두경부암에서 항체-약물 중합체
Antibody-Drug Conjugates in Head and Neck Cancer
1
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
Antibody-drug conjugates (ADCs) represent a promising therapeutic treatment for cancer patients by combining the antigen-targeting specificity of monoclonal antibodies (mAbs) with the cytotoxic potency of chemotherapeutic drugs. ADCs consist of three components, mAbs specific for ad tumor antigen, a linker species, and a cytotoxic payload. ADCs offer selective delivery of cytotoxic agents into targeted cancer cells, thereby allowing for reduced general cellular cytotoxicity caused by chemotherapeutic agents through antibody mediated specific recognition of tumor antigen. Ideally, in blood, after systemic administration, ADCs are nontoxic. Upon binding of the antibody to the targeted tumor antigen and internalization of the complex into the cancer cell, the drug is then released in its active form and in sufficient quantity to kill the cell. ADCs technology has been an active area of research in recent years, resulting in a number of ADCs in development for various tumor types. ADCs are able to be new treatment options for head and neck cancer. The number of ADCs undergoing clinical trial will further increase, possibly replacing some of the existing mAbs, and becoming the next generation of anticancer biotherapeutics. Korean J Otorhinolaryngol-Head Neck Surg 2017;60(7):331-5
Abstract
Antibody-drug conjugates (ADCs) represent a promising therapeutic treatment for cancer patients by combining the antigen-targeting specificity of monoclonal antibodies (mAbs) with the cytotoxic potency of chemotherapeutic drugs. ADCs consist of three components, mAbs specific for ad tumor antigen, a linker species, and a cytotoxic payload. ADCs offer selective delivery of cytotoxic agents into targeted cancer cells, thereby allowing for reduced general cellular cytotoxicity caused by chemotherapeutic agents through antibody mediated specific recognition of tumor antigen. Ideally, in blood, after systemic administration, ADCs are nontoxic. Upon binding of the antibody to the targeted tumor antigen and internalization of the complex into the cancer cell, the drug is then released in its active form and in sufficient quantity to kill the cell. ADCs technology has been an active area of research in recent years, resulting in a number of ADCs in development for various tumor types. ADCs are able to be new treatment options for head and neck cancer. The number of ADCs undergoing clinical trial will further increase, possibly replacing some of the existing mAbs, and becoming the next generation of anticancer biotherapeutics. Korean J Otorhinolaryngol-Head Neck Surg 2017;60(7):331-5
참고문헌 (29)
- Siegel R, "Cancer statistics, 2013", CA Cancer J Clin, 63(1), pp.11~30 (2013)
- Parslow AC, "Antibody-drug conjugates for cancer therapy", Biomedicines, 4(3), pp.E14~ (2016)
- Panowski S, "Site-specific antibody drug conjugates for cancer therapy", MAbs, 6(1), pp.34~45 (2014)
- Schwartz RS, "Paul Ehrlich’s magic bullets", N Engl J Med, 350(11), pp.1079~1080 (2004)
- Perez HL, "Antibody-drug conjugates: current status and future directions", Drug Discov Today, 19(7), pp.869~881 (2014)
- Sievers EL, "Efficacy and safety of gemtuzumab ozogamicin in patients with CD33-positive acute myeloid leukemia in first relapse", J Clin Oncol, 19(13), pp.3244~3254 (2001)
- Linenberger ML, "Multidrug-resistance phenotype and clinical responses to gemtuzumab ozogamicin", Blood, 98(4), pp.988~994 (2001)
- Younes A, "Brentuximab vedotin (SGN-35) for relapsed CD30-positive lymphomas", N Engl J Med, 363(19), pp.1812~1821 (2010)
- Senter PD, "The discovery and development of brentuximab vedotin for use in relapsed Hodgkin lymphoma and systemic anaplastic large cell lymphoma", Nat Biotechnol, 30(7), pp.631~637 (2012)
- LoRusso PM, "Trastuzumab emtansine: a unique antibody-drug conjugate in development for human epidermal growth factor receptor 2-positive cancer", Clin Cancer Res, 17(20), pp.6437~6447 (2011)
- Verma S, "Trastuzumab emtansine for HER2-positive advanced breast cancer", N Engl J Med, 367(19), pp.1783~1791 (2012)
- Mullard A, "Maturing antibody-drug conjugate pipeline hits 30", Nat Rev Drug Discov, 12(5), pp.329~332 (2013)
- Ecker DM, "The therapeutic monoclonal antibody market", MAbs, 7(1), pp.9~14 (2015)
- Ritchie M, "Implications of receptor-mediated endocytosis and intracellular trafficking dynamics in the development of antibody drug conjugates", MAbs, 5(1), pp.13~21 (2013)
- Kyoji Tsuchikama, "Antibody-drug conjugates: recent advances in conjugation and linker chemistries", Protein & Cell (2016), Springer Nature[DOI]
- Sassoon I, "Antibody-drug conjugate (ADC) clinical pipeline:a review", Methods Mol Biol, 1045, pp.1~27 (2013)
- McCombs JR, "Antibody drug conjugates: design and selection of linker, payload and conjugation chemistry", AAPS J, 17(2), pp.339~351 (2015)
- Dubowchik GM, "Cathepsin B-sensitive dipeptide prodrugs. 1. A model study of structural requirements for efficient release of doxorubicin", Bioorg Med Chem Lett, 8(23), pp.3341~3346 (1998)
- Dubowchik GM, "Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: model studies of enzymatic drug release and antigen-specific in vitro anticancer activity", Bioconjug Chem, 13(4), pp.855~869 (2002)
- Doronina SO, "Development of potent monoclonal antibody auristatin conjugates for cancer therapy", Nat Biotechnol, 21(7), pp.778~784 (2003)
- Ducry L, "Antibody-drug conjugates: linking cytotoxic payloads to monoclonal antibodies", Bioconjug Chem, 21(1), pp.5~13 (2010)
- Hamann PR, "Gemtuzumab ozogamicin, a potent and selective anti-CD33antibody-calicheamicin conjugate for treatment of acute myeloid leukemia", Bioconjug Chem, 13(1), pp.47~58 (2002)
- Sapra P, "Investigational antibody drug conjugates for solid tumors", Expert Opin Investig Drugs, 20(8), pp.1131~1149 (2011)
- Ciardiello F, "EGFR antagonists in cancer treatment", N Engl J Med, 358(11), pp.1160~1174 (2008)
- Vankemmelbeke M, "Third-generation antibody drug conjugates for cancer therapy--a balancing act", Ther Deliv, 7(3), pp.141~144 (2016)
- Gébleux R, "Antibody-drug conjugates: current status and future perspectives", Pharmacol Ther, 167, pp.48~59 (2016)
- Wheeler DL, "Mechanisms of acquired resistance to cetuximab:role of HER (ErbB) family members", Oncogene, 27(28), pp.3944~3956 (2008)
- Yonesaka K, "Activation of ERBB2 signaling causes resistance to the EGFRdirected therapeutic antibody cetuximab", Sci Transl Med, 3(99), pp.99ra86~ (2011)
- Schmitz S, "Cetuximab promotes epithelial to mesenchymal transition and cancer associated fibroblasts in patients with head and neck cancer", Oncotarget, 6(33), pp.34288~34299 (2015)