메뉴 건너뛰기




Volumn 176, Issue 7, 2015, Pages 1985-1995

Production of Novel VHH Nanobody Inhibiting Angiogenesis by Targeting Binding Site of VEGF

Author keywords

Angiogenesis; Cancer; Phage display; VEGF; VHH nanobody

Indexed keywords

ANTIBODIES; BINDING ENERGY; BINS; CELL ENGINEERING; CLONING; DISEASES; ONCOLOGY; POLYMERASE CHAIN REACTION; TUMORS; UREA;

EID: 84939259648     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-015-1695-y     Document Type: Article
Times cited : (33)

References (37)
  • 1
    • 14644440555 scopus 로고    scopus 로고
    • Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis
    • COI: 1:CAS:528:DC%2BD2MXit1Gnsro%3D
    • Hicklin, D. J., & Ellis, L. M. (2005). Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis. Journal of Clinical Oncology, 23, 1011–1027.
    • (2005) Journal of Clinical Oncology , vol.23 , pp. 1011-1027
    • Hicklin, D.J.1    Ellis, L.M.2
  • 2
    • 0033513497 scopus 로고    scopus 로고
    • Targeting vascular endothelial growth factor (VEGF) for anti-tumor therapy, by anti-VEGF neutralizing monoclonal antibodies or by VEGF receptor tyrosine-kinase inhibitors
    • COI: 1:CAS:528:DC%2BD3cXksFSqsLs%3D
    • Schlaeppi, J.-M., & Wood, J. M. (1999). Targeting vascular endothelial growth factor (VEGF) for anti-tumor therapy, by anti-VEGF neutralizing monoclonal antibodies or by VEGF receptor tyrosine-kinase inhibitors. Cancer and Metastasis Reviews, 18, 473–481.
    • (1999) Cancer and Metastasis Reviews , vol.18 , pp. 473-481
    • Schlaeppi, J.-M.1    Wood, J.M.2
  • 3
    • 0036985699 scopus 로고    scopus 로고
    • Role of vascular endothelial growth factor in physiologic and pathologic angiogenesis: therapeutic implications
    • Ferrara, N. (2002). Role of vascular endothelial growth factor in physiologic and pathologic angiogenesis: therapeutic implications. Seminars in Oncology, 29, 10–14.
    • (2002) Seminars in Oncology , vol.29 , pp. 10-14
    • Ferrara, N.1
  • 4
    • 0036316846 scopus 로고    scopus 로고
    • A common polymorphism in the 5′-untranslated region of the VEGF gene is associated with diabetic retinopathy in type 2 diabetes
    • COI: 1:CAS:528:DC%2BD38XjtlGmurk%3D
    • Awata, T., Inoue, K., Kurihara, S., Ohkubo, T., Watanabe, M., Inukai, K., Inoue, I., & Katayama, S. (2002). A common polymorphism in the 5′-untranslated region of the VEGF gene is associated with diabetic retinopathy in type 2 diabetes. Diabetes, 51, 1635–1639.
    • (2002) Diabetes , vol.51 , pp. 1635-1639
    • Awata, T.1    Inoue, K.2    Kurihara, S.3    Ohkubo, T.4    Watanabe, M.5    Inukai, K.6    Inoue, I.7    Katayama, S.8
  • 5
    • 27944473690 scopus 로고    scopus 로고
    • VEGF as a key mediator of angiogenesis in cancer
    • COI: 1:CAS:528:DC%2BD2MXht1aqsrnE
    • Carmeliet, P. (2005). VEGF as a key mediator of angiogenesis in cancer. Oncology, 69, 4–10.
    • (2005) Oncology , vol.69 , pp. 4-10
    • Carmeliet, P.1
  • 6
    • 17144402207 scopus 로고    scopus 로고
    • VEGF-A induces tumor and sentinel lymph node lymphangiogenesis and promotes lymphatic metastasis
    • COI: 1:CAS:528:DC%2BD2MXjtFWls78%3D
    • Hirakawa, S., Kodama, S., Kunstfeld, R., Kajiya, K., Brown, L. F., & Detmar, M. (2005). VEGF-A induces tumor and sentinel lymph node lymphangiogenesis and promotes lymphatic metastasis. The Journal of Experimental Medicine, 201, 1089–1099.
    • (2005) The Journal of Experimental Medicine , vol.201 , pp. 1089-1099
    • Hirakawa, S.1    Kodama, S.2    Kunstfeld, R.3    Kajiya, K.4    Brown, L.F.5    Detmar, M.6
  • 7
    • 0031789314 scopus 로고    scopus 로고
