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01-12-2020 | Multiple Myeloma | Review

Role of CD47 in Hematological Malignancies

Authors: Entsar Eladl, Rosemarie Tremblay-LeMay, Nasrin Rastgoo, Rumina Musani, Wenming Chen, Aijun Liu, Hong Chang

Published in: Journal of Hematology & Oncology | Issue 1/2020

Abstract

CD47, or integrin-associated protein, is a cell surface ligand expressed in low levels by nearly all cells of the body. It plays an integral role in various immune responses as well as autoimmunity, by sending a potent “don’t eat me” signal to prevent phagocytosis. A growing body of evidence demonstrates that CD47 is overexpressed in various hematological malignancies and its interaction with SIRPα on the phagocytic cells prevents phagocytosis of cancer cells. Additionally, it is expressed by different cell types in the tumor microenvironment and is required for establishing tumor metastasis. Overexpression of CD47 is thus often associated with poor clinical outcomes. CD47 has emerged as a potential therapeutic target and is being investigated in various preclinical studies as well as clinical trials to prove its safety and efficacy in treating hematological neoplasms. This review focuses on different therapeutic mechanisms to target CD47, either alone or in combination with other cell surface markers, and its pivotal role in impairing tumor growth and metastatic spread of various types of hematological malignancies.

Brown E, Hooper L, Ho T, Gresham H. Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins. J Cell Biol. 1990;111:2785–94.PubMed

Reinhold MI, Lindberg FP, Plas D, Reynolds S, Peters MG, Brown EJ. In vivo expression of alternatively spliced forms of integrin-associated protein (CD47). J Cell Sci. 1995;108:3419–25.PubMed

Oldenborg P-A. CD47: a cell surface glycoprotein which regulates multiple functions of hematopoietic cells in health and disease. ISRN Hematol. 2013;2013:1–19.

Kaur S, Martin-Manso G, Pendrak ML, Garfield SH, Isenberg JS, Roberts DD. Thrombospondin-1 inhibits VEGF receptor-2 signaling by disrupting its association with CD47. J Biol Chem. 2010;285:38923–32.PubMedPubMedCentral

Sick E, Jeanne A, Schneider C, Dedieu S, Takeda K, Martiny L. CD47 update: a multifaceted actor in the tumour microenvironment of potential therapeutic interest. Br J Pharmacol. 2012;167:1415–30.PubMedPubMedCentral

Lamy L, Ticchioni M, Rouquette-Jazdanian AK, Samson M, Deckert M, Greenberg AH, et al. CD47 and the 19 kDA interacting protein-3 (BNIP3) in T cell apoptosis. J Biol Chem. 2003;278:23915–21.PubMed

Isenberg JS, Annis DS, Pendrak ML, Ptaszynska M, Frazier WA, Mosher DF, et al. Differential interactions of thrombospondin-1, -2, and -4 with CD47 and effects on cGMP signaling and ischemic injury responses. J Biol Chem. 2009;284:1116–25.PubMedPubMedCentral

Miller TW, Isenberg JS, Shih HB, Wang Y, Roberts DD. Amyloid-b inhibits no-cgmp signaling in a cd36- and cd47-dependent manner. PLoS One. 2010;5:1–10.

Shinohara M, Ohyama N, Murata Y, Okazawa H, Ohnishi H, Ishikawa O, et al. CD47 regulation of epithelial cell spreading and migration, and its signal transduction. Cancer Sci. 2006;97:889–95.PubMed

10.

Manna PP, Dimitry J, Oldenborg PA, Frazier WA. CD47 augments fas/CD95-mediated apoptosis. J Biol Chem. 2005;280:29637–44.PubMed

11.

Manna PP, Frazier WA. The mechanism of CD47-dependent killing of T cells: heterotrimeric Gi-dependent inhibition of protein kinase a. J Immunol. 2003;170:3544–53.PubMed

12.

Bruce LJ, Ghosh S, King MJ, Layton DM, Mawby WJ, Stewart GW, et al. Absence of CD47 in protein 4.2– deficient hereditary spherocytosis in man: an interaction between the Rh complex and the band 3 complex. Blood. 2002;100:1878–85.PubMed

13.

Van Beek EM, Cochrane F, Barclay AN, van den Berg TK. Signal regulatory proteins in the immune system. J Immunol. 2005;175:7781–7.PubMed

14.

Hatherley D, Graham SC, Turner J, Harlos K, Stuart DI, Barclay AN. Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47. Mol Cell. 2008;31:266–77.PubMed

15.

