Nanobody-based CAR-T cells for cancer immunotherapy
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Prasad V. Immunotherapy: Tisagenlecleucel - the first approved CAR-T-cell therapy: implications for payers and policy makers. Nat Rev Clin Oncol. 2018;15(1):11–2.
Hashem Boroojerdi M, et al. Strategies for having a more effective and less toxic CAR T-cell therapy for acute lymphoblastic leukemia. Med Oncol. 2020;37(11):100.
SafarzadehKozani P, SafarzadehKozani P, Rahbarizadeh F. Optimizing the Clinical Impact of CAR-T Cell Therapy in B-Cell Acute Lymphoblastic Leukemia: Looking Back While Moving Forward. Front Immunol. 2021;12:765097.
SafarzadehKozani P, SafarzadehKozani P, O’Connor RS. In Like a Lamb; Out Like a Lion: Marching CAR T Cells Toward Enhanced Efficacy in B-ALL. Molecular Cancer Therapeutics. 2021;20(7):1223–33.
Bouchkouj N, et al. FDA approval summary: Axicabtagene ciloleucel for relapsed or refractory large B-cell lymphoma. Clin Cancer Res. 2019;25(6):1702–8.
Mullard A. FDA approves first BCMA-targeted CAR-T cell therapy. Nat Rev Drug Discov. 2021;20(5):332.
Voelker R. CAR-T Therapy Is Approved for Mantle Cell Lymphoma. JAMA. 2020;324(9):832.
Mullard A. FDA approves first CAR T therapy. Nat Rev Drug Discov. 2017;16(10):669.
Mullard A. FDA approves fourth CAR-T cell therapy. Nat Rev Drug Discov. 2021;20(3):166.
Mullard A. FDA approves second BCMA-targeted CAR-T cell therapy. Nat Rev Drug Discov, 2022;21(4):249. https://www.nature.com/articles/d41573-022-00048-8.
Wang D, et al. Chlorotoxin-directed CAR T cells for specific and effective targeting of glioblastoma. Sci Transl Med. 2020;12(533):eaaw2672.
Xie YJ, et al. Nanobody-based CAR T cells that target the tumor microenvironment inhibit the growth of solid tumors in immunocompetent mice. Proc Natl Acad Sci U S A. 2019;116(16):7624–31.
Wang Y, et al. Targeting FLT3 in acute myeloid leukemia using ligand-based chimeric antigen receptor-engineered T cells. J Hematol Oncol. 2018;11(1):60.
SafarzadehKozani P, SafarzadehKozani P, Rahbarizadeh F. Novel antigens of CAR T cell therapy: New roads; old destination. Transl Oncol. 2021;14(7):101079.
SafarzadehKozani P, et al. Strategies for Dodging the Obstacles in CAR T Cell Therapy. Front Oncol. 2021;11:627549.
Eshhar Z, et al. Specific activation and targeting of cytotoxic lymphocytes through chimeric single chains consisting of antibody-binding domains and the gamma or zeta subunits of the immunoglobulin and T-cell receptors. Proc Natl Acad Sci U S A. 1993;90(2):720–4.
Tokarew N, et al. Teaching an old dog new tricks: next-generation CAR T cells. Br J Cancer. 2019;120(1):26–37.
Hong M, Clubb JD, Chen YY. Engineering CAR-T Cells for Next-Generation Cancer Therapy. Cancer Cell. 2020;38(4):473–88.
Finney HM, et al. Chimeric receptors providing both primary and costimulatory signaling in T cells from a single gene product. J Immunol. 1998;161(6):2791–7.
Imai C, et al. Chimeric receptors with 4–1BB signaling capacity provoke potent cytotoxicity against acute lymphoblastic leukemia. Leukemia. 2004;18(4):676–84.
Finney HM, Akbar AN, Lawson AD. Activation of resting human primary T cells with chimeric receptors: costimulation from CD28, inducible costimulator, CD134, and CD137 in series with signals from the TCR zeta chain. J Immunol. 2004;172(1):104–13.
Gimmi CD, et al. Human T-cell clonal anergy is induced by antigen presentation in the absence of B7 costimulation. Proc Natl Acad Sci U S A. 1993;90(14):6586–90.
