Shiravand, Y. et al. Immune checkpoint inhibitors in cancer therapy. Front. Oncol. 12, 1234–1245 (2022).
Scott, L. J. Brentuximab vedotin: A review in CD30-positive hodgkin lymphoma. Drugs 77, 435–445 (2017).
Ramos, C. A., Heslop, H. E. & Brenner, M. K. CAR-T cell therapy for lymphoma. Annu. Rev. Med. 67, 165–183 (2016).
Pasqui, D. M., Latorraca, C. D. O. C., Pacheco, R. L. & Riera, R. CAR-T cell therapy for patients with hematological malignancies. A systematic review. Eur. J. Haematol. 109, 601–618 (2022).
Batlevi, C. L., Matsuki, E., Brentjens, R. J. & Younes, A. Novel immunotherapies in lymphoid malignancies. Nat. Rev. Clin. Oncol. 13, 25–40 (2016).
Coiffier, B. et al. CHOP chemotherapy plus rituximab compared with CHOP alone in elderly patients with diffuse large-B-cell lymphoma. N. Engl. J. Med. 346, 235–242 (2002).
Ishida, T. & Ueda, R. Antibody therapy for adult T-cell leukemia-lymphoma. Int. J. Hematol. 94, 443–452 (2011).
Kesavan, M., Eyre, T. A. & Collins, G. P. Front-line treatment of high grade B cell non-Hodgkin lymphoma. Curr. Hematol. Malig. Rep. 14, 207–218 (2019).
Niitsu, N. Current treatment strategy of diffuse large B-cell lymphomas. Int. J. Hematol. 92, 231–237 (2010).
Tobinai, K., Klein, C., Oya, N. & Fingerle-Rowson, G. A review of obinutuzumab (GA101), a novel type II anti-CD20 monoclonal antibody, for the treatment of patients with B-cell malignancies. Adv. Ther. 34, 324–356 (2017).
Ishitsuka, K. et al. Safety and effectiveness of Mogamulizumab in relapsed or refractory adult T-cell leukemia-lymphoma. Eur. J. Haematol. 102, 407–415 (2019).
Zhang, T. et al. Safety and efficacy profile of Mogamulizumab (Poteligeo) in the treatment of cancers: An update evidence from 14 studies. BMC Cancer 21, 618 (2021).
Campbell, P. & Marcus, R. Monoclonal antibody therapy for lymphoma. Blood Rev. 17, 143–152 (2003).
Tse, E. & Kwong, Y. L. How I treat NK/T-cell lymphomas. Blood 121, 4997–5005 (2013).
Kwong, Y. L. Natural killer-cell malignancies: Diagnosis and treatment. Leukemia 19, 2186–2194 (2005).
Sánchez-Romero, C. et al. Extranodal NK/T cell lymphoma, nasal type: An updated overview. J. Hematol. Oncol. 15, 345–352 (2022).
Oshimi, K. Progress in understanding and managing natural killer-cell malignancies. Br. J. Haematol. 139, 532–544 (2007).
Qi, S. N. et al. First-line non-anthracycline-based chemotherapy for extranodal nasal-type NK/T-cell lymphoma: A retrospective analysis from the CLCG. Blood Adv. 4, 3141–3153 (2020).
Yamaguchi, M. et al. Phase II study of SMILE chemotherapy for newly diagnosed stage IV, relapsed, or refractory extranodal natural killer (NK)/T-cell lymphoma, nasal type: The NK-Cell tumor study group study. J. Clin. Oncol. 29, 4410–4416 (2011).
Kwong, Y. L. et al. SMILE for natural killer/T-cell lymphoma: Analysis of safety and efficacy from the Asia lymphoma study group. Blood 120, 2973–2980 (2012).
Li, X. et al. DDGP versus SMILE in newly diagnosed advanced natural killer/t-cell lymphoma: A randomized controlled, multicenter, open-label study in China. Clin. Cancer Res. 22, 5223–5228 (2016).
Yi, W. et al. New approaches for treatment of advanced extranodal NK/T-cell lymphoma. Cancer Manag. Res. 14, 401–407 (2022).
Kwong, Y. L. et al. PD1 Blockade with pembrolizumab is highly effective in relapsed or refractory NK/T-cell lymphoma failing l-asparaginase. Blood 129, 2437–2442 (2017).
Golay, J. & Taylor, R. P. The role of complement in the mechanism of action of therapeutic anti-cancer mAbs. Antibodies 9, 58 (2020).
Fernández-Marrero, Y. & López-Requena, A. Lonely killers: Effector cell- and complement-independent non-proapoptotic cytotoxic antibodies inducing membrane lesions. mAbs 3, 528–534 (2011).