Tsai RK, Discher DE. Inhibition of “self” engulfment through deactivation of myosin-II at the phagocytic synapse between human cells. J Cell Biol. 2008;180:989–1003.PubMedPubMedCentral

16.

Murata Y, Kotani T, Ohnishi H, Matozaki T. The CD47-SIRPα signalling system: Its physiological roles and therapeutic application. J Biochem. 2014:335–44.

17.

Adams JC, Lawler J. The thrombospondins. Cold Spring Harb Perspect Biol. 2011;3:1–29.

18.

Broom OJ, Zhang Y, Oldenborg PA, Massoumi R, Sjölander A. CD47 regulates collagen I-induced cyclooxygenase-2 expression and intestinal epithelial cell migration. PLoS One. 2009.

19.

Gao AG, Frazier WA. Identification of a receptor candidate for the carboxyl-terminal cell binding domain of thrombospondins. J Biol Chem. 1994;269:29650–7.PubMed

20.

Isenberg JS, Ridnour LA, Dimitry J, Frazier WA, Wink DA, Roberts DD. CD47 is necessary for inhibition of nitric oxide-stimulated vascular cell responses by thrombospondin-1. J Biol Chem. 2006;281:26069–80.PubMed

21.

Lorenzo J, Choi Y, Horowitz M. Takayanagi H. Osteoimmunology: Osteoimmunology; 2011.

22.

Kukreja A, Radfar S, Sun BH, Insogna K, Dhodapkar MV. Dominant role of CD47-thrombospondin-1 interactions in myeloma-induced fusion of human dendritic cells: implications for bone disease. Blood. 2009;114:3413–21.PubMedPubMedCentral

23.

Oaks J, Wang M, Zou H. Abstract 5623: Development of a CD47-blocking antibody as a cancer therapy. Cancer Res. 2018;78:5623 LP – 5623.

24.

Wang XQ, Frazier WA. The thrombospondin receptor CD47 (IAP) modulates and associates with α2β1 integrin in vascular smooth muscle cells. Mol Biol Cell. 1998;9:865–74.PubMedPubMedCentral

25.

Brittain JE, Han J, Ataga KI, Orringer EP, Parise LV. Mechanism of CD47-induced α4β1 integrin activation and adhesion in sickle reticulocytes. J Biol Chem. 2004;279:42393–402.PubMed

26.

Orazizadeh M, Lee HS, Groenendijk B, Sadler SJM, Wright MO, Lindberg FP, et al. CD47 associates with alpha 5 integrin and regulates responses of human articular chondrocytes to mechanical stimulation in an in vitro model. Arthritis Res Ther. 2008;10.

27.

Koenigsknecht J, Landreth G. Microglial phagocytosis of fibrillar β-amyloid through a β1 integrin-dependent mechanism. J Neurosci. 2004;24:9838–46.PubMedPubMedCentral

28.

Strasser A, Connor LO, Dixit VM. APoptosis signaling. Annu Rev Biochem. 2000;69:217–45.PubMed

29.

Brown E. Integrin-associated protein (CD47): an unusual activator of G protein signaling. J Clin Invest. 2001;107:1499–500.PubMedPubMedCentral

30.

Chao MP, Alizadeh AA, Tang C, Jan M, Weissman-Tsukamoto R, Zhao F, et al. Therapeutic antibody targeting of CD47 eliminates human acute lymphoblastic leukemia. Cancer Res. 2011;71:1374–84.PubMed

31.

Ring NG, Herndler-Brandstetter D, Weiskopf K, Shan L, Volkmer JP, George BM, et al. Anti-SIRPα antibody immunotherapy enhances neutrophil and macrophage antitumor activity. Proc Natl Acad Sci U S A. 2017;114:E10578–85.PubMedPubMedCentral

32.

Chao MP, Alizadeh AA, Tang C, Myklebust JH, Varghese B, Gill S, et al. Anti-CD47 antibody synergizes with rituximab to promote phagocytosis and eradicate non-Hodgkin lymphoma. Cell. 2010;142:699–713.PubMedPubMedCentral

33.

Chao MP, Tang C, Pachynski RK, Chin R, Majeti R, Weissman IL. Extranodal dissemination of non-Hodgkin lymphoma requires CD47 and is inhibited by anti-CD47 antibody therapy. Blood. 2011;118:4890–901.PubMedPubMedCentral

34.

Advani R, Flinn I, Popplewell L, Forero A, Bartlett NL, Ghosh N, et al. CD47 blockade by Hu5F9-G4 and rituximab in non-Hodgkin’s lymphoma. N Engl J Med. 2018;379:1711–21.PubMed

35.

