TIMPs: versatile extracellular regulators in cancer
作者： Hartland W. Jackson , Virginie Defamie , Paul Waterhouse , Rama Khokha
DOI: 10.1038/NRC.2016.115
关键词:
摘要: A compelling long-term goal of cancer biology is to understand the crucial players during tumorigenesis in order develop new interventions. Here, we review how four non-redundant tissue inhibitors metalloproteinases (TIMPs) regulate pericellular proteolysis a vast range matrix and cell surface proteins, generating simultaneous effects on tumour architecture signalling. Experimental studies demonstrate contribution TIMPs majority hallmarks, human cancers invariably show TIMP deregulation or stroma. Of TIMPs, TIMP1 overexpression TIMP3 silencing consistently associated with progression poor patient prognosis. Future efforts will align mouse model systems changes patients, delineate protease-independent function, pinpoint therapeutic targets within TIMP-metalloproteinase-substrate network use liquid biopsy samples as biomarkers for
nature.com
sci-hub.se 参考文章(208)
Caroline M. Alexander, Frieda Reichsman, Michael T. Hinkes, John Lincecum, Klaus A. Becker, Susan Cumberledge, Merton Bernfield, Syndecan-1 is required for Wnt-1-induced mammary tumorigenesis in mice Nature Genetics. ,vol. 25, pp. 329- 332 ,(2000) , 10.1038/77108
K.J. Leco, R. Khokha, N. Pavloff, S.P. Hawkes, D.R. Edwards, Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. Journal of Biological Chemistry. ,vol. 269, pp. 9352- 9360 ,(1994) , 10.1016/S0021-9258(17)37115-6
Wael Sakr, J. Edson Pontes, Javier Angulo, David J. Grignon, Falah Shamsa, John C. Crissman, Marta Toth, Vincent Ravery, Rafael Fridman, High Levels of Tissue Inhibitor of Metalloproteinase-2 (TIMP-2) Expression Are Associated with Poor Outcome in Invasive Bladder Cancer Cancer Research. ,vol. 56, pp. 1654- 1659 ,(1996)
D R Edwards, C L Parfett, D T Denhardt, Transcriptional regulation of two serum-induced RNAs in mouse fibroblasts: equivalence of one species to B2 repetitive elements. Molecular and Cellular Biology. ,vol. 5, pp. 3280- 3288 ,(1985) , 10.1128/MCB.5.11.3280
Krishna C. Vallabhaneni, Patrice Penfornis, Santosh Dhule, Francois Guillonneau, Kristen V. Adams, Yin Yuan Mo, Rui Xu, Yiming Liu, Kounosuke Watabe, Mohan C. Vemuri, Radhika Pochampally, Extracellular vesicles from bone marrow mesenchymal stem/stromal cells transport tumor regulatory microRNA, proteins, and metabolites Oncotarget. ,vol. 6, pp. 4953- 4967 ,(2015) , 10.18632/ONCOTARGET.3211
Dezhi Mu, Stephanie Cambier, Lars Fjellbirkeland, Jody L. Baron, John S. Munger, Hisaaki Kawakatsu, Dean Sheppard, V. Courtney Broaddus, Stephen L. Nishimura, The integrin αvβ8 mediates epithelial homeostasis through MT1-MMP–dependent activation of TGF-β1 Journal of Cell Biology. ,vol. 157, pp. 493- 507 ,(2002) , 10.1083/JCB.200109100
Hibret A. Adissu, Colin McKerlie, Marco Di Grappa, Paul Waterhouse, Qiang Xu, Hui Fang, Rama Khokha, Geoffrey A. Wood, Timp3 loss accelerates tumour invasion and increases prostate inflammation in a mouse model of prostate cancer. The Prostate. ,vol. 75, pp. 1831- 1843 ,(2015) , 10.1002/PROS.23056
M E Taube, X-W Liu, R Fridman, H-R C Kim, TIMP-1 regulation of cell cycle in human breast epithelial cells via stabilization of p27KIP1 protein Oncogene. ,vol. 25, pp. 3041- 3048 ,(2006) , 10.1038/SJ.ONC.1209336
Z Wang, B Wang, Y Shi, C Xu, H L Xiao, L N Ma, S L Xu, L Yang, Q L Wang, W Q Dang, W Cui, S C Yu, Y F Ping, Y H Cui, H F Kung, C Qian, X Zhang, X W Bian, Oncogenic miR-20a and miR-106a Enhance the Invasiveness of Human Glioma Stem Cells by Directly Targeting TIMP-2 Oncogene. ,vol. 34, pp. 1407- 1419 ,(2015) , 10.1038/ONC.2014.75
Mitsutoshi Nakamura, Eiwa Ishida, Keiji Shimada, Munehiro Kishi, Hiroyuki Nakase, Toshisuke Sakaki, Noboru Konishi, Frequent LOH on 22q12.3 and TIMP-3 inactivation occur in the progression to secondary glioblastomas. Laboratory Investigation. ,vol. 85, pp. 165- 175 ,(2005) , 10.1038/LABINVEST.3700223