메뉴 건너뛰기




Volumn 92, Issue 11, 2010, Pages 1618-1624

Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model

Author keywords

Cancer; Cysteine cathepsin; Protease; Therapy

Indexed keywords

ANTINEOPLASTIC AGENT; CATHEPSIN B; CATHEPSIN L; CATHEPSIN S; CATHEPSIN V; CYSTEINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG; VBY 825;

EID: 78149358974     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.04.023     Document Type: Article
Times cited : (51)

References (48)
  • 1
    • 70350233406 scopus 로고    scopus 로고
    • Navigating ECM barriers at the invasive front: the cancer cell-stroma interface
    • Rowe R.G., Weiss S.J. Navigating ECM barriers at the invasive front: the cancer cell-stroma interface. Annu. Rev. Cell Dev. Biol. 2009, 25:567-595.
    • (2009) Annu. Rev. Cell Dev. Biol. , vol.25 , pp. 567-595
    • Rowe, R.G.1    Weiss, S.J.2
  • 2
    • 78149361375 scopus 로고    scopus 로고
    • Proteolytic Cascades in Invasion and Metastasis, Cancer Metastasis: Biologic Basis and Therapeutics. Cambridge University Press. Welsh DR, Lyden DC, Psaila B (Eds.), in press.
    • S.D. Mason, J.A. Joyce, Proteolytic Cascades in Invasion and Metastasis, Cancer Metastasis: Biologic Basis and Therapeutics. Cambridge University Press. Welsh DR, Lyden DC, Psaila B (Eds.), in press.
    • Mason, S.D.1    Joyce, J.A.2
  • 3
    • 33644545381 scopus 로고    scopus 로고
    • Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • Overall C.M., Kleifeld O. Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat. Rev. Cancer 2006, 6:227-239.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 4
    • 37549070672 scopus 로고    scopus 로고
    • Cysteine cathepsin proteases as pharmacological targets in cancer
    • Palermo C., Joyce J.A. Cysteine cathepsin proteases as pharmacological targets in cancer. Trends Pharmacol. Sci. 2008, 29:22-28.
    • (2008) Trends Pharmacol. Sci. , vol.29 , pp. 22-28
    • Palermo, C.1    Joyce, J.A.2
  • 5
  • 6
    • 33947604810 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • Vasiljeva O., Reinheckel T., Peters C., Turk D., Turk V., Turk B. Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des. 2007, 13:385-401.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 385-401
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 7
    • 10044296973 scopus 로고    scopus 로고
    • Cysteine cathepsins in human cancer
    • Jedeszko C., Sloane B.F. Cysteine cathepsins in human cancer. Biol. Chem. 2004, 385:1017-1027.
    • (2004) Biol. Chem. , vol.385 , pp. 1017-1027
    • Jedeszko, C.1    Sloane, B.F.2
  • 11
    • 34547640302 scopus 로고    scopus 로고
    • Inhibition of cysteine cathepsin protease activity enhances chemotherapy regimens by decreasing tumor growth and invasiveness in a mouse model of multistage cancer
    • Bell-McGuinn K.M., Garfall A.L., Bogyo M., Hanahan D., Joyce J.A. Inhibition of cysteine cathepsin protease activity enhances chemotherapy regimens by decreasing tumor growth and invasiveness in a mouse model of multistage cancer. Cancer Res. 2007, 67:7378-7385.
    • (2007) Cancer Res. , vol.67 , pp. 7378-7385
    • Bell-McGuinn, K.M.1    Garfall, A.L.2    Bogyo, M.3    Hanahan, D.4    Joyce, J.A.5
  • 13
    • 78149358666 scopus 로고    scopus 로고
    • Deletion of cathepsin H perturbs angiogenic switching, vascularization and the growth of tumors in a mouse model of pancreatic islet cancer, Biol. Chem., in press.
    • V. Gocheva, X. Chen, C. Peters, T. Reinheckel, J.A. Joyce, Deletion of cathepsin H perturbs angiogenic switching, vascularization and the growth of tumors in a mouse model of pancreatic islet cancer, Biol. Chem., in press.
    • Gocheva, V.1    Chen, X.2    Peters, C.3    Reinheckel, T.4    Joyce, J.A.5
  • 16
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: multifunctional enzymes in cancer
    • Mohamed M.M., Sloane B.F. Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 2006, 6:764-775.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 17
    • 77955950794 scopus 로고    scopus 로고
