6, pp. 881–891, 2004. View at Google Scholar · View at Scopus
  9. C. C. Reed, A. Waterhouse, S. Kirby et al., “Decorin prevents metastatic spreading of breast cancer,” Oncogene, vol. 24, no. 6, pp. 1104–1110, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. S. Ghatak, S. Misra, and B. P. Toole, “Hyaluronan constitutively regulates ErbB2 phosphorylation and signaling complex formation in carcinoma cells,” Journal of Biological Chemistry, vol. 280, no. 10, pp. 8875–8883, 2005. View at Publisher · View at Google Scholar · View at Scopus
  11. S. Misra, S. Ghatak, and B. P. Toole, “Regulation of MDR1 expression and drug resistance by a positive feedback loop involving hyaluronan, phosphoinositide 3-kinase, and ErbB2,” The Journal of Biological Chemistry, vol. 280, no. 21, pp. 20310–20315, 2005. View at Publisher · View at Google Scholar · View at Scopus
  12. S. Misra, L. M. Obeid, Y. A. Hannun et al., “Hyaluronan constitutively regulates activation of COX-2-mediated cell survival activity in intestinal epithelial and colon carcinoma cells,” Journal of Biological Chemistry, vol. 283, no. 21, pp. 14335–14344, 2008. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Misra, B. P. Toole, and S. Ghatak, “Hyaluronan constitutively regulates activation of multiple receptor tyrosine kinases in epithelial and carcinoma cells,” Journal of Biological Chemistry, vol. 281, no. 46, pp. 34936–34941, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. M. A. Simpson, C. M. Wilson, and J. B. McCarthy, “Inhibition of prostate tumor cell hyaluronan synthesis impairs subcutaneous growth and vascularization in immunocompromised mice,” The American Journal of Pathology, vol. 161, no. 3, pp. 849–857, 2002. View at Publisher · View at Google Scholar · View at Scopus
  15. L. Udabage, G. R. Brownlee, M. Waltham et al., “Antisense-mediated suppression of hyaluronan synthase 2 inhibits the tumorigenesis and progression of breast cancer,” Cancer Research, vol. 65, no. 14, pp. 6139–6150, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. T. D. Camenisch, J. A. Schroeder, J. Bradley, S. E. Klewer, and J. A. McDonald, “Heart-valve mesenchyme formation is dependent on hyaluronan-augmented activation of ErbB2-ErbB3 receptors,” Nature Medicine, vol. 8, no. 8, pp. 850–855, 2002. View at Publisher · View at Google Scholar · View at Scopus
  17. T. D. Camenisch, A. P. Spicer, T. Brehm-Gibson et al., “Disruption of hyaluronan synthase-2 abrogates normal cardiac morphogenesis and hyaluronan-mediated transformation of epithelium to mesenchyme,” Journal of Clinical Investigation, vol. 106, no. 3, pp. 349–360, 2000. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Misra, P. Heldin, V. C. Hascall et al., “Hyaluronan-CD44 interactions as potential targets for cancer therapy,” FEBS Journal, vol. 278, no. 9, pp. 1429–1443, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Misra, V. Hascall, N. Karamanos, R. A. Markwald, and S. Ghatak, Targeting Tumor Microenvironment in Cancer Progression, DeGruyter, Berlin, Germany, 2012.
  20. V. C. Hascall and T. Laurent, Hyaluronan: Structure and Physical Properties, 1997, http://www.glycoforum.gr.jp.
  21. V. C. Hascall, A. K. Majors, C. A. De La Motte et al., “Intracellular hyaluronan: a new frontier for inflammation?” Biochimica et Biophysica Acta—General Subjects, vol. 1673, no. 1-2, pp. 3–12, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. A. P. Spicer and J. Y. L. Tien, “Hyaluronan and morphogenesis,” Birth Defects Research Part C: Embryo Today, vol. 72, no. 1, pp. 89–108, 2004. View at Publisher · View at Google Scholar · View at Scopus
  23. P. Heldin and H. Pertoft, “Synthesis and assembly of the hyaluronan-containing coats around normal human mesothelial cells,” Experimental Cell Research, vol. 208, no. 2, pp. 422–429, 1993. View at Publisher · View at Google Scholar · View at Scopus
  24. S. P. Evanko, T. Parks, and T. N. Wight, “Intracellular hyaluronan in arterial smooth muscle cells: association with microtubules, RHAMM, and the mitotic spindle,” Journal of Histochemistry & Cytochemistry, vol. 52, no. 12, pp. 1525–1535, 2004. View at Publisher · View at Google Scholar · View at Scopus
  25. B. P. Toole, “Hyaluronan: from extracellular glue to pericellular cue,” Nature Reviews Cancer, vol. 4, no. 7, pp. 528–539, 2004. View at Publisher · View at Google Scholar · View at Scopus
  26. K. Meyer and J. W. Palmer, “The polysaccharide of the vitreous humor,” Journal of Biological Chemistry, vol. 107, pp. 629–634, 1934. View at Google Scholar
  27. P. Olczyk, K. Komosińska-Vassev, K. Winsz-Szczotka, K. Kuźnik-Trocha, and K. Olczyk, “Hyaluronan: structure, metabolism, functions, and role in wound healing,” Postępy Higieny i Medycyny Doświadczalnej, vol. 62, pp. 651–659, 2008. View at Google Scholar · View at Scopus
  28. N. S. Gandhi and R. L. Mancera, “The structure of glycosaminoglycans and their interactions with proteins,” Chemical Biology and Drug Design, vol. 72, no. 6, pp. 455–482, 2008. View at Publisher · View at Google Scholar · View at Scopus
  29. T. C. Laurent and J. R. E. Fraser, “Hyaluronan,” The FASEB Journal, vol. 6, no. 7, pp. 2397–2404, 1992. View at Google Scholar · View at Scopus
  30. W. Y. J. Chen and G. Abatangelo, “Functions of hyaluronan in wound repair,” Wound Repair and Regeneration, vol. 7, no. 2, pp. 79–89, 1999. View at Publisher · View at Google Scholar · View at Scopus
  31. P. H. Weigel and P. L. DeAngelis, “Hyaluronan synthases: a decade-plus of novel glycosyltransferases,” The Journal of Biological Chemistry, vol. 282, no. 51, pp. 36777–36781, 2007. View at Publisher · View at Google Scholar · View at Scopus
  32. R. Stern and M. J. Jedrzejas, “Hyaluronidases: their genomics, structures, and mechanisms of action,” Chemical Reviews, vol. 106, no. 3, pp. 818–839, 2006. View at Publisher · View at Google Scholar · View at Scopus
  33. S. Banerji, J. Ni, S. X. Wang et al., “LYVE-1, a new homologue of the CD44 glycoprotein, is a lymph-specific receptor for hyaluronan,” Journal of Cell Biology, vol. 144, no. 4, pp. 789–801, 1999. View at Publisher · View at Google Scholar · View at Scopus
  34. B. Zhou, J. A. Weigel, L. Fauss, and P. H. Weigel, “Identification of the hyaluronan receptor for endocytosis (HARE),” The Journal of Biological Chemistry, vol. 275, no. 48, pp. 37733–37741, 2000. View at Publisher · View at Google Scholar · View at Scopus
  35. B. P. Toole, A. Zoltan-Jones, S. Misra, and S. Ghatak, “Hyaluronan: a critical component of epithelial-mesenchymal and epithelial-carcinoma transitions,” Cells Tissues Organs, vol. 179, no. 1-2, pp. 66–72, 2005. View at Publisher · View at Google Scholar · View at Scopus
  36. L. M. Pilarski, A. Masellis-Smith, A. R. Belch, B. Yang, R. C. Savani, and E. A. Turley, “RHAMM, a receptor for hyaluronan-mediated motility, on normal human lymphocytes, thymocytes and malignant B cells: a mediator in B cell malignancy?” Leukemia and Lymphoma, vol. 14, no. 5-6, pp. 363–374, 1994. View at Publisher · View at Google Scholar · View at Scopus
  37. Y. Wang, H. Du, and G. Zhai, “Recent advances in active hepatic targeting drug delivery system,” Current Drug Targets, vol. 15, no. 6, pp. 573–599, 2014. View at Publisher · View at Google Scholar · View at Scopus
  38. S. Ghatak, G. S. Bogatkevich, I. Atnelishvilis et al., “Overexpression of c-Met and CD44v6 receptors contributes to autocrine TGF-β1 signaling in interstitial lung disease,” Journal of Biological Chemistry, vol. 289, no. 11, pp. 7856–7872, 2014. View at Publisher · View at Google Scholar · View at Scopus
  39. S. Ghatak, V. C. Hascall, R. R. Markwald, and S. Misra, “Stromal hyaluronan interaction with epithelial CD44 variants promotes prostate cancer invasiveness by augmenting expression and function of hepatocyte growth factor and androgen receptor,” Journal of Biological Chemistry, vol. 285, no. 26, pp. 19821–19832, 2010. View at Publisher · View at Google Scholar · View at Scopus
  40. S. Ghatak, S. Misra, R. A. Norris et al., “Periostin induces intracellular cross-talk between kinases and hyaluronan in atrioventricular valvulogenesis,” The Journal of Biological Chemistry, vol. 289, no. 12, pp. 8545–8561, 2014. View at Publisher · View at Google Scholar · View at Scopus
  41. S. Ghatak, S. Misra, and B. P. Toole, “Hyaluronan oligosaccharides inhibit anchorage-independent growth of tumor cells by suppressing the phosphoinositide 3-kinase/Akt cell survival pathway,” Journal of Biological Chemistry, vol. 277, no. 41, pp. 38013–38020, 2002. View at Publisher · View at Google Scholar · View at Scopus
  42. S. Misra, V. C. Hascall, F. G. Berger, R. R. Markwald, and S. Ghatak, “Hyaluronan, CD44, and cyclooxygenase-2 in colon cancer,” Connective Tissue Research, vol. 49, no. 3-4, pp. 219–224, 2008. View at Publisher · View at Google Scholar · View at Scopus
  43. S. Misra, V. C. Hascall, C. De Giovanni, R. R. Markwald, and S. Ghatak, “Delivery of CD44 shRNA/nanoparticles within cancer cells. Perturbation of hyaluronan/CD44v6 interactions and reduction in adenoma growth in Apc Min/+mice,” Journal of Biological Chemistry, vol. 284, no. 18, pp. 12432–12446, 2009. View at Publisher · View at Google Scholar · View at Scopus
  44. S. Misra, V. C. Hascall, N. K. Karamanos, R. R. Markwald, and S. Ghatak, Delivery Systems Targeting Cancer at the Level of ECM, DeGruyter, Berlin, Germany, 2012.
