Regulation of chondrocyte differentiation by ADAMTS-12 metalloproteinase depends on its enzymatic activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-02

AUTHORS

X. H. Bai, D. W. Wang, Y. Luan, X. P. Yu, C. J. Liu

ABSTRACT

ADAMTS-12, a metalloproteinase that belongs to ADAMTS family, is strongly upregulated during chondrogenesis and demonstrates prominent expression in the growth plate chondrocytes. ADAMTS-12 potently inhibits chondrocyte differentiation, as revealed by altered expression of both early and later genes critical for chondrogenesis. In addition, ADAMTS-12-mediated inhibition of chondrogenesis depends on its enzymatic activity, since its point mutant lacking enzymatic activity completely loses this activity. Furthermore, the C-terminal four thrombospondin motifs known to bind COMP substrate is necessary for its full proteolytic activity and inhibition of chondrocyte differentiation. Mechanism studies demonstrate that ADAMTS-12 induces PTHrP, whereas it inhibits IHH during chondrogenesis. Furthermore, PTHrP induces ADAMTS-12 and ADAMTS-12 is hardly detectable in PTHrP-/-growth plate chondrocytes. Importantly, knocking down ADAMTS-12 mRNA levels or blocking ADAMTS-12 activity almost abolishes the PTHrP-mediated inhibition of type X collagen expression. Collectively, these findings demonstrate that ADAMTS-12, a downstream molecule of PTHrP signaling, is a novel regulator of chondrogenesis. More... »

PAGES

667

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00018-008-8633-x

DOI

http://dx.doi.org/10.1007/s00018-008-8633-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1044356790

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19151918


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