Incorporation of Tenascin-C into the Extracellular Matrix by Periostin Underlies an Extracellular Meshwork Architecture

作者: Isao Kii , Takashi Nishiyama , Minqi Li , Ken-ichi Matsumoto , Mitsuru Saito

DOI: 10.1074/JBC.M109.051961

关键词: ExtracellularPeriostinMatricellular proteinType I collagenExtracellular matrixFibrilAnatomyTenascin CChemistryFibronectinCell biology

摘要: Extracellular matrix (ECM) underlies a complicated multicellular architecture that is subjected to significant forces from mechanical environment. Although various components of the ECM have been enumerated, mechanisms evolve sophisticated remain be addressed. Here we show periostin, matricellular protein, promotes incorporation tenascin-C into and organizes meshwork ECM. We found both periostin null mice exhibited similar phenotype, confined tibial periostitis, which possibly corresponds medial stress syndrome in human sports injuries. Periostin possessed adjacent domains bind other protein: fibronectin type I collagen, respectively. These functioned as bridge between ECM, increased deposition on The hexabrachions may stabilize bifurcations fibrils, integrated extracellular architecture. This study suggests role for adaptation

参考文章(61)
Roumen Pankov, Kenneth M Yamada, Fibronectin at a glance. Journal of Cell Science. ,vol. 115, pp. 3861- 3863 ,(2002) , 10.1242/JCS.00059
Pierre-Jean Wipff, Daniel B. Rifkin, Jean-Jacques Meister, Boris Hinz, Myofibroblast contraction activates latent TGF-β1 from the extracellular matrix Journal of Cell Biology. ,vol. 179, pp. 1311- 1323 ,(2007) , 10.1083/JCB.200704042
Amy D Bradshaw, Pauli Puolakkainen, Thomas N Wight, E Helene Sage, Jayasri Dasgupta, Jeffrey M Davidson, None, SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. Journal of Investigative Dermatology. ,vol. 120, pp. 949- 955 ,(2003) , 10.1046/J.1523-1747.2003.12241.X
Hsiang-Hsi Hong, Nicole Pischon, Ronaldo B. Santana, Amitha H. Palamakumbura, Hermik Babakhanlou Chase, Donald Gantz, Ying Guo, Mehmet Ilhan Uzel, Daniel Ma, Philip C. Trackman, A role for lysyl oxidase regulation in the control of normal collagen deposition in differentiating osteoblast cultures Journal of Cellular Physiology. ,vol. 200, pp. 53- 62 ,(2004) , 10.1002/JCP.10476
O. Boussif, F. Lezoualc'h, M. A. Zanta, M. D. Mergny, D. Scherman, B. Demeneix, J. P. Behr, A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine Proceedings of the National Academy of Sciences of the United States of America. ,vol. 92, pp. 7297- 7301 ,(1995) , 10.1073/PNAS.92.16.7297
Nicole Pischon, Hermik Babakhanlou-Chase, Laurent Darbois, Wen-Bin Ho, Mitchell C. Brenner, Efrat Kessler, Amitha H. Palamakumbura, Philip C. Trackman, A procollagen C-proteinase inhibitor diminishes collagen and lysyl oxidase processing but not collagen cross-linking in osteoblastic cultures. Journal of Cellular Physiology. ,vol. 203, pp. 111- 117 ,(2005) , 10.1002/JCP.20206
Peter Duckert, Søren Brunak, Nikolaj Blom, Prediction of proprotein convertase cleavage sites Protein Engineering Design & Selection. ,vol. 17, pp. 107- 112 ,(2004) , 10.1093/PROTEIN/GZH013
Justin P. Annes, Yan Chen, John S. Munger, Daniel B. Rifkin, Integrin αVβ6-mediated activation of latent TGF-β requires the latent TGF-β binding protein-1 Journal of Cell Biology. ,vol. 165, pp. 723- 734 ,(2004) , 10.1083/JCB.200312172
Sumito Koshida, Yasuyuki Kishimoto, Hideko Ustumi, Toshihiro Shimizu, Makoto Furutani-Seiki, Hisato Kondoh, Shinji Takada, Integrinα5-dependent fibronectin accumulation for maintenance of somite boundaries in zebrafish embryos Developmental Cell. ,vol. 8, pp. 587- 598 ,(2005) , 10.1016/J.DEVCEL.2005.03.006
Yumiko Saga, Tetsuya Tsukamoto, Naihe Jing, Moriaki Kusakabe, Teruyo Sakakura, Murine tenascin: cDNA cloning, structure and temporal expression of isoforms Gene. ,vol. 104, pp. 177- 185 ,(1991) , 10.1016/0378-1119(91)90248-A