  45. L. Y. W. Bourguignon, K. Peyrollier, W. Xia, and E. Gilad, “Hyaluronan-CD44 interaction activates stem cell marker Nanog, Stat-3-mediated MDR1 gene expression, and ankyrin-regulated multidrug efflux in breast and ovarian tumor cells,” The Journal of Biological Chemistry, vol. 283, no. 25, pp. 17635–17651, 2008. View at Publisher · View at Google Scholar · View at Scopus
  46. L. Y. W. Bourguignon, P. A. Singleton, H. Zhu, and F. Diedrich, “Hyaluronan-mediated CD44 interaction with RhoGEF and Rho kinase promotes Grb2-associated binder-1 phosphorylation and phosphatidylinositol 3-kinase signaling leading to cytokine (macrophage-colony stimulating factor) production and breast tumor progression,” Journal of Biological Chemistry, vol. 278, no. 32, pp. 29420–29434, 2003. View at Publisher · View at Google Scholar · View at Scopus
  47. L. Y. W. Bourguignon, K. Peyrollier, E. Gilad, and A. Brightman, “Hyaluronan-CD44 interaction with neural Wiskott-Aldrich syndrome protein (N-WASP) promotes actin polymerization and ErbB2 activation leading to beta-catenin nuclear translocation, transcriptional up-regulation, and cell migration in ovarian tumor cells,” The Journal of Biological Chemistry, vol. 282, no. 2, pp. 1265–1280, 2007. View at Publisher · View at Google Scholar · View at Scopus
  48. D. Naor, S. Nedvetzki, I. Golan, L. Melnik, and Y. Faitelson, “CD44 in cancer,” Critical Reviews in Clinical Laboratory Sciences, vol. 39, no. 6, pp. 527–579, 2002. View at Google Scholar · View at Scopus
  49. L. Y. W. Bourguignon, H. Zhu, L. Shao, and Y. W. Chen, “CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid- mediated breast tumor cell migration,” The Journal of Biological Chemistry, vol. 275, no. 3, pp. 1829–1838, 2000. View at Publisher · View at Google Scholar · View at Scopus
  50. K. Akima, H. Ito, Y. Iwata et al., “Evaluation of antitumor activities of hyaluronate binding antitumor drugs: synthesis, characterization and antitumor activity,” Journal of Drug Targeting, vol. 4, no. 1, pp. 1–8, 1996. View at Google Scholar · View at Scopus
  51. J. I. Park, L. Cao, V. M. Platt et al., “Antitumor therapy mediated by 5-fluorocytosine and a recombinant fusion protein containing TSG-6 hyaluronan binding domain and yeast cytosine deaminase,” Molecular Pharmaceutics, vol. 6, no. 3, pp. 801–812, 2009. View at Publisher · View at Google Scholar · View at Scopus
  52. M.-S. Sy, Y.-J. Guo, and I. Stamenkovic, “Inhibition of tumor growth in vivo with a soluble CD44-immunoglobulin fusion protein,” The Journal of Experimental Medicine, vol. 176, no. 2, pp. 623–627, 1992. View at Publisher · View at Google Scholar · View at Scopus
  53. V. B. Lokeshwar, L. E. Lopez, D. Munoz et al., “Antitumor activity of hyaluronic acid synthesis inhibitor 4-methylumbelliferone in prostate cancer cells,” Cancer Research, vol. 70, no. 7, pp. 2613–2623, 2010. View at Publisher · View at Google Scholar · View at Scopus
  54. E. Arai, Y. Nishida, J. Wasa et al., “Inhibition of hyaluronan retention by 4-methylumbelliferone suppresses osteosarcoma cells in vitro and lung metastasis in vivo,” British Journal of Cancer, vol. 105, no. 12, pp. 1839–1849, 2011. View at Publisher · View at Google Scholar · View at Scopus
  55. H. Nakazawa, S. Yoshihara, D. Kudo et al., “4-methylumbelliferone, a hyaluronan synthase suppressor, enhances the anticancer activity of gemcitabine in human pancreatic cancer cells,” Cancer Chemotherapy and Pharmacology, vol. 57, no. 2, pp. 165–170, 2006. View at Publisher · View at Google Scholar · View at Scopus
  56. J. Klocker, H. Sabitzer, W. Raunik, S. Wieser, and J. Schumer, “Hyaluronidase as additive to induction chemotherapy in advanced squamous cell carcinoma of the head and neck,” Cancer Letters, vol. 131, no. 1, pp. 113–115, 1998. View at Publisher · View at Google Scholar · View at Scopus
  57. K. Pillwein, R. Fuiko, I. Slavc et al., “Hyaluronidase additional to standard chemotherapy improves outcome for children with malignant brain tumors,” Cancer Letters, vol. 131, no. 1, pp. 101–108, 1998. View at Publisher · View at Google Scholar · View at Scopus
  58. C. J. Whatcott, H. Han, R. G. Posner, G. Hostetter, and D. D. Von Hoff, “Targeting the tumor microenvironment in cancer: why hyaluronidase deserves a second look,” Cancer Discovery, vol. 1, no. 4, pp. 291–296, 2011. View at Publisher · View at Google Scholar · View at Scopus
  59. J. R. E. Fraser, W. G. Kimpton, T. C. Laurent, R. N. P. Cahill, and N. Vakakis, “Uptake and degradation of hyaluronan in lymphatic tissue,” Biochemical Journal, vol. 256, no. 1, pp. 153–158, 1988. View at Google Scholar · View at Scopus
  60. J. R. Fraser and T. C. Laurent, “Turnover and metabolism of hyaluronan,” Ciba Foundation Symposium, vol. 143, pp. 41–53, 1989. View at Google Scholar
  61. G. Ostgaard and R. K. Reed, “Hyaluronan turnover in the rat small intestine,” Acta Physiologica Scandinavica, vol. 149, no. 2, pp. 237–244, 1993. View at Publisher · View at Google Scholar · View at Scopus
  62. G. Ostgaard and R. K. Reed, “Intravenous saline infusion in rat increases hyaluronan efflux in intestinal lymph by increasing lymph flow,” Acta Physiologica Scandinavica, vol. 147, no. 3, pp. 329–335, 1993. View at Publisher · View at Google Scholar · View at Scopus
  63. G. Ostgaard and R. K. Reed, “Increased lymphatic hyaluronan output and preserved hyaluronan content of the rat small intestine in prolonged hypoproteinaemia,” Acta Physiologica Scandinavica, vol. 152, no. 1, pp. 51–56, 1994. View at Publisher · View at Google Scholar · View at Scopus
  64. L. B. Dahl, T. C. Laurent, and B. Smedsrød, “Preparation of biologically intact radioiodinated hyaluronan of high specific radioactivity: coupling of 125I-tyramine-cellobiose to amino groups after partial N-deacetylation,” Analytical Biochemistry, vol. 175, no. 2, pp. 397–407, 1988. View at Publisher · View at Google Scholar · View at Scopus
  65. J. R. E. Fraser, T. C. Laurent, H. Pertoft, and E. Baxter, “Plasma clearance, tissue distribution and metabolism of hyaluronic acid injected intravenously in the rabbit,” Biochemical Journal, vol. 200, no. 2, pp. 415–424, 1981. View at Google Scholar · View at Scopus
  66. E. Feusi, L. Sun, A. Sibalic, B. Beck-Schimmer, B. Oertli, and R. P. Wüthrich, “Enhanced hyaluronan synthesis in the MRL-Faslpr kidney: role of cytokines,” Nephron, vol. 83, no. 1, pp. 66–73, 1999. View at Publisher · View at Google Scholar · View at Scopus
  67. L.-K. Sun, E. Feusi, A. Sibalic, B. Beck-Schimmer, and R. P. Wüthrich, “Expression profile of hyaluronidase mRNA transcripts in the kidney and in renal cells,” Kidney and Blood Pressure Research, vol. 21, no. 6, pp. 413–418, 1998. View at Publisher · View at Google Scholar · View at Scopus
  68. V. Sibalic, X. Fan, J. Loffing, and R. P. Wüthrich, “Upregulated renal tubular CD44, hyaluronan, and osteopontin in kdkd mice with interstitial nephritis,” Nephrology Dialysis Transplantation, vol. 12, no. 7, pp. 1344–1353, 1997. View at Publisher · View at Google Scholar · View at Scopus
  69. P. S. Benz, X. Fan, and R. P. Wüthrich, “Enhanced tubular epithelial CD44 expression in MRL-lpr lupus nephritis,” Kidney International, vol. 50, no. 1, pp. 156–163, 1996. View at Publisher · View at Google Scholar · View at Scopus
  70. H. Ponta, L. Sherman, and P. A. Herrlich, “CD44: from adhesion molecules to signalling regulators,” Nature Reviews Molecular Cell Biology, vol. 4, no. 1, pp. 33–45, 2003. View at Publisher · View at Google Scholar · View at Scopus
  71. R. van der Voort, T. E. I. Taher, V. J. M. Wielenga et al., “Heparan sulfate-modified CD44 promotes hepatocyte growth factor/scatter factor-induced signal transduction through the receptor tyro sine kinase c- Met,” The Journal of Biological Chemistry, vol. 274, no. 10, pp. 6499–6506, 1999. View at Publisher · View at Google Scholar · View at Scopus
  72. T. P. Skelton, C. Zeng, A. Nocks, and I. Stamenkovic, “Glycosylation provides both stimulatory and inhibitory effects on cell surface and soluble CD44 binding to hyaluronan,” Journal of Cell Biology, vol. 140, no. 2, pp. 431–446, 1998. View at Publisher · View at Google Scholar · View at Scopus
  73. D. Naor, S. B. Wallach-Dayan, M. A. Zahalka, and R. V. Sionov, “Involvement of CD44, a molecule with a thousand faces, in cancer dissemination,” Seminars in Cancer Biology, vol. 18, no. 4, pp. 260–267, 2008. View at Publisher · View at Google Scholar · View at Scopus
  74. C. Echiburú-Chau, D. Roy, and G. M. Calaf, “Metastatic suppressor CD44 is related with oxidative stress in breast cancer cell lines,” International Journal of Oncology, vol. 39, no. 6, pp. 1481–1489, 2011. View at Publisher · View at Google Scholar · View at Scopus
