Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization

被引:102
作者
Kalamajski, Sebastian [1 ]
Aspberg, Anders [2 ]
Lindblom, Karin [1 ]
Heinegard, Dick [1 ]
Oldberg, Ake [1 ]
机构
[1] Lund Univ, Dept Expt Med Sci, SE-22184 Lund, Sweden
[2] Univ Copenhagen, Dept Biol, DK-2200 Copenhagen, Denmark
基金
瑞典研究理事会;
关键词
asporin; biomineralization; calcium; collagen binding; decorin; small leucine-rich repeat proteoglycan/protein (SLRP); BONE MORPHOGENETIC PROTEIN-2; LEUCINE-RICH REPEATS; GROWTH-FACTOR-BETA; OXALATE CRYSTALLIZATION; MOLECULAR MODULATION; TISSUE FORMATION; EXPRESSION; CELLS; FIBROMODULIN; OSTEOARTHRITIS;
D O I
10.1042/BJ20090542
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 interactions of the ECM (extracellular matrix) protein asporin with ECM components have previously not been investigated. Here, we show that asporin binds collagen type I. This binding is inhibited by recombinant asporin fragment LRR (leucine-rich repeat) 10-12 and by full-length decorin, but not by biglycan. We demonstrate that the polyaspartate domain binds calcium and regulates hydroxyapatite formation in vitro. In the presence of asporin, the number of collagen nodules, and mRNA of osteoblastic markers Osterix and Runx2 were increased. Moreover, decorin or the collagen-binding asporin fragment LRR 10-12 inhibited the pro-osteoblastic activity of full-length asporin. Our results suggest that asporin and decorin compete for binding to collagen and that the polyaspartate in asporin directly regulates collagen mineralization. Therefore asporin has a role in osteoblast-driven collagen biomineralization activity. We also show that asporin can be expressed in Escherichia coli (Rosettagami (TM)) with correctly positioned cysteine bridges, and a similar system can possibly be used for the expression of other SLRPs (small LRR proteoglycans/proteins).
引用
收藏
页码:53 / 59
页数:7
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