Jain S, Van Scoyk A, Morgan EA, Matthews A, Stevenson K, Newton G, et al. Targeted inhibition of CD47-SIRPa requires fc-FcgR interactions to maximize activity in T-cell lymphomas. Blood. 2019;134:1430–40.PubMed

36.

Johnson LDS, Banerjee S, Kruglov O, Viller NN, Horwitz SM, Lesokhin A, et al. Targeting CD47 in Sézary syndrome with SIRPaFc. Blood Adv. 2019;3:1145–53.PubMedPubMedCentral

37.

Goto H, Kojima Y, Matsuda K, Kariya R, Taura M, Kuwahara K, et al. Efficacy of anti-CD47 antibody-mediated phagocytosis with macrophages against primary effusion lymphoma. Eur J Cancer. 2014;50:1836–46.PubMed

38.

Yang K, Xu J, Liu Q, Li J, Xi Y. Expression and significance of CD47, PD1 and PDL1 in T-cell acute lymphoblastic lymphoma/leukemia. Pathol Res Pract. 2019;215:265–71.PubMed

39.

Casey SC, Tong L, Li Y, Do R, Walz S, Fitzgerald KN, et al. Erratum: MYC regulates the antitumor immune response through CD47 and PD-L1. Science (80). 2016;352.

40.

Jaiswal S, Jamieson CHM, Pang WW, Park CY, Chao MP, Majeti R, et al. CD47 is upregulated on circulating hematopoietic stem cells and leukemia cells to avoid phagocytosis. Cell. 2009;138:271–85.PubMedPubMedCentral

41.

Majeti R, Chao MP, Alizadeh AA, Pang WW, Jaiswal S, Gibbs KD, et al. CD47 is an adverse prognostic factor and therapeutic antibody target on human acute myeloid leukemia stem cells. Cell. 2009;138:286–99.PubMedPubMedCentral

42.

Chao MP, Takimoto CH, Feng DD, McKenna K, Gip P, Liu J, et al. Therapeutic targeting of the macrophage immune checkpoint CD47 in myeloid malignancies. Front Oncol. 2020;9.

43.

Pietsch EC, Dong J, Cardoso R, Zhang X, Chin D, Hawkins R, et al. Anti-leukemic activity and tolerability of anti-human CD47 monoclonal antibodies. Blood Cancer J. 2017;7:e536–8.PubMedPubMedCentral

44.

Brierley CK, Staves J, Roberts C, Johnson H, Vyas P, Goodnough LT, et al. The effects of monoclonal anti-CD47 on RBCs, compatibility testing, and transfusion requirements in refractory acute myeloid leukemia. Transfusion. 2019;59:2248–54.PubMed

45.

Rendtlew Danielsen JM, Knudsen LM, Dahl IM, Lodahl M, Rasmussen T. Dysregulation of CD47 and the ligands thrombospondin 1 and 2 in multiple myeloma. Br J Haematol. 2007;138:756–60.PubMed

46.

Muz B, Azab F, de la Puente P, Landesman Y, Azab AK. Selinexor overcomes hypoxia-induced drug resistance in multiple myeloma. Transl Oncol. 2017;10:632–40.PubMedPubMedCentral

47.

Sun J, Muz B, Alhallak K, Markovic M, Gurley S, Wang Z, et al. Targeting CD47 as a novel immunotherapy for multiple myeloma. Cancers. 2020;12.

48.

Kim D, Wang J, Willingham SB, Martin R, Wernig G, Weissman IL. Anti-CD47 antibodies promote phagocytosis and inhibit the growth of human myeloma cells. Leukemia. 2012;26:2538–45.PubMed

49.

Nasrin Rastgoo, Jian Wu, Mariah Liu, Maryam Pourabdollah, Eshetu G. Atenafu, Donna Reece, Weimin Chen, and Hong Chang. Targeting CD47 and TNFAIP8 By Mir-155 Overcomes drug resistance and inhibits tumor growth through induction of phagocytosis and apoptosis in multiple myeloma. Haematologica. 2019; 104:xxx doi:https://doi.org/10.3324/haematol.2019.227579.

50.

Murata Y, Saito Y, Kotani T, Matozaki T. CD47-signal regulatory protein α signaling system and its application to cancer immunotherapy. Cancer Sci. 2018;109:2349–57.PubMedPubMedCentral

51.