    • Roles of cysteine proteases in tumor progression: analysis of cysteine cathepsin knockout mice in cancer models
    • Springer Publishing, D.R. Edwards, G. Hoer-Hansen, F. Blasi, B.F. Sloane (Eds.)
    • Reinheckel T., Gocheva V., Peters C., Joyce J.A. Roles of cysteine proteases in tumor progression: analysis of cysteine cathepsin knockout mice in cancer models. The Cancer Degradome- Proteases and Cancer Biology 2008, 279-302. Springer Publishing. D.R. Edwards, G. Hoer-Hansen, F. Blasi, B.F. Sloane (Eds.).
    • (2008) The Cancer Degradome- Proteases and Cancer Biology , pp. 279-302
    • Reinheckel, T.1    Gocheva, V.2    Peters, C.3    Joyce, J.A.4
  • 18
    • 18944365919 scopus 로고    scopus 로고
    • The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics
    • Yasuda Y., Kaleta J., Bromme D. The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics. Adv. Drug Deliv. Rev. 2005, 57:973-993.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 973-993
    • Yasuda, Y.1    Kaleta, J.2    Bromme, D.3
  • 19
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: successes, failures and future prospects
    • Turk B. Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug Discov. 2006, 5:785-799.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 20
    • 77949483288 scopus 로고    scopus 로고
    • Development of nitrile-based peptidic inhibitors of cysteine cathepsins
    • Frizler M., Stirnberg M., Sisay M.T., Gutschow M. Development of nitrile-based peptidic inhibitors of cysteine cathepsins. Curr. Top. Med. Chem. 2010, 10:294-322.
    • (2010) Curr. Top. Med. Chem. , vol.10 , pp. 294-322
    • Frizler, M.1    Stirnberg, M.2    Sisay, M.T.3    Gutschow, M.4
  • 21
    • 0029744988 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors
    • Meara J.P., Rich D.H. Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors. J. Med. Chem. 1996, 39:3357-3366.
    • (1996) J. Med. Chem. , vol.39 , pp. 3357-3366
    • Meara, J.P.1    Rich, D.H.2
  • 22
    • 0030966971 scopus 로고    scopus 로고
    • Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64
    • Navab R., Mort J.S., Brodt P. Inhibition of carcinoma cell invasion and liver metastases formation by the cysteine proteinase inhibitor E-64. Clin. Exp. Metastasis. 1997, 15:121-129.
    • (1997) Clin. Exp. Metastasis. , vol.15 , pp. 121-129
    • Navab, R.1    Mort, J.S.2    Brodt, P.3
  • 23
    • 34248549740 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of in vivo potency and selectivity of epoxysuccinyl-based inhibitors of papain-family cysteine proteases
    • Sadaghiani A.M., Verhelst S.H., Gocheva V., Hill K., Majerova E., Stinson S., Joyce J.A., Bogyo M. Design, synthesis, and evaluation of in vivo potency and selectivity of epoxysuccinyl-based inhibitors of papain-family cysteine proteases. Chem. Biol. 2007, 14:499-511.
    • (2007) Chem. Biol. , vol.14 , pp. 499-511
    • Sadaghiani, A.M.1    Verhelst, S.H.2    Gocheva, V.3    Hill, K.4    Majerova, E.5    Stinson, S.6    Joyce, J.A.7    Bogyo, M.8
  • 27
    • 0021888904 scopus 로고
    • Heritable formation of pancreatic beta-cell tumours in transgenic mice expressing recombinant insulin/simian virus 40 oncogenes
    • Hanahan D. Heritable formation of pancreatic beta-cell tumours in transgenic mice expressing recombinant insulin/simian virus 40 oncogenes. Nature 1985, 315:115-122.
    • (1985) Nature , vol.315 , pp. 115-122
    • Hanahan, D.1
  • 28
    • 0036559535 scopus 로고    scopus 로고
    • Elevated levels of IGF-1 receptor convey invasive and metastatic capability in a mouse model of pancreatic islet tumorigenesis
    • Lopez T., Hanahan D. Elevated levels of IGF-1 receptor convey invasive and metastatic capability in a mouse model of pancreatic islet tumorigenesis. Cancer Cell 2002, 1:339-353.
    • (2002) Cancer Cell , vol.1 , pp. 339-353
    • Lopez, T.1    Hanahan, D.2
  • 29
    • 0036491615 scopus 로고    scopus 로고
    • VEGF-A has a critical, nonredundant role in angiogenic switching and pancreatic beta cell carcinogenesis