Hombach A, et al. T-cell activation by recombinant receptors: CD28 costimulation is required for interleukin 2 secretion and receptor-mediated T-cell proliferation but does not affect receptor-mediated target cell lysis. Cancer Res. 2001;61(5):1976–82.
Kowolik CM, et al. CD28 costimulation provided through a CD19-specific chimeric antigen receptor enhances in vivo persistence and antitumor efficacy of adoptively transferred T cells. Cancer Res. 2006;66(22):10995–1004.
Milone MC, et al. Chimeric receptors containing CD137 signal transduction domains mediate enhanced survival of T cells and increased antileukemic efficacy in vivo. Mol Ther. 2009;17(8):1453–64.
Prasad V. Tisagenlecleucel—the first approved CAR-T-cell therapy: implications for payers and policy makers. Nat Rev Clin Oncol. 2018;15(1):11–2.
Ramos CA, et al. In Vivo Fate and Activity of Second- versus Third-Generation CD19-Specific CAR-T Cells in B Cell Non-Hodgkin’s Lymphomas. Mol Ther. 2018;26(12):2727–37.
Kawalekar OU, et al. Distinct Signaling of Coreceptors Regulates Specific Metabolism Pathways and Impacts Memory Development in CAR T Cells. Immunity. 2016;44(2):380–90.
Long AH, et al. 4–1BB costimulation ameliorates T cell exhaustion induced by tonic signaling of chimeric antigen receptors. Nat Med. 2015;21(6):581–90.
Frigault MJ, et al. Identification of chimeric antigen receptors that mediate constitutive or inducible proliferation of T cells. Cancer Immunol Res. 2015;3(4):356–67.
Vezys V, et al. 4–1BB signaling synergizes with programmed death ligand 1 blockade to augment CD8 T cell responses during chronic viral infection. J Immunol. 2011;187(4):1634–42.
Wang C, et al. 4–1BBL induces TNF receptor-associated factor 1-dependent Bim modulation in human T cells and is a critical component in the costimulation-dependent rescue of functionally impaired HIV-specific CD8 T cells. J Immunol. 2007;179(12):8252–63.
Cappell KM, Kochenderfer JN. A comparison of chimeric antigen receptors containing CD28 versus 4–1BB costimulatory domains. Nat Rev Clin Oncol. 2021;18(11):715–27.
Chmielewski M, Abken H. TRUCKs: the fourth generation of CARs. Expert Opin Biol Ther. 2015;15(8):1145–54.
Safarzadeh Kozani P, Safarzadeh Kozani P, Rahbarizadeh F. Addressing the obstacles of CAR T cell migration in solid tumors: wishing a heavy traffic. Crit Rev Biotechnol. 2021:1–20. https://doi.org/10.1080/07388551.2021.1988509.
Yeku OO, Brentjens RJ. Armored CAR T-cells: utilizing cytokines and pro-inflammatory ligands to enhance CAR T-cell anti-tumour efficacy. Biochem Soc Trans. 2016;44(2):412–8.
Strohl WR, Naso M. Bispecific T-Cell Redirection versus Chimeric Antigen Receptor (CAR)-T Cells as Approaches to Kill Cancer Cells. Antibodies (Basel). 2019;8(3):41.
Greenberg AS, et al. A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. Nature. 1995;374(6518):168–73.
Völkel T, et al. Optimized linker sequences for the expression of monomeric and dimeric bispecific single-chain diabodies. Protein Eng. 2001;14(10):815–23.
Gorovits B, Koren E. Immunogenicity of Chimeric Antigen Receptor T-Cell Therapeutics. BioDrugs. 2019;33(3):275–84.
Shah NN, Fry TJ. Mechanisms of resistance to CAR T cell therapy. Nat Rev Clin Oncol. 2019;16(6):372–85.
DeNardo GL, et al. Human antiglobulin response to foreign antibodies: therapeutic benefit? Cancer Immunol Immunother. 2003;52(5):309–16.
Gruber R, et al. The human antimouse immunoglobulin response and the anti-idiotypic network have no influence on clinical outcome in patients with minimal residual colorectal cancer treated with monoclonal antibody CO17-1A. Cancer Res. 2000;60(7):1921–6.