Abrisqueta P, Sancho J-M, Cordoba R, Persky DO, Andreadis C, Huntington SF, et al. Anti-CD47 antibody, CC-90002, in combination with rituximab in subjects with relapsed and/or refractory non-Hodgkin lymphoma (R/R NHL). Blood. 2019;134:4089.

52.

Holland PM, Normant E, Adam A, Armet CM, O’Connor RW, Lake AC, et al. CD47 monoclonal antibody SRF231 is a potent inducer of macrophage-mediated tumor cell phagocytosis and reduces tumor burden in murine models of hematologic malignancies. Blood. 2016.

53.

Kauder SE, Kuo TC, Harrabi O, Chen A, Sangalang E, Doyle L, et al. ALX148 blocks CD47 and enhances innate and adaptive antitumor immunity with a favorable safety profile. PLoS One. 2018;13:1–33.

54.

Johansson U, Londei M. Ligation of CD47 during monocyte differentiation into dendritic cells results in reduced capacity for interleukin-12 production. Scand J Immunol. 2004;59:50–7.PubMed

55.

Petrova PS, Viller NN, Wong M, Pang X, Lin GHY, Dodge K, et al. TTI-621 (SIRPαFc): a CD47-blocking innate immune checkpoint inhibitor with broad antitumor activity and minimal erythrocyte binding. Clin Cancer Res. 2017;23:1068–79.PubMed

56.

Hayat SMG, Bianconi V, Pirro M, Jaafari MR, Hatamipour M, Sahebkar A. CD47: role in the immune system and application to cancer therapy. Cell Oncol. 2020;43:19–30.

57.

Uscanga-Palomeque AC, Calvillo-Rodríguez KM, Gómez-Morales L, Lardé E, Denèfle T, Caballero-Hernández D, et al. CD47 agonist peptide PKHB1 induces immunogenic cell death in T-cell acute lymphoblastic leukemia cells. Cancer Sci. 2019;110:256–68.PubMed

58.

Martínez-Torres AC, Calvillo-Rodríguez KM, Uscanga-Palomeque AC, Gómez-Morales L, Mendoza-Reveles R, Caballero-Hernández D, et al. PKHB1 tumor cell lysate induces antitumor immune system stimulation and tumor regression in syngeneic mice with tumoral T lymphoblasts. J Oncol. 2019;2019.

59.

Logtenberg MEW, Jansen JHM, Raaben M, Toebes M, Franke K, Brandsma AM, et al. Glutaminyl cyclase is an enzymatic modifier of the CD47- SIRPα axis and a target for cancer immunotherapy. Nat Med. 2019;25:612–9.PubMedPubMedCentral

60.

Huang W, Wang WT, Fang K, Chen ZH, Sun YM, Han C, et al. MIR-708 promotes phagocytosis to eradicate T-ALL cells by targeting CD47. Mol Cancer. 2018;17:1–6.

61.

Buatois V, Johnson Z, Salgado-Pires S, Papaioannou A, Hatterer E, Chauchet X, et al. Preclinical development of a bispecific antibody that safely and effectively targets CD19 and CD47 for the treatment of B-cell lymphoma and leukemia. Mol Cancer Ther. 2018;17:1739–51.PubMedPubMedCentral

62.

Tremblay-Lemay R, Rastgoo N, Chang H. Modulating PD-L1 expression in multiple myeloma: an alternative strategy to target the PD-1/PD-L1 pathway. J Hematol Oncol. 2018;11:1–16.

63.

Gravelle P, Burroni B, Péricart S, Rossi C, Bezombes C, Tosolini M, et al. Mechanisms of PD-1/PD-L1 expression and prognostic relevance in non-Hodgkin lymphoma: a summary of immunohistochemical studies. Oncotarget. 2017;8:44960–75.PubMedPubMedCentral

64.

Hu L-Y, Xu X-L, Rao H-L, Chen J, Lai R-C, Huang H-Q, et al. Expression and clinical value of programmed cell death-ligand 1 (PD-L1) in diffuse large B cell lymphoma: a retrospective study. Chin J Cancer. 2017;36:1–11.

65.

Xu-Monette ZY, Zhou J, Young KH. PD-1 expression and clinical PD-1 blockade in B-cell lymphomas. Blood. 2018;131:68–83.PubMedPubMedCentral

66.

Piccione EC, Juarez S, Tseng S, Liu J, Stafford M, Narayanan C, et al. SIRPα-antibody fusion proteins selectively bind and eliminate dual antigen-expressing tumor cells. Clin Cancer Res. 2016;22:5109–19.PubMed

67.