  75. J. M. V. Louderbough, J. A. Brown, R. B. Nagle, and J. A. Schroeder, “CD44 promotes epithelial mammary gland development and exhibits altered localization during cancer progression,” Genes and Cancer, vol. 2, no. 8, pp. 771–781, 2011. View at Publisher · View at Google Scholar · View at Scopus
  76. J. M. V. Louderbough and J. A. Schroeder, “Understanding the dual nature of CD44 in breast cancer progression,” Molecular Cancer Research, vol. 9, no. 12, pp. 1573–1586, 2011. View at Publisher · View at Google Scholar · View at Scopus
  77. S. V. Vinogradov, T. K. Bronich, and A. V. Kabanov, “Nanosized cationic hydrogels for drug delivery: preparation, properties and interactions with cells,” Advanced Drug Delivery Reviews, vol. 54, no. 1, pp. 135–147, 2002. View at Publisher · View at Google Scholar · View at Scopus
  78. L. Y. Qiu and Y. H. Bae, “Polymer architecture and drug delivery,” Pharmaceutical Research, vol. 23, no. 1, pp. 1–30, 2006. View at Publisher · View at Google Scholar · View at Scopus
  79. S. Svenson and D. A. Tomalia, “Dendrimers in biomedical applications—reflections on the field,” Advanced Drug Delivery Reviews, vol. 57, no. 15, pp. 2106–2129, 2005. View at Publisher · View at Google Scholar · View at Scopus
  80. U. Häcker, K. Nybakken, and N. Perrimon, “Heparan sulphate proteoglycans: the sweet side of development,” Nature Reviews Molecular Cell Biology, vol. 6, no. 7, pp. 530–541, 2005. View at Publisher · View at Google Scholar · View at Scopus
  81. R. K. Jain, L. L. Munn, and D. Fukumura, “Dissecting tumour pathophysiology using intravital microscopy,” Nature Reviews Cancer, vol. 2, no. 4, pp. 266–276, 2002. View at Publisher · View at Google Scholar · View at Scopus
  82. V. P. Chauhan, T. Stylianopoulos, Y. Boucher, and R. K. Jain, “Delivery of molecular and nanoscale medicine to tumors: transport barriers and strategies,” Annual Review of Chemical and Biomolecular Engineering, vol. 2, pp. 281–298, 2011. View at Publisher · View at Google Scholar · View at Scopus
  83. R. J. Linhardt, “2003 Claude S. Hudson award address in carbohydrate chemistry. Heparin: structure and activity,” Journal of Medicinal Chemistry, vol. 46, no. 13, pp. 2551–2564, 2003. View at Publisher · View at Google Scholar · View at Scopus
  84. K. V. Clemons, D. F. Ranney, and D. A. Stevens, “A novel heparin-coated hydrophilic preparation of amphotericin B hydrosomes,” Current Opinion in Investigational Drugs, vol. 2, no. 4, pp. 480–487, 2001. View at Google Scholar · View at Scopus
  85. D. Y. Lee, Z. Khatun, J.-H. Lee, Y.-K. Lee, and I. In, “Blood compatible graphene/heparin conjugate through noncovalent chemistry,” Biomacromolecules, vol. 12, no. 2, pp. 336–341, 2011. View at Publisher · View at Google Scholar · View at Scopus
  86. Z. Khatun, M. Nurunnabi, G. R. Reeck, K. J. Cho, and Y.-K. Lee, “Oral delivery of taurocholic acid linked heparin-docetaxel conjugates for cancer therapy,” Journal of Controlled Release, vol. 170, no. 1, pp. 74–82, 2013. View at Publisher · View at Google Scholar · View at Scopus
  87. Z. Khatun, M. Nurunnabi, K. J. Cho, Y. Byun, Y. H. Bae, and Y.-K. Lee, “Oral absorption mechanism and anti-angiogenesis effect of taurocholic acid-linked heparin-docetaxel conjugates,” Journal of Controlled Release, vol. 177, no. 1, pp. 64–73, 2014. View at Publisher · View at Google Scholar · View at Scopus
  88. H. Tan, Q. Shen, X. Jia, Z. Yuan, and D. Xiong, “Injectable nanohybrid scaffold for biopharmaceuticals delivery and soft tissue engineering,” Macromolecular Rapid Communications, vol. 33, no. 23, pp. 2015–2022, 2012. View at Publisher · View at Google Scholar · View at Scopus
  89. D.-W. Tang, S.-H. Yu, Y.-C. Ho, F.-L. Mi, P.-L. Kuo, and H.-W. Sung, “Heparinized chitosan/poly(γ-glutamic acid) nanoparticles for multi-functional delivery of fibroblast growth factor and heparin,” Biomaterials, vol. 31, no. 35, pp. 9320–9332, 2010. View at Publisher · View at Google Scholar · View at Scopus
  90. X. Xu, A. K. Jha, R. L. Duncan, and X. Jia, “Heparin-decorated, hyaluronic acid-based hydrogel particles for the controlled release of bone morphogenetic protein 2,” Acta Biomaterialia, vol. 7, no. 8, pp. 3050–3059, 2011. View at Publisher · View at Google Scholar · View at Scopus
  91. P. P. Srinivasan, S. Y. McCoy, A. K. Jha et al., “Injectable perlecan domain 1-hyaluronan microgels potentiate the cartilage repair effect of BMP2 in a murine model of early osteoarthritis,” Biomedical Materials, vol. 7, no. 2, Article ID 024109, 2012. View at Publisher · View at Google Scholar · View at Scopus
  92. A. R. Poole, “Proteoglycans in health and disease: structures and functions,” Biochemical Journal, vol. 236, no. 1, pp. 1–14, 1986. View at Google Scholar · View at Scopus
  93. K. Prydz and K. T. Dalen, “Synthesis and sorting of proteoglycans,” Journal of Cell Science, vol. 113, part 2, pp. 193–205, 2000. View at Google Scholar · View at Scopus
  94. M. Bernfield, R. Kokenyesi, M. Kato et al., “Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans,” Annual Review of Cell Biology, vol. 8, pp. 365–393, 1992. View at Publisher · View at Google Scholar · View at Scopus
  95. H. C. Christianson and M. Belting, “Heparan sulfate proteoglycan as a cell-surface endocytosis receptor,” Matrix Biology, vol. 35, pp. 51–55, 2014. View at Publisher · View at Google Scholar · View at Scopus
  96. Y.-M. Guo, M. Liu, J.-L. Yang et al., “Intercellular imaging by a polyarginine derived cell penetrating peptide labeled magnetic resonance contrast agent, diethylenetriamine pentaacetic acid gadolinium,” Chinese Medical Journal, vol. 120, no. 1, pp. 50–55, 2007. View at Google Scholar · View at Scopus
  97. T. Letoha, A. Keller-Pintér, E. Kusz et al., “Cell-penetrating peptide exploited syndecans,” Biochimica et Biophysica Acta, vol. 1798, no. 12, pp. 2258–2265, 2010. View at Publisher · View at Google Scholar · View at Scopus
  98. J. Wang, Z. Lu, M. G. Wientjes, and J. L.-S. Au, “Delivery of siRNA therapeutics: barriers and carriers,” AAPS Journal, vol. 12, no. 4, pp. 492–503, 2010. View at Publisher · View at Google Scholar · View at Scopus
  99. F. Said Hassane, A. F. Saleh, R. Abes, M. J. Gait, and B. Lebleu, “Cell penetrating peptides: overview and applications to the delivery of oligonucleotides,” Cellular and Molecular Life Sciences, vol. 67, no. 5, pp. 715–726, 2010. View at Publisher · View at Google Scholar · View at Scopus
  100. N. A. Brooks, D. S. Pouniotis, K. C. Sheng, V. Apostolopoulos, and G. A. Pietersz, “A membrane penetrating multiple antigen peptide (MAP) incorporating ovalbumin CD8 epitope induces potent immune responses in mice,” Biochimica et Biophysica Acta—Biomembranes, vol. 1798, no. 12, pp. 2286–2295, 2010. View at Publisher · View at Google Scholar · View at Scopus
  101. N. A. Brooks, D. S. Pouniotis, C.-K. Tang, V. Apostolopoulos, and G. A. Pietersz, “Cell-penetrating peptides: application in vaccine delivery,” Biochimica et Biophysica Acta, vol. 1805, no. 1, pp. 25–34, 2010. View at Publisher · View at Google Scholar · View at Scopus
  102. M. M. Fretz and G. Storm, “TAT-peptide modified liposomes: preparation, characterization, and cellular interaction,” Methods in Molecular Biology, vol. 605, pp. 349–359, 2010. View at Publisher · View at Google Scholar · View at Scopus
  103. L. N. Patel, J. Wang, K.-J. Kim, Z. Borok, E. D. Crandall, and W.-C. Shen, “Conjugation with cationic cell-penetrating peptide increases pulmonary absorption of insulin,” Molecular Pharmaceutics, vol. 6, no. 2, pp. 492–503, 2009. View at Publisher · View at Google Scholar · View at Scopus
  104. J. Kleeff, T. Ishiwata, A. Kumbasar et al., “The cell-surface heparan sulfate proteoglycan glypican-1 regulates growth factor action in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer,” Journal of Clinical Investigation, vol. 102, no. 9, pp. 1662–1673, 1998. View at Publisher · View at Google Scholar · View at Scopus
  105. B. Sharma, M. Handler, I. Eichstetter, J. M. Whitelock, M. A. Nugent, and R. V. Iozzo, “Antisense targeting of perlecan blocks tumor growth and angiogenesis in vivo,” The Journal of Clinical Investigation, vol. 102, no. 8, pp. 1599–1608, 1998. View at Publisher · View at Google Scholar · View at Scopus
  106. J. H. Grubb, C. Vogler, and W. S. Sly, “New strategies for enzyme replacement therapy for lysosomal storage diseases,” Rejuvenation Research, vol. 13, no. 2-3, pp. 229–236, 2010. View at Publisher · View at Google Scholar · View at Scopus
  107. J. E. Wraith, “Lysosomal disorders,” Seminars in Neonatology, vol. 7, no. 1, pp. 75–83, 2002. View at Publisher · View at Google Scholar · View at Scopus
