The roles of protein tyrosine phosphatases in bone-resorbing osteoclasts.
作者： Moran Shalev , Ari Elson
DOI: 10.1016/J.BBAMCR.2018.07.005
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摘要: Abstract Maintaining the proper balance between osteoblast-mediated production of bone and its degradation by osteoclasts is essential for health. Osteoclasts are giant phagocytic cells that formed fusion monocyte-macrophage precursor cells; mature adhere to tightly secrete protons proteases degrade matrix. Phosphorylation tyrosine residues in proteins, which regulated biochemically-antagonistic activities protein kinases phosphatases (PTPs), central regulating their bone-resorbing activity. Here we review roles individual PTPs classical dual-specificity sub-families known support these processes (SHP2, cyt-PTPe, PTPRO, PTP-PEST, CD45) or inhibit them (SHP1, PTEN, MKP1). Characterizing functions complete molecular level understanding resorption designing novel therapeutic approaches treating disease.
sci-hub.se 参考文章(112)
H Yu, Q Li, B Herbert, R Zinna, K Martin, C R Junior, K L Kirkwood, Anti-inflammatory effect of MAPK phosphatase-1 local gene transfer in inflammatory bone loss Gene Therapy. ,vol. 18, pp. 344- 353 ,(2011) , 10.1038/GT.2010.139
Dan Georgess, Irma Machuca-Gayet, Anne Blangy, Pierre Jurdic, Podosome organization drives osteoclast-mediated bone resorption Cell Adhesion & Migration. ,vol. 8, pp. 191- 204 ,(2014) , 10.4161/CAM.27840
Andres Alonso, Joanna Sasin, Nunzio Bottini, Ilan Friedberg, Iddo Friedberg, Andrei Osterman, Adam Godzik, Tony Hunter, Jack Dixon, Tomas Mustelin, Protein Tyrosine Phosphatases in the Human Genome Cell. ,vol. 117, pp. 699- 711 ,(2004) , 10.1016/J.CELL.2004.05.018
Eynat Finkelshtein, Sutada Lotinun, Einat Levy-Apter, Esther Arman, Jeroen den Hertog, Roland Baron, Ari Elson, Protein tyrosine phosphatases ε and α perform nonredundant roles in osteoclasts Molecular Biology of the Cell. ,vol. 25, pp. 1808- 1818 ,(2014) , 10.1091/MBC.E14-03-0788
Koji Nakamura, Yusuke Mizuno, Kunimi Kikuchi, Molecular Cloning of a Novel Cytoplasmic Protein Tyrosine Phosphatase PTPϵ Biochemical and Biophysical Research Communications. ,vol. 218, pp. 726- 732 ,(1996) , 10.1006/BBRC.1996.0129
Benjamin Geiger, Chen Luxenburg, Lia Addadi, The molecular dynamics of osteoclast adhesions. European Journal of Cell Biology. ,vol. 85, pp. 203- 211 ,(2006) , 10.1016/J.EJCB.2005.11.002
SM Brady-Kalnay, AJ Flint, NK Tonks, Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation. Journal of Cell Biology. ,vol. 122, pp. 961- 972 ,(1993) , 10.1083/JCB.122.4.961
Archana Sanjay, Adam Houghton, Lynn Neff, Emilia DiDomenico, Chantal Bardelay, Evelyne Antoine, Joan Levy, James Gailit, David Bowtell, William C. Horne, Roland Baron, Cbl Associates with Pyk2 and Src to Regulate Src Kinase Activity, αvβ3 Integrin-Mediated Signaling, Cell Adhesion, and Osteoclast Motility Journal of Cell Biology. ,vol. 152, pp. 181- 196 ,(2001) , 10.1083/JCB.152.1.181
Mehran Amoui, David J. Baylink, John B. Tillman, K.-H. William Lau, Expression of a Structurally Unique Osteoclastic Protein-tyrosine Phosphatase Is Driven by an Alternative Intronic, Cell Type-specific Promoter Journal of Biological Chemistry. ,vol. 278, pp. 44273- 44280 ,(2003) , 10.1074/JBC.M303933200
Peter A. Steck, Mark A. Pershouse, Samar A. Jasser, W.K. Alfred Yung, Huai Lin, Azra H. Ligon, Lauren A. Langford, Michelle L. Baumgard, Thomas Hattier, Thaylon Davis, Cheryl Frye, Rong Hu, Bradley Swedlund, David H.R. Teng, Sean V. Tavtigian, Identification of a candidate tumour suppressor gene, MMAC1 , at chromosome 10q23.3 that is mutated in multiple advanced cancers Nature Genetics. ,vol. 15, pp. 356- 362 ,(1997) , 10.1038/NG0497-356