    • Predictive value of vascular endothelial growth factor (VEGF) in metastasis and prognosis of human colorectal cancer
    • COI: 1:CAS:528:DyaK1cXns1Wlsb8%3D
    • Ishigami, S., Arii, S., Furutani, M., Niwano, M., Harada, T., Mizumoto, M., Mori, A., Onodera, H., & Imamura, M. (1998). Predictive value of vascular endothelial growth factor (VEGF) in metastasis and prognosis of human colorectal cancer. British Journal of Cancer, 78, 1379.
    • (1998) British Journal of Cancer , vol.78 , pp. 1379
    • Ishigami, S.1    Arii, S.2    Furutani, M.3    Niwano, M.4    Harada, T.5    Mizumoto, M.6    Mori, A.7    Onodera, H.8    Imamura, M.9
  • 8
    • 33646562554 scopus 로고    scopus 로고
    • Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin™ Fab
    • COI: 1:CAS:528:DC%2BD28XhvFOgsLo%3D
    • Fuh, G., Wu, P., Liang, W.-C., Ultsch, M., Lee, C. V., Moffat, B., & Wiesmann, C. (2006). Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin™ Fab. Journal of Biological Chemistry, 281, 6625–6631.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 6625-6631
    • Fuh, G.1    Wu, P.2    Liang, W.-C.3    Ultsch, M.4    Lee, C.V.5    Moffat, B.6    Wiesmann, C.7
  • 9
    • 84939289158 scopus 로고    scopus 로고
    • Lien, S., & Lowman, H. B. (2008). In therapeutic anti-VEGF antibodies (vol 181 p 6). Berlin Heidelberg: Springer.
    • Lien, S., & Lowman, H. B. (2008). In therapeutic anti-VEGF antibodies (vol 181 p 6). Berlin Heidelberg: Springer.
  • 12
    • 0032530717 scopus 로고    scopus 로고
    • VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 Å resolution and mutational analysis of the interface
    • COI: 1:CAS:528:DyaK1cXmsVKjt7Y%3D
    • Muller, Y. A., Chen, Y., Christinger, H. W., Li, B., Cunningham, B. C., Lowman, H. B., & de Vos, A. M. (1998). VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 Å resolution and mutational analysis of the interface. Structure, 6, 1153–1167.
    • (1998) Structure , vol.6 , pp. 1153-1167
    • Muller, Y.A.1    Chen, Y.2    Christinger, H.W.3    Li, B.4    Cunningham, B.C.5    Lowman, H.B.6    de Vos, A.M.7
  • 13
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site
    • COI: 1:CAS:528:DyaK2sXksFOiu7k%3D
    • Muller, Y. A., Li, B., Christinger, H. W., Wells, J. A., Cunningham, B. C., & De Vos, A. M. (1997). Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site. Proceedings of the National Academy of Sciences, 94, 7192–7197.
    • (1997) Proceedings of the National Academy of Sciences , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham, B.C.5    De Vos, A.M.6
  • 16
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • COI: 1:CAS:528:DC%2BD2sXhtFGgs7bO
    • Harmsen, M., & De Haard, H. (2007). Properties, production, and applications of camelid single-domain antibody fragments. Applied Microbiology and Biotechnology, 77, 13–22.
    • (2007) Applied Microbiology and Biotechnology , vol.77 , pp. 13-22
    • Harmsen, M.1    De Haard, H.2
  • 18
    • 84904004062 scopus 로고    scopus 로고
    • Bacteriophage vehicles for phage display: biology, mechanism, and application
    • COI: 1:CAS:528:DC%2BC2cXksFyrtL0%3D
    • Ebrahimizadeh, W., & Rajabibazl, M. (2014). Bacteriophage vehicles for phage display: biology, mechanism, and application. Current Microbiology, 69, 109–120.
    • (2014) Current Microbiology , vol.69 , pp. 109-120
    • Ebrahimizadeh, W.1    Rajabibazl, M.2
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • COI: 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 84877784402 scopus 로고    scopus 로고
    • Isolation and characterization of protective anti-LPS nanobody against V. cholerae O1 recognizing Inaba and Ogawa serotypes