  108. K. Hamada, C. Yoshihara, T. Ito et al., “Antitumor effect of chondroitin sulfate-coated ternary granulocyte macrophage-colony-stimulating factor plasmid complex for ovarian cancer,” Journal of Gene Medicine, vol. 14, no. 2, pp. 120–127, 2012. View at Publisher · View at Google Scholar · View at Scopus
  109. Z. Liu, Y. Jiao, Y. Wang, C. Zhou, and Z. Zhang, “Polysaccharides-based nanoparticles as drug delivery systems,” Advanced Drug Delivery Reviews, vol. 60, no. 15, pp. 1650–1662, 2008. View at Publisher · View at Google Scholar · View at Scopus
  110. V. R. Sinha and R. Kumria, “Polysaccharides in colon-specific drug delivery,” International Journal of Pharmaceutics, vol. 224, no. 1-2, pp. 19–38, 2001. View at Publisher · View at Google Scholar · View at Scopus
  111. K. S. Soppimath, T. M. Aminabhavi, A. R. Kulkarni, and W. E. Rudzinski, “Biodegradable polymeric nanoparticles as drug delivery devices,” Journal of Controlled Release, vol. 70, no. 1-2, pp. 1–20, 2001. View at Publisher · View at Google Scholar · View at Scopus
  112. S. Mitra, U. Gaur, P. C. Ghosh, and A. N. Maitra, “Tumour targeted delivery of encapsulated dextran-doxorubicin conjugate using chitosan nanoparticles as carrier,” Journal of Controlled Release, vol. 74, no. 1–3, pp. 317–323, 2001. View at Publisher · View at Google Scholar · View at Scopus
  113. C.-T. Lee, C.-P. Huang, and Y.-D. Lee, “Preparation of amphiphilic poly(L-lactide)-graft-chondroitin sulfate copolymer self-aggregates and its aggregation behavior,” Biomacromolecules, vol. 7, no. 4, pp. 1179–1186, 2006. View at Publisher · View at Google Scholar · View at Scopus
  114. G. Mocanu, D. Mihai, L. Picton, D. LeCerf, and G. Muller, “Associative pullulan gels and their interaction with biological active substances,” Journal of Controlled Release, vol. 83, no. 1, pp. 41–51, 2002. View at Publisher · View at Google Scholar · View at Scopus
  115. M. R. Campoli, C.-C. Chang, T. Kageshita, X. Wang, J. B. McCarthy, and S. Ferrone, “Human high molecular weight-melanoma-associated antigen (HMW-MAA): a melanoma cell surface chondroitin sulfate proteoglycan (MSCP) with biological and clinical significance,” Critical Reviews in Immunology, vol. 24, no. 4, pp. 267–296, 2004. View at Publisher · View at Google Scholar · View at Scopus
  116. J. Yang, M. A. Price, Y. L. Gui et al., “Melanoma proteoglycan modifies gene expression to stimulate tumor cell motility, growth, and epithelial-to-mesenchymal transition,” Cancer Research, vol. 69, no. 19, pp. 7538–7547, 2009. View at Publisher · View at Google Scholar · View at Scopus
  117. J. Iida, K. L. Wilhelmson, J. Ng et al., “Cell surface chondroitin sulfate glycosaminoglycan in melanoma: role in the activation of pro-MMP-2 (pro-gelatinase A),” Biochemical Journal, vol. 403, no. 3, pp. 553–563, 2007. View at Publisher · View at Google Scholar · View at Scopus
  118. C.-C. Chang, M. Campoli, W. Luo, W. Zhao, K. S. Zaenker, and S. Ferrone, “Immunotherapy of melanoma targeting human high molecular weight melanoma-associated antigen: potential role of nonimmunological mechanisms,” Annals of the New York Academy of Sciences, vol. 1028, pp. 340–350, 2004. View at Publisher · View at Google Scholar · View at Scopus
  119. M. Schwenkert, K. Birkholz, M. Schwemmlein et al., “A single chain immunotoxin, targeting the melanoma-associated chondroitin sulfate proteoglycan, is a potent inducer of apoptosis in cultured human melanoma cells,” Melanoma Research, vol. 18, no. 2, pp. 73–84, 2008. View at Publisher · View at Google Scholar · View at Scopus
  120. J. Xi, L. Zhou, and Y. Fei, “Preparation of chondroitin sulfate nanocapsules for use as carries by the interfacial polymerization method,” International Journal of Biological Macromolecules, vol. 50, no. 1, pp. 157–163, 2012. View at Publisher · View at Google Scholar · View at Scopus
  121. J. Xi, J. Qin, and L. Fan, “Chondroitin sulfate functionalized mesostructured silica nanoparticles as biocompatible carriers for drug delivery,” International Journal of Nanomedicine, vol. 7, pp. 5235–5247, 2012. View at Publisher · View at Google Scholar · View at Scopus
  122. W. Park, S.-J. Park, and K. Na, “Potential of self-organizing nanogel with acetylated chondroitin sulfate as an anti-cancer drug carrier,” Colloids and Surfaces B: Biointerfaces, vol. 79, no. 2, pp. 501–508, 2010. View at Publisher · View at Google Scholar · View at Scopus
  123. S.-J. Huang, S.-L. Sun, T.-H. Feng, K.-H. Sung, W.-L. Lui, and L.-F. Wang, “Folate-mediated chondroitin sulfate-Pluronic 127 nanogels as a drug carrier,” European Journal of Pharmaceutical Sciences, vol. 38, no. 1, pp. 64–73, 2009. View at Publisher · View at Google Scholar · View at Scopus
  124. G. Mascellani, L. Liverani, P. Bianchini et al., “Structure and contribution to the heparin cofactor II-mediated inhibition of thrombin of naturally oversulphated sequences of dermatan sulphate,” Biochemical Journal, vol. 296, no. 3, pp. 639–648, 1993. View at Google Scholar · View at Scopus
  125. K. Meyer, A. Linker, E. A. Davidson, and B. Weissmann, “The mucopolysaccharides of bovine cornea,” The Journal of Biological Chemistry, vol. 205, no. 2, pp. 611–616, 1953. View at Google Scholar · View at Scopus
  126. J. R. Hassell, D. A. Newsome, J. H. Krachmer, and M. M. Rodrigues, “Macular corneal dystrophy: failure to synthesize a mature keratan sulfate proteoglycan,” Proceedings of the National Academy of Sciences of the United States of America, vol. 77, no. 6, pp. 3705–3709, 1980. View at Publisher · View at Google Scholar · View at Scopus
  127. T. C. Li, J. D. Aplin, A. Warren, R. A. Graham, P. Dockery, and I. D. Cooke, “Endometrial responses to three different progestins in artificial cycles: a prospective, crossover study,” Fertility and Sterility, vol. 62, no. 1, pp. 191–193, 1994. View at Google Scholar · View at Scopus
  128. R. A. Graham, T. C. Li, I. D. Cooke, and J. D. Aplin, “Keratan sulphate as a secretory product of human endometrium: cyclic expression in normal women,” Human Reproduction, vol. 9, no. 5, pp. 926–930, 1994. View at Google Scholar · View at Scopus
  129. J. L. Funderburgh, “Keratan sulfate: structure, biosynthesis, and function,” Glycobiology, vol. 10, no. 10, pp. 951–958, 2000. View at Publisher · View at Google Scholar · View at Scopus
  130. J. L. Funderburgh, M. L. Funderburgh, M. M. Mann, and G. W. Conrad, “Physical and biological properties of keratan sulphate proteoglycan,” Biochemical Society Transactions, vol. 19, no. 4, pp. 871–876, 1991. View at Google Scholar · View at Scopus
  131. V. C. Hascall, “Structure and biosynthesis of proteoglycans with keratan sulfate,” Progress in Clinical and Biological Research, vol. 110, pp. 3–15, 1982. View at Google Scholar · View at Scopus
  132. H. Greiling, “Structure and biological functions of keratan sulfate proteoglycans,” EXS, vol. 70, pp. 101–122, 1994. View at Google Scholar · View at Scopus
  133. S. Tomatsu, A. M. Montão, V. C. Dung et al., “Enhancement of drug delivery: enzyme-replacement therapy for murine Morquio A syndrome,” Molecular Therapy, vol. 18, no. 6, pp. 1094–1102, 2010. View at Publisher · View at Google Scholar · View at Scopus
  134. S. Liu, M.-N. Jin, Y.-S. Quan et al., “The development and characteristics of novel microneedle arrays fabricated from hyaluronic acid, and their application in the transdermal delivery of insulin,” Journal of Controlled Release, vol. 161, no. 3, pp. 933–941, 2012. View at Publisher · View at Google Scholar · View at Scopus
  135. A. R. Mathers and A. T. Larregina, “Professional antigen-presenting cells of the skin,” Immunologic Research, vol. 36, no. 1–3, pp. 127–136, 2006. View at Publisher · View at Google Scholar · View at Scopus
  136. K. Sugita, K. Kabashima, K. Atarashi, T. Shimauchi, M. Kobayashi, and Y. Tokura, “Innate immunity mediated by epidermal keratinocytes promotes acquired immunity involving Langerhans cells and T cells in the skin,” Clinical & Experimental Immunology, vol. 147, no. 1, pp. 176–183, 2007. View at Publisher · View at Google Scholar · View at Scopus
  137. C. L. Berger, J. G. Vasquez, J. Shofner, K. Mariwalla, and R. L. Edelson, “Langerhans cells: mediators of immunity and tolerance,” International Journal of Biochemistry and Cell Biology, vol. 38, no. 10, pp. 1632–1636, 2006. View at Publisher · View at Google Scholar · View at Scopus
  138. N. Romani, B. E. Clausen, and P. Stoitzner, “Langerhans cells and more: langerin-expressing dendritic cell subsets in the skin,” Immunological Reviews, vol. 234, no. 1, pp. 120–141, 2010. View at Publisher · View at Google Scholar · View at Scopus
