Functional role of periostin in development and wound repair: implications for connective tissue disease

Journal of Cell Communication and Signaling - 2008
David A. Hamilton1
1CIHR Group in Skeletal Development & Remodeling, Schulich School of Medicine and Dentistry, Dental Sciences Building, University of Western Ontario, London, Ontario, Canada, N6A 5C1

Tóm tắt

AbstractIntegrity of the extracellular matrix (ECM) is essential for maintaining the normal structure and function of connective tissues. ECM is secreted locally by cells and organized into a complex meshwork providing physical support to cells, tissues, and organs. Initially thought to act only as a scaffold, the ECM is now known to provide a myriad of signals to cells regulating all aspects of their phenotype from morphology to differentiation. Matricellular proteins are a class of ECM related molecules defined through their ability to modulate cell–matrix interactions. Matricellular proteins are expressed at high levels during development, but typically only appear in postnatal tissue in wound repair or disease, where their levels increase substantially. Members of the CCN family, tenascin‐C, osteopontin, secreted protein acidic rich in cysteine (SPARC), bone sialoprotein, thrombospondins, and galectins have all been classed as matricellular proteins. Periostin, a 90 kDa secreted homophilic cell adhesion protein, was recently added to matricellular class of proteins based on its expression pattern and function during development as well as in wound repair. Periostin is expressed in connective tissues including the periodontal ligament, tendons, skin and bone, and is also prominent in neoplastic tissues, cardiovascular disease, as well as in connective tissue wound repair. This review will focus on the functional role of periostin in tissue physiology. Fundamentally, it appears that periostin influences cell behaviour as well as collagen fibrillogenesis, and therefore exerts control over the structural and functional properties of connective tissues in both health and disease. Periostin is a novel matricellular protein with close homology to Drosophila fasciclin 1. In this review, the functional role of periostin is discussed in the context of connective tissue physiology, in development, disease, and wound repair.

Từ khóa


Tài liệu tham khảo

10.1172/JCI110723

10.1016/j.bone.2005.11.017

10.1038/sj.onc.1210009

10.1172/JCI31044

10.1002/jcp.21237

10.1097/01.hco.0000162398.21972.cd

10.1161/CIRCRESAHA.107.159103

10.1016/S0945‐053X(00)00103‐7

10.1016/S0955‐0674(02)00361‐7

10.1046/j.1087‐0024.2000.00005.x

10.1016/j.biocel.2004.01.012

10.1016/j.ydbio.2006.09.048

10.1073/pnas.78.12.7745

10.1016/j.berh.2007.12.005

10.1242/jcs.01731

10.1016/S0945‐053X(00)00107‐4

10.1038/sj.ejhg.5200876

10.1093/ptj/79.3.308

10.1016/S0074‐7696(07)57004‐X

De Coster PJ, 2004, Orofacial manifestations of congenital fibrillin deficiency: pathogenesis and clinical diagnostics, Pediatr Dent, 26, 535

10.1056/NEJMcibr074816

10.1007/s00018‐007‐7044‐8

10.1053/j.gastro.2007.01.031

10.1007/BF01919835

10.2741/2157

Gillan L, 2002, Periostin secreted by epithelial ovarian carcinoma is a ligand for alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell motility, Cancer Res, 62, 5358

10.1152/physiolgenomics.00056.2003

10.1369/jhc.5A6687.2005

10.1177/154411130201300605

10.1016/j.biomaterials.2006.11.041

10.1007/s00223‐005‐0238‐x

10.1016/j.biomaterials.2007.01.026

10.1016/S0076‐6879(06)17017‐2

10.1160/TH03-05-0328

10.1359/jbmr.1999.14.7.1239

10.1042/BST0320407

10.1161/HYPERTENSIONAHA.106.080994

Kii I, 2007, Periostin function in the periodontal ligament and the periosteum, Clin Calcium, 17, 202

10.1016/j.bbrc.2006.02.016

10.2220/biomedres.28.219

10.1002/dvdy.10453

10.1016/j.ydbio.2003.12.007

Kudo Y, 2007, Periostin: novel diagnostic and therapeutic target for cancer, Histol Histopathol, 22, 1167

10.1038/nm1619

10.1369/jhc.7A7258.2007

10.1160/TH03-06-0399

10.1007/s00441‐006‐0282‐5

10.1016/j.ceb.2006.08.009

10.1242/jcs.03270

10.1046/j.0022‐202X.2003.22133.x

10.1152/japplphysiol.01311.2003

10.1016/j.atherosclerosis.2005.11.002

10.1161/01.ATV.0000149141.81230.c6

10.1002/jcb.20115

10.1152/ajpcell.00153.2006

10.1016/j.semcancer.2007.10.001

10.1016/S0962‐8924(98)01362‐2

Majesky MW, 1994, Neointima formation after acute vascular injury. Role of counteradhesive extracellular matrix proteins, Tex Heart Inst J, 21, 78

10.1177/154405910708600402

10.1016/j.biocel.2003.12.003

10.1016/S0925‐4773(99)00021‐0

10.1172/JCI12609

10.1016/j.orthres.2003.10.007

10.1016/S0003‐4975(03)01584‐4

10.1002/jcb.21224

10.1196/annals.1420.005

10.1016/j.ydbio.2008.01.003

10.1161/CIRCRESAHA.107.149047

10.1007/s12185‐008‐0095‐2

10.1002/jcb.10272

10.1016/S0002-9440(10)63259-2

10.1080/000163598428310

10.1038/245264a0

10.1046/j.1365‐2613.2000.00155.x

10.1128/MCB.25.24.11131‐11144.2005

10.1007/PL00000807

10.1073/pnas.0706793104

10.1016/j.biomaterials.2006.03.009

10.1084/jem.20071297

10.1161/CIRCRESAHA.107.159517

10.1002/path.1400

10.1002/ar.a.20080

10.1093/carcin/bgi034

10.1016/j.jaci.2006.02.046

10.1042/bj2940271

10.1097/00004872‐200312000‐00002

10.1186/1476‐4598‐6‐80

10.1111/j.1432‐0436.2007.00233.x

10.1111/1523‐1747.ep12530093

10.1111/1523‐1747.ep12481404

10.1016/S0735‐1097(99)00272‐7

10.1016/S0021‐9150(01)00627‐X

Westling L, 1998, Craniofacial manifestations in the Marfan syndrome: palatal dimensions and a comparative cephalometric analysis, J Craniofac Genet Dev Biol, 18, 211

10.1089/ars.2006.8.338

10.1007/s00441‐002‐0664‐2

10.1073/pnas.0707413104

10.1177/002215549904701201

10.1091/mbc.11.10.3353

10.1387/ijdb.041871pz

Thông tin
Thông tin xuất bản

Journal of Cell Communication and Signaling

Thông tin tác giả