Tumor targeting of doxorubicin by anti-MT1-MMP antibody-modified PEG liposomes

International Journal of Pharmaceutics

Volumn 342, Issue 1-2, 2007, Pages 194-200

  Hatakeyama, Hiroto ^a   Akita, Hidetaka ^a   Ishida, Emi ^b   Hashimoto, Koichi ^b   Kobayashi, Hideo ^b   Aoki, Takanori ^c   Yasuda, Junko ^c   Obata, Kenichi ^c   Kikuchi, Hiroshi ^b   Ishida, Tatsuhiro ^d   Kiwada, Hiroshi ^d   Harashima, Hideyoshi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b DAIICHI SANKYO CO   (Japan)

^c Daiichi Fine Chemical Co Ltd   (Japan)

^d UNIVERSITY OF TOKUSHIMA   (Japan)

Author keywords

Cancer therapy; Drug delivery; Immunoliposomes; Matrix metalloproteinase

Indexed keywords

DOXORUBICIN; ENZYME ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOLIPOSOME; MACROGOL; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE 14 ANTIBODY; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG;

ANGIOGENESIS; ANTINEOPLASTIC ACTIVITY; ARTICLE; CONTROLLED STUDY; DRUG ACTIVITY; DRUG DELIVERY SYSTEM; IN VIVO STUDY; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; ANTIBIOTICS, ANTINEOPLASTIC; ANTIBODIES, MONOCLONAL; DOXORUBICIN; DRUG COMPOUNDING; DRUG DELIVERY SYSTEMS; EXCIPIENTS; IMMUNOCHEMISTRY; IMMUNOGLOBULIN FAB FRAGMENTS; LIPOSOMES; MALE; MATRIX METALLOPROTEINASE 14; MICE; MICE, INBRED BALB C; NEOPLASMS, EXPERIMENTAL; POLYETHYLENE GLYCOLS;

EID: 34547891537     PISSN: 03785173     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2007.04.037     Document Type: Article

References (31)