  139. J.-H. Park, M. G. Allen, and M. R. Prausnitz, “Biodegradable polymer microneedles: fabrication, mechanics and transdermal drug delivery,” Journal of Controlled Release, vol. 104, no. 1, pp. 51–66, 2005. View at Publisher · View at Google Scholar · View at Scopus
  140. J. W. Lee, J.-H. Park, and M. R. Prausnitz, “Dissolving microneedles for transdermal drug delivery,” Biomaterials, vol. 29, no. 13, pp. 2113–2124, 2008. View at Publisher · View at Google Scholar · View at Scopus
  141. S. P. Sullivan, D. G. Koutsonanos, M. del Pilar Martin et al., “Dissolving polymer microneedle patches for influenza vaccination,” Nature Medicine, vol. 16, no. 8, pp. 915–920, 2010. View at Publisher · View at Google Scholar · View at Scopus
  142. K. Matsuo, S. Hirobe, Y. Yokota et al., “Transcutaneous immunization using a dissolving microneedle array protects against tetanus, diphtheria, malaria, and influenza,” Journal of Controlled Release, vol. 160, no. 3, pp. 495–501, 2012. View at Publisher · View at Google Scholar · View at Scopus
  143. F. J. Verbaan, S. M. Bal, D. J. van den Berg et al., “Assembled microneedle arrays enhance the transport of compounds varying over a large range of molecular weight across human dermatomed skin,” Journal of Controlled Release, vol. 117, no. 2, pp. 238–245, 2007. View at Publisher · View at Google Scholar · View at Scopus
  144. T. J. Brown, D. Alcorn, and J. R. E. Fraser, “Absorption of hyaluronan applied to the surface of intact skin,” Journal of Investigative Dermatology, vol. 113, no. 5, pp. 740–746, 1999. View at Publisher · View at Google Scholar · View at Scopus
  145. M. B. Brown and S. A. Jones, “Hyaluronic acid: a unique topical vehicle for the localized delivery of drugs to the skin,” Journal of the European Academy of Dermatology and Venereology, vol. 19, no. 3, pp. 308–318, 2005. View at Publisher · View at Google Scholar · View at Scopus
  146. J. J. Skehel and M. D. Waterfield, “Studies on the primary structure of the influenza virus hemagglutinin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 72, no. 1, pp. 93–97, 1975. View at Publisher · View at Google Scholar · View at Scopus
  147. J. W. Shupp, T. J. Nasabzadeh, D. S. Rosenthal, M. H. Jordan, P. Fidler, and J. C. Jeng, “A review of the local pathophysiologic bases of burn wound progression,” Journal of Burn Care and Research, vol. 31, no. 6, pp. 849–873, 2010. View at Publisher · View at Google Scholar · View at Scopus
  148. G. Arturson, “Pathophysiology of the burn wound and pharmacological treatment. The Rudi Hermans Lecture, 1995,” Burns, vol. 22, no. 4, pp. 255–274, 1996. View at Publisher · View at Google Scholar · View at Scopus
  149. M. G. Schwacha, B. M. Thobe, T. Daniel, and W. J. Hubbard, “Impact of thermal injury on wound infiltration and the dermal inflammatory response,” Journal of Surgical Research, vol. 158, no. 1, pp. 112–120, 2010. View at Publisher · View at Google Scholar · View at Scopus
  150. M. S. Pandey, B. A. Baggenstoss, J. Washburn, E. N. Harris, and P. H. Weigel, “The hyaluronan receptor for endocytosis (HARE) activates NF-κB-mediated gene expression in response to 40–400-kDa, but not smaller or larger, hyaluronans,” Journal of Biological Chemistry, vol. 288, no. 20, pp. 14068–14079, 2013. View at Publisher · View at Google Scholar · View at Scopus
  151. L. T. Sun, E. Friedrich, J. L. Heuslein et al., “Reduction of burn progression with topical delivery of (antitumor necrosis factor-alpha)-hyaluronic acid conjugates,” Wound Repair and Regeneration, vol. 20, no. 4, pp. 563–572, 2012. View at Publisher · View at Google Scholar · View at Scopus
  152. C. Le Bourlais, L. Acar, H. Zia, P. A. Sado, T. Needham, and R. Leverge, “Ophthalmic drug delivery systems—recent advances,” Progress in Retinal and Eye Research, vol. 17, no. 1, pp. 33–58, 1998. View at Publisher · View at Google Scholar · View at Scopus
  153. E. L. Graue, F. M. Polack, and E. A. Balazs, “The protective effect of Na-hyaluronate to corneal endothelium,” Experimental Eye Research, vol. 31, no. 1, pp. 119–127, 1980. View at Publisher · View at Google Scholar · View at Scopus
  154. R. Gurny, J. E. Ryser, C. Tabatabay, M. Martenet, P. Edman, and O. Camber, “Precorneal residence time in humans of sodium hyaluronate as measured by gamma scintigraphy,” Graefe's Archive for Clinical and Experimental Ophthalmology, vol. 228, no. 6, pp. 510–512, 1990. View at Publisher · View at Google Scholar · View at Scopus
  155. J. A. P. Gomes, R. Amankwah, A. Powell-Richards, and H. S. Dua, “Sodium hyaluronate (hyaluronic acid) promotes migration of human corneal epithelial cells in vitro,” British Journal of Ophthalmology, vol. 88, no. 6, pp. 821–825, 2004. View at Publisher · View at Google Scholar · View at Scopus
  156. E. Tani, C. Katakami, and A. Negi, “Effects of various eye drops on corneal wound healing after superficial keratectomy in rabbits,” Japanese Journal of Ophthalmology, vol. 46, no. 5, pp. 488–495, 2002. View at Publisher · View at Google Scholar · View at Scopus
  157. T. C. Laurent, U. B. G. Laurent, and J. R. E. Fraser, “The structure and function of hyaluronan: an overview,” Immunology & Cell Biology, vol. 74, no. 2, pp. A1–A7, 1996. View at Publisher · View at Google Scholar · View at Scopus
  158. M. F. Saettone, D. Monti, M. T. Torracca, and P. Chetoni, “Mucoadhesive ophthalmic vehicles: evaluation of polymeric low-viscosity formulations,” Journal of Ocular Pharmacology, vol. 10, no. 1, pp. 83–92, 1994. View at Publisher · View at Google Scholar · View at Scopus
  159. O. Camber, P. Edman, and R. Gurny, “Influence of sodium hyaluronate on the meiotic effect of pilocarpine in rabbits,” Current Eye Research, vol. 6, no. 6, pp. 779–784, 1987. View at Publisher · View at Google Scholar · View at Scopus
  160. C. Bucolo and P. Mangiafico, “Pharmacological profile of a new topical pilocarpine formulation,” Journal of Ocular Pharmacology and Therapeutics, vol. 15, no. 6, pp. 567–573, 1999. View at Publisher · View at Google Scholar · View at Scopus
  161. C. Bucolo, S. Mangiafico, and A. Spadaro, “Methylprednisolone delivery by Hyalobend corneal shields and its effects on rabbit ocular inflammation,” Journal of Ocular Pharmacology and Therapeutics, vol. 12, no. 2, pp. 141–149, 1996. View at Publisher · View at Google Scholar · View at Scopus
  162. R. Herrero-Vanrell, A. Fernandez-Carballido, G. Frutos, and R. Cadórniga, “Enhancement of the mydriatic response to tropicamide by bioadhesive polymers,” Journal of Ocular Pharmacology and Therapeutics, vol. 16, no. 5, pp. 419–428, 2000. View at Publisher · View at Google Scholar · View at Scopus
  163. S. A. Gandolfi, A. Massari, and J. G. Orsoni, “Low-molecular-weight sodium hyaluronate in the treatment of bacterial corneal ulcers,” Graefe's Archive for Clinical and Experimental Ophthalmology, vol. 230, no. 1, pp. 20–23, 1992. View at Publisher · View at Google Scholar · View at Scopus
  164. K. Y. Cho, T. W. Chung, B. C. Kim et al., “Release of ciprofloxacin from poloxamer-graft-hyaluronic acid hydrogels in vitro,” International Journal of Pharmaceutics, vol. 260, no. 1, pp. 83–91, 2003. View at Publisher · View at Google Scholar · View at Scopus
  165. K. Y. Choi, G. Saravanakumar, J. H. Park, and K. Park, “Hyaluronic acid-based nanocarriers for intracellular targeting: interfacial interactions with proteins in cancer,” Colloids and Surfaces B: Biointerfaces, vol. 99, pp. 82–94, 2012. View at Publisher · View at Google Scholar · View at Scopus
  166. T. Pouyani and G. D. Prestwich, “Functionalized derivatives of hyaluronic acid oligosaccharides: drug carriers and novel biomaterials,” Bioconjugate Chemistry, vol. 5, no. 4, pp. 339–347, 1994. View at Publisher · View at Google Scholar · View at Scopus
  167. M. B. Duncan, M. Liu, C. Fox, and J. Liu, “Characterization of the N-deacetylase domain from the heparan sulfate N-deacetylase/N-sulfotransferase 2,” Biochemical and Biophysical Research Communications, vol. 339, no. 4, pp. 1232–1237, 2006. View at Publisher · View at Google Scholar · View at Scopus
  168. S. Mochizuki, A. Kano, N. Shimada, and A. Maruyama, “Uptake of enzymatically-digested hyaluronan by liver endothelial cells in vivo and in vitro,” Journal of Biomaterials Science, Polymer Edition, vol. 20, no. 1, pp. 83–97, 2009. View at Publisher · View at Google Scholar · View at Scopus
  169. E. N. Harris, S. V. Kyosseva, J. A. Weigel, and P. H. Weigel, “Expression, processing, and glycosaminoglycan binding activity of the recombinant human 315-kDa Hyaluronic Acid Receptor for Endocytosis (HARE),” The Journal of Biological Chemistry, vol. 282, no. 5, pp. 2785–2797, 2007. View at Publisher · View at Google Scholar · View at Scopus