Honeychurch, J. et al. Antibody-induced nonapoptotic cell death in human lymphoma and leukemia cells is mediated through a novel reactive oxygen species-dependent pathway. Blood 119, 3523–3533 (2012).
Ivanov, A. et al. Monoclonal antibodies directed to CD20 and HLA-DR can elicit homotypic adhesion followed by lysosome-mediated cell death in human lymphoma and leukemia cells. J. Clin. Invest. 119, 2143–2159 (2009).
Matsuoka, S. et al. Establishment of a therapeutic anti-pan HLA-class II monoclonal antibody that directly induces lymphoma cell death via large pore formation. PLOS ONE 11, e0150496 (2016).
Matsuoka, S. et al. A novel type of cell death of lymphocytes induced by a monoclonal antibody without participation of complement. J. Exp. Med. 181, 2007–2015 (1995).
Matsuoka, S. et al. A monoclonal antibody to the alpha2 domain of murine major histocompatibility complex class I that specifically kills activated lymphocytes and blocks liver damage in the Concanavalin A hepatitis model. J. Exp. Med. 198, 497–503 (2003).
Constantinides, M. et al. Direct cell death induced by CD20 monoclonal antibodies on B cell lymphoma cells revealed by new protocols of analysis. Cancers 15, 1109 (2023).
Khoy, K., Mariotte, D., Defer, G., Petit, G., Toutirais, O. & Le Mauff, B. Natalizumab in multiple sclerosis treatment: From biological effects to immune monitoring. Front. Immunol. 11, 549842 (2020).
Shimizu, T. & Pommier, Y. Camptothecin-induced apoptosis in p53-null human leukemia HL60 cells and their isolated nuclei: Effects of the protease inhibitors Z-VAD-fmk and dichloroisocoumarin suggest an involvement of both caspases and Serine proteases. Leukemia 11, 1238–1244 (1997).
Brockhaus, F. & Brüne, B. U937 apoptotic cell death by nitric oxide: Bcl-2 downregulation and caspase activation. Exp. Cell. Res. 238, 33–41 (1998).
Nyiramana, M. M. et al. Sea hare hydrolysate-induced reduction of human non-small cell lung cancer cell growth through regulation of macrophage polarization and non-apoptotic regulated cell death pathways. Cancers 12, 726 (2020).
Skov, S., Klausen, P. & Claesson, M. H. Ligation of major histocompatability complex (MHC) class I molecules on human T cells induces cell death through PI-3 kinase-induced c-Jun NH2-terminal kinase activity: a novel apoptotic pathway distinct from Fas-induced apoptosis. J. Cell. Biol. 139, 1523–1531 (1997).
Curnock, A. P. & Knox, K. A. LY294002-mediated Inhibition of phosphatidylinositol 3-kinase activity triggers growth Inhibition and apoptosis in CD40-triggered Ramos-Burkitt lymphoma B cells. Cell. Immunol. 187, 77–87 (1998).
Wu, Y. W. & Waldmann, H. Toward the role of cholesterol and cholesterol transfer protein in autophagosome biogenesis. Autophagy 15, 2167–2168 (2019).
Xie, T. et al. Structural basis of RIP1 Inhibition by Necrostatins. Structure 21, 493–499 (2013).
Sodeoka, M. & Dodo, K. Development of selective inhibitors of necrosis. Chem. Rec. 10, 308–314 (2010).
Bellosillo, B. et al. Complement-mediated cell death induced by rituximab in B-cell lymphoproliferative disorders is mediated in vitro by a caspase-independent mechanism involving the generation of reactive oxygen species. Blood 98, 2771–2777 (2001).
MacLean-Fletcher, S. & Pollard, T. D. Mechanism of action of cytochalasin B on actin. Cell 20, 329–341 (1980).
Wakatsuki, T., Schwab, B., Thompson, N. C. & Elson, E. L. Effects of cytochalasin D and latrunculin B on mechanical properties of cells. J. Cell. Sci. 114, 1025–1036 (2001).
Spector, I., Shochet, N. R., Kashman, Y. & Groweiss, A. Latrunculins: Novel marine toxins that disrupt microfilament organization in cultured cells. Science 219, 493–495 (1983).
Kong, D., Yamazaki, K. & Yamori, T. Discovery of phosphatidylinositol 3-kinase inhibitory compounds from the screening committee of anticancer drugs (SCADS) library. Biol. Pharm. Bull. 33, 1600–1604 (2010).
Knecht, D. A. et al. Cucurbitacin I inhibits cell motility by indirectly interfering with actin dynamics. PLOS ONE 5, e14039 (2010).