Ponce LP, Fenn NC, Moritz N, Krupka C, Kozik JH, Lauber K, et al. SIRPα-antibody fusion proteins stimulate phagocytosis and promote elimination of acute myeloid leukemia cells. Oncotarget. 2017;8:11284–301.PubMedPubMedCentral

68.

Lin GHY, Chai V, Lee V, Dodge K, Truong T, Wong M, et al. TTI-621 (SIRPαFc), a CD47-blocking cancer immunotherapeutic, triggers phagocytosis of lymphoma cells by multiple polarized macrophage subsets. PLoS One. 2017;12:1–16.

69.

Narla RK, Modi H, Wong L, Abassian M, Bauer D, Desai P, et al. Abstract 4694: The humanized anti-CD47 monclonal antibody, CC-90002, has antitumor activity in vitro and in vivo. Cancer Res. 2017;77:4694 LP – 4694.abstract.

70.

Barazi HO, Li Z, Cashel JA, Krutzsch HC, Annis DS, Mosher DF, et al. Regulation of integrin function by CD47 ligands: differential effects on αvβ3 and α4β1 integrin-mediated adhesion. J Biol Chem. 2002;277:42859–66.PubMed

71.

Lin GHY, Viller NN, Chabonneau M, Brinen L, Mutukura T, Dodge K, et al. Abstract 2709: TTI-622 (SIRPα-IgG4 Fc), a CD47-blocking innate immune checkpoint inhibitor, suppresses tumor growth and demonstrates enhanced efficacy in combination with antitumor antibodies in both hematologic and solid tumor models. 2018;2709–2709.

72.

Suzuki S, Yokobori T, Tanaka N, Sakai M, Sano A, Inose T, et al. CD47 expression regulated by the miR-133a tumor suppressor is a novel prognostic marker in esophageal squamous cell carcinoma. Oncol Rep. 2012;28:465–72.PubMed

73.

Wang Y, Xu Z, Guo S, Zhang L, Sharma A, Robertson GP, et al. Intravenous delivery of siRNA targeting CD47 effectively inhibits melanoma tumor growth and lung metastasis. Mol Ther. 2013;21:1919–29.PubMedPubMedCentral

74.

Boussiotis VA. Molecular and biochemical aspects of the PD-1 checkpoint pathway. N Engl J Med. 2016;375:1767–78.PubMedPubMedCentral

75.

Liu B, Guo H, Xu J, Qin T, Guo Q, Gu N, et al. Elimination of tumor by CD47/PD-L1 dual-targeting fusion protein that engages innate and adaptive immune responses. MAbs. 2018;10:315–24.PubMed

76.

Sockolosky JT, Dougan M, Ingram JR, Ho CCM, Kauke MJ, Almo SC, et al. Durable antitumor responses to CD47 blockade require adaptive immune stimulation. Proc Natl Acad Sci U S A. 2016;113:E2646–54.PubMedPubMedCentral

77.

Lian S, Xie R, Ye Y, Xie X, Li S, Lu Y, et al. Simultaneous blocking of CD47 and PD-L1 increases innate and adaptive cancer immune responses and cytokine release. EBioMedicine. 2019;42:281–95.PubMedPubMedCentral

78.

Piccione EC, Juarez S, Liu J, Tseng S, Ryan CE, Narayanan C, et al. A bispecific antibody targeting CD47 and CD20 selectively binds and eliminates dual antigen expressing lymphoma cells. MAbs. 2015;7:946–56.PubMedPubMedCentral

79.

Zhang X, Fan J, Ju D. Insights into CD47/SIRPα axis-targeting tumor immunotherapy. Antib Ther. 2018;1:27–32.PubMedCentral

80.

Zhang W, Huang Q, Xiao W, Zhao Y, Pi J, Xu H, et al. Advances in anti-tumor treatments targeting the CD47/SIRPα Axis. Front Immunol. 2020;11:1–15.

81.

Feliz-Mosquea YR, Christensen AA, Wilson AS, Westwood B, Varagic J, Meléndez GC, et al. Combination of anthracyclines and anti-CD47 therapy inhibit invasive breast cancer growth while preventing cardiac toxicity by regulation of autophagy. Breast Cancer Res Treat. 2018;172:69–82.PubMedPubMedCentral

82.

Ho CCM, Guo N, Sockolosky JT, Ring AM, Weiskopf K, Özkan E, et al. “Velcro” engineering of high affinity CD47 Ectodomain as signal regulatory protein α (SIRPα) antagonists that enhance antibody-dependent cellular phagocytosis. J Biol Chem. 2015;290:12650–63.PubMedPubMedCentral

83.