  170. E. Ruoslahti, S. N. Bhatia, and M. J. Sailor, “Targeting of drugs and nanoparticles to tumors,” The Journal of Cell Biology, vol. 188, no. 6, pp. 759–768, 2010. View at Publisher · View at Google Scholar · View at Scopus
  171. J. Lesley, V. C. Hascall, M. Tammi, and R. Hyman, “Hyaluronan binding by cell surface CD44,” Journal of Biological Chemistry, vol. 275, no. 35, pp. 26967–26975, 2000. View at Publisher · View at Google Scholar · View at Scopus
  172. Y. Luo and G. D. Prestwich, “Synthesis and selective cytotoxicity of a hyaluronic acid-antitumor bioconjugate,” Bioconjugate Chemistry, vol. 10, no. 5, pp. 755–763, 1999. View at Publisher · View at Google Scholar · View at Scopus
  173. D. Coradini, C. Pellizzaro, G. Miglierini, M. G. Daidone, and A. Perbellini, “Hyaluronic acid as drug delivery for sodium butyrate: improvement of the anti-proliferative activity on a breast-cancer cell line,” International Journal of Cancer, vol. 81, no. 3, pp. 411–416, 1999. View at Google Scholar · View at Scopus
  174. J. Gaffney, S. Matou-Nasri, M. Grau-Olivares, and M. Slevin, “Therapeutic applications of hyaluronan,” Molecular BioSystems, vol. 6, no. 3, pp. 437–443, 2010. View at Publisher · View at Google Scholar · View at Scopus
  175. V. M. Plattt and F. C. Szoka Jr., “Anticancer therapeutics: targeting macromolecules and nanocarriers to hyaluronan or CD44, a hyaluronan receptor,” Molecular Pharmaceutics, vol. 5, no. 4, pp. 474–486, 2008. View at Publisher · View at Google Scholar · View at Scopus
  176. Y. Luo, M. R. Ziebell, and G. D. Prestwich, “A hyaluronic acid—taxol antitumor bioconjugate targeted to cancer cells,” Biomacromolecules, vol. 1, no. 2, pp. 208–218, 2000. View at Publisher · View at Google Scholar · View at Scopus
  177. A. Rosato, A. Banzato, G. de Luca et al., “HYTAD1-p20: a new paclitaxel-hyaluronic acid hydrosoluble bioconjugate for treatment of superficial bladder cancer,” Urologic Oncology, vol. 24, no. 3, pp. 207–215, 2006. View at Publisher · View at Google Scholar · View at Scopus
  178. A. Serafino, M. Zonfrillo, F. Andreola et al., “CD44-targeting for antitumor drug delivery: a new SN-38-hyaluronan bioconjugate for locoregional treatment of peritoneal carcinomatosis,” Current Cancer Drug Targets, vol. 11, no. 5, pp. 572–585, 2011. View at Publisher · View at Google Scholar · View at Scopus
  179. P. F. Bassi, A. Volpe, D. D'Agostino et al., “Paclitaxel-hyaluronic acid for intravesical therapy of bacillus Calmette-Guerin refractory carcinoma in situ of the bladder: results of a phase I study,” Journal of Urology, vol. 185, no. 2, pp. 445–449, 2011. View at Publisher · View at Google Scholar · View at Scopus
  180. I. M. Montagner, A. Banzato, G. Zuccolotto et al., “Paclitaxel-hyaluronan hydrosoluble bioconjugate: mechanism of action in human bladder cancer cell lines,” Urologic Oncology, vol. 31, no. 7, pp. 1261–1269, 2013. View at Publisher · View at Google Scholar · View at Scopus
  181. Y. Luo, K. R. Kirker, and G. D. Prestwich, “Cross-linked hyaluronic acid hydrogel films: new biomaterials for drug delivery,” Journal of Controlled Release, vol. 69, no. 1, pp. 169–184, 2000. View at Publisher · View at Google Scholar · View at Scopus
  182. G. Tringali, F. Bettella, M. C. Greco, M. Campisi, D. Renier, and P. Navarra, “Pharmacokinetic profile of Oncofid-S after intraperitoneal and intravenous administration in the rat,” Journal of Pharmacy and Pharmacology, vol. 64, no. 3, pp. 360–365, 2012. View at Publisher · View at Google Scholar · View at Scopus
  183. S. M. Cohen, N. Rockefeller, R. Mukerji et al., “Efficacy and toxicity of peritumoral delivery of nanoconjugated cisplatin in an in vivo murine model of head and neck squamous cell carcinoma,” JAMA Otolaryngology: Head and Neck Surgery, vol. 139, no. 4, pp. 382–387, 2013. View at Publisher · View at Google Scholar · View at Scopus
  184. T. J. Brown, “The development of hyaluronan as a drug transporter and excipient for chemotherapeutic drugs,” Current Pharmaceutical Biotechnology, vol. 9, no. 4, pp. 253–260, 2008. View at Publisher · View at Google Scholar · View at Scopus
  185. M. A. Rosenthal, P. Gibbs, T. J. Brown et al., “Phase I and pharmacokinetic evaluation of intravenous hyaluronic acid in combination with doxorubicin or 5-fluorouracil,” Chemotherapy, vol. 51, no. 2-3, pp. 132–141, 2005. View at Publisher · View at Google Scholar · View at Scopus
  186. P. Gibbs, T. J. Brown, R. Ng et al., “A pilot human evaluation of a formulation of irinotecan and hyaluronic acid in 5-fluorouracil-refractory metastatic colorectal cancer patients,” Chemotherapy, vol. 55, no. 1, pp. 49–59, 2009. View at Publisher · View at Google Scholar · View at Scopus
  187. O. P. Varghese, W. Sun, J. Hilborn, and D. A. Ossipov, “In situ cross-linkable high molecular weight hyaluronan-bisphosphonate conjugate for localized delivery and cell-specific targeting: a hydrogel linked prodrug approach,” Journal of the American Chemical Society, vol. 131, no. 25, pp. 8781–8783, 2009. View at Publisher · View at Google Scholar · View at Scopus
  188. C. Di Meo, L. Panza, D. Capitani et al., “Hyaluronan as carrier of carboranes for tumor targeting in boron neutron capture therapy,” Biomacromolecules, vol. 8, no. 2, pp. 552–559, 2007. View at Publisher · View at Google Scholar · View at Scopus
  189. C. di Meo, L. Panza, F. Campo et al., “Novel types of carborane-carrier hyaluronan derivatives via ‘click chemistry’,” Macromolecular Bioscience, vol. 8, no. 7, pp. 670–681, 2008. View at Publisher · View at Google Scholar · View at Scopus
  190. A. Jain and S. K. Jain, “In vitro and cell uptake studies for targeting of ligand anchored nanoparticles for colon tumors,” European Journal of Pharmaceutical Sciences, vol. 35, no. 5, pp. 404–416, 2008. View at Publisher · View at Google Scholar · View at Scopus
  191. A. Jain, S. K. Jain, N. Ganesh, J. Barve, and A. M. Beg, “Design and development of ligand-appended polysaccharidic nanoparticles for the delivery of oxaliplatin in colorectal cancer,” Nanomedicine: Nanotechnology, Biology, and Medicine, vol. 6, no. 1, pp. e179–e190, 2010. View at Publisher · View at Google Scholar · View at Scopus
  192. G. Bachar, K. Cohen, R. Hod et al., “Hyaluronan-grafted particle clusters loaded with Mitomycin C as selective nanovectors for primary head and neck cancers,” Biomaterials, vol. 32, no. 21, pp. 4840–4848, 2011. View at Publisher · View at Google Scholar · View at Scopus
  193. D. Peer and R. Margalit, “Loading mitomycin C inside long circulating hyaluronan targeted nano-liposomes increases its antitumor activity in three mice tumor models,” International Journal of Cancer, vol. 108, no. 5, pp. 780–789, 2004. View at Publisher · View at Google Scholar · View at Scopus
  194. D. Peer and R. Margalit, “Tumor-targeted hyaluronan nanoliposomes increase the antitumor activity of liposomal doxorubicin in syngeneic and human xenograft mouse tumor models,” Neoplasia, vol. 6, no. 4, pp. 343–353, 2004. View at Google Scholar · View at Scopus
  195. C. Surace, S. Arpicco, A. Dufaÿ-Wojcicki et al., “Lipoplexes targeting the CD44 hyaluronic acid receptor for efficient transfection of breast cancer cells,” Molecular Pharmaceutics, vol. 6, no. 4, pp. 1062–1073, 2009. View at Publisher · View at Google Scholar · View at Scopus
  196. R. E. Eliaz and F. C. Szoka Jr., “Liposome-encapsulated doxorubicin targeted to CD44: a strategy to kill CD44-overexpressing tumor cells,” Cancer Research, vol. 61, no. 6, pp. 2592–2601, 2001. View at Google Scholar · View at Scopus
  197. D. Ruhela, K. Riviere, and F. C. Szoka Jr., “Efficient synthesis of an aldehyde functionalized hyaluronic acid and its application in the preparation of hyaluronan-lipid conjugates,” Bioconjugate Chemistry, vol. 17, no. 5, pp. 1360–1363, 2006. View at Publisher · View at Google Scholar · View at Scopus
  198. A. Dufaÿ Wojcicki, H. Hillaireau, T. L. Nascimento et al., “Hyaluronic acid-bearing lipoplexes: physico-chemical characterization and in vitro targeting of the CD44 receptor,” Journal of Controlled Release, vol. 162, no. 3, pp. 545–552, 2012. View at Publisher · View at Google Scholar · View at Scopus
  199. Y. Liu, J. Sun, W. Cao et al., “Dual targeting folate-conjugated hyaluronic acid polymeric micelles for paclitaxel delivery,” International Journal of Pharmaceutics, vol. 421, no. 1, pp. 160–169, 2011. View at Publisher · View at Google Scholar · View at Scopus