Kawada, M., Amemiya, M., Ishizuka, M. & Takeuchi, T. Cytostatin, an inhibitor of cell adhesion to extracellular matrix, selectively inhibits protein phosphatase 2A. Biochim. Biophys. Acta 1452, 209–217 (1999).
Ho, W. S. et al. LB-100, a novel protein phosphatase 2A (PP2A) inhibitor, sensitizes malignant meningioma cells to the therapeutic effects of radiation. Cancer Lett. 415, 217–226 (2018).
Teo, E. C., Chew, Y. & Phipps, C. A review of monoclonal antibody therapies in lymphoma. Crit. Rev. Oncol. Hematol. 97, 72–84 (2016).
Majeti, R. Monoclonal antibody therapy directed against human acute myeloid leukemia stem cells. Oncogene 30, 1009–1019 (2011).
Naujokat, C. Monoclonal antibodies against human cancer stem cells. Immunotherapy 6, 290–308 (2014).
Young, J. D., Cohn, Z. A. & Podack, E. R. The ninth component of complement and the pore-forming protein (perforin 1) from cytotoxic T cells: Structural, immunological, and functional similarities. Science 233, 184–190 (1986).
Shinkai, Y., Takio, K. & Okumura, K. Homology of Perforin to the ninth component of complement (C9). Nature 334, 525–527 (1988).
Alduaij, W. et al. Novel type II anti-CD20 monoclonal antibody (GA101) evokes homotypic adhesion and actin-dependent, lysosome-mediated cell death in B-cell malignancies. Blood 117, 4519–4529 (2011).
Vince, J. E. et al. Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity 36, 215–227 (2012).
Vince, J. E. & Silke, J. The intersection of cell death and inflammasome activation. Cell. Mol. Life Sci. 73, 2349–2367 (2016).
Kang, T. B., Yang, S. H., Toth, B., Kovalenko, A. & Wallach, D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity 38, 27–40 (2013).
Kuriakose, T. et al. ZBP1/DAI is an innate sensor of influenza virus triggering the NLRP3 inflammasome and programmed cell death pathways. Sci. Immunol. 1, aag2045 (2016).
Declercq, W., Vanden Berghe, T. & Vandenabeele, P. RIP kinases at the crossroads of cell death and survival. Cell 138, 229–232 (2009).
Festjens, N., Vanden Berghe, T., Cornelis, S. & Vandenabeele, P. RIP1, a kinase on the crossroads of a cell’s decision to live or die. Cell. Death Differ. 14, 400–410 (2007).
Duprez, L. et al. Intermediate domain of receptor-interacting protein kinase 1 (RIPK1) determines switch between necroptosis and RIPK1 kinase-dependent apoptosis. J. Biol. Chem. 287, 14863–14872 (2012).
Gabrielsen, M. et al. Cucurbitacin covalent bonding to cysteine thiols: The filamentous-actin severing protein cofilin1 as an exemplary target. Cell. Commun. Signal. 11, 58 (2013).
Dong, Y. et al. Cucurbitacin E, a tetracyclic triterpenes compound from Chinese medicine, inhibits tumor angiogenesis through VEGFR2-mediated Jak2-STAT3 signaling pathway. Carcinogenesis 31, 2097–2104 (2010).
Jackson, J. L. & Young, M. R. I. Protein phosphatase-2A modulates the Serine and tyrosine phosphorylation of paxillin in Lewis lung carcinoma tumor variants. Clin. Exp. Metastasis 19, 409–415 (2002).
Ronk, H., Rosenblum, J. S., Kung, T. & Zhuang, Z. Targeting PP2A for cancer therapeutic modulation. Cancer Biol. Med. 19, 1428–1439 (2022).
Chang, K. E. et al. The protein phosphatase 2A inhibitor LB100 sensitizes ovarian carcinoma cells to cisplatin-mediated cytotoxicity. Mol. Cancer Ther. 14, 90–100 (2015).
Pharmaceuticals and Medical Devices Agency (PMDA). Review Report: GAZYVA for Intravenous Infusion 1000 mg (Obinutuzumab). Nonclinical Evaluation Section 2.4. https://www.pmda.go.jp/drugs/2018/P20180730001/450045000_23000AMX00488_F100_1.pdf (2018).
Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685 (1970).
Oda-Sakurai, R. et al. NUP62: The target of an anti-sperm auto-monoclonal antibody during testicular development. Reproduction 158, 503–516 (2019).
Fukuhara, T. et al. A novel immunotoxin reveals a new role for CD321 in endothelial cells. PLOS ONE 12, e0181502 (2017).