    • COI: 1:CAS:528:DC%2BC3sXntFyrtbc%3D
    • Ebrahimizadeh, W., Gargari, S. M., Rajabibazl, M., Ardekani, L. S., Zare, H., & Bakherad, H. (2013). Isolation and characterization of protective anti-LPS nanobody against V. cholerae O1 recognizing Inaba and Ogawa serotypes. Applied Microbiology and Biotechnology, 97, 4457–4466.
    • (2013) Applied Microbiology and Biotechnology , vol.97 , pp. 4457-4466
    • Ebrahimizadeh, W.1    Gargari, S.M.2    Rajabibazl, M.3    Ardekani, L.S.4    Zare, H.5    Bakherad, H.6
  • 23
    • 84891640552 scopus 로고    scopus 로고
    • A novel VHH nanobody against the active site (the CA domain) of tumor-associated, carbonic anhydrase isoform IX and its usefulness for cancer diagnosis
    • COI: 1:CAS:528:DC%2BC3sXhsFaqtb%2FF
    • Araste, F., Ebrahimizadeh, W., Rasooli, I., Rajabibazl, M., & Gargari, S. L. M. (2014). A novel VHH nanobody against the active site (the CA domain) of tumor-associated, carbonic anhydrase isoform IX and its usefulness for cancer diagnosis. Biotechnology Letters, 36, 21–28.
    • (2014) Biotechnology Letters , vol.36 , pp. 21-28
    • Araste, F.1    Ebrahimizadeh, W.2    Rasooli, I.3    Rajabibazl, M.4    Gargari, S.L.M.5
  • 24
    • 0023258208 scopus 로고
    • Measurement of monoclonal antibody affinity by non-competitive enzyme immunoassay
    • COI: 1:STN:280:DyaL2s3lt1aruw%3D%3D
    • Beatty, J. D., Beatty, B. G., & Vlahos, W. G. (1987). Measurement of monoclonal antibody affinity by non-competitive enzyme immunoassay. Journal of Immunological Methods, 100, 173–179.
    • (1987) Journal of Immunological Methods , vol.100 , pp. 173-179
    • Beatty, J.D.1    Beatty, B.G.2    Vlahos, W.G.3
  • 25
    • 78149343713 scopus 로고    scopus 로고
    • Nanobodies—from llamas to therapeutic proteins
    • COI: 1:CAS:528:DC%2BC3MXhsVegsb0%3D
    • Kolkman, J. A., & Law, D. A. (2010). Nanobodies—from llamas to therapeutic proteins. Drug Discov Today Tech., 7, e139–e146.
    • (2010) Drug Discov Today Tech. , vol.7 , pp. 139-146
    • Kolkman, J.A.1    Law, D.A.2
  • 26
    • 20544455330 scopus 로고    scopus 로고
    • Bevacizumab (Avastin), a humanized anti-VEGF monoclonal antibody for cancer therapy
    • COI: 1:CAS:528:DC%2BD2MXlsVChtLs%3D
    • Ferrara, N., Hillan, K. J., & Novotny, W. (2005). Bevacizumab (Avastin), a humanized anti-VEGF monoclonal antibody for cancer therapy. Biochemical and Biophysical Research Communications, 333, 328–335.
    • (2005) Biochemical and Biophysical Research Communications , vol.333 , pp. 328-335
    • Ferrara, N.1    Hillan, K.J.2    Novotny, W.3
  • 27
    • 0034087691 scopus 로고    scopus 로고
    • Continuous low-dose therapy with vinblastine and VEGF receptor-2 antibody induces sustained tumor regression without overt toxicity
    • COI: 1:CAS:528:DC%2BD3cXisFOlurc%3D
    • Klement, G., Baruchel, S., Rak, J., Man, S., Clark, K., Hicklin, D. J., Bohlen, P., & Kerbel, R. S. (2000). Continuous low-dose therapy with vinblastine and VEGF receptor-2 antibody induces sustained tumor regression without overt toxicity. Journal of Clinical Investigation, 105, R15.
    • (2000) Journal of Clinical Investigation , vol.105 , pp. 15
    • Klement, G.1    Baruchel, S.2    Rak, J.3    Man, S.4    Clark, K.5    Hicklin, D.J.6    Bohlen, P.7    Kerbel, R.S.8
  • 28
    • 0036984640 scopus 로고    scopus 로고
    • Role of angiogenesis in tumor growth and metastasis
    • COI: 1:CAS:528:DC%2BD3sXlvFSqtg%3D%3D
    • Folkman, J. (2002). Role of angiogenesis in tumor growth and metastasis. Seminar in Oncology, 29, 15–18.