Herlyn D, et al. Anti-idiotypic antibodies to monoclonal antibody CO17-1A. Hybridoma. 1986;5(Suppl 1):S51–8.
Lamers CH, et al. Immune responses to transgene and retroviral vector in patients treated with ex vivo-engineered T cells. Blood. 2011;117(1):72–82.
Kim JH, Hong HJ. Humanization by CDR grafting and specificity-determining residue grafting. Methods Mol Biol. 2012;907:237–45.
Vincke C, et al. General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold. J Biol Chem. 2009;284(5):3273–84.
Han L, et al. Safety and efficacy of CAR-T cell targeting BCMA in patients with multiple myeloma coinfected with chronic hepatitis B virus. J Immunother Cancer. 2020;8(2):e000927.
Han L, et al. The clinical study of anti-BCMA CAR-T with single-domain antibody as antigen binding domain. Journal of Clinical Oncology. 2021;39(15_suppl):8025–8025.
Han L, et al. The phase I clinical study of CART targeting BCMA with humanized alpaca-derived single-domain antibody as antigen recognition domain. Journal of Clinical Oncology. 2019;37(15_suppl):2535–2535.
Cao J, et al. Potent anti-leukemia activities of humanized CD19-targeted Chimeric antigen receptor T (CAR-T) cells in patients with relapsed/refractory acute lymphoblastic leukemia. Am J Hematol. 2018;93(7):851–8.
Heng G, et al. Sustained Therapeutic Efficacy of Humanized Anti-CD19 Chimeric Antigen Receptor T Cells in Relapsed/Refractory Acute Lymphoblastic Leukemia. Clin Cancer Res. 2020;26(7):1606–15.
Myers RM, et al. Humanized CD19-Targeted Chimeric Antigen Receptor (CAR) T Cells in CAR-Naive and CAR-Exposed Children and Young Adults With Relapsed or Refractory Acute Lymphoblastic Leukemia. J Clin Oncol. 2021;39(27):3044–55.
SafarzadehKozani P, SafarzadehKozani P, O’Connor RS. Humanized Chimeric Antigen Receptor (CAR) T cells. J Cancer Immunol (Wilmington). 2021;3(4):183–7.
Sun W, et al. A combined strategy improves the solubility of aggregation-prone single-chain variable fragment antibodies. Protein Expr Purif. 2012;83(1):21–9.
Nieba L, et al. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng. 1997;10(4):435–44.
Gil D, Schrum AG. Strategies to stabilize compact folding and minimize aggregation of antibody-based fragments. Adv Biosci Biotechnol. 2013;4(4a):73–84.
Jäger M, Plückthun A. Domain interactions in antibody Fv and scFv fragments: effects on unfolding kinetics and equilibria. FEBS Lett. 1999;462(3):307–12.
Jayaraman J, et al. CAR-T design: Elements and their synergistic function. EBioMedicine. 2020;58:102931.
Hegde M, et al. Tandem CAR T cells targeting HER2 and IL13Rα2 mitigate tumor antigen escape. J Clin Invest. 2016;126(8):3036–52.
Kumar M, et al. Systematic determination of the packaging limit of lentiviral vectors. Hum Gene Ther. 2001;12(15):1893–905.
Bos TJ, et al. Large double copy vectors are functional but show a size-dependent decline in transduction efficiency. J Biotechnol. 2010;150(1):37–40.
al Yacoub N, et al. Optimized production and concentration of lentiviral vectors containing large inserts. J Gene Med. 2007;9(7):579–84.
Vu KB, et al. Comparison of llama VH sequences from conventional and heavy chain antibodies. Mol Immunol. 1997;34(16–17):1121–31.
Bannas P, Hambach J, Koch-Nolte F. Nanobodies and Nanobody-Based Human Heavy Chain Antibodies As Antitumor Therapeutics. Front Immunol. 2017;8:1603.
Gulati S, et al. Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor. Nat Commun. 2018;9(1):1996.
Xu HM, et al. VEGFR2 Expression in Head and Neck Squamous Cell Carcinoma Cancer Cells Mediates Proliferation and Invasion. Asian Pac J Cancer Prev. 2016;17(4):2217–21.
Lanitis E, et al. VEGFR-2 redirected CAR-T cells are functionally impaired by soluble VEGF-A competition for receptor binding. J Immunother Cancer. 2021;9(8):e002151.