    • Inoue M., Hager J.H., Ferrara N., Gerber H.P., Hanahan D. VEGF-A has a critical, nonredundant role in angiogenic switching and pancreatic beta cell carcinogenesis. Cancer Cell 2002, 1:193-202.
    • (2002) Cancer Cell , vol.1 , pp. 193-202
    • Inoue, M.1    Hager, J.H.2    Ferrara, N.3    Gerber, H.P.4    Hanahan, D.5
  • 30
    • 0001306637 scopus 로고
    • Regression models for ordinal data
    • Cullagh Mc Regression models for ordinal data. J.R. Statist. Soc. 1980, 109-142.
    • (1980) J.R. Statist. Soc. , pp. 109-142
    • Cullagh, M.1
  • 36
    • 76149146398 scopus 로고    scopus 로고
    • IL-4 induces cathepsin protease activity in tumor-associated macrophages to promote cancer growth and invasion
    • Gocheva V., Wang H.W., Gadea B.B., Shree T., Hunter K.E., Garfall A.L., Berman T., Joyce J.A. IL-4 induces cathepsin protease activity in tumor-associated macrophages to promote cancer growth and invasion. Genes Dev. 2010, 24:241-255.
    • (2010) Genes Dev. , vol.24 , pp. 241-255
    • Gocheva, V.1    Wang, H.W.2    Gadea, B.B.3    Shree, T.4    Hunter, K.E.5    Garfall, A.L.6    Berman, T.7    Joyce, J.A.8
  • 38
    • 66249098899 scopus 로고    scopus 로고
    • VEGF-A induces angiogenesis by perturbing the cathepsin-cysteine protease inhibitor balance in venules, causing basement membrane degradation and mother vessel formation
    • Chang S.H., Kanasaki K., Gocheva V., Blum G., Harper J., Moses M.A., Shih S.C., Nagy J.A., Joyce J., Bogyo M., Kalluri R., Dvorak H.F. VEGF-A induces angiogenesis by perturbing the cathepsin-cysteine protease inhibitor balance in venules, causing basement membrane degradation and mother vessel formation. Cancer Res. 2009, 69:4537-4544.
    • (2009) Cancer Res. , vol.69 , pp. 4537-4544
    • Chang, S.H.1    Kanasaki, K.2    Gocheva, V.3    Blum, G.4    Harper, J.5    Moses, M.A.6    Shih, S.C.7    Nagy, J.A.8    Joyce, J.9    Bogyo, M.10    Kalluri, R.11    Dvorak, H.F.12
  • 40
    • 1642535587 scopus 로고    scopus 로고
    • Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment
    • Rousselet N., Mills L., Jean D., Tellez C., Bar-Eli M., Frade R. Inhibition of tumorigenicity and metastasis of human melanoma cells by anti-cathepsin L single chain variable fragment. Cancer Res. 2004, 64:146-151.
    • (2004) Cancer Res. , vol.64 , pp. 146-151
    • Rousselet, N.1    Mills, L.2    Jean, D.3    Tellez, C.4    Bar-Eli, M.5    Frade, R.6
  • 41
  • 42
    • 41649103656 scopus 로고    scopus 로고
    • Recombinant cathepsin S propeptide attenuates cell invasion by inhibition of cathepsin L-like proteases in tumor microenvironment
    • Burden R.E., Snoddy P., Buick R.J., Johnston J.A., Walker B., Scott C.J. Recombinant cathepsin S propeptide attenuates cell invasion by inhibition of cathepsin L-like proteases in tumor microenvironment. Mol. Cancer Ther. 2008, 7:538-547.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 538-547
    • Burden, R.E.1    Snoddy, P.2    Buick, R.J.3    Johnston, J.A.4    Walker, B.5    Scott, C.J.6
  • 44
    • 78149362328 scopus 로고    scopus 로고
    • Biologic protease inhibitors as novel therapeutic agents, Biochimie, in press.
    • C.J. Scott, C.C. Taggart, Biologic protease inhibitors as novel therapeutic agents, Biochimie, in press.
    • Scott, C.J.1    Taggart, C.C.2
  • 47
    • 71249111374 scopus 로고    scopus 로고
    • Odanacatib, a cathepsin K inhibitor for the treatment of osteoporosis and other skeletal disorders associated with excessive bone remodeling
    • Lewiecki E.M. Odanacatib, a cathepsin K inhibitor for the treatment of osteoporosis and other skeletal disorders associated with excessive bone remodeling. IDrugs 2009, 12:799-809.
    • (2009) IDrugs , vol.12 , pp. 799-809
    • Lewiecki, E.M.1
  • 48
    • 67649628133 scopus 로고    scopus 로고
    • Cathepsin K inhibitors for osteoporosis and potential off-target effects
    • Bromme D., Lecaille F. Cathepsin K inhibitors for osteoporosis and potential off-target effects. Expert Opin. Investig. Drugs 2009, 18:585-600.
    • (2009) Expert Opin. Investig. Drugs , vol.18 , pp. 585-600
    • Bromme, D.1    Lecaille, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.