The proprotein convertase furin in tumour progression

International Journal of Cancer - Tập 141 Số 4 - Trang 654-663 - 2017
Patricia Jaaks1,2, Michele Bernasconi1,2
1Children’s Research Centre, University Children’s Hospital Zurich, Zurich, Switzerland
2Department of Oncology, University Children's Hospital Zurich, Zurich, Switzerland

Tóm tắt

Proprotein convertases are proteases that have been implicated in the activation of a wide variety of proteins. These proteins are generally synthesised as precursor proteins and require limited proteolysis for conversion into their mature bioactive counterparts. Many of these proteins, including metalloproteases, growth factors and their receptors or adhesion molecules, have been shown to facilitate tumour formation and progression. Hence, this review will focus on the proprotein convertase furin and its role in cancer. The expression of furin has been confirmed in a large spectrum of cancers such as head and neck squamous cell carcinoma, breast cancer and rhabdomyosarcoma. Functional studies modulating furin activity uncovered its importance for the processing of many cancer‐related substrates and strongly indicate that high furin activity promotes the malignant phenotype of cancer cells. In this review, we summarise the expression and function of furin in different cancer types, discuss its role in processing cancer‐related proproteins and give examples of potential therapeutic approaches that take advantage of the proteolytic activity of furin in cancer cells.

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Tài liệu tham khảo

10.1038/nrd3699

10.1038/ng0797-303

10.1074/jbc.M005339200

10.1016/S0002-9440(10)61140-6

10.1002/mc.20134

10.1111/j.1749-6632.1998.tb10727.x

10.1093/emboj/16.7.1508

10.1016/S0021-9258(18)42016-9

10.1038/nsb941

10.1021/cb500087x

10.1002/cmdc.201500103

10.1073/pnas.1613630113

10.1074/jbc.M413248200

10.1182/blood-2007-07-100677

Krijt J, 2010, Hepcidin downregulation by repeated bleeding is not mediated by soluble hemojuvelin, Physiol Res, 59, 53

10.1002/mc.22131

10.1002/jcp.22792

10.1172/JCI119365

10.1002/jcp.1116

10.1210/en.2007-0989

10.1002/mc.21963

10.1016/S0021-9258(19)74548-7

10.1016/0042-6822(89)90103-7

10.1172/JCI113240

10.1038/bjc.1997.258

Bassi DE, 2016, Targeting proprotein convertases in furin‐rich lung cancer cells results in decreased in vitro and in vivo growth, Mol Carcinog, 50, 1182

10.1371/journal.pone.0055752

10.1002/mc.1057

Lopez de Cicco R, 2002, Furin expression in squamous cell carcinomas of the oral cavity and other sites evaluated by tissue microarray technology, Acta Odontol Latinoam, 15, 29

10.1186/1475-2867-14-43

10.1073/pnas.191199198

10.1016/S0002-9440(10)63838-2

10.1158/0008-5472.CAN-04-2820

10.1158/1078-0432.CCR-03-0670

Aznavoorian S, 2001, Membrane type I‐matrix metalloproteinase‐mediated degradation of type I collagen by oral squamous cell carcinoma cells, Cancer Res, 61, 6264

10.21873/anticanres.11081

10.1002/(SICI)1097-0215(19970611)71:6<966::AID-IJC10>3.0.CO;2-4

10.1677/jme.0.0260095

10.1158/0008-5472.CAN-07-0807

10.1007/s12079-016-0373-3

10.1093/carcin/bgt345

10.1016/j.bbrc.2012.02.111

10.7150/jca.16331

10.18632/oncotarget.10287

10.1158/0008-5472.CAN-10-1470

Page RE, 2007, Increased expression of the pro‐protein convertase furin predicts decreased survival in ovarian cancer, Cell Oncol, 29, 289

10.1016/j.tranon.2014.04.008

Fu Y, 2003, Epigenetic regulation of proprotein convertase PACE4 gene expression in human ovarian cancer cells, Mol Cancer Res, 1, 569

10.1023/A:1021005221934

10.1074/jbc.M101725200

10.1172/JCI32040

10.1371/journal.pone.0161396

10.18632/oncotarget.11648

10.1016/S0014-5793(98)00187-2

10.3892/ol.2014.1839

Mercapide J, 2002, Inhibition of furin‐mediated processing results in suppression of astrocytoma cell growth and invasiveness, Clin Cancer Res, 8, 1740

10.1111/j.1471-4159.2004.02806.x

10.1593/neo.12166

10.1593/neo.121846

10.1006/viro.1998.9464

10.1073/pnas.89.21.10277

10.1093/nar/gkv1118

10.1074/jbc.272.10.6663

10.1083/jcb.111.6.2851

10.1042/bj3140951

Siegfried G, 2003, The proteolytic processing of pro‐platelet‐derived growth factor‐A at RRKR(86) by members of the proprotein convertase family is functionally correlated to platelet‐derived growth factor‐A‐induced functions and tumorigenicity, Cancer Res, 63, 1458

10.1038/sj.onc.1208838

10.1016/0014-5793(95)00249-9

10.1074/jbc.270.16.9517

10.1074/jbc.270.18.10618

10.4049/jimmunol.166.12.7238

10.1091/mbc.11.7.2387

10.1038/370061a0

10.1074/jbc.272.4.2446

10.1073/pnas.94.9.4424

10.1074/jbc.M412370200

Kang T, 2002, Activation of membrane‐type matrix metalloproteinase 3 zymogen by the proprotein convertase furin in the trans‐Golgi network, Cancer Res, 62, 675

10.1074/jbc.M103680200

10.1038/375244a0

10.1042/bj3150953

10.1074/jbc.274.26.18821

10.1074/jbc.273.27.16993

Schlöndorff J, 2000, Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE), Biochem J, 347, 131, 10.1042/bj3470131

10.1158/1078-0432.CCR-15-2449

10.1042/bj3170803

Lissitzky JC, 2000, Endoproteolytic processing of integrin pro‐alpha subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7, Biochem J, 346, 133, 10.1042/bj3460133

10.1042/bj20021630

10.1016/S0014-5793(98)01330-1

10.1593/neo.10954

10.1593/neo.121250

10.1016/S0967-2109(98)00044-1

10.1016/S0014-2999(99)00042-4

10.1093/emboj/16.13.3898

10.1096/fj.06-7060com

10.1172/JCI200317220

10.1038/nm.2575

10.1172/JCI24652

10.1016/j.cell.2014.01.066

10.1093/emboj/16.20.6077

10.1158/0008-5472.CAN-04-4309

10.1158/0008-5472.CAN-07-5408

10.1021/bi100327r

10.1002/emmm.201100205

10.1517/13543776.2014.1000303

10.1042/BJ20120537

10.1038/srep34303

10.1016/j.biocel.2008.01.030

10.1038/mt.2011.269

10.1159/000360993

10.1038/mt.2015.43

10.1038/mt.2016.86

10.1016/j.ygyno.2016.09.018

10.1371/journal.pone.0010445

10.1158/1535-7163.MCT-12-0336

Shan LQ, 2011, A novel recombinant immuno‐tBid with a furin site effectively suppresses the growth of HER2‐positive osteosarcoma cells in vitro, Oncol Rep, 25, 325

10.1096/fj.09-144220

10.1021/bc9002508

10.1021/ja4010078

10.1038/srep01024

10.1021/acs.analchem.5b01656

10.1371/journal.pone.0040738

10.1155/2015/148651

10.1093/nar/gku1071

10.1093/nar/gku989

10.1093/nar/gkv1290

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International Journal of Cancer

Tập 141 Số 4

654-663

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