  200. L. Qiu, Z. Li, M. Qiao et al., “Self-assembled pH-responsive hyaluronic acid-g-poly(l-histidine) copolymer micelles for targeted intracellular delivery of doxorubicin,” Acta Biomaterialia, vol. 10, no. 5, pp. 2024–2035, 2014. View at Publisher · View at Google Scholar · View at Scopus
  201. Y. Zhang, H. Zhang, X. Wang, J. Wang, X. Zhang, and Q. Zhang, “The eradication of breast cancer and cancer stem cells using octreotide modified paclitaxel active targeting micelles and salinomycin passive targeting micelles,” Biomaterials, vol. 33, no. 2, pp. 679–691, 2012. View at Publisher · View at Google Scholar · View at Scopus
  202. H. Lee, H. Mok, S. Lee, Y.-K. Oh, and T. G. Park, “Target-specific intracellular delivery of siRNA using degradable hyaluronic acid nanogels,” Journal of Controlled Release, vol. 119, no. 2, pp. 245–252, 2007. View at Publisher · View at Google Scholar · View at Scopus
  203. T. Pellegrino, S. Kudera, T. Liedl, A. M. Javier, L. Manna, and W. J. Parak, “On the development of colloidal nanoparticles towards multifunctional structures and their possible use for biological applications,” Small, vol. 1, no. 1, pp. 48–63, 2005. View at Publisher · View at Google Scholar · View at Scopus
  204. R. Tenne, “Inorganic nanotubes and fullerene-like nanoparticles,” Nature Nanotechnology, vol. 1, no. 2, pp. 103–111, 2006. View at Publisher · View at Google Scholar · View at Scopus
  205. S. N. Baker and G. A. Baker, “Luminescent carbon nanodots: emergent nanolights,” Angewandte Chemie, vol. 49, no. 38, pp. 6726–6744, 2010. View at Publisher · View at Google Scholar · View at Scopus
  206. A. K. Geim, “Graphene: status and prospects,” Science, vol. 324, no. 5934, pp. 1530–1534, 2009. View at Publisher · View at Google Scholar · View at Scopus
  207. M.-Y. Lee, J.-A. Yang, H. S. Jung et al., “Hyaluronic acid-gold nanoparticle/interferon α complex for targeted treatment of hepatitis C virus infection,” ACS Nano, vol. 6, no. 11, pp. 9522–9531, 2012. View at Publisher · View at Google Scholar · View at Scopus
  208. A. Kumar, B. Sahoo, A. Montpetit, S. Behera, R. F. Lockey, and S. S. Mohapatra, “Development of hyaluronic acid-Fe2O3 hybrid magnetic nanoparticles for targeted delivery of peptides,” Nanomedicine: Nanotechnology, Biology, and Medicine, vol. 3, no. 2, pp. 132–137, 2007. View at Publisher · View at Google Scholar · View at Scopus
  209. J. Lu, M. Liong, Z. Li, J. I. Zink, and F. Tamanoi, “Biocompatibility, biodistribution, and drug-delivery efficiency of mesoporous silica nanoparticles for cancer therapy in animals,” Small, vol. 6, no. 16, pp. 1794–1805, 2010. View at Publisher · View at Google Scholar · View at Scopus
  210. H.-J. Cho, H. Y. Yoon, H. Koo et al., “Self-assembled nanoparticles based on hyaluronic acid-ceramide (HA-CE) and Pluronic for tumor-targeted delivery of docetaxel,” Biomaterials, vol. 32, no. 29, pp. 7181–7190, 2011. View at Publisher · View at Google Scholar · View at Scopus
  211. J. Lesley, N. English, C. Charles, and R. Hyman, “The role of the CD44 cytoplasmic and transmembrane domains in constitutive and inducible hyaluronan binding,” European Journal of Immunology, vol. 30, no. 1, pp. 245–253, 2000. View at Publisher · View at Google Scholar
  212. J. Lesley and R. Hyman, “CD44 can be activated to function as an hyaluronic acid receptor in normal murine T cells,” European Journal of Immunology, vol. 22, no. 10, pp. 2719–2723, 1992. View at Publisher · View at Google Scholar · View at Scopus
  213. M. Culty, H. A. Nguyen, and C. B. Underhill, “The hyaluronan receptor (CD44) participates in the uptake and degradation of hyaluronan,” The Journal of Cell Biology, vol. 116, no. 4, pp. 1055–1062, 1992. View at Publisher · View at Google Scholar · View at Scopus
  214. J. Cichy and E. Puré, “The liberation of CD44,” Journal of Cell Biology, vol. 161, no. 5, pp. 839–843, 2003. View at Publisher · View at Google Scholar · View at Scopus
  215. M. Allouche, R. S. Charrad, A. Bettaieb, C. Greenland, C. Grignon, and F. Smadja- Joffe, “Ligation of the CD44 adhesion molecule inhibits drug-induced apoptosis in human myeloid leukemia cells,” Blood, vol. 96, no. 3, pp. 1187–1190, 2000. View at Google Scholar · View at Scopus
  216. S. Legras, J.-P. Lévesque, R. Charrad et al., “CD44-mediated adhesiveness of human hematopoietic progenitors to hyaluronan is modulated by cytokines,” Blood, vol. 89, no. 6, pp. 1905–1914, 1997. View at Google Scholar · View at Scopus
  217. S. Katoh, Z. Zheng, K. Oritani, T. Shimozato, and P. W. Kincade, “Glycosylation of CD44 negatively regulates its recognition of hyaluronan,” Journal of Experimental Medicine, vol. 182, no. 2, pp. 419–429, 1995. View at Publisher · View at Google Scholar · View at Scopus
  218. Q. He, J. Lesley, R. Hyman, K. Ishihara, and P. W. Kincade, “Molecular isoforms of murine CD44 and evidence that the membrane proximal domain is not critical for hyaluronate recognition,” Journal of Cell Biology, vol. 119, no. 6, pp. 1711–1719, 1992. View at Publisher · View at Google Scholar · View at Scopus
  219. J. Sleeman, W. Rudy, M. Hofmann, J. Moll, P. Herrlich, and H. Ponta, “Regulated clustering of variant CD44 proteins increases their hyaluronate binding capacity,” Journal of Cell Biology, vol. 135, no. 4, pp. 1139–1150, 1996. View at Publisher · View at Google Scholar · View at Scopus
  220. J. P. Sleeman, S. Arming, J. F. Moll et al., “Hyaluronate-independent metastatic behavior of CD44 variant-expressing pancreatic carcinoma cells,” Cancer Research, vol. 56, no. 13, pp. 3134–3141, 1996. View at Google Scholar · View at Scopus
  221. J. P. Sleeman, K. Kondo, J. Moll, H. Ponta, and P. Herrlich, “Variant exons v6 and v7 together expand the repertoire of glycosaminoglycans bound by CD44,” The Journal of Biological Chemistry, vol. 272, no. 50, pp. 31837–31844, 1997. View at Publisher · View at Google Scholar · View at Scopus
  222. K. P. Vercruysse, G. D. Prestwich, and J.-W. Kuo, “Hyaluronate derivatives in drug delivery,” Critical Reviews in Therapeutic Drug Carrier Systems, vol. 15, no. 5, pp. 513–555, 1998. View at Google Scholar · View at Scopus
  223. S. Jaracz, J. Chen, L. V. Kuznetsova, and I. Ojima, “Recent advances in tumor-targeting anticancer drug conjugates,” Bioorganic and Medicinal Chemistry, vol. 13, no. 17, pp. 5043–5054, 2005. View at Publisher · View at Google Scholar · View at Scopus
  224. T. Pouyani and G. D. Prestwich, “Biotinylated hyaluronic acid: a new tool for probing hyaluronate-receptor interactions,” Bioconjugate Chemistry, vol. 5, no. 4, pp. 370–372, 1994. View at Publisher · View at Google Scholar · View at Scopus
  225. G. D. Prestwich, D. M. Marecak, J. F. Marecek, K. P. Vercruysse, and M. R. Ziebell, “Controlled chemical modification of hyaluronic acid: synthesis, applications, and biodegradation of hydrazide derivatives,” Journal of Controlled Release, vol. 53, no. 1–3, pp. 93–103, 1998. View at Publisher · View at Google Scholar · View at Scopus
  226. Y.-H. Liao, S. A. Jones, B. Forbes, G. P. Martin, and M. B. Brown, “Hyaluronan: pharmaceutical characterization and drug delivery,” Drug Delivery, vol. 12, no. 6, pp. 327–342, 2005. View at Publisher · View at Google Scholar · View at Scopus
  227. A. K. Yadav, P. Mishra, and G. P. Agrawal, “An insight on hyaluronic acid in drug targeting and drug delivery,” Journal of Drug Targeting, vol. 16, no. 2, pp. 91–107, 2008. View at Publisher · View at Google Scholar · View at Scopus
  228. N. Afratis, C. Gialeli, D. Nikitovic et al., “Glycosaminoglycans: key players in cancer cell biology and treatment,” FEBS Journal, vol. 279, no. 7, pp. 1177–1197, 2012. View at Publisher · View at Google Scholar · View at Scopus
  229. V. Orian-Rousseau, “CD44, a therapeutic target for metastasising tumours,” European Journal of Cancer, vol. 46, no. 7, pp. 1271–1277, 2010. View at Google Scholar · View at Scopus
  230. M. Zöller, “CD44: can a cancer-initiating cell profit from an abundantly expressed molecule?” Nature Reviews Cancer, vol. 11, no. 4, pp. 254–267, 2011. View at Publisher · View at Google Scholar · View at Scopus
  231. K.-H. Heider, H. Kuthan, G. Stehle, and G. Munzert, “CD44v6: a target for antibody-based cancer therapy,” Cancer Immunology, Immunotherapy, vol. 53, no. 7, pp. 567–579, 2004. View at Publisher · View at Google Scholar · View at Scopus
  232. J. Zeilstra, S. P. J. Joosten, H. van Andel et al., “Stem cell CD44v isoforms promote intestinal cancer formation in Apc(min) mice downstream of Wnt signaling,” Oncogene, vol. 33, no. 5, pp. 665–670, 2014. View at Publisher · View at Google Scholar · View at Scopus
  233. R. Stauder, W. Eisterer, J. Thaler, and U. Gunthert, “CD44 variant isoforms in non-Hodgkin's lymphoma: a new independent prognostic factor,” Blood, vol. 85, no. 10, pp. 2885–2899, 1995. View at Google Scholar · View at Scopus