    • (2002) Seminar in Oncology , vol.29 , pp. 15-18
    • Folkman, J.1
  • 29
    • 34249689557 scopus 로고    scopus 로고
    • VEGF-targeted cancer therapy strategies: current progress, hurdles and future prospects
    • COI: 1:CAS:528:DC%2BD2sXmtVGgtLY%3D
    • Duda, D. G., Batchelor, T. T., Willett, C. G., & Jain, R. K. (2007). VEGF-targeted cancer therapy strategies: current progress, hurdles and future prospects. Trends in Molecular Medicine, 13, 223–230.
    • (2007) Trends in Molecular Medicine , vol.13 , pp. 223-230
    • Duda, D.G.1    Batchelor, T.T.2    Willett, C.G.3    Jain, R.K.4
  • 30
    • 84859575611 scopus 로고    scopus 로고
    • Anti-angiogenesis therapy in cancer: current challenges and future perspectives
    • COI: 1:CAS:528:DC%2BC38XltVamtLY%3D
    • Shojaei, F. (2012). Anti-angiogenesis therapy in cancer: current challenges and future perspectives. Cancer Letters, 320, 130–137.
    • (2012) Cancer Letters , vol.320 , pp. 130-137
    • Shojaei, F.1
  • 31
    • 80052047659 scopus 로고    scopus 로고
    • Recent advances in anti-angiogenic therapy of cancer
    • Samant, R. S., & Shevde, L. A. (2011). Recent advances in anti-angiogenic therapy of cancer. Oncotarget, 2, 122.
    • (2011) Oncotarget , vol.2 , pp. 122
    • Samant, R.S.1    Shevde, L.A.2
  • 32
    • 55649103188 scopus 로고    scopus 로고
    • Sequential use of the tyrosine kinase inhibitors sorafenib and sunitinib in metastatic renal cell carcinoma: a retrospective outcome analysis
    • COI: 1:CAS:528:DC%2BD1MXps1Cltw%3D%3D
    • Eichelberg, C., Heuer, R., Chun, F. K., Hinrichs, K., Zacharias, M., Huland, H., & Heinzer, H. (2008). Sequential use of the tyrosine kinase inhibitors sorafenib and sunitinib in metastatic renal cell carcinoma: a retrospective outcome analysis. European Urology, 54, 1373–1378.
    • (2008) European Urology , vol.54 , pp. 1373-1378
    • Eichelberg, C.1    Heuer, R.2    Chun, F.K.3    Hinrichs, K.4    Zacharias, M.5    Huland, H.6    Heinzer, H.7
  • 33
    • 33749505836 scopus 로고    scopus 로고
    • Efficacy and safety of sunitinib in patients with advanced gastrointestinal stromal tumour after failure of imatinib: a randomised controlled trial
    • COI: 1:CAS:528:DC%2BD28XhtVOrtL%2FL
    • Demetri, G. D., van Oosterom, A. T., Garrett, C. R., Blackstein, M. E., Shah, M. H., Verweij, J., McArthur, G., Judson, I. R., Heinrich, M. C., & Morgan, J. A. (2006). Efficacy and safety of sunitinib in patients with advanced gastrointestinal stromal tumour after failure of imatinib: a randomised controlled trial. The Lancet, 368, 1329–1338.
    • (2006) The Lancet , vol.368 , pp. 1329-1338
    • Demetri, G.D.1    van Oosterom, A.T.2    Garrett, C.R.3    Blackstein, M.E.4    Shah, M.H.5    Verweij, J.6    McArthur, G.7    Judson, I.R.8    Heinrich, M.C.9    Morgan, J.A.10
  • 34
    • 47949089077 scopus 로고    scopus 로고
    • VEGF-targeted therapy: mechanisms of anti-tumour activity
    • COI: 1:CAS:528:DC%2BD1cXovV2lsro%3D
    • Ellis, L. M., & Hicklin, D. J. (2008). VEGF-targeted therapy: mechanisms of anti-tumour activity. Nature Reviews Cancer, 8, 579–591.
    • (2008) Nature Reviews Cancer , vol.8 , pp. 579-591
    • Ellis, L.M.1    Hicklin, D.J.2
  • 35
    • 78249286217 scopus 로고    scopus 로고
    • Cancer metabolism: the Warburg effect today
    • COI: 1:CAS:528:DC%2BC3cXhsVans7vL
    • Ferreira, L. M. R. (2010). Cancer metabolism: the Warburg effect today. Experimental and Molecular Pathology, 89, 372–380.
    • (2010) Experimental and Molecular Pathology , vol.89 , pp. 372-380
    • Ferreira, L.M.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.