Hajari Taheri F, et al. T cell engineered with a novel nanobody-based chimeric antigen receptor against VEGFR2 as a candidate for tumor immunotherapy. IUBMB Life. 2019;71(9):1259–67.
Iqbal N, Iqbal N. Human Epidermal Growth Factor Receptor 2 (HER2) in Cancers: Overexpression and Therapeutic Implications. Mol Biol Int. 2014;2014:852748.
Vitanza NA, et al. Locoregional infusion of HER2-specific CAR T cells in children and young adults with recurrent or refractory CNS tumors: an interim analysis. Nat Med. 2021;27(9):1544–52.
Li P, et al. The Third Generation Anti-HER2 Chimeric Antigen Receptor Mouse T Cells Alone or Together With Anti-PD1 Antibody Inhibits the Growth of Mouse Breast Tumor Cells Expressing HER2 in vitro and in Immune Competent Mice. Front Oncol. 2020;10:1143.
Jamnani FR, et al. T cells expressing VHH-directed oligoclonal chimeric HER2 antigen receptors: towards tumor-directed oligoclonal T cell therapy. Biochim Biophys Acta. 2014;1840(1):378–86.
Thor A, et al. Distribution of oncofetal antigen tumor-associated glycoprotein-72 defined by monoclonal antibody B72.3. Cancer Res. 1986;46(6):3118–24.
Sharifzadeh Z, et al. Genetically engineered T cells bearing chimeric nanoconstructed receptors harboring TAG-72-specific camelid single domain antibodies as targeting agents. Cancer Lett. 2013;334(2):237–44.
Chang SS. Overview of prostate-specific membrane antigen. Rev Urol. 2004;6 Suppl 10(Suppl 10):S13-8.
Alzubi J, et al. PSMA-Directed CAR T Cells Combined with Low-Dose Docetaxel Treatment Induce Tumor Regression in a Prostate Cancer Xenograft Model. Molecular Therapy - Oncolytics. 2020;18:226–35.
Hassani M, et al. Construction of a chimeric antigen receptor bearing a nanobody against prostate a specific membrane antigen in prostate cancer. J Cell Biochem. 2019;120(6):10787–95.
Hassani M, et al. Engineered Jurkat Cells for Targeting Prostate-Specific Membrane Antigen on Prostate Cancer Cells by Nanobody-Based Chimeric Antigen Receptor. Iran Biomed J. 2020;24(2):81–8.
Ivins JK, et al. Cerebroglycan, a developmentally regulated cell-surface heparan sulfate proteoglycan, is expressed on developing axons and growth cones. Dev Biol. 1997;184(2):320–32.
Li N, et al. Therapeutically targeting glypican-2 via single-domain antibody-based chimeric antigen receptors and immunotoxins in neuroblastoma. Proc Natl Acad Sci U S A. 2017;114(32):E6623-e6631.
Morandi F, et al. CD38: A Target for Immunotherapeutic Approaches in Multiple Myeloma. Front Immunol. 2018;9:2722.
Drent E, et al. Pre-clinical evaluation of CD38 chimeric antigen receptor engineered T cells for the treatment of multiple myeloma. Haematologica. 2016;101(5):616–25.
An N, et al. Anti-Multiple Myeloma Activity of Nanobody-Based Anti-CD38 Chimeric Antigen Receptor T Cells. Mol Pharm. 2018;15(10):4577–88.
Walter RB. The role of CD33 as therapeutic target in acute myeloid leukemia. Expert Opin Ther Targets. 2014;18(7):715–8.
Kenderian SS, et al. CD33-specific chimeric antigen receptor T cells exhibit potent preclinical activity against human acute myeloid leukemia. Leukemia. 2015;29(8):1637–47.
De Munter S, et al. Rapid and Effective Generation of Nanobody Based CARs using PCR and Gibson Assembly. Int J Mol Sci. 2020;21(3):883.
Sempowski GD, et al. Structure and function of the CD7 molecule. Crit Rev Immunol. 1999;19(4):331–48.
Campana D, et al. Stages of T-cell receptor protein expression in T-cell acute lymphoblastic leukemia. Blood. 1991;77(7):1546–54.