Sim J, Sockolosky JT, Sangalang E, Izquierdo S, Pedersen D, Harriman W, et al. Discovery of high affinity, pan-allelic, and pan-mammalian reactive antibodies against the myeloid checkpoint receptor SIRPα. MAbs. 2019;11:1036–52.PubMedPubMedCentral

84.

Anniss AM, Sparrow RL. Expression of CD47 (integrin-associated protein) decreases on red blood cells during storage. Transfus Apher Sci. 2002;27:233–8.PubMed

85.

Weiskopf K, Ring AM, Ho CCM, Volkmer J, Levin M, Volkmer AK, et al. Engineered SIRPa variants as immunotherapeutic adjuvants to anticancer antibodies. Science AAAS. 2013;341:88–91.

86.

Yanagita T, Murata Y, Tanaka D, Motegi SI, Arai E, Daniwijaya EW, et al. anti-SIRPα antibodies as a potential new tool for cancer immunotherapy. JCI Insight. 2017;2.

87.

Chen Q, Wang C, Zhang X, Chen G, Hu Q, Li H, et al. In situ sprayed bioresponsive immunotherapeutic gel for post-surgical cancer treatment. Nat Nanotechnol. 2019;14:89–97.PubMed

88.

Chowdhury S, Castro S, Coker C, Hinchliffe TE, Arpaia N, Danino T. Programmable bacteria induce durable tumor regression and systemic antitumor immunity. Nat Med. 2019;25:1057–63.PubMedPubMedCentral

89.

Trabulo S, Aires A, Aicher A, Heeschen C, Cortajarena AL. Multifunctionalized iron oxide nanoparticles for selective targeting of pancreatic cancer cells. Biochim Biophys Acta. 1861;2017:1597–605.

90.

Liu XJ, Li L, Liu XJ, Li Y, Zhao CY, Wang RQ, et al. Mithramycin-loaded mPEG-PLGA nanoparticles exert potent antitumor efficacy against pancreatic carcinoma. Int J Nanomedicine. 2017;12:5255–69.PubMedPubMedCentral

91.

Davis RM, Campbell JL, Burkitt S, Qiu Z, Kang S, Mehraein M, et al. A raman imaging approach using CD47 antibody-labeled SERS nanoparticles for identifying breast cancer and its potential to guide surgical resection. Nanomaterials. 2018;8.

92.

Mansoori B, Mohammadi A, Davudian S, Shirjang S, Baradaran B. The different mechanisms of cancer drug resistance: a brief review. Adv Pharm Bull. 2017;7:339–48.PubMedPubMedCentral

93.

Ishikawa-Sekigami T, Kaneko Y, Saito Y, Murata Y, Okazawa H, Ohnishi H, et al. Enhanced phagocytosis of CD47-deficient red blood cells by splenic macrophages requires SHPS-1. Biochem Biophys Res Commun. 2006;343:1197–200.PubMed

94.

Oldenborg PA. Role of CD47 in erythroid cells and in autoimmunity. Leuk Lymphoma. 2004;45:1319–27.PubMed

95.

Catani L, Sollazzo D, Ricci F, Polverelli N, Palandri F, Baccarani M, et al. Society for Hematology and Stem Cells. 2011;39:486–94.

96.

Willingham SB, Volkmer JP, Gentles AJ, Sahoo D, Dalerba P, Mitra SS, 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;109:6662–7.PubMedPubMedCentral

97.

Liu J, Wang L, Zhao F, Tseng S, Narayanan C, Shura L, et al. Pre-clinical development of a humanized anti-CD47 antibody with anti-cancer therapeutic potential. PLoS One. 2015;10:1–23.

98.

Weiskopf K. Cancer immunotherapy targeting the CD47/SIRPα axis. Eur J Cancer. 2017;76:100–9.PubMed

Title: Role of CD47 in Hematological Malignancies
Authors: Entsar Eladl
Rosemarie Tremblay-LeMay
Nasrin Rastgoo
Rumina Musani
Wenming Chen
Aijun Liu
Hong Chang
Publication date: 01-12-2020
Publisher: BioMed Central
Keywords: Multiple Myeloma
Acute Myeloid Leukemia
Rituximab
Rituximab
Published in: Journal of Hematology & Oncology / Issue 1/2020
Electronic ISSN: 1756-8722
DOI: https://doi.org/10.1186/s13045-020-00930-1

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