  234. M. Todaro, M. P. Alea, A. B. di Stefano et al., “Colon cancer stem cells dictate tumor growth and resist cell death by production of interleukin-4,” Cell Stem Cell, vol. 1, no. 4, pp. 389–402, 2007. View at Publisher · View at Google Scholar · View at Scopus
  235. W. Guo and P. S. Frenette, “Alternative CD44 splicing in intestinal stem cells and tumorigenesis,” Oncogene, vol. 33, no. 5, pp. 537–538, 2014. View at Publisher · View at Google Scholar · View at Scopus
  236. C. Kainz, P. Kohlberger, G. Sliutz et al., “Splice variants of CD44 in human cervical cancer stage IB to IIB,” Gynecologic Oncology, vol. 57, no. 3, pp. 383–387, 1995. View at Publisher · View at Google Scholar · View at Scopus
  237. C. Kainz, P. Kohlberger, C. Tempfer et al., “Prognostic value of CD44 splice variants in human stage III cervical cancer,” European Journal of Cancer Part A: General Topics, vol. 31, no. 10, pp. 1706–1709, 1995. View at Publisher · View at Google Scholar · View at Scopus
  238. H.-F. Hsieh, J.-C. Yu, L.-I. Ho, S.-C. Chiu, and H.-J. Harn, “Molecular studies into the role of CD44 variants in metastasis in gastric cancer,” Journal of Clinical Pathology: Molecular Pathology, vol. 52, no. 1, pp. 25–28, 1999. View at Publisher · View at Google Scholar · View at Scopus
  239. E. Shtivelman and J. M. Bishop, “Expression of CD44 is repressed in neuroblastoma cells,” Molecular and Cellular Biology, vol. 11, no. 11, pp. 5446–5453, 1991. View at Google Scholar · View at Scopus
  240. A. M. de Marzo, C. Bradshaw, J. Sauvageot, J. I. Epstein, and G. J. Miller, “CD44 and CD44v6 downregulation in clinical prostatic carcinoma: relation to Gleason grade and cytoarchitecture,” The Prostate, vol. 34, no. 3, pp. 162–168, 1998. View at Google Scholar
  241. S. Seiter, R. Arch, S. Reber et al., “Prevention of tumor metastasis formation by anti-variant CD44,” Journal of Experimental Medicine, vol. 177, no. 2, pp. 443–455, 1993. View at Publisher · View at Google Scholar · View at Scopus
  242. D. R. Colnot, A. J. Wilhelm, J. Cloos et al., “Evaluation of limited blood sampling in a preceding 99mTc-labeled diagnostic study to predict the pharmacokinetics and myelotoxicity of 186Re-cMAb U36 radioimmunotherapy,” Journal of Nuclear Medicine, vol. 42, no. 9, pp. 1364–1367, 2001. View at Google Scholar · View at Scopus
  243. R. De Bree, J. C. Roos, J. J. Quak, W. Den Hollander, G. B. Snow, and G. A. M. S. Van Dongen, “Radioimmunoscintigraphy and biodistribution of technetium-99m-labeled monoclonal antibody U36 in patients with head and neck cancer,” Clinical Cancer Research, vol. 1, no. 6, pp. 591–598, 1995. View at Google Scholar · View at Scopus
  244. R. de Bree, J. C. Roos, J. J. Quak et al., “Biodistribution of radiolabeled monoclonal antibody E48 IgG and F(ab′)2 in patients with head and neck cancer,” Clinical Cancer Research, vol. 1, no. 3, pp. 277–286, 1995. View at Google Scholar · View at Scopus
  245. P. K. E. Börjesson, E. J. Postema, J. C. Roos et al., “Phase I therapy study with 186Re-labeled humanized monoclonal antibody BIWA 4 (Bivatuzumab) in patients with head and neck squamous cell carcinoma,” Clinical Cancer Research, vol. 9, no. 10, part 2, pp. 3961S–3972S, 2003. View at Google Scholar · View at Scopus
  246. D. R. Colnot, J. C. Roos, R. de Bree et al., “Safety, biodistribution, pharmacokinetics, and immunogenicity of 99mTc-labeled humanized monoclonal antibody BIWA 4 (bivatuzumab) in patients with squamous cell carcinoma of the head and neck,” Cancer Immunology, Immunotherapy, vol. 52, no. 9, pp. 576–582, 2003. View at Publisher · View at Google Scholar · View at Scopus
  247. B. M. Tijink, J. Buter, R. de Bree et al., “A phase I dose escalation study with anti-CD44v6 bivatuzumab mertansine in patients with incurable squamous cell carcinoma of the head and neck or esophagus,” Clinical Cancer Research, vol. 12, no. 20, part 1, pp. 6064–6072, 2006. View at Publisher · View at Google Scholar · View at Scopus
  248. H. Urakawa, Y. Nishida, W. Knudson et al., “Therapeutic potential of hyaluronan oligosaccharides for bone metastasis of breast cancer,” Journal of Orthopaedic Research, vol. 30, no. 4, pp. 662–672, 2012. View at Publisher · View at Google Scholar · View at Scopus
  249. S. Misra, S. Ghatak, A. Zoltan-Jones, and B. P. Toole, “Regulation of multidrug resistance in cancer cells by hyaluronan,” The Journal of Biological Chemistry, vol. 278, no. 28, pp. 25285–25288, 2003. View at Publisher · View at Google Scholar · View at Scopus
  250. B. St. Croix, J. W. Rak, S. Kapitain, C. Sheehan, C. H. Graham, and R. S. Kerbel, “Reversal by hyaluronidase of adhesion-dependent multicellular drug resistance in mammary carcinoma cells,” Journal of the National Cancer Institute, vol. 88, no. 18, pp. 1285–1296, 1996. View at Publisher · View at Google Scholar · View at Scopus
  251. B. St. Croix, S. Man, and R. S. Kerbel, “Reversal of intrinsic and acquired forms of drug resistance by hyaluronidase treatment of solid tumors,” Cancer Letters, vol. 131, no. 1, pp. 35–44, 1998. View at Publisher · View at Google Scholar · View at Scopus
  252. V. B. Lokeshwar, V. Estrella, L. Lopez et al., “HYAL1-v1, an alternatively spliced variant of HYAL1 hyaluronidase: a negative regulator of bladder cancer,” Cancer Research, vol. 66, no. 23, pp. 11219–11227, 2006. View at Publisher · View at Google Scholar · View at Scopus
  253. M. Kursa, G. F. Walker, V. Roessler et al., “Novel shielded transferrin-polyethylene glycol-polyethylenimine/DNA complexes for systemic tumor-targeted gene transfer,” Bioconjugate Chemistry, vol. 14, no. 1, pp. 222–231, 2003. View at Publisher · View at Google Scholar · View at Scopus
  254. N. C. Bellocq, S. H. Pun, G. S. Jensen, and M. E. Davis, “Transferrin-containing, cyclodextrin polymer-based particles for tumor-targeted gene delivery,” Bioconjugate Chemistry, vol. 14, no. 6, pp. 1122–1132, 2003. View at Publisher · View at Google Scholar · View at Scopus
  255. S. Ghatak, V. C. Hascall, F. G. Berger et al., “Tissue-Specific shRNA delivery: a novel approach for gene therapy in cancer,” Connective Tissue Research, vol. 49, no. 3-4, pp. 265–269, 2008. View at Publisher · View at Google Scholar · View at Scopus
  256. G. Song, X. Liao, L. Zhou, L. Wu, Y. Feng, and Z. C. Han, “HI44a, an anti-CD44 monoclonal antibody, induces differentiation and apoptosis of human acute myeloid leukemia cells,” Leukemia Research, vol. 28, no. 10, pp. 1089–1096, 2004. View at Publisher · View at Google Scholar · View at Scopus
  257. H. Riechelmann, A. Sauter, W. Golze et al., “Phase I trial with the CD44v6-targeting immunoconjugate bivatuzumab mertansine in head and neck squamous cell carcinoma,” Oral Oncology, vol. 44, no. 9, pp. 823–829, 2008. View at Publisher · View at Google Scholar · View at Scopus
  258. M. Koppe, F. van Schaijk, J. Roos et al., “Safety, pharmacokinetics, immunogenicity, and biodistribution of 186Re-labeled humanized monoclonal antibody BIWA 4 (Bivatuzumab) in patients with early-stage breast cancer,” Cancer Biotherapy and Radiopharmaceuticals, vol. 19, no. 6, pp. 720–729, 2004. View at Publisher · View at Google Scholar · View at Scopus
  259. B. P. Toole, S. Ghatak, and S. Misra, “Hyaluronan oligosaccharides as a potential anticancer therapeutic,” Current Pharmaceutical Biotechnology, vol. 9, no. 4, pp. 249–252, 2008. View at Publisher · View at Google Scholar · View at Scopus
  260. C. P. Paul, P. D. Good, I. Winer, and D. R. Engelke, “Effective expression of small interfering RNA in human cells,” Nature Biotechnology, vol. 20, no. 5, pp. 505–508, 2002. View at Publisher · View at Google Scholar · View at Scopus
  261. S. E. Raper, N. Chirmule, F. S. Lee et al., “Fatal systemic inflammatory response syndrome in a ornithine transcarbamylase deficient patient following adenoviral gene transfer,” Molecular Genetics and Metabolism, vol. 80, no. 1-2, pp. 148–158, 2003. View at Publisher · View at Google Scholar · View at Scopus
  262. L. E. Ailles and I. L. Weissman, “Cancer stem cells in solid tumors,” Current Opinion in Biotechnology, vol. 18, no. 5, pp. 460–466, 2007. View at Publisher · View at Google Scholar · View at Scopus
  263. N. A. Lobo, Y. Shimono, D. Qian, and M. F. Clarke, “The biology of cancer stem cells,” Annual Review of Cell and Developmental Biology, vol. 23, pp. 675–699, 2007. View at Publisher · View at Google Scholar · View at Scopus
  264. P. Dalerba, R. W. Cho, and M. F. Clarke, “Cancer stem cells: models and concepts,” Annual Review of Medicine, vol. 58, pp. 267–284, 2007. View at Publisher · View at Google Scholar · View at Scopus