Gomes-Silva D, et al. CD7-edited T cells expressing a CD7-specific CAR for the therapy of T-cell malignancies. Blood. 2017;130(3):285–96.
Frankel AE, et al. Therapy of patients with T-cell lymphomas and leukemias using an anti-CD7 monoclonal antibody-ricin A chain immunotoxin. Leuk Lymphoma. 1997;26(3–4):287–98.
Yu Y, et al. Humanized CD7 nanobody-based immunotoxins exhibit promising anti-T-cell acute lymphoblastic leukemia potential. Int J Nanomedicine. 2017;12:1969–83.
SafarzadehKozani P, SafarzadehKozani P, Rahbarizadeh F. CAR-T cell therapy in T-cell malignancies: Is success a low-hanging fruit? Stem Cell Res Ther. 2021;12(1):527.
Zhang M, et al. A Single-Arm, Open-Label, Pilot Trial of Autologous CD7-CAR-T Cells for CD7 Positive Relapsed and Refractory T-Lymphoblastic Leukemia/Lymphoma. Blood. 2021;138(Supplement 1):3829–3829.
Pan J, et al. Donor-Derived CD7 Chimeric Antigen Receptor T Cells for T-Cell Acute Lymphoblastic Leukemia: First-in-Human. Phase I Trial J Clin Oncol. 2021;39(30):3340–51.
Kufe DW. MUC1-C oncoprotein as a target in breast cancer: activation of signaling pathways and therapeutic approaches. Oncogene. 2013;32(9):1073–81.
Bakhtiari SH, et al. Anti-MUC1 nanobody can redirect T-body cytotoxic effector function. Hybridoma (Larchmt). 2009;28(2):85–92.
Iri-Sofla FJ, et al. Nanobody-based chimeric receptor gene integration in Jurkat cells mediated by φC31 integrase. Exp Cell Res. 2011;317(18):2630–41.
Khaleghi S, et al. A caspase 8-based suicide switch induces apoptosis in nanobody-directed chimeric receptor expressing T cells. Int J Hematol. 2012;95(4):434–44.
Kobayashi S, et al. EGFR mutation and resistance of non-small-cell lung cancer to gefitinib. N Engl J Med. 2005;352(8):786–92.
Dong YH, et al. The functional verification of EGFR-CAR T-cells targeted to hypopharyngeal squamous cell carcinoma. Onco Targets Ther. 2018;11:7053–9.
Albert S, et al. A novel nanobody-based target module for retargeting of T lymphocytes to EGFR-expressing cancer cells via the modular UniCAR platform. Oncoimmunol. 2017;6(4):e1287246.
Albert S, et al. From mono- to bivalent: improving theranostic properties of target modules for redirection of UniCAR T cells against EGFR-expressing tumor cells in vitro and in vivo. Oncotarget. 2018;9(39):25597–616.
Boross P, Leusen JH. Mechanisms of action of CD20 antibodies. Am J Cancer Res. 2012;2(6):676–90.
Shadman M, et al. CD20 Targeted CAR-T for High-Risk B-Cell Non-Hodgkin Lymphomas. Blood. 2019;134(Supplement 1):3235–3235.
Liang A, et al. Safety and efficacy of a novel anti-CD20 chimeric antigen receptor (CAR)-T cell therapy in relapsed/refractory (r/r) B-cell non-Hodgkin lymphoma (B-NHL) patients after failing CD19 CAR-T therapy. J Clin Oncol. 2021;39(15):2508–2508.
Blank C, et al. PD-L1/B7H-1 inhibits the effector phase of tumor rejection by T cell receptor (TCR) transgenic CD8+ T cells. Cancer Res. 2004;64(3):1140–5.
Iwai Y, et al. Involvement of PD-L1 on tumor cells in the escape from host immune system and tumor immunotherapy by PD-L1 blockade. Proc Natl Acad Sci U S A. 2002;99(19):12293–7.
Astrof S, et al. Direct test of potential roles of EIIIA and EIIIB alternatively spliced segments of fibronectin in physiological and tumor angiogenesis. Mol Cell Biol. 2004;24(19):8662–70.
Castellani P, et al. The fibronectin isoform containing the ED-B oncofetal domain: a marker of angiogenesis. Int J Cancer. 1994;59(5):612–8.