1. Aoki T., Yonezawa K., Ohuchi E., Fujimoto N., Iwata K., Shimada T., Okada Y., and Seiki M. Two-step sandwich enzyme immunoassay using monoclonal antibodies for detection of soluble and membrane-associated human membrane type 1-matrix metalloproteinase. J. Immunoassay Immunochem. 23 (2002) 49-68
2. Čeh B., Winterhalter M., Frederik P.M., Vallner J.J., and Lasic D.D. Stealth liposomes: from theory to product. Adv. Drug Del. Rev. 24 (1997) 165-177
3. Haran G., Cohen R., Bar L.K., and Barenholz Y. Transmembrane ammonium sulfate gradients in liposomes produce efficient and stable entrapment of amphipathic weak bases. Biochim. Biophys. Acta 1151 (1993) 201-215
4. Hatakeyama H., Akita H., Maruyama K., Suhara T., and Harashima H. Factors governing the in vivo tissue uptake of transferrin-coupled polyethylene glycol liposomes in vivo. Int. J. Pharm. 281 (2004) 25-33
5. Huwyler J., Wu D., and Pardridge W.M. Brain drug delivery of small molecules using immunoliposomes. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 14164-14169
6. Itoh Y., and Seiki M. MT1-MMP: an enzyme with multidimensional regulation. Trends Biochem. Sci. 29 (2004) 285-289
7. Klibanov A.L., Maruyama K., Torchilin V.P., and Hunag L. Amphipathic polyethylenglycols effectively prolong the circulation time of liposomes. FEBS Lett. 268 (1990) 235-237
8. Knauper V., Will H., Lopez-Otin C., Smith B., Atkinson S.J., Stanton H., Hembry R.M., and Murphy G. Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J. Biol. Chem. 271 (1996) 17124-17131
9. Kondo M., Asai T., Sadzuka Y., Katanasaka Y., Ogino K., Taki T., Baba K., and Oku N. Anti-neovascular therapy by liposomal drug targeted to membrane type-1 matrixmetalloproteinase. Int. J. Cancer 108 (2004) 301-306
10. Lukyanov A.N., Elbayoumi T.A., Chakilam A.R., and Torchilin V.P. Tumor-targeted liposomes: doxorubicin-loaded long-circulating liposomes modified with anti-cancer antibody. J. Control. Release 100 (2004) 135-144
11. Maeda N., Takeuchi Y., Takada M., Sadzuka Y., Namba Y., and Oku N. Anti-neovascular therapy by use of tumor neovasculature-targeted long-circulating liposomes. J. Control. Release 100 (2004) 41-52
12. Maekawa R., Maki H., Yoshida H., Hojo K., Tanaka H., Wada T., Uchida N., Takeda Y., Kasai H., Okamoto H., Tsuzuki H., Kambayashi Y., Watanabe F., Kawada K., Toda K., Ohtani M., Sugita K., and Yoshioka T. Correlation of antiangiogenic and antitumor efficacy of N-biphenyl sulfonyl-phenylalanine hydroxiamic acid (BPHA), an orally active, selective matrix metalloproteinase inhibitor. Cancer Res. 59 (1999) 1231-1235
13. Maruyama K., Takahashi N., Tagawa T., Nagaike K., and Iwatsuru M. Immunoliposomes bearing polyethyleneglycol-coupled Fab′ fragment show prolonged circulation time and high extravasation into targeted solid tumors in vivo. FEBS Lett. 413 (1997) 177-180
14. Matsumura Y., and Maeda H. A new concept for macromolecular therapeutics in cancer chemotherapy: mechanism of tumoritropic accumulation of proteins and the antitumor agent smancs. Cancer Res. 46 (1986) 6387-6392
15. Mendelsohnand J., and Baselga J. Status of epidermal growth factor receptor antagonists in the biology and treatment of cancer. J. Clin. Oncol. 21 (2003) 2787-2799
16. Nelson N.J. Inhibitors of angiogenesis enter phase III testing. J. Natl. Cancer Inst. 90 (1998) 960-963
17. Noel A., Santavicca M., Stoll I., L'Hoir C., Staub A., Murphy G., Rio M.C., and Basset P. Identification of structural determinants controlling human and mouse stromelysin-3 proteolytic activities. J. Biol. Chem. 270 (1995) 22866-22872
18. Ohuchi E., Imai K., Fujii Y., Sato H., Seiki M., and Okada Y. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272 (1997) 2446-2451
19. Pagenstecher A., Stalder A.K., Kincaid C.L., Shapiro S.D., and Campbell I.L. Differential expression of matrix metalloproteinase and tissue inhibitor of matrix metalloproteinase genes in the mouse central nervous system in normal and inflammatory states. Am. J. Pathol. 152 (1998) 729-741
20. Pardridge W.M. Intravenous, non-viral RNAi gene therapy of brain cancer. Expert Opin. Biol. Ther. 4 (2004) 1103-1113
21. Pei D., and Weiss S.J. Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J. Biol. Chem. 271 (1996) 9135-9140
22. Pei D., Majmudar G., and Weiss S.J. Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3. J. Biol. Chem. 269 (1994) 25849-25855
23. Ponkaand P., and Lok C.N. The transferrin receptor: role in health and disease. Int. J. Biochem. Cell Biol. 31 (1999) 1111-1137
24. Qian A.M., Li H., Sun H., and ho K. Targeted drug delivery via the transferrin receptor-mediated endocytosis pathway. Pharmacol. Rev. 54 (2002) 561-587
25. Sato H., Takino T., Okada Y., Cao J., Shinagawa A., Yamamoto E., and Seiki M. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370 (1994) 61-65
26. Strongin A.Y., Collier I., Bannikov G., Marmer B.L., Grant G.A., and Goldberg G.I. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270 (1995) 5331-5338
27. Uekita T., Itoh Y., Yana I., Ohno H., and Seiki M. Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity. J. Cell Biol. 155 (2001) 1345-1356
28. Voinea M., Manduteanu I., Dragomir E., Capraru M., and Simionescu M. Immunoliposomes directed toward VCAM-1 interact specifically with activated endothelial cells-a potential tool for specific drug delivery. Pharm. Res. 22 (2005) 1906-1917
29. Wang X., Ma D., Keski-Oja J., and Pei D. Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal. J. Biol. Chem. 279 (2004) 9331-9336
30. Xu L., Huang C.C., Huang W., Tang W.H., Rait A., Yin Y.Z., Cruz I., Xiang L.M., Pirollo K.F., and Chang E.H. Systemic tumor-targeted gene delivery by anti-transferrin receptor scFv-immunoliposomes. Mol. Cancer Ther. 1 (2002) 337-346
31. Zhang Y., Boado R.J., and Pardridge W.M. Marked enhancement in gene expression by targeting the human insulin receptor. J. Gene Med. 5 (2003) 157-163