Interactions between lysyl oxidases and ADAMTS proteins suggest a novel crosstalk between two extracellular matrix families

被引:17
作者
Aviram, Rohtem [1 ,2 ]
Zaffryar-Eilot, Shelly [1 ,2 ]
Hubmacher, Dirk [3 ]
Grunwald, Hagar [1 ,2 ]
Maki, Joni M. [4 ,5 ]
Myllyharju, Johanna [4 ,5 ]
Apte, Suneel S. [3 ]
Hasson, Peleg [1 ,2 ]
机构
[1] Technion Israel Inst Technol, Rappaport Fac Med, IL-31096 Haifa, Israel
[2] Technion Israel Inst Technol, Res Inst, IL-31096 Haifa, Israel
[3] Cleveland Clin, Dept Biomed Engn, Lerner Res Inst, Cleveland, OH 44120 USA
[4] Univ Oulu, Bioctr Oulu, Oulu Ctr Cell Matrix Res, Oulu, Finland
[5] Univ Oulu, Fac Biochem & Mol Med, Oulu, Finland
基金
芬兰科学院; 美国国家卫生研究院;
关键词
SECRETED GLYCOPROTEIN; BETA; FIBRILLIN-1; MUTATION; BINDS; INHIBITION; DISSECTION; DYSPLASIA; MECHANISM; INSIGHTS;
D O I
10.1016/j.matbio.2018.05.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The extracellular matrix (ECM) regulates numerous cellular events in addition to providing structural integrity. Among several protein and enzyme families implicated in functions of the ECM, the lysyl oxidases and ADAMTS proteins are known to participate in microfibril and elastic fiber formation as well as ECM-associated signaling. A yeast two-hybrid screen to identify lysyl oxidase (LOX) binding proteins identified ADAMTSL4 as a potential interactor. We demonstrate here that several members of the LOX and ADAMTS families interact with one another. Upon investigating the interaction between LOX and ADAMTSL2 we found that the absence or inhibition of Lox affected ADAMTSL2 molecular forms and reduced its tissue levels. Thus, ADAMTSL2 stability and inter-molecular complexes may depend on the activity of lysyl oxidases. (C) 2018 Elsevier B.V. All rights reserved.
引用
收藏
页码:114 / 125
页数:12
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