Xie YJ, et al. Nanobody-based CAR T cells that target the tumor microenvironment inhibit the growth of solid tumors in immunocompetent mice. Proc Natl Acad Sci. 2019;116(16):7624.
Xie YJ, et al. Improved Antitumor Efficacy of Chimeric Antigen Receptor T Cells that Secrete Single-Domain Antibody Fragments. Cancer Immunol Res. 2020;8(4):518–29.
Willingham SB, et al. The CD47-signal regulatory protein alpha (SIRPa) interaction is a therapeutic target for human solid tumors. Proc Natl Acad Sci U S A. 2012;109(17):6662–7.
Sockolosky JT, et al. Durable antitumor responses to CD47 blockade require adaptive immune stimulation. Proc Natl Acad Sci U S A. 2016;113(19):E2646–54.
Majeti R, et al. CD47 is an adverse prognostic factor and therapeutic antibody target on human acute myeloid leukemia stem cells. Cell. 2009;138(2):286–99.
Ingram JR, et al. Localized CD47 blockade enhances immunotherapy for murine melanoma. Proc Natl Acad Sci U S A. 2017;114(38):10184–9.
Chao MP, et al. Anti-CD47 antibody synergizes with rituximab to promote phagocytosis and eradicate non-Hodgkin lymphoma. Cell. 2010;142(5):699–713.
Advani R, et al. CD47 Blockade by Hu5F9-G4 and Rituximab in Non-Hodgkin’s Lymphoma. N Engl J Med. 2018;379(18):1711–21.
Nassiri F, et al. Endoglin (CD105): a review of its role in angiogenesis and tumor diagnosis, progression and therapy. Anticancer Res. 2011;31(6):2283–90.
Dallas NA, et al. Endoglin (CD105): a marker of tumor vasculature and potential target for therapy. Clin Cancer Res. 2008;14(7):1931–7.
Mo F, et al. Nanobody-based chimeric antigen receptor T cells designed by CRISPR/Cas9 technology for solid tumor immunotherapy. Signal Transduct Target Ther. 2021;6(1):80.
Tai YT, Anderson KC. Targeting B-cell maturation antigen in multiple myeloma. Immunotherapy. 2015;7(11):1187–99.
Yu B, Jiang T, Liu D. BCMA-targeted immunotherapy for multiple myeloma. J Hematol Oncol. 2020;13(1):125.
Teoh PJ, Chng WJ. CAR T-cell therapy in multiple myeloma: more room for improvement. Blood Cancer J. 2021;11(4):84.
Zhao WH, et al. A phase 1, open-label study of LCAR-B38M, a chimeric antigen receptor T cell therapy directed against B cell maturation antigen, in patients with relapsed or refractory multiple myeloma. J Hematol Oncol. 2018;11(1):141.
Xu J, et al. Exploratory trial of a biepitopic CAR T-targeting B cell maturation antigen in relapsed/refractory multiple myeloma. Proc Natl Acad Sci. 2019;116(19):9543.
Martin T, et al. Updated Results from CARTITUDE-1: Phase 1b/2Study of Ciltacabtagene Autoleucel, a B-Cell Maturation Antigen-Directed Chimeric Antigen Receptor T Cell Therapy. Patients With Relapsed/Refractory Multiple Myeloma Blood. 2021;138(Supplement 1):549–549.
Madduri D, et al. CARTITUDE-1: Phase 1b/2 Study of Ciltacabtagene Autoleucel, a B-Cell Maturation Antigen-Directed Chimeric Antigen Receptor T Cell Therapy. Relapsed/Refractory Multiple Myeloma Blood. 2020;136(Supplement 1):22–5.
Berdeja JG, et al. Ciltacabtagene autoleucel, a B-cell maturation antigen-directed chimeric antigen receptor T-cell therapy in patients with relapsed or refractory multiple myeloma (CARTITUDE-1): a phase 1b/2 open-label study. Lancet. 2021;398(10297):314–24.
Weatherill EE, et al. Towards a universal disulphide stabilised single chain Fv format: importance of interchain disulphide bond location and vL-vH orientation. Protein Eng Des Sel. 2012